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Conserved domains on  [gi|193912267|gb|EDW11134|]
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uncharacterized protein Dmoj_GI16990 [Drosophila mojavensis]

Protein Classification

cytochrome P450( domain architecture ID 15296490)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
70-496 6.26e-143

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: 417.71  E-value: 6.26e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  70 GKERAVGVFLTRQPQILVLDPQLAHEILVTNFSDFRDTVTssYVTHSKDYDkyvSRNPFFSAGDEWKKHRVDAGAGLTPN 149
Cdd:cd11056    1 GGEPFVGIYLFRRPALLVRDPELIKQILVKDFAHFHDRGL--YSDEKDDPL---SANLFSLDGEKWKELRQKLTPAFTSG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 150 KLKQAYAIWEQTGEQLVSFIQSCIEERgsNIIETRDLCYRYTAQAMGDFIWGIDAgsltgsaketSSFQRISTEWVTHAF 229
Cdd:cd11056   76 KLKNMFPLMVEVGDELVDYLKKQAEKG--KELEIKDLMARYTTDVIASCAFGLDA----------NSLNDPENEFREMGR 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 230 LGM--TRLNR-----TTIAPIVRRLFRMRFFTQAADDFYLKLTRDAAKLRQsGSGGERSDYLAHLLQLQEKGA------- 295
Cdd:cd11056  144 RLFepSRLRGlkfmlLFFFPKLARLLRLKFFPKEVEDFFRKLVRDTIEYRE-KNNIVRNDFIDLLLELKKKGKieddkse 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 296 ---SLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDV-DKRISYEQLNALPYLDQCVYESMRM 371
Cdd:cd11056  223 kelTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKhGGELTYEALQEMKYLDQVVNETLRK 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 372 TSVIGFLLKICTRPTKIDlgnDRILNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISElTKRGCLLAFGDGPR 451
Cdd:cd11056  303 YPPLPFLDRVCTKDYTLP---GTDVVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKKK-RHPYTYLPFGDGPR 378
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 193912267 452 ICLGMRVGLLSVKMALLRILSQYKIEQTKK----LSLSSDSGLGMYLNG 496
Cdd:cd11056  379 NCIGMRFGLLQVKLGLVHLLSNFRVEPSSKtkipLKLSPKSFVLSPKGG 427
 
Name Accession Description Interval E-value
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
70-496 6.26e-143

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: 417.71  E-value: 6.26e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  70 GKERAVGVFLTRQPQILVLDPQLAHEILVTNFSDFRDTVTssYVTHSKDYDkyvSRNPFFSAGDEWKKHRVDAGAGLTPN 149
Cdd:cd11056    1 GGEPFVGIYLFRRPALLVRDPELIKQILVKDFAHFHDRGL--YSDEKDDPL---SANLFSLDGEKWKELRQKLTPAFTSG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 150 KLKQAYAIWEQTGEQLVSFIQSCIEERgsNIIETRDLCYRYTAQAMGDFIWGIDAgsltgsaketSSFQRISTEWVTHAF 229
Cdd:cd11056   76 KLKNMFPLMVEVGDELVDYLKKQAEKG--KELEIKDLMARYTTDVIASCAFGLDA----------NSLNDPENEFREMGR 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 230 LGM--TRLNR-----TTIAPIVRRLFRMRFFTQAADDFYLKLTRDAAKLRQsGSGGERSDYLAHLLQLQEKGA------- 295
Cdd:cd11056  144 RLFepSRLRGlkfmlLFFFPKLARLLRLKFFPKEVEDFFRKLVRDTIEYRE-KNNIVRNDFIDLLLELKKKGKieddkse 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 296 ---SLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDV-DKRISYEQLNALPYLDQCVYESMRM 371
Cdd:cd11056  223 kelTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKhGGELTYEALQEMKYLDQVVNETLRK 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 372 TSVIGFLLKICTRPTKIDlgnDRILNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISElTKRGCLLAFGDGPR 451
Cdd:cd11056  303 YPPLPFLDRVCTKDYTLP---GTDVVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKKK-RHPYTYLPFGDGPR 378
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 193912267 452 ICLGMRVGLLSVKMALLRILSQYKIEQTKK----LSLSSDSGLGMYLNG 496
Cdd:cd11056  379 NCIGMRFGLLQVKLGLVHLLSNFRVEPSSKtkipLKLSPKSFVLSPKGG 427
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
40-477 4.98e-60

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: 204.43  E-value: 4.98e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267   40 PLTLLGSYPGLFGGGSsfiedIGKIYNKYKGKERAV-GVFLTRQPQILVLDPQLAHEILVTNFSDFRDTVTSSYVTHSKD 118
Cdd:pfam00067   6 PLPLFGNLLQLGRKGN-----LHSVFTKLQKKYGPIfRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  119 YDKyvSRNPFFSAGDEWKKHRVDAGAGLTPNKLKQAYAIWEQTGEQLVSFIQSCIEERGSniIETRDLCYRYTAQAMGDF 198
Cdd:pfam00067  81 PFL--GKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGV--IDITDLLFRAALNVICSI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  199 IWGIDAGSLTGSAKETS--SFQRISTEWVT--HAFLGMTRLNRTTIAPIVRRLFRMRfftQAADDFYLKLTRDAAKLRQS 274
Cdd:pfam00067 157 LFGERFGSLEDPKFLELvkAVQELSSLLSSpsPQLLDLFPILKYFPGPHGRKLKRAR---KKIKDLLDKLIEERRETLDS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  275 GSGGERsDYLAHLLQLQEKGA----SLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRI 350
Cdd:pfam00067 234 AKKSPR-DFLDALLLAKEEEDgsklTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  351 SYEQLNALPYLDQCVYESMRMTSVIGFLL-KICTRPTKIDlgnDRilNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERF 429
Cdd:pfam00067 313 TYDDLQNMPYLDAVIKETLRLHPVVPLLLpREVTKDTVIP---GY--LIPKGTLVIVNLYALHRDPEVFPNPEEFDPERF 387
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 193912267  430 DNGAISELTKRGcLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIE 477
Cdd:pfam00067 388 LDENGKFRKSFA-FLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVE 434
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
79-474 4.78e-33

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: 129.63  E-value: 4.78e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  79 LTRQPQILVLDPQLAHEILVTnfsdfRDTVTSSYVTHSKDYDKYVSRNPFFSA-GDEWKKHR--VDAGagLTPNKLKqAY 155
Cdd:COG2124   39 LPGGGAWLVTRYEDVREVLRD-----PRTFSSDGGLPEVLRPLPLLGDSLLTLdGPEHTRLRrlVQPA--FTPRRVA-AL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 156 A--IWEQTGEQLVSFiqsciEERGS-NIIEtrDLCYRYTAQAMGDFIwGIDAGsltgsakETSSFQRISTEWVtHAFLGM 232
Cdd:COG2124  111 RprIREIADELLDRL-----AARGPvDLVE--EFARPLPVIVICELL-GVPEE-------DRDRLRRWSDALL-DALGPL 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 233 TRLNRTTIAPIVRRLFRmrFFTQAAddfylkltrdaAKLRQSGsggeRSDYLAHLLQLQEKGASLDD--MVGHALTVLMD 310
Cdd:COG2124  175 PPERRRRARRARAELDA--YLRELI-----------AERRAEP----GDDLLSALLAARDDGERLSDeeLRDELLLLLLA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 311 GFETSSAVLYHMLYTLGAYPEQQEKLRSEvlaaldvdkrisyeqlnaLPYLDQCVYESMRMTSVIGFLLKICTRPTkiDL 390
Cdd:COG2124  238 GHETTANALAWALYALLRHPEQLARLRAE------------------PELLPAAVEETLRLYPPVPLLPRTATEDV--EL 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 391 GNDRIlnvEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGaiseltkrgcLLAFGDGPRICLGMRVGLLSVKMALLRI 470
Cdd:COG2124  298 GGVTI---PAGDRVLLSLAAANRDPRVFPDPDRFDPDRPPNA----------HLPFGGGPHRCLGAALARLEARIALATL 364

                 ....
gi 193912267 471 LSQY 474
Cdd:COG2124  365 LRRF 368
PTZ00404 PTZ00404
cytochrome P450; Provisional
40-490 2.65e-22

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 99.80  E-value: 2.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  40 PLTLLGSypgLFGGGSSFIEDIGKIYNKYKGKERavgVFLTRQPQILVLDPQLAHEILVTNFSDFRDTVTSSYVTHSKDY 119
Cdd:PTZ00404  36 PIPILGN---LHQLGNLPHRDLTKMSKKYGGIFR---IWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHGTFY 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 120 DKYVSrnpffSAGDEWKKHRVDAGAGLTPNKLKQAYAIWEQTGEQLVSFIQScIEERGsNIIETRDLCYRYTAQAMGDFI 199
Cdd:PTZ00404 110 HGIVT-----SSGEYWKRNREIVGKAMRKTNLKHIYDLLDDQVDVLIESMKK-IESSG-ETFEPRYYLTKFTMSAMFKYI 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 200 WGID---------------------------AGSLTGSAKETSSFQRISTEWVTHAFlgmtrlnrttiaPIVRRLFRMRF 252
Cdd:PTZ00404 183 FNEDisfdedihngklaelmgpmeqvfkdlgSGSLFDVIEITQPLYYQYLEHTDKNF------------KKIKKFIKEKY 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 253 FTQaaddfylKLTRDAAKLRQsgsggersdyLAHLLqLQEKGASLDDMVGHALTVLMD----GFETSSAVLYHMLYTLGA 328
Cdd:PTZ00404 251 HEH-------LKTIDPEVPRD----------LLDLL-IKEYGTNTDDDILSILATILDfflaGVDTSATSLEWMVLMLCN 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 329 YPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGF-LLKICTRPTKIDLGNdrilNVEPGVTVAIP 407
Cdd:PTZ00404 313 YPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPVSPFgLPRSTSNDIIIGGGH----FIPKDAQILIN 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 408 AYHFHHDEAYFPQPDEFRPERFDNGAISEltkrgCLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKI--EQTKKLSLS 485
Cdd:PTZ00404 389 YYSLGRNEKYFENPEQFDPSRFLNPDSND-----AFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLksIDGKKIDET 463

                 ....*
gi 193912267 486 SDSGL 490
Cdd:PTZ00404 464 EEYGL 468
 
Name Accession Description Interval E-value
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
70-496 6.26e-143

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: 417.71  E-value: 6.26e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  70 GKERAVGVFLTRQPQILVLDPQLAHEILVTNFSDFRDTVTssYVTHSKDYDkyvSRNPFFSAGDEWKKHRVDAGAGLTPN 149
Cdd:cd11056    1 GGEPFVGIYLFRRPALLVRDPELIKQILVKDFAHFHDRGL--YSDEKDDPL---SANLFSLDGEKWKELRQKLTPAFTSG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 150 KLKQAYAIWEQTGEQLVSFIQSCIEERgsNIIETRDLCYRYTAQAMGDFIWGIDAgsltgsaketSSFQRISTEWVTHAF 229
Cdd:cd11056   76 KLKNMFPLMVEVGDELVDYLKKQAEKG--KELEIKDLMARYTTDVIASCAFGLDA----------NSLNDPENEFREMGR 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 230 LGM--TRLNR-----TTIAPIVRRLFRMRFFTQAADDFYLKLTRDAAKLRQsGSGGERSDYLAHLLQLQEKGA------- 295
Cdd:cd11056  144 RLFepSRLRGlkfmlLFFFPKLARLLRLKFFPKEVEDFFRKLVRDTIEYRE-KNNIVRNDFIDLLLELKKKGKieddkse 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 296 ---SLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDV-DKRISYEQLNALPYLDQCVYESMRM 371
Cdd:cd11056  223 kelTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKhGGELTYEALQEMKYLDQVVNETLRK 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 372 TSVIGFLLKICTRPTKIDlgnDRILNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISElTKRGCLLAFGDGPR 451
Cdd:cd11056  303 YPPLPFLDRVCTKDYTLP---GTDVVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKKK-RHPYTYLPFGDGPR 378
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 193912267 452 ICLGMRVGLLSVKMALLRILSQYKIEQTKK----LSLSSDSGLGMYLNG 496
Cdd:cd11056  379 NCIGMRFGLLQVKLGLVHLLSNFRVEPSSKtkipLKLSPKSFVLSPKGG 427
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
62-481 6.56e-79

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: 252.89  E-value: 6.56e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  62 GKIYnkykgkeravGVFLTRQPQILVLDPQLAHEILVTNFSDFRDTVtsSYVTHSKDYDKYVsrnpFFSAGDEWKKHRVD 141
Cdd:cd11055    3 GKVF----------GLYFGTIPVIVVSDPEMIKEILVKEFSNFTNRP--LFILLDEPFDSSL----LFLKGERWKRLRTT 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 142 AGAGLTPNKLKQAYAIWEQTGEQLVSFIQScIEERGSnIIETRDLCYRYTAQAMGDFIWGIDA-------GSLTGSAKET 214
Cdd:cd11055   67 LSPTFSSGKLKLMVPIINDCCDELVEKLEK-AAETGK-PVDMKDLFQGFTLDVILSTAFGIDVdsqnnpdDPFLKAAKKI 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 215 SSFQRISTEWVTHAFLGMtrlnrttiaPIVRRLFRMRFFTQAADdFYLKLTRDAAKLRQSGSGGERSDYLAHLL------ 288
Cdd:cd11055  145 FRNSIIRLFLLLLLFPLR---------LFLFLLFPFVFGFKSFS-FLEDVVKKIIEQRRKNKSSRRKDLLQLMLdaqdsd 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 289 -QLQEKGASLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYE 367
Cdd:cd11055  215 eDVSKKKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKYLDMVINE 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 368 SMRMTSVIGFLLKICTRPTKIdlGNDRILNvepGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISeltKR--GCLLA 445
Cdd:cd11055  295 TLRLYPPAFFISRECKEDCTI--NGVFIPK---GVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKA---KRhpYAYLP 366
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 193912267 446 FGDGPRICLGMRVGLLSVKMALLRILSQYKIEQTKK 481
Cdd:cd11055  367 FGAGPRNCIGMRFALLEVKLALVKILQKFRFVPCKE 402
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
40-477 4.98e-60

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: 204.43  E-value: 4.98e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267   40 PLTLLGSYPGLFGGGSsfiedIGKIYNKYKGKERAV-GVFLTRQPQILVLDPQLAHEILVTNFSDFRDTVTSSYVTHSKD 118
Cdd:pfam00067   6 PLPLFGNLLQLGRKGN-----LHSVFTKLQKKYGPIfRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  119 YDKyvSRNPFFSAGDEWKKHRVDAGAGLTPNKLKQAYAIWEQTGEQLVSFIQSCIEERGSniIETRDLCYRYTAQAMGDF 198
Cdd:pfam00067  81 PFL--GKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGV--IDITDLLFRAALNVICSI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  199 IWGIDAGSLTGSAKETS--SFQRISTEWVT--HAFLGMTRLNRTTIAPIVRRLFRMRfftQAADDFYLKLTRDAAKLRQS 274
Cdd:pfam00067 157 LFGERFGSLEDPKFLELvkAVQELSSLLSSpsPQLLDLFPILKYFPGPHGRKLKRAR---KKIKDLLDKLIEERRETLDS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  275 GSGGERsDYLAHLLQLQEKGA----SLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRI 350
Cdd:pfam00067 234 AKKSPR-DFLDALLLAKEEEDgsklTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  351 SYEQLNALPYLDQCVYESMRMTSVIGFLL-KICTRPTKIDlgnDRilNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERF 429
Cdd:pfam00067 313 TYDDLQNMPYLDAVIKETLRLHPVVPLLLpREVTKDTVIP---GY--LIPKGTLVIVNLYALHRDPEVFPNPEEFDPERF 387
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 193912267  430 DNGAISELTKRGcLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIE 477
Cdd:pfam00067 388 LDENGKFRKSFA-FLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVE 434
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
75-477 2.41e-58

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: 198.12  E-value: 2.41e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  75 VGVFLTRQPQILVLDPQLAHEILVTNFSDFRDTVTSSYVTHSkdydkYVSRNPFFSAGDEWKKHRVDAGAGLTPNKLKQA 154
Cdd:cd00302    4 FRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGD-----FLGDGLLTLDGPEHRRLRRLLAPAFTPRALAAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 155 YAIWEQTGEQLVSFIqsciEERGSNIIETRDLCYRYTAQAMGDFIWGIDAGSLTGSAKEtssfqristeWVTHAFLGMTR 234
Cdd:cd00302   79 RPVIREIARELLDRL----AAGGEVGDDVADLAQPLALDVIARLLGGPDLGEDLEELAE----------LLEALLKLLGP 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 235 LNRTTIAPIVRRLFRmrfftQAADDFYlKLTRDAAKLRQSgSGGERSDYLAHLLQLQEKGASLDDMVGHALTVLMDGFET 314
Cdd:cd00302  145 RLLRPLPSPRLRRLR-----RARARLR-DYLEELIARRRA-EPADDLDLLLLADADDGGGLSDEEIVAELLTLLLAGHET 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 315 SSAVLYHMLYTLGAYPEQQEKLRSEVLAaldVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTRPTKIDlgnDR 394
Cdd:cd00302  218 TASLLAWALYLLARHPEVQERLRAEIDA---VLGDGTPEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVELG---GY 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 395 IlnVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAiseLTKRGCLLAFGDGPRICLGMRVGLLSVKMALLRILSQY 474
Cdd:cd00302  292 T--IPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPER---EEPRYAHLPFGAGPHRCLGARLARLELKLALATLLRRF 366

                 ...
gi 193912267 475 KIE 477
Cdd:cd00302  367 DFE 369
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
128-481 4.22e-46

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: 166.16  E-value: 4.22e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 128 FFSAGDEWKKHRVDAGAGLTPNKLKQAYAIW-EQTGEQLVSFIQSCIEERGSNIIETRDLCYRYTAQAMGDFIWGIDAGS 206
Cdd:cd11054   59 LNSNGEEWHRLRSAVQKPLLRPKSVASYLPAiNEVADDFVERIRRLRDEDGEEVPDLEDELYKWSLESIGTVLFGKRLGC 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 207 LtgSAKETSSFQRISTewVTHAFLGMTrlNRTTIAPIVRRLFRMRF---FTQAADDFY---LKLTRDAAK--LRQSGSGG 278
Cdd:cd11054  139 L--DDNPDSDAQKLIE--AVKDIFESS--AKLMFGPPLWKYFPTPAwkkFVKAWDTIFdiaSKYVDEALEelKKKDEEDE 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 279 ERSDYLAHLLQlqEKGASLDDMVGHALTVLMDGFET-SSAVLYhMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNA 357
Cdd:cd11054  213 EEDSLLEYLLS--KPGLSKKEIVTMALDLLLAGVDTtSNTLAF-LLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKK 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 358 LPYLDQCVYESMRMTSVIGFLLKICTRPtkIDLGNdriLNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISEL 437
Cdd:cd11054  290 MPYLKACIKESLRLYPVAPGNGRILPKD--IVLSG---YHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDDSENK 364
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 193912267 438 TKRG-CLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIEQTKK 481
Cdd:cd11054  365 NIHPfASLPFGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEYHHE 409
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
76-480 2.79e-44

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: 161.43  E-value: 2.79e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  76 GVFLTRQPQILVLDPQLAHEILV----TNFSDFRDT----VTSSYVTHSKDydkyvsrnpffsagDEWKKHRVDAGAGLT 147
Cdd:cd20650    7 GIYDGRQPVLAITDPDMIKTVLVkecySVFTNRRPFgpvgFMKSAISIAED--------------EEWKRIRSLLSPTFT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 148 PNKLKQAYAIWEQTGEQLVSFIQSCIEERGSniIETRDLCYRYTAQAMGDFIWGIDAGSLTGS----AKETSSFQRISte 223
Cdd:cd20650   73 SGKLKEMFPIIAQYGDVLVKNLRKEAEKGKP--VTLKDVFGAYSMDVITSTSFGVNIDSLNNPqdpfVENTKKLLKFD-- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 224 WVTHAFLGMTRLnrTTIAPIVRRLfRMRFFTQAADDFYLKLTRDAAKLRQSGSGGERSDYLAHLLQLQ-----EKGASLD 298
Cdd:cd20650  149 FLDPLFLSITVF--PFLTPILEKL-NISVFPKDVTNFFYKSVKKIKESRLDSTQKHRVDFLQLMIDSQnsketESHKALS 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 299 DM--VGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIG 376
Cdd:cd20650  226 DLeiLAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLRLFPIAG 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 377 FLLKICTRPTKIDlGndriLNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISELTKRgCLLAFGDGPRICLGM 456
Cdd:cd20650  306 RLERVCKKDVEIN-G----VFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDNIDPY-IYLPFGSGPRNCIGM 379
                        410       420
                 ....*....|....*....|....
gi 193912267 457 RVGLLSVKMALLRILSQYKIEQTK 480
Cdd:cd20650  380 RFALMNMKLALVRVLQNFSFKPCK 403
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
83-477 2.57e-40

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: 150.88  E-value: 2.57e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  83 PQILVLDPQLAHEILVTNfsdfrdtvtSSYVTHSKDYDKYVSR----NPFFSAGDEWKKHRVDAGAGLTPNKLKQAYAIW 158
Cdd:cd11069   14 ERLLVTDPKALKHILVTN---------SYDFEKPPAFRRLLRRilgdGLLAAEGEEHKRQRKILNPAFSYRHVKELYPIF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 159 EQTGEQLVSFIQSCIEERG--SNIIETRDLCYRYTAQAMGDFIWGIDAGSLTGSAKETS-SFQRISTEwvTHAFLGMTRL 235
Cdd:cd11069   85 WSKAEELVDKLEEEIEESGdeSISIDVLEWLSRATLDIIGLAGFGYDFDSLENPDNELAeAYRRLFEP--TLLGSLLFIL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 236 NRTTIAPIVRRL-----FRMRFFTQAADDFYLKLTRDAAKLRQSGSGGERSDYLAHLLQL----QEKGASLDDMVGHALT 306
Cdd:cd11069  163 LLFLPRWLVRILpwkanREIRRAKDVLRRLAREIIREKKAALLEGKDDSGKDILSILLRAndfaDDERLSDEELIDQILT 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 307 VLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAAL--DVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTR 384
Cdd:cd11069  243 FLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALpdPPDGDLSYDDLDRLPYLNAVCRETLRLYPPVPLTSREATK 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 385 PTKIdlGNDRIlnvEPGVTVAIPAYHFHHD-EAYFPQPDEFRPERFDN----GAISELTKRGCLLAFGDGPRICLGMRVG 459
Cdd:cd11069  323 DTVI--KGVPI---PKGTVVLIPPAAINRSpEIWGPDAEEFNPERWLEpdgaASPGGAGSNYALLTFLHGPRSCIGKKFA 397
                        410
                 ....*....|....*...
gi 193912267 460 LLSVKMALLRILSQYKIE 477
Cdd:cd11069  398 LAEMKVLLAALVSRFEFE 415
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
163-477 5.50e-40

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: 149.30  E-value: 5.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 163 EQLVSFIQSCIEERGSNIIETRDLCYRYTAQAMGDFIWGIDAGSLTGSAKEtssfqristeWVTHAFL-GMTRLNRTTIA 241
Cdd:cd11061   82 EQLCEQLDDRAGKPVSWPVDMSDWFNYLSFDVMGDLAFGKSFGMLESGKDR----------YILDLLEkSMVRLGVLGHA 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 242 PIVRRLFRMR-FFTQAADDF--YLKLTRDAAKLRQSGSGGERSDYLAHLLQ--LQEKGASLD--DMVGHALTVLMDGFET 314
Cdd:cd11061  152 PWLRPLLLDLpLFPGATKARkrFLDFVRAQLKERLKAEEEKRPDIFSYLLEakDPETGEGLDleELVGEARLLIVAGSDT 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 315 SSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRI-SYEQLNALPYLDQCVYESMRMTSVIGFLLKICTRPTKIDLGND 393
Cdd:cd11061  232 TATALSAIFYYLARNPEAYEKLRAELDSTFPSDDEIrLGPKLKSLPYLRACIDEALRLSPPVPSGLPRETPPGGLTIDGE 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 394 RIlnvEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISELTKRGCLLAFGDGPRICLGMRVGLLSVKMALLRILSQ 473
Cdd:cd11061  312 YI---PGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRPEELVRARSAFIPFSIGPRGCIGKNLAYMELRLVLARLLHR 388

                 ....
gi 193912267 474 YKIE 477
Cdd:cd11061  389 YDFR 392
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
82-482 8.35e-40

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: 149.21  E-value: 8.35e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  82 QPQILVLDPQLAHEILvtnfsdfrdtvtSSYVTHSKDYDKYVSRnPFF------SAGDEWKKHRvdagAGLTP----NKL 151
Cdd:cd20628   11 KPYVVVTNPEDIEVIL------------SSSKLITKSFLYDFLK-PWLgdglltSTGEKWRKRR----KLLTPafhfKIL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 152 KQAYAIWEQTGEQLVSFIQSCIEERGSNIIEtrdLCYRYTAQAMGDFIWGIDAGSLTGSAKETSsfqristewvtHAFLG 231
Cdd:cd20628   74 ESFVEVFNENSKILVEKLKKKAGGGEFDIFP---YISLCTLDIICETAMGVKLNAQSNEDSEYV-----------KAVKR 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 232 MTRLnrttiapIVRRLFR--MRFftqaadDFYLKLTRDAAKLRQS-------------------------------GSGG 278
Cdd:cd20628  140 ILEI-------ILKRIFSpwLRF------DFIFRLTSLGKEQRKAlkvlhdftnkvikerreelkaekrnseeddeFGKK 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 279 ERSDYLAHLLQLQEKGASLD--DMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAAL-DVDKRISYEQL 355
Cdd:cd20628  207 KRKAFLDLLLEAHEDGGPLTdeDIREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFgDDDRRPTLEDL 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 356 NALPYLDQCVYESMRMTSVIGFLLKICTRPTKIDlgnDRILnveP-GVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAI 434
Cdd:cd20628  287 NKMKYLERVIKETLRLYPSVPFIGRRLTEDIKLD---GYTI---PkGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENS 360
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 193912267 435 SeltKR--GCLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIEQTKKL 482
Cdd:cd20628  361 A---KRhpYAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFRVLPVPPG 407
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
79-478 2.24e-38

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


Pssm-ID: 410704 [Multi-domain]  Cd Length: 421  Bit Score: 145.16  E-value: 2.24e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  79 LTRQPQILVLDPQLAHEILVTNFSDFRDTvtSSYVTHSKDydkyVSRNPFFSA-GDEWKKHRVDAGAGLTPNKLKQAYAI 157
Cdd:cd11083    8 LGRQPVLVISDPELIREVLRRRPDEFRRI--SSLESVFRE----MGINGVFSAeGDAWRRQRRLVMPAFSPKHLRYFFPT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 158 WEQTGEQLVSFIQSCIEERgsNIIETRDLCYRYTAQAMGDFIWGIDAGSLTGSAKETS-SFQRIstewvthaflgMTRLN 236
Cdd:cd11083   82 LRQITERLRERWERAAAEG--EAVDVHKDLMRYTVDVTTSLAFGYDLNTLERGGDPLQeHLERV-----------FPMLN 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 237 RTTIAPI----VRRLFRMRFFTQA-------ADDFYLKlTRDAakLRQSGSGGERS-DYLAHLLQLQEKGASLDD--MVG 302
Cdd:cd11083  149 RRVNAPFpywrYLRLPADRALDRAlvevralVLDIIAA-ARAR--LAANPALAEAPeTLLAMMLAEDDPDARLTDdeIYA 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 303 HALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAAL-DVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKI 381
Cdd:cd11083  226 NVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLgGARVPPLLEALDRLPYLEAVARETLRLKPVAPLLFLE 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 382 CTRPTKIDlgnDriLNVEPGVTVAI---PAYhfhHDEAYFPQPDEFRPERF-DNGAISELTKRGCLLAFGDGPRICLGMR 457
Cdd:cd11083  306 PNEDTVVG---D--IALPAGTPVFLltrAAG---LDAEHFPDPEEFDPERWlDGARAAEPHDPSSLLPFGAGPRLCPGRS 377
                        410       420
                 ....*....|....*....|.
gi 193912267 458 VGLLSVKMALLRILSQYKIEQ 478
Cdd:cd11083  378 LALMEMKLVFAMLCRNFDIEL 398
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
74-477 6.27e-38

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: 144.39  E-value: 6.27e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  74 AVGVFLTRQPQILVLDPQLAHEILvTNFSDFRdtvtssyvthsKDYDKYvsRNPFF-------SAGDEWKKHR-VDAGAG 145
Cdd:cd11070    4 AVKILFVSRWNILVTKPEYLTQIF-RRRDDFP-----------KPGNQY--KIPAFygpnvisSEGEDWKRYRkIVAPAF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 146 LTPNKLKQAYAIWEQTgEQLVSFIQSCIEERGSNIIETRDLCYRYTAQAMGDFIWGIDAGSLTG-SAKETSSFQRISTEW 224
Cdd:cd11070   70 NERNNALVWEESIRQA-QRLIRYLLEEQPSAKGGGVDVRDLLQRLALNVIGEVGFGFDLPALDEeESSLHDTLNAIKLAI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 225 VTHAFLGMtrlnrttiaPIVRRLFRMRFFT--QAADDF-----YLKLTRDAAKLRQSGSGGERSDYLAHLLQLQEKGASL 297
Cdd:cd11070  149 FPPLFLNF---------PFLDRLPWVLFPSrkRAFKDVdeflsELLDEVEAELSADSKGKQGTESVVASRLKRARRSGGL 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 298 DD--MVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRI--SYEQLNALPYLDQCVYESMRMTS 373
Cdd:cd11070  220 TEkeLLGNLFIFFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDwdYEEDFPKLPYLLAVIYETLRLYP 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 374 VIGFLLKICTRPTKIDLGNDRILNVEPGVTVAIPAYHFHHDEAY-FPQPDEFRPERF--DNGAISELT----KRGCLLAF 446
Cdd:cd11070  300 PVQLLNRKTTEPVVVITGLGQEIVIPKGTYVGYNAYATHRDPTIwGPDADEFDPERWgsTSGEIGAATrftpARGAFIPF 379
                        410       420       430
                 ....*....|....*....|....*....|.
gi 193912267 447 GDGPRICLGMRVGLLSVKMALLRILSQYKIE 477
Cdd:cd11070  380 SAGPRACLGRKFALVEFVAALAELFRQYEWR 410
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
83-483 5.63e-37

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: 141.20  E-value: 5.63e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  83 PQILVLDPQLAHEILvtnfsdfrdtvTSSY-VTHSKDYDKYVSRNPFFSA-GDEWKKHRVDAGAGLTPNKLKQAYAIWEQ 160
Cdd:cd11057   12 PFVITSDPEIVQVVL-----------NSPHcLNKSFFYDFFRLGRGLFSApYPIWKLQRKALNPSFNPKILLSFLPIFNE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 161 TGEQLVSFIQSCIEERGSNIIetrDLCYRYT-----AQAMGDFIWG--IDAGSLTGSAKE--TSSFQRISTEWVTHAFLG 231
Cdd:cd11057   81 EAQKLVQRLDTYVGGGEFDIL---PDLSRCTlemicQTTLGSDVNDesDGNEEYLESYERlfELIAKRVLNPWLHPEFIY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 232 -MTRLNRttiapivRRLFRMRFFTQAADDFYLKLTRDAAKLRQSGSGGERSDY------LAHLLQLQEKGASLDDM--VG 302
Cdd:cd11057  158 rLTGDYK-------EEQKARKILRAFSEKIIEKKLQEVELESNLDSEEDEENGrkpqifIDQLLELARNGEEFTDEeiMD 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 303 HALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAAL-DVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKI 381
Cdd:cd11057  231 EIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFpDDGQFITYEDLQQLVYLEMVLKETMRLFPVGPLVGRE 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 382 CTRPTKIDLGNdrilNVEPGVTVAIPAYHFHHDEAYF-PQPDEFRPERF--DNGAiseltKRG--CLLAFGDGPRICLGM 456
Cdd:cd11057  311 TTADIQLSNGV----VIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFlpERSA-----QRHpyAFIPFSAGPRNCIGW 381
                        410       420
                 ....*....|....*....|....*..
gi 193912267 457 RVGLLSVKMALLRILSQYKIEQTKKLS 483
Cdd:cd11057  382 RYAMISMKIMLAKILRNYRLKTSLRLE 408
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
76-491 7.97e-37

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: 141.51  E-value: 7.97e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  76 GVFLTRQPQILVLDPQLAHEILVTNFSDFRDTVTSSYVThskdydKYVSRNPFFSAGDEWKKHRVDAGAGLTPNKLKQAY 155
Cdd:cd20649    7 GYYIGRRMFVVIAEPDMIKQVLVKDFNNFTNRMKANLIT------KPMSDSLLCLRDERWKRVRSILTPAFSAAKMKEMV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 156 AIWEQTGEQLVSFIQSCIE-ERGSNIIEtrdlCYR-YTAQAMGDFIWGIDAGS-------LTGSAK---ETSSFQRISTE 223
Cdd:cd20649   81 PLINQACDVLLRNLKSYAEsGNAFNIQR----CYGcFTMDVVASVAFGTQVDSqknpddpFVKNCKrffEFSFFRPILIL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 224 WVTHAFLgmtrlnrttIAPIVRRLFRMRffTQAADDFYLKLTRDAAKLRQSGSGGER-SDYLAHLLQL------------ 290
Cdd:cd20649  157 FLAFPFI---------MIPLARILPNKS--RDELNSFFTQCIRNMIAFRDQQSPEERrRDFLQLMLDArtsakflsvehf 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 291 ---------------------------QEKGASLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAA 343
Cdd:cd20649  226 divndadesaydghpnspaneqtkpskQKRMLTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEF 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 344 LDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTRPTKIdLGndriLNVEPGVTVAIPAYHFHHDEAYFPQPDE 423
Cdd:cd20649  306 FSKHEMVDYANVQELPYLDMVIAETLRMYPPAFRFAREAAEDCVV-LG----QRIPAGAVLEIPVGFLHHDPEHWPEPEK 380
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193912267 424 FRPERFDNGAISElTKRGCLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKI---EQTK-KLSLSSDSGLG 491
Cdd:cd20649  381 FIPERFTAEAKQR-RHPFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFqacPETEiPLQLKSKSTLG 451
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
85-492 1.44e-35

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: 137.34  E-value: 1.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  85 ILVL-DPQLAHEILVTNFSDFRD-TVTSSYVTHSKDYdkyvsrNPFFSAGDEWKKHRVDAGAGLTPNKLKQAYaiwEQTG 162
Cdd:cd20617   13 TVVLsDPEIIKEAFVKNGDNFSDrPLLPSFEIISGGK------GILFSNGDYWKELRRFALSSLTKTKLKKKM---EELI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 163 E-QLVSFIQSCIEERGSN-IIETRDLCYRYTAQAMGDFIWGIDAGSLtgsakETSSFQRIsTEWVTHAFLGMTRLNRTTI 240
Cdd:cd20617   84 EeEVNKLIESLKKHSKSGePFDPRPYFKKFVLNIINQFLFGKRFPDE-----DDGEFLKL-VKPIEEIFKELGSGNPSDF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 241 APIVRRLFRMRF--FTQAADDFYlKLTRDAAK--LRQSGSGGERSDYLAHLLQLQEKGASLDDMVGHALTVLMD----GF 312
Cdd:cd20617  158 IPILLPFYFLYLkkLKKSYDKIK-DFIEKIIEehLKTIDPNNPRDLIDDELLLLLKEGDSGLFDDDSIISTCLDlflaGT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 313 ETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGF-LLKICTRPTKIDlG 391
Cdd:cd20617  237 DTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLgLPRVTTEDTEIG-G 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 392 ndriLNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISELTKRgcLLAFGDGPRICLGMRVGLLSVKMALLRIL 471
Cdd:cd20617  316 ----YFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDGNKLSEQ--FIPFGIGKRNCVGENLARDELFLFFANLL 389
                        410       420
                 ....*....|....*....|...
gi 193912267 472 SQYKIE--QTKKLSLSSDSGLGM 492
Cdd:cd20617  390 LNFKFKssDGLPIDEKEVFGLTL 412
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
190-479 4.07e-34

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: 133.19  E-value: 4.07e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 190 YTAQAMGDFIWGIDAGSLTGSAKEtSSFQRISTEWVTHA----FLGMTRLNRTTIAPIVRRLFR-MRFFTQAAddfyLKL 264
Cdd:cd11059  110 LAMDVVSHLLFGESFGTLLLGDKD-SRERELLRRLLASLapwlRWLPRYLPLATSRLIIGIYFRaFDEIEEWA----LDL 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 265 TRDAAKLRQSGSGGERSDYLAHLLQLQEKGASLDDMvgHALTVLMD----GFETSSAVLYHMLYTLGAYPEQQEKLRSEV 340
Cdd:cd11059  185 CARAESSLAESSDSESLTVLLLEKLKGLKKQGLDDL--EIASEALDhivaGHDTTAVTLTYLIWELSRPPNLQEKLREEL 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 341 LAA-LDVDKRISYEQLNALPYLDQCVYESMRMTSVI-GFLLKICTRPTKIDLGndriLNVEPGVTVAIPAYHFHHDEAYF 418
Cdd:cd11059  263 AGLpGPFRGPPDLEDLDKLPYLNAVIRETLRLYPPIpGSLPRVVPEGGATIGG----YYIPGGTIVSTQAYSLHRDPEVF 338
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193912267 419 PQPDEFRPERFDNGAISELT-KRGCLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIEQT 479
Cdd:cd11059  339 PDPEEFDPERWLDPSGETAReMKRAFWPFGSGSRMCIGMNLALMEMKLALAAIYRNYRTSTT 400
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
79-474 4.78e-33

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: 129.63  E-value: 4.78e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  79 LTRQPQILVLDPQLAHEILVTnfsdfRDTVTSSYVTHSKDYDKYVSRNPFFSA-GDEWKKHR--VDAGagLTPNKLKqAY 155
Cdd:COG2124   39 LPGGGAWLVTRYEDVREVLRD-----PRTFSSDGGLPEVLRPLPLLGDSLLTLdGPEHTRLRrlVQPA--FTPRRVA-AL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 156 A--IWEQTGEQLVSFiqsciEERGS-NIIEtrDLCYRYTAQAMGDFIwGIDAGsltgsakETSSFQRISTEWVtHAFLGM 232
Cdd:COG2124  111 RprIREIADELLDRL-----AARGPvDLVE--EFARPLPVIVICELL-GVPEE-------DRDRLRRWSDALL-DALGPL 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 233 TRLNRTTIAPIVRRLFRmrFFTQAAddfylkltrdaAKLRQSGsggeRSDYLAHLLQLQEKGASLDD--MVGHALTVLMD 310
Cdd:COG2124  175 PPERRRRARRARAELDA--YLRELI-----------AERRAEP----GDDLLSALLAARDDGERLSDeeLRDELLLLLLA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 311 GFETSSAVLYHMLYTLGAYPEQQEKLRSEvlaaldvdkrisyeqlnaLPYLDQCVYESMRMTSVIGFLLKICTRPTkiDL 390
Cdd:COG2124  238 GHETTANALAWALYALLRHPEQLARLRAE------------------PELLPAAVEETLRLYPPVPLLPRTATEDV--EL 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 391 GNDRIlnvEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGaiseltkrgcLLAFGDGPRICLGMRVGLLSVKMALLRI 470
Cdd:COG2124  298 GGVTI---PAGDRVLLSLAAANRDPRVFPDPDRFDPDRPPNA----------HLPFGGGPHRCLGAALARLEARIALATL 364

                 ....
gi 193912267 471 LSQY 474
Cdd:COG2124  365 LRRF 368
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
272-477 9.51e-31

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: 123.46  E-value: 9.51e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 272 RQSGSGGERSDYLAHLLQLQ-EKGASLDD--MVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEvLAALDVDK 348
Cdd:cd11053  193 RRAEPDAERDDILSLLLSARdEDGQPLSDeeLRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAE-LDALGGDP 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 349 RIsyEQLNALPYLDQCVYESMRMTSVIGFLLKICTRPTKIDlGNDrilnVEPGVTVAIPAYHFHHDEAYFPQPDEFRPER 428
Cdd:cd11053  272 DP--EDIAKLPYLDAVIKETLRLYPVAPLVPRRVKEPVELG-GYT----LPAGTTVAPSIYLTHHRPDLYPDPERFRPER 344
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 193912267 429 FDNGAISELTkrgcLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIE 477
Cdd:cd11053  345 FLGRKPSPYE----YLPFGGGVRRCIGAAFALLEMKVVLATLLRRFRLE 389
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
82-498 2.17e-30

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: 122.67  E-value: 2.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  82 QPQILVLDPQLAHEILVTNFsdfrdtvtssyvthsKDYDKYVSRNPFF----------SAGDEWKKHRvdagAGLTPNKL 151
Cdd:cd11063   12 TRVIFTIEPENIKAVLATQF---------------KDFGLGERRRDAFkpllgdgiftSDGEEWKHSR----ALLRPQFS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 152 KqayaiwEQTG--EQLVSFIQ---SCIEERGSNIiETRDLCYRYTAQAMGDFIWGIDAGSLTgSAKETSSFQRIStewvt 226
Cdd:cd11063   73 R------DQISdlELFERHVQnliKLLPRDGSTV-DLQDLFFRLTLDSATEFLFGESVDSLK-PGGDSPPAARFA----- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 227 HAF-LGMTRLNRTTIAPIVRRLFRMRFFTQAAD------DFYLKLTRDAAKLRQSGSGGERSDYLAHLLQlqekgaSLDD 299
Cdd:cd11063  140 EAFdYAQKYLAKRLRLGKLLWLLRDKKFREACKvvhrfvDPYVDKALARKEESKDEESSDRYVFLDELAK------ETRD 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 300 MV---GHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIG 376
Cdd:cd11063  214 PKelrDQLLNILLAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPVP 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 377 FLLKICTRPTKI-----DLGNDRILnVEPGVTVAIPAYHFHHDEA-YFPQPDEFRPERFDngaisELTKRGC-LLAFGDG 449
Cdd:cd11063  294 LNSRVAVRDTTLprgggPDGKSPIF-VPKGTRVLYSVYAMHRRKDiWGPDAEEFRPERWE-----DLKRPGWeYLPFNGG 367
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 193912267 450 PRICLGMRVGLLSVKMALLRILSQY-KIEQTKKLSLSSDSGLGMYLNGDV 498
Cdd:cd11063  368 PRICLGQQFALTEASYVLVRLLQTFdRIESRDVRPPEERLTLTLSNANGV 417
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
225-477 4.89e-30

cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, and similar cytochrome P450s; CYP46A1 is also called cholesterol 24-hydroxylase (EC 1.14.14.25), CH24H, cholesterol 24-monooxygenase, or cholesterol 24S-hydroxylase. It catalyzes the conversion of cholesterol into 24S-hydroxycholesterol and, to a lesser extent, 25-hydroxycholesterol. CYP46A1 is associated with high-order brain functions; increased expression improves cognition while a reduction leads to a poor cognitive performance. It also plays a role in the pathogenesis or progression of neurodegenerative disorders. CYP46A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410706 [Multi-domain]  Cd Length: 429  Bit Score: 121.86  E-value: 4.89e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 225 VTHAFLGMTRLNRttiAPivrrLFRMRFFTQAaddfYLKLTRDAAK-LRQSGSG-----------GE--RSDYLAHLLQL 290
Cdd:cd20613  155 ISLVLEGIQESFR---NP----LLKYNPSKRK----YRREVREAIKfLRETGREcieerlealkrGEevPNDILTHILKA 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 291 QEKGASLD--DMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYES 368
Cdd:cd20613  224 SEEEPDFDmeELLDDFVTFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKQYVEYEDLGKLEYLSQVLKET 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 369 MRMTSVIGFLLKICTRPTKIDlGndriLNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAiSELTKRGCLLAFGD 448
Cdd:cd20613  304 LRLYPPVPGTSRELTKDIELG-G----YKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEA-PEKIPSYAYFPFSL 377
                        250       260
                 ....*....|....*....|....*....
gi 193912267 449 GPRICLGMRVGLLSVKMALLRILSQYKIE 477
Cdd:cd20613  378 GPRSCIGQQFAQIEAKVILAKLLQNFKFE 406
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
231-479 1.32e-29

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: 120.38  E-value: 1.32e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 231 GMTRLNRTTIAPIVRRLFRMRFFTQAADD--FYLKLTRDAAKL---RQ---SGSGGERSDYLAHLLQLQEKGA---SLDD 299
Cdd:cd11060  143 LLPYFAVVGQIPWLDRLLLKNPLGPKRKDktGFGPLMRFALEAvaeRLaedAESAKGRKDMLDSFLEAGLKDPekvTDRE 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 300 MVGHALTVLMDGFETSS----AVLYHMLYTlgayPEQQEKLRSEVLAALDVDK---RISYEQLNALPYLDQCVYESMRMT 372
Cdd:cd11060  223 VVAEALSNILAGSDTTAialrAILYYLLKN----PRVYAKLRAEIDAAVAEGKlssPITFAEAQKLPYLQAVIKEALRLH 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 373 SVIGFLLK---------ICTRptkidlgndrilNVEPGVTVAIPAYHFHHDEAYF-PQPDEFRPERF-DNGAISELTKRG 441
Cdd:cd11060  299 PPVGLPLErvvppggatICGR------------FIPGGTIVGVNPWVIHRDKEVFgEDADVFRPERWlEADEEQRRMMDR 366
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 193912267 442 CLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIEQT 479
Cdd:cd11060  367 ADLTFGAGSRTCLGKNIALLELYKVIPELLRRFDFELV 404
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
63-476 2.66e-29

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: 119.75  E-value: 2.66e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  63 KIYNKykgkeravgVFLT---RQPQILVLDPQLAHEILVTNFsdfrdtVTSSYVTHSKDYDKYVSRNPFFSAGDEWKKHR 139
Cdd:cd11052    9 KQYGK---------NFLYwygTDPRLYVTEPELIKELLSKKE------GYFGKSPLQPGLKKLLGRGLVMSNGEKWAKHR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 140 VDAGAGLTPNKLK-QAYAIWEQTgEQLVSFIQSCIEERGSNIIETRDLcYRYTAqamgDFIWGIDAGSLTGSAKETSS-- 216
Cdd:cd11052   74 RIANPAFHGEKLKgMVPAMVESV-SDMLERWKKQMGEEGEEVDVFEEF-KALTA----DIISRTAFGSSYEEGKEVFKll 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 217 --FQRISTEWVTHAFLGMTRLNRTtiapivRRLFRMRFFTQAADDFYLKLT---RDAAKLRQSGSGGerSDYLAHLLQ-- 289
Cdd:cd11052  148 reLQKICAQANRDVGIPGSRFLPT------KGNKKIKKLDKEIEDSLLEIIkkrEDSLKMGRGDDYG--DDLLGLLLEan 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 290 ---LQEKGASLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKrISYEQLNALPYLDQCVY 366
Cdd:cd11052  220 qsdDQNKNMTVQEIVDECKTFFFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDK-PPSDSLSKLKTVSMVIN 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 367 ESMRMTSVIGFLLKICTRPTKidLGNdriLNVEPGVTVAIPAYHFHHDEAYFPQ-PDEFRPERFDNGAISELTKRGCLLA 445
Cdd:cd11052  299 ESLRLYPPAVFLTRKAKEDIK--LGG---LVIPKGTSIWIPVLALHHDEEIWGEdANEFNPERFADGVAKAAKHPMAFLP 373
                        410       420       430
                 ....*....|....*....|....*....|.
gi 193912267 446 FGDGPRICLGMRVGLLSVKMALLRILSQYKI 476
Cdd:cd11052  374 FGLGPRNCIGQNFATMEAKIVLAMILQRFSF 404
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
217-477 3.47e-29

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: 119.22  E-value: 3.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 217 FQRISTEWVTHAFLGMTRLNRTTIAPIVRRLFRMRFFtqaaddfYLKLTRDAAKLRQSgSGGERSDYLAHLLQLQEKGAS 296
Cdd:cd11058  141 FDSIKALTIIQALRRYPWLLRLLRLLIPKSLRKKRKE-------HFQYTREKVDRRLA-KGTDRPDFMSYILRNKDEKKG 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 297 L--DDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMT-S 373
Cdd:cd11058  213 LtrEELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIRSAFSSEDDITLDSLAQLPYLNAVIQEALRLYpP 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 374 VIGFLLKICtrPTKIDLGNDRIlnVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISELT--KRGCLLAFGDGPR 451
Cdd:cd11058  293 VPAGLPRVV--PAGGATIDGQF--VPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLGDPRFEFDndKKEAFQPFSVGPR 368
                        250       260
                 ....*....|....*....|....*.
gi 193912267 452 ICLGMRVGLLSVKMALLRILSQYKIE 477
Cdd:cd11058  369 NCIGKNLAYAEMRLILAKLLWNFDLE 394
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
102-456 7.65e-29

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: 118.12  E-value: 7.65e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 102 SDFRDTVTSSYVTHSKDYDKYVSRNPF----FSAGDeWKKHRVDAGAgLTP-----NKLKQAYAIWEQTgEQLVSFIQSc 172
Cdd:cd11062   16 PDFYDEIYAGGSRRRKDPPYFYGAFGApgstFSTVD-HDLHRLRRKA-LSPffskrSILRLEPLIQEKV-DKLVSRLRE- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 173 iEERGSNIIETRDLCYRYTAQAMGDFIWGIDAGSLTGSAKETSSFQristewVTHAFLGMTRLNRT--TIAPIVRRL--- 247
Cdd:cd11062   92 -AKGTGEPVNLDDAFRALTADVITEYAFGRSYGYLDEPDFGPEFLD------ALRALAEMIHLLRHfpWLLKLLRSLpes 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 248 FRMRFFTQAAD-DFYLKLTRD--AAKLRQSGSGGERSD-------YLAHLLQLQEKgaSLDDMVGHALTVLMDGFETSSA 317
Cdd:cd11062  165 LLKRLNPGLAVfLDFQESIAKqvDEVLRQVSAGDPPSIvtslfhaLLNSDLPPSEK--TLERLADEAQTLIGAGTETTAR 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 318 VLYHMLYTLGAYPEQQEKLRSEVLAAL-DVDKRISYEQLNALPYLDQCVYESMRMT-SVIGFLLKICTRPTkIDLGNDRI 395
Cdd:cd11062  243 TLSVATFHLLSNPEILERLREELKTAMpDPDSPPSLAELEKLPYLTAVIKEGLRLSyGVPTRLPRVVPDEG-LYYKGWVI 321
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193912267 396 LnvePGVTVAIPAYHFHHDEAYFPQPDEFRPER-FDNGAISELTKrgCLLAFGDGPRICLGM 456
Cdd:cd11062  322 P---PGTPVSMSSYFVHHDEEIFPDPHEFRPERwLGAAEKGKLDR--YLVPFSKGSRSCLGI 378
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
232-477 7.71e-29

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


Pssm-ID: 410672 [Multi-domain]  Cd Length: 441  Bit Score: 118.62  E-value: 7.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 232 MTRLNRTTIAPI-VRRLFRMRFFTQAADDFYLKLtRDAAKLR-QSGSGGERSDylahLLQLQekgaslDDMvghaLTVLM 309
Cdd:cd11046  186 LKLLNDTLDDLIrKRKEMRQEEDIELQQEDYLNE-DDPSLLRfLVDMRDEDVD----SKQLR------DDL----MTMLI 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 310 DGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTRPTKID 389
Cdd:cd11046  251 AGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRRVLNESLRLYPQPPVLIRRAVEDDKLP 330
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 390 LGNDRILNvepGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISELTKRGCLLA---FGDGPRICLGMRVGLLSVKMA 466
Cdd:cd11046  331 GGGVKVPA---GTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPNEVIDDFAflpFGGGPRKCLGDQFALLEATVA 407
                        250
                 ....*....|.
gi 193912267 467 LLRILSQYKIE 477
Cdd:cd11046  408 LAMLLRRFDFE 418
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
75-496 3.31e-28

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: 116.54  E-value: 3.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  75 VGVFLTRQPQILVLDPQLAHEILVTNFSDFrdtvtssyvthskdydkyvSRNPFFSA--------------GDEWKKHRV 140
Cdd:cd11064    4 RGPWPGGPDGIVTADPANVEHILKTNFDNY-------------------PKGPEFRDlffdllgdgifnvdGELWKFQRK 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 141 DAGAGLTPNKLKQAYA--IWEQTGEQLVSFIQSCIEErgSNIIETRDLCYRYTAQAMGDFIWGIDAGSLTGSAKEtSSFQ 218
Cdd:cd11064   65 TASHEFSSRALREFMEsvVREKVEKLLVPLLDHAAES--GKVVDLQDVLQRFTFDVICKIAFGVDPGSLSPSLPE-VPFA 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 219 RiSTEWVTHAFLGmtrlnRTTIAPIVRRLfrMRFFT-----------QAADDFYLKL--TRDAAKLRQSGSGGERSDYLA 285
Cdd:cd11064  142 K-AFDDASEAVAK-----RFIVPPWLWKL--KRWLNigsekklreaiRVIDDFVYEVisRRREELNSREEENNVREDLLS 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 286 HLLQLQEKGASLD------DMVghaLTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAAL-----DVDKRISYEQ 354
Cdd:cd11064  214 RFLASEEEEGEPVsdkflrDIV---LNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLpklttDESRVPTYEE 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 355 LNALPYLDQCVYESMRMTSVIGFLLKICTrptkidlgNDRIL----NVEPGVTVAIPAYhfhhdeA-------YFPQPDE 423
Cdd:cd11064  291 LKKLVYLHAALSESLRLYPPVPFDSKEAV--------NDDVLpdgtFVKKGTRIVYSIY------AmgrmesiWGEDALE 356
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 424 FRPERFdngaISEltKRGCL-------LAFGDGPRICLGMRVGLLSVKMALLRILSQYKIEQTKKLSLSSDSGLGMYLNG 496
Cdd:cd11064  357 FKPERW----LDE--DGGLRpespykfPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVVPGHKVEPKMSLTLHMKG 430
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
79-471 8.69e-28

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: 115.34  E-value: 8.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  79 LTRQPQILVLDPQLAHEILVTN---FSDFRDTVTSSYVTHskDYDKYVsrnpFFSAGDEWKKHR-VDAGAGLTPNKLKQA 154
Cdd:cd20618    8 LGSVPTVVVSSPEMAKEVLKTQdavFASRPRTAAGKIFSY--NGQDIV----FAPYGPHWRHLRkICTLELFSAKRLESF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 155 YAIWEQTGEQLVSFIQSCIeeRGSNIIETRDLCYRYTAQAMGDFIWGIDA-GSLTGSAKETSSFQRISTEWvthaFLGMT 233
Cdd:cd20618   82 QGVRKEELSHLVKSLLEES--ESGKPVNLREHLSDLTLNNITRMLFGKRYfGESEKESEEAREFKELIDEA----FELAG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 234 RLNRTTIAPIVRRLF------RMRFFTQAADDFYLKLTRD-AAKLRQSGSGGERSDYLAHLLQLQEKG-ASLDDMVGHAL 305
Cdd:cd20618  156 AFNIGDYIPWLRWLDlqgyekRMKKLHAKLDRFLQKIIEEhREKRGESKKGGDDDDDLLLLLDLDGEGkLSDDNIKALLL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 306 TVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEvlaaLDV----DKRISYEQLNALPYLDQCVYESMRMTSVIGFLL-K 380
Cdd:cd20618  236 DMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEE----LDSvvgrERLVEESDLPKLPYLQAVVKETLRLHPPGPLLLpH 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 381 ICTRPTKIdLGNDrilnVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISELTKRG-CLLAFGDGPRICLGMRVG 459
Cdd:cd20618  312 ESTEDCKV-AGYD----IPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIDDVKGQDfELLPFGSGRRMCPGMPLG 386
                        410
                 ....*....|..
gi 193912267 460 LLSVKMALLRIL 471
Cdd:cd20618  387 LRMVQLTLANLL 398
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
82-477 4.81e-27

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: 113.06  E-value: 4.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  82 QPQILVLDPQLAHEILV---TNFSDfRdtvTSSYVThskdyDKYVSRNPFFSA---GDEWKKHRVDAGAGLTPNKLKQAY 155
Cdd:cd11065   12 QTIIVLNSPKAAKDLLEkrsAIYSS-R---PRMPMA-----GELMGWGMRLLLmpyGPRWRLHRRLFHQLLNPSAVRKYR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 156 AIWEQTGEQLVSfiqscieergsNIIET----RDLCYRYTAQAMGDFIWGIDAGSltgsaketssfqrISTEWVTHAFLG 231
Cdd:cd11065   83 PLQELESKQLLR-----------DLLESpddfLDHIRRYAASIILRLAYGYRVPS-------------YDDPLLRDAEEA 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 232 MTRLNRTTIA--------PIVRRL-------FRM--RFFTQAADDFYLKLTRDAakLRQSGSGGERSDYLAHLLQLQEKG 294
Cdd:cd11065  139 MEGFSEAGSPgaylvdffPFLRYLpswlgapWKRkaRELRELTRRLYEGPFEAA--KERMASGTATPSFVKDLLEELDKE 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 295 ASL-DDMVGHALTVLMD-GFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMT 372
Cdd:cd11065  217 GGLsEEEIKYLAGSLYEaGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWR 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 373 SVigFLLKICTRPTKIDLGND-RIlnveP-GVTVAIPAYHFHHDEAYFPQPDEFRPERF--DNGAISELTKRGcLLAFGD 448
Cdd:cd11065  297 PV--APLGIPHALTEDDEYEGyFI----PkGTTVIPNAWAIHHDPEVYPDPEEFDPERYldDPKGTPDPPDPP-HFAFGF 369
                        410       420
                 ....*....|....*....|....*....
gi 193912267 449 GPRICLGMRVGLLSVKMALLRILSQYKIE 477
Cdd:cd11065  370 GRRICPGRHLAENSLFIAIARLLWAFDIK 398
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
276-474 9.32e-27

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: 111.90  E-value: 9.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 276 SGGERSDYLAHLLQLQ--EKGASLDD--MVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDvDKRIS 351
Cdd:cd20620  185 APADGGDLLSMLLAARdeETGEPMSDqqLRDEVMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLG-GRPPT 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 352 YEQLNALPYLDQCVYESMRMTSVIGFLLKICTRPTKIdlGNDRIlnvEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDN 431
Cdd:cd20620  264 AEDLPQLPYTEMVLQESLRLYPPAWIIGREAVEDDEI--GGYRI---PAGSTVLISPYVTHRDPRFWPDPEAFDPERFTP 338
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 193912267 432 GAISELTKrgclLA---FGDGPRICLGMRVGLLSVKMALLRILSQY 474
Cdd:cd20620  339 EREAARPR----YAyfpFGGGPRICIGNHFAMMEAVLLLATIAQRF 380
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
255-477 1.26e-26

cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate cytochrome P450 family 26 enzymes, and similar cytochrome P450s; This family includes cyanobacterial CYP120A1 and vertebrate cytochrome P450s 26A1 (CYP26A1), 26B1 (CYP26B1), and 26C1 (CYP26C1). These are retinoic acid-metabolizing cytochromes that play key roles in retinoic acid (RA) metabolism. Human and zebrafish CYP26a1, as well as Synechocystis CYP120A1 are characterized as RA hydroxylases. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410670 [Multi-domain]  Cd Length: 420  Bit Score: 111.99  E-value: 1.26e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 255 QAADDFYLKLTRDAAKLRQSGSGGERSDYLAHLLQLQ-EKGASL--DDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPE 331
Cdd:cd11044  176 IRARNKLLARLEQAIRERQEEENAEAKDALGLLLEAKdEDGEPLsmDELKDQALLLLFAGHETTASALTSLCFELAQHPD 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 332 QQEKLRSEvLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTRPtkIDLGNDRIlnvEPGVTVAIPAYHF 411
Cdd:cd11044  256 VLEKLRQE-QDALGLEEPLTLESLKKMPYLDQVIKEVLRLVPPVGGGFRKVLED--FELGGYQI---PKGWLVYYSIRDT 329
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193912267 412 HHDEAYFPQPDEFRPERFDNGAISELTKRGCLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIE 477
Cdd:cd11044  330 HRDPELYPDPERFDPERFSPARSEDKKKPFSLIPFGGGPRECLGKEFAQLEMKILASELLRNYDWE 395
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
268-477 1.71e-26

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: 111.49  E-value: 1.71e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 268 AAKLRQSGSGGERSDYLAHLLQLQE---KGASLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAAL 344
Cdd:cd20659  193 EDNKDEALSKRKYLDFLDILLTARDedgKGLTDEEIRDEVDTFLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVL 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 345 DVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTRPTKIDlgnDRILnvEPGVTVAIPAYHFHHDEAYFPQPDEF 424
Cdd:cd20659  273 GDRDDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPITID---GVTL--PAGTLIAINIYALHHNPTVWEDPEEF 347
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 193912267 425 RPERFDNGAIselTKRG--CLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIE 477
Cdd:cd20659  348 DPERFLPENI---KKRDpfAFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFELS 399
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
227-478 1.89e-26

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: 111.51  E-value: 1.89e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 227 HAFLG-MTR-----LNRTTIAPIVRRLFRMRFFTQAAD-DFYLKLTRDAAKLRQSGSGGERSDYLAHLLQLQEK--GASL 297
Cdd:cd11068  147 HPFVEaMVRalteaGRRANRPPILNKLRRRAKRQFREDiALMRDLVDEIIAERRANPDGSPDDLLNLMLNGKDPetGEKL 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 298 DD--MVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDkRISYEQLNALPYLDQCVYESMRMTSVI 375
Cdd:cd11068  227 SDenIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGDD-PPPYEQVAKLRYIRRVLDETLRLWPTA 305
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 376 GFLLKICTRPTKIDLGNDrilnVEPGVTVAIPAYHFHHD-EAYFPQPDEFRPERFDNGAISELtKRGCLLAFGDGPRICL 454
Cdd:cd11068  306 PAFARKPKEDTVLGGKYP----LKKGDPVLVLLPALHRDpSVWGEDAEEFRPERFLPEEFRKL-PPNAWKPFGNGQRACI 380
                        250       260
                 ....*....|....*....|....
gi 193912267 455 GMRVGLLSVKMALLRILSQYKIEQ 478
Cdd:cd11068  381 GRQFALQEATLVLAMLLQRFDFED 404
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
217-477 2.58e-26

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: 111.23  E-value: 2.58e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 217 FQRISTEWVTHAFLGMTRLNRTT--IAPIVRRLF----RMRFFTQAADDFYLKLTRDAAKLRQSGSGGERSDYLAHLLQL 290
Cdd:cd11041  137 WLDLTINYTIDVFAAAAALRLFPpfLRPLVAPFLpeprRLRRLLRRARPLIIPEIERRRKLKKGPKEDKPNDLLQWLIEA 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 291 Q--EKGASLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYES 368
Cdd:cd11041  217 AkgEGERTPYDLADRQLALSFAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKES 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 369 MRMTSVIGFLLK-ICTRPTKIDLGndriLNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFdngaiSELTKRGCL---- 443
Cdd:cd11041  297 QRLNPLSLVSLRrKVLKDVTLSDG----LTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRF-----YRLREQPGQekkh 367
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 193912267 444 ---------LAFGDGPRICLGMRVGLLSVKMALLRILSQYKIE 477
Cdd:cd11041  368 qfvstspdfLGFGHGRHACPGRFFASNEIKLILAHLLLNYDFK 410
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
83-477 5.90e-26

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: 110.06  E-value: 5.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  83 PQILVLDPQLAHEILvTNFSDFRDTVTSSYVthskdydKYVSRNPFFSAGDEWKKHRVDAGAGLTPNKLKQayaiweqtg 162
Cdd:cd20642   23 PRVIIMDPELIKEVL-NKVYDFQKPKTNPLT-------KLLATGLASYEGDKWAKHRKIINPAFHLEKLKN--------- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 163 eQLVSFIQSCIE--ERGSNIIETRDLC----YRYTAQAMGDFIWGIDAGSltgSAKETSSFQRISTEwvtHAFLGMTRLn 236
Cdd:cd20642   86 -MLPAFYLSCSEmiSKWEKLVSSKGSCeldvWPELQNLTSDVISRTAFGS---SYEEGKKIFELQKE---QGELIIQAL- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 237 RTTIAPIVRRL-----FRMRFFTQAADDFYLKLTRDAAKLRQSGSGGErSDYLAHLLQ--LQEK--------GASLDDMV 301
Cdd:cd20642  158 RKVYIPGWRFLptkrnRRMKEIEKEIRSSLRGIINKREKAMKAGEATN-DDLLGILLEsnHKEIkeqgnkngGMSTEDVI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 302 GHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDvDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKI 381
Cdd:cd20642  237 EECKLFYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFG-NNKPDFEGLNHLKVVTMILYEVLRLYPPVIQLTRA 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 382 CTRPTKidLGNdriLNVEPGVTVAIPAYHFHHD-EAYFPQPDEFRPERFDNGaISELTK-RGCLLAFGDGPRICLGMRVG 459
Cdd:cd20642  316 IHKDTK--LGD---LTLPAGVQVSLPILLVHRDpELWGDDAKEFNPERFAEG-ISKATKgQVSYFPFGWGPRICIGQNFA 389
                        410
                 ....*....|....*...
gi 193912267 460 LLSVKMALLRILSQYKIE 477
Cdd:cd20642  390 LLEAKMALALILQRFSFE 407
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
222-479 1.01e-25

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: 109.27  E-value: 1.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 222 TEWVTHAFLGMTR--LNRTTIAPIVRRLFRM--RFFTQAADDFYLKLTRDAAKLRQSGsgGERSDYLAHLLQLQ-EKGAS 296
Cdd:cd11049  138 AAELRQALPVVLAgmLRRAVPPKFLERLPTPgnRRFDRALARLRELVDEIIAEYRASG--TDRDDLLSLLLAARdEEGRP 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 297 LDD--MVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDvDKRISYEQLNALPYLDQCVYESMRMTSV 374
Cdd:cd11049  216 LSDeeLRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLG-GRPATFEDLPRLTYTRRVVTEALRLYPP 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 375 IGFLLKICTRPTkiDLGNDRIlnvEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISELTkRGCLLAFGDGPRICL 454
Cdd:cd11049  295 VWLLTRRTTADV--ELGGHRL---PAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVP-RGAFIPFGAGARKCI 368
                        250       260
                 ....*....|....*....|....*
gi 193912267 455 GMRVGLLSVKMALLRILSQYKIEQT 479
Cdd:cd11049  369 GDTFALTELTLALATIASRWRLRPV 393
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
282-490 4.08e-25

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: 107.68  E-value: 4.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 282 DYLAHLLQLQEK----GASLDDMV--GHALTVLMD----GFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRIS 351
Cdd:cd11027  202 DLTDALIKAKKEaedeGDEDSGLLtdDHLVMTISDifgaGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPT 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 352 YEQLNALPYLDQCVYESMRMTSVIGFLL-KICTRPTKIDlGNDrilnVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFD 430
Cdd:cd11027  282 LSDRKRLPYLEATIAEVLRLSSVVPLALpHKTTCDTTLR-GYT----IPKGTTVLVNLWALHHDPKEWDDPDEFRPERFL 356
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193912267 431 NGAISELTKRGCLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIEQ---TKKLSLSSDSGL 490
Cdd:cd11027  357 DENGKLVPKPESFLPFSAGRRVCLGESLAKAELFLFLARLLQKFRFSPpegEPPPELEGIPGL 419
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
272-476 4.98e-25

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: 107.02  E-value: 4.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 272 RQSGSGGersDYLAHLLQL-QEKGASL--DDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLaALDvDK 348
Cdd:cd11045  184 RRAGGGD---DLFSALCRAeDEDGDRFsdDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESL-ALG-KG 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 349 RISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTRPTKIdLGNDrilnVEPGVTVAIPAYHFHHDEAYFPQPDEFRPER 428
Cdd:cd11045  259 TLDYEDLGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTEV-LGYR----IPAGTLVAVSPGVTHYMPEYWPNPERFDPER 333
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 193912267 429 FDNGAISELTKRGCLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKI 476
Cdd:cd11045  334 FSPERAEDKVHRYAWAPFGGGAHKCIGLHFAGMEVKAILHQMLRRFRW 381
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
217-484 1.07e-24

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: 106.19  E-value: 1.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 217 FQRISTEWVTHAFLG---------------------MTRLNRTTIAPIVRrLFRMRFFTQAADDFYLKLTRDAAK----L 271
Cdd:cd20621  104 LQKITGEVVIRSFFGeeakdlkingkeiqvelveilIESFLYRFSSPYFQ-LKRLIFGRKSWKLFPTKKEKKLQKrvkeL 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 272 RQ-------------SGSGGERSDYLAHLLQL------QEKGASLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQ 332
Cdd:cd20621  183 RQfiekiiqnrikqiKKNKDEIKDIIIDLDLYllqkkkLEQEITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEI 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 333 QEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRM-TSVIGFLLKICTRPTKIdlGNdriLNVEPGvTVAIPAYHF 411
Cdd:cd20621  263 QEKLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKEVLRLyNPAPFLFPRVATQDHQI--GD---LKIKKG-WIVNVGYIY 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 412 HH-DEAYFPQPDEFRPERF-------DNGAIseltkrgcLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIEQTKKLS 483
Cdd:cd20621  337 NHfNPKYFENPDEFNPERWlnqnnieDNPFV--------FIPFSAGPRNCIGQHLALMEAKIILIYILKNFEIEIIPNPK 408

                 .
gi 193912267 484 L 484
Cdd:cd20621  409 L 409
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
83-469 4.51e-24

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: 104.63  E-value: 4.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  83 PQILVLDPQLAHEILVTNFSDFRD----TVTSSYVT------HSKDYdkyvsrnpffsaGDEWK--KHRVDAGAgLTPNK 150
Cdd:cd11075   14 PLIVVASRELAHEALVQKGSSFASrppaNPLRVLFSsnkhmvNSSPY------------GPLWRtlRRNLVSEV-LSPSR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 151 LKQAYAIWEQTGEQLVSFIQSCIEErGSNIIETRDLCYR-----YTAQAMGDfiwgidagsltGSAKETssFQRISTE-- 223
Cdd:cd11075   81 LKQFRPARRRALDNLVERLREEAKE-NPGPVNVRDHFRHalfslLLYMCFGE-----------RLDEET--VRELERVqr 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 224 WVTHAFLGMTRLNrttIAPIVRRLFRMRFFTQAA------DDFYLKLTRDAAKLRQSGSGGERSD----YLAHLLQLQEK 293
Cdd:cd11075  147 ELLLSFTDFDVRD---FFPALTWLLNRRRWKKVLelrrrqEEVLLPLIRARRKRRASGEADKDYTdfllLDLLDLKEEGG 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 294 GASL--DDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRM 371
Cdd:cd11075  224 ERKLtdEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRR 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 372 TSVIGFLLKI-CTRPTKIDlGNDrilnVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNG----AISELTKRGCLLAF 446
Cdd:cd11075  304 HPPGHFLLPHaVTEDTVLG-GYD----IPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGgeaaDIDTGSKEIKMMPF 378
                        410       420
                 ....*....|....*....|...
gi 193912267 447 GDGPRICLGMRVGLLSVKMALLR 469
Cdd:cd11075  379 GAGRRICPGLGLATLHLELFVAR 401
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
272-503 1.03e-23

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: 103.06  E-value: 1.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 272 RQSGSGGERsDYLAHLL-QLQEKGASLDD--MVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAAL-DVD 347
Cdd:cd11042  183 RKSPDKDED-DMLQTLMdAKYKDGRPLTDdeIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLgDGD 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 348 KRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTRPTKIDLGNDRIlnvEPGVTVAIPAYHFHHDEAYFPQPDEFRPE 427
Cdd:cd11042  262 DPLTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKPFEVEGGGYVI---PKGHIVLASPAVSHRDPEIFKNPDEFDPE 338
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193912267 428 RF--DNGAISELTKRGcLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIEQTKKLSLSSD-SGLGMYLNGDVDLRYT 503
Cdd:cd11042  339 RFlkGRAEDSKGGKFA-YLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDFELVDSPFPEPDyTTMVVWPKGPARVRYK 416
PTZ00404 PTZ00404
cytochrome P450; Provisional
40-490 2.65e-22

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 99.80  E-value: 2.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  40 PLTLLGSypgLFGGGSSFIEDIGKIYNKYKGKERavgVFLTRQPQILVLDPQLAHEILVTNFSDFRDTVTSSYVTHSKDY 119
Cdd:PTZ00404  36 PIPILGN---LHQLGNLPHRDLTKMSKKYGGIFR---IWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHGTFY 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 120 DKYVSrnpffSAGDEWKKHRVDAGAGLTPNKLKQAYAIWEQTGEQLVSFIQScIEERGsNIIETRDLCYRYTAQAMGDFI 199
Cdd:PTZ00404 110 HGIVT-----SSGEYWKRNREIVGKAMRKTNLKHIYDLLDDQVDVLIESMKK-IESSG-ETFEPRYYLTKFTMSAMFKYI 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 200 WGID---------------------------AGSLTGSAKETSSFQRISTEWVTHAFlgmtrlnrttiaPIVRRLFRMRF 252
Cdd:PTZ00404 183 FNEDisfdedihngklaelmgpmeqvfkdlgSGSLFDVIEITQPLYYQYLEHTDKNF------------KKIKKFIKEKY 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 253 FTQaaddfylKLTRDAAKLRQsgsggersdyLAHLLqLQEKGASLDDMVGHALTVLMD----GFETSSAVLYHMLYTLGA 328
Cdd:PTZ00404 251 HEH-------LKTIDPEVPRD----------LLDLL-IKEYGTNTDDDILSILATILDfflaGVDTSATSLEWMVLMLCN 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 329 YPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGF-LLKICTRPTKIDLGNdrilNVEPGVTVAIP 407
Cdd:PTZ00404 313 YPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPVSPFgLPRSTSNDIIIGGGH----FIPKDAQILIN 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 408 AYHFHHDEAYFPQPDEFRPERFDNGAISEltkrgCLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKI--EQTKKLSLS 485
Cdd:PTZ00404 389 YYSLGRNEKYFENPEQFDPSRFLNPDSND-----AFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLksIDGKKIDET 463

                 ....*
gi 193912267 486 SDSGL 490
Cdd:PTZ00404 464 EEYGL 468
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
77-487 2.71e-22

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: 99.06  E-value: 2.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  77 VFLT---RQPQILVLDPQLAHEILVTNFSDFRDTVTSSYVThskdydKYVSRNPFFSAGDEWKKHRVDAGAGLTPNKLKQ 153
Cdd:cd20641   14 TFLYwqgTTPRICISDHELAKQVLSDKFGFFGKSKARPEIL------KLSGKGLVFVNGDDWVRHRRVLNPAFSMDKLKS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 154 AYAIWEQTGEQLvsFIQSCIEERGSNIIETRDLCYRYTAQAMGDFIWGIDAGSLTGSAKET----SSFQRISTEWVTHAF 229
Cdd:cd20641   88 MTQVMADCTERM--FQEWRKQRNNSETERIEVEVSREFQDLTADIIATTAFGSSYAEGIEVflsqLELQKCAAASLTNLY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 230 LGMTRLNRTTIAPIVRRLFR-MRFftqaaddfylKLTRDAAKLRQSGSGGERSDYLAHLL---------QLQEKGASLDD 299
Cdd:cd20641  166 IPGTQYLPTPRNLRVWKLEKkVRN----------SIKRIIDSRLTSEGKGYGDDLLGLMLeaassneggRRTERKMSIDE 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 300 MVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLL 379
Cdd:cd20641  236 IIDECKTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDADTLSKLKLMNMVLMETLRLYGPVINIA 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 380 KICTrpTKIDLGNdriLNVEPGVTVAIPAYHFHHDEAYF-PQPDEFRPERFDNGAISELTKRGCLLAFGDGPRICLGMRV 458
Cdd:cd20641  316 RRAS--EDMKLGG---LEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGVSRAATHPNALLSFSLGPRACIGQNF 390
                        410       420
                 ....*....|....*....|....*....
gi 193912267 459 GLLSVKMALLRILSQYkieqtkKLSLSSD 487
Cdd:cd20641  391 AMIEAKTVLAMILQRF------SFSLSPE 413
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
83-477 1.16e-21

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: 96.94  E-value: 1.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  83 PQILVLDPQLAHEILVTNfSDFRDTVTSSYVTHSkdydkyVSRNPFFSA-GDEWKKHRVDAGAGLTPNKLKQ-AYAIWEQ 160
Cdd:cd11051   11 PLLVVTDPELAEQITQVT-NLPKPPPLRKFLTPL------TGGSSLISMeGEEWKRLRKRFNPGFSPQHLMTlVPTILDE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 161 TgeqlVSFIQSCIEERGSN-IIETRDLCYRYTAQAMGDFIWGIDAGSLTGSAKetssfqristewVTHAFLGMTRLNRTT 239
Cdd:cd11051   84 V----EIFAAILRELAESGeVFSLEELTTNLTFDVIGRVTLDIDLHAQTGDNS------------LLTALRLLLALYRSL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 240 IAPiVRRLFRMRfftqaaddfYLKLTRDAAKLRqsgsggersdylAHLLQLQEKGASLDDMVGHALTVLMDGFETSSAVL 319
Cdd:cd11051  148 LNP-FKRLNPLR---------PLRRWRNGRRLD------------RYLKPEVRKRFELERAIDQIKTFLFAGHDTTSSTL 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 320 YHMLYTLGAYPEQQEKLRSEVLAALDVDK-------RISYEQLNALPYLDQCVYESMRMtsvigFLLKICTRPTKIDLG- 391
Cdd:cd11051  206 CWAFYLLSKHPEVLAKVRAEHDEVFGPDPsaaaellREGPELLNQLPYTTAVIKETLRL-----FPPAGTARRGPPGVGl 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 392 ---NDRILNVEpGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISELT-KRGCLLAFGDGPRICLGMRVGLLSVKMAL 467
Cdd:cd11051  281 tdrDGKEYPTD-GCIVYVCHHAIHRDPEYWPRPDEFIPERWLVDEGHELYpPKSAWRPFERGPRNCIGQELAMLELKIIL 359
                        410
                 ....*....|
gi 193912267 468 LRILSQYKIE 477
Cdd:cd11051  360 AMTVRRFDFE 369
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
66-477 2.23e-21

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: 96.28  E-value: 2.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  66 NKYKGKERAVGVFLTRQPQILVLDPQLAHEIlvtnFSDFRDTVTSSYVThskdydkYVSRNPFFSAGDEWKKHRVDAGAG 145
Cdd:cd11040    6 KKYFSGGPIFTIRLGGQKIYVITDPELISAV----FRNPKTLSFDPIVI-------VVVGRVFGSPESAKKKEGEPGGKG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 146 LtPNKLKQAYAIWEQTGEQL----------VSFIQSCIEERGSNIIETRDL---CYRYTAQAMGDFIWGIDAGSLT-GSA 211
Cdd:cd11040   75 L-IRLLHDLHKKALSGGEGLdrlneamlenLSKLLDELSLSGGTSTVEVDLyewLRDVLTRATTEALFGPKLPELDpDLV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 212 KETSSFQRistewvthaflGMTRLNRTTIAPIVRRLFRMRFFTQAA-DDFYlkltRDAAKLRQSGSG--GERSDYLAhll 288
Cdd:cd11040  154 EDFWTFDR-----------GLPKLLLGLPRLLARKAYAARDRLLKAlEKYY----QAAREERDDGSEliRARAKVLR--- 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 289 qlqEKGASLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISY-----EQLNALPYLDQ 363
Cdd:cd11040  216 ---EAGLSEEDIARAELALLWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTNAildltDLLTSCPLLDS 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 364 CVYESMRMTSvIGFLLKICTRPTkiDLGNDRILnvEPGVTVAIPAYHFHHDEAYF-PQPDEFRPERF--DNGAISELTKR 440
Cdd:cd11040  293 TYLETLRLHS-SSTSVRLVTEDT--VLGGGYLL--RKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFlkKDGDKKGRGLP 367
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 193912267 441 GCLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIE 477
Cdd:cd11040  368 GAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFDVE 404
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
77-475 3.46e-21

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: 95.71  E-value: 3.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  77 VFLTR---QPQILVLDPQLAHEILVTNFSDFRDTVTSSYVthskdyDKYVSRNPFFSAGDEWKKHRVDAGAGLTPNKLKQ 153
Cdd:cd11043    8 VFKTSlfgRPTVVSADPEANRFILQNEGKLFVSWYPKSVR------KLLGKSSLLTVSGEEHKRLRGLLLSFLGPEALKD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 154 AYAiweQTGEQLVsfIQSCIEERGSNIIETRDLCYRYTAQAMGDFIWGIDAGSLTGSAKEtsSFQRISTEWvtHAF---L 230
Cdd:cd11043   82 RLL---GDIDELV--RQHLDSWWRGKSVVVLELAKKMTFELICKLLLGIDPEEVVEELRK--EFQAFLEGL--LSFplnL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 231 GMTRLN-----RTTIAPIVRRLFRMRfftqaaddfylkltrdaaklRQSGSGGE-RSDYLAHLLQ-LQEKGASLDD--MV 301
Cdd:cd11043  153 PGTTFHralkaRKRIRKELKKIIEER--------------------RAELEKASpKGDLLDVLLEeKDEDGDSLTDeeIL 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 302 GHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSE---VLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFL 378
Cdd:cd11043  213 DNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLEEheeIAKRKEEGEGLTWEDYKSMKYTWQVINETLRLAPIVPGV 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 379 LkictRPTKIDlgndrilnVE------P-GVTVAIPAYHFHHDEAYFPQPDEFRPERFDNgaiSELTKRGCLLAFGDGPR 451
Cdd:cd11043  293 F----RKALQD--------VEykgytiPkGWKVLWSARATHLDPEYFPDPLKFNPWRWEG---KGKGVPYTFLPFGGGPR 357
                        410       420
                 ....*....|....*....|....
gi 193912267 452 ICLGMRVGLLSVKMALLRILSQYK 475
Cdd:cd11043  358 LCPGAELAKLEILVFLHHLVTRFR 381
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
239-477 5.07e-20

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: 92.48  E-value: 5.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 239 TIAPIVRR-----LFRMRFFTQAADDFYLKLTRDAAKLRQSGSGGERSDYLAHLL--QLQEKGAS--LDDMVgHALTV-- 307
Cdd:cd20674  156 DSIPFLRFfpnpgLRRLKQAVENRDHIVESQLRQHKESLVAGQWRDMTDYMLQGLgqPRGEKGMGqlLEGHV-HMAVVdl 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 308 LMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKIC-TRPT 386
Cdd:cd20674  235 FIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRPVVPLALPHRtTRDS 314
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 387 KIdLGNDRilnvePGVTVAIP-AYHFHHDEAYFPQPDEFRPERF-DNGAISEltkrgCLLAFGDGPRICLGMRVGLLSVK 464
Cdd:cd20674  315 SI-AGYDI-----PKGTVVIPnLQGAHLDETVWEQPHEFRPERFlEPGAANR-----ALLPFGCGARVCLGEPLARLELF 383
                        250
                 ....*....|...
gi 193912267 465 MALLRILSQYKIE 477
Cdd:cd20674  384 VFLARLLQAFTLL 396
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
287-481 1.19e-19

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: 91.17  E-value: 1.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 287 LLQLQEKGASLDDM-----VGhalTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAAL-DVDKRISYEQLNALPY 360
Cdd:cd20660  218 LLEASEEGTKLSDEdireeVD---TFMFEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFgDSDRPATMDDLKEMKY 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 361 LDQCVYESMRM-TSVIGFllkicTRPTK--IDLGNDRILNvepGVTVAIPAYHFHHDEAYFPQPDEFRPERF--DNGAis 435
Cdd:cd20660  295 LECVIKEALRLfPSVPMF-----GRTLSedIEIGGYTIPK---GTTVLVLTYALHRDPRQFPDPEKFDPDRFlpENSA-- 364
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 193912267 436 eltKRG--CLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIEQTKK 481
Cdd:cd20660  365 ---GRHpyAYIPFSAGPRNCIGQKFALMEEKVVLSSILRNFRIESVQK 409
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
240-492 1.79e-19

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: 90.82  E-value: 1.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 240 IAPIVRRLFR-----MRFFTQAADDFYLKLTRDAAKLRQSGSGGERSDYL---AHLLQLQEKGAS-LDDmvGHALTVLMD 310
Cdd:cd11028  161 VMPWLRYLTRrklqkFKELLNRLNSFILKKVKEHLDTYDKGHIRDITDALikaSEEKPEEEKPEVgLTD--EHIISTVQD 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 311 ----GFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTrpT 386
Cdd:cd11028  239 lfgaGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFILETMRHSSFVPFTIPHAT--T 316
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 387 KidlgnDRILN---VEPGVTVAIPAYHFHHDEAYFPQPDEFRPERF--DNGAISElTKRGCLLAFGDGPRICLGMRVGLL 461
Cdd:cd11028  317 R-----DTTLNgyfIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFldDNGLLDK-TKVDKFLPFGAGRRRCLGEELARM 390
                        250       260       270
                 ....*....|....*....|....*....|...
gi 193912267 462 SVKMALLRILSQYKIEQT--KKLSLSSDSGLGM 492
Cdd:cd11028  391 ELFLFFATLLQQCEFSVKpgEKLDLTPIYGLTM 423
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
273-481 4.98e-19

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: 89.43  E-value: 4.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 273 QSGSGGERSDYLAHLLQLQE---KGASLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEvlaaLD---- 345
Cdd:cd20680  214 ESPSKKKRKAFLDMLLSVTDeegNKLSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKE----LDevfg 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 346 -VDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTRPTKIdlgndRILNVEPGVTVAIPAYHFHHDEAYFPQPDEF 424
Cdd:cd20680  290 kSDRPVTMEDLKKLRYLECVIKESLRLFPSVPLFARSLCEDCEI-----RGFKVPKGVNAVIIPYALHRDPRYFPEPEEF 364
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 425 RPERFdngaISE-LTKRG--CLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIEQTKK 481
Cdd:cd20680  365 RPERF----FPEnSSGRHpyAYIPFSAGPRNCIGQRFALMEEKVVLSCILRHFWVEANQK 420
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
83-471 6.42e-19

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: 89.06  E-value: 6.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  83 PQILVLDPQLAHEILVTN---FSDFRDTVTSSYVT-HSKDydkyVSRNPFfsaGDEWKKHR----VDAgagLTPNKLKQA 154
Cdd:cd11072   14 PTVVVSSPEAAKEVLKTHdlvFASRPKLLAARILSyGGKD----IAFAPY---GEYWRQMRkicvLEL---LSAKRVQSF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 155 YAIWEQTGEQLVSFIQSCieERGSNIIETRDLCYRYTA-----QAMGDFIWGIDAGSLTGSAKETSSFqrISTEWVTHAF 229
Cdd:cd11072   84 RSIREEEVSLLVKKIRES--ASSSSPVNLSELLFSLTNdivcrAAFGRKYEGKDQDKFKELVKEALEL--LGGFSVGDYF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 230 LGMTRLNRTTIAPivRRLFRMRfftQAADDFYLKLTRDAAKLRQSGSGGERSDyLAHLLQLQEkgaslDDMVGHALT--- 306
Cdd:cd11072  160 PSLGWIDLLTGLD--RKLEKVF---KELDAFLEKIIDEHLDKKRSKDEDDDDD-DLLDLRLQK-----EGDLEFPLTrdn 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 307 ---VLMD----GFETSSAVlyhMLYT---LGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIG 376
Cdd:cd11072  229 ikaIILDmflaGTDTSATT---LEWAmteLIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPPAP 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 377 FLL-KICTRPTKIDlGNDrilnVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNgaiSELTKRGC---LLAFGDGPRI 452
Cdd:cd11072  306 LLLpRECREDCKIN-GYD----IPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLD---SSIDFKGQdfeLIPFGAGRRI 377
                        410
                 ....*....|....*....
gi 193912267 453 CLGMRVGLLSVKMALLRIL 471
Cdd:cd11072  378 CPGITFGLANVELALANLL 396
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
81-476 8.19e-19

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: 88.66  E-value: 8.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  81 RQPQILVLDPQLAHEILVTNFSDFrDTVTSSYVTHSKDYDKYVSRNpffsaGDEWKKHRVDAGAGLTPNKLKQayaiweq 160
Cdd:cd20639   21 PTPRLTVADPELIREILLTRADHF-DRYEAHPLVRQLEGDGLVSLR-----GEKWAHHRRVITPAFHMENLKR------- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 161 tgeqLVSFIQScieergsniietrdlcyryTAQAMGDfIWGIDAGSLTGSAKETSS-FQRISTEWVTHAFLGMTRLNRtt 239
Cdd:cd20639   88 ----LVPHVVK-------------------SVADMLD-KWEAMAEAGGEGEVDVAEwFQNLTEDVISRTAFGSSYEDG-- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 240 iapivRRLFR-----MRFFTQAADDFYL--------KLTRDAAKL--------------RQSGSGGERSD-YLAHLLQL- 290
Cdd:cd20639  142 -----KAVFRlqaqqMLLAAEAFRKVYIpgyrflptKKNRKSWRLdkeirksllklierRQTAADDEKDDeDSKDLLGLm 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 291 -------QEKGASLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQ 363
Cdd:cd20639  217 isaknarNGEKMTVEEIIEECKTFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDHLPKLKTLGM 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 364 CVYESMRMTSVIGFLLKICTRPTKidLGNdriLNVEPGVTVAIPAYHFHHDEAYF-PQPDEFRPERFDNGAISELTKRGC 442
Cdd:cd20639  297 ILNETLRLYPPAVATIRRAKKDVK--LGG---LDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADGVARAAKHPLA 371
                        410       420       430
                 ....*....|....*....|....*....|....
gi 193912267 443 LLAFGDGPRICLGMRVGLLSVKMALLRILSQYKI 476
Cdd:cd20639  372 FIPFGLGPRTCVGQNLAILEAKLTLAVILQRFEF 405
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
287-476 1.50e-18

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: 87.83  E-value: 1.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 287 LLQLQEKGASL--DDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAAL-DVD-KRISYEQLNALPYLD 362
Cdd:cd20679  230 LLSKDEDGKELsdEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLkDREpEEIEWDDLAQLPFLT 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 363 QCVYESMRMTSVIGFLLKICTRptKIDLGNDRIlnVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDngaiSELTKRGC 442
Cdd:cd20679  310 MCIKESLRLHPPVTAISRCCTQ--DIVLPDGRV--IPKGIICLISIYGTHHNPTVWPDPEVYDPFRFD----PENSQGRS 381
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 193912267 443 LLA---FGDGPRICLGMRVGLLSVKMALLRILSQYKI 476
Cdd:cd20679  382 PLAfipFSAGPRNCIGQTFAMAEMKVVLALTLLRFRV 418
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
227-488 2.48e-18

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: 86.96  E-value: 2.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 227 HAFLGmtRLNRTTIAPIVRRLF--RMRFFTQAADDFYLKLTRDAaklRQSGSGGERSDYLAHLLQ----LQEKGASLDDM 300
Cdd:cd20615  149 YVIKG--GLYRFKISRYLPTAAnrRLREFQTRWRAFNLKIYNRA---RQRGQSTPIVKLYEAVEKgditFEELLQTLDEM 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 301 vghaltvLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDvDKRISYEQLNAL--PYLDQCVYESMRMTSVIGFL 378
Cdd:cd20615  224 -------LFANLDVTTGVLSWNLVFLAANPAVQEKLREEISAARE-QSGYPMEDYILStdTLLAYCVLESLRLRPLLAFS 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 379 LKICTrPTKIDLGNDRIlnvEPGVTVAIPAYHFHHDEAYF-PQPDEFRPERFDNGAISELTKRgcLLAFGDGPRICLGMR 457
Cdd:cd20615  296 VPESS-PTDKIIGGYRI---PANTPVVVDTYALNINNPFWgPDGEAYRPERFLGISPTDLRYN--FWRFGFGPRKCLGQH 369
                        250       260       270
                 ....*....|....*....|....*....|.
gi 193912267 458 VGLLSVKMALLRILSQYKIEQTKKLSLSSDS 488
Cdd:cd20615  370 VADVILKALLAHLLEQYELKLPDQGENEEDT 400
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
117-477 3.09e-18

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: 86.69  E-value: 3.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 117 KDYDKYVSRN--PFFSAGDEWKKHRVDAGAG-LTPNKLKQAYAIWEQTGEQLVSFIQSCIEERGSNIIET---RDLcYRY 190
Cdd:cd20643   46 VAYRDYRKRKygVLLKNGEAWRKDRLILNKEvLAPKVIDNFVPLLNEVSQDFVSRLHKRIKKSGSGKWTAdlsNDL-FRF 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 191 TAQAMGDFIWGIDAGSLTGSAKETSsfQRIsTEWVTHAFlgmtrlnRTT-----IAPIVRRLFRMR-----------FFT 254
Cdd:cd20643  125 ALESICNVLYGERLGLLQDYVNPEA--QRF-IDAITLMF-------HTTspmlyIPPDLLRLINTKiwrdhveawdvIFN 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 255 QAaDDFYLKLTRDaakLRQSGSG-GERSDYLAHLLqLQEKgASLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQ 333
Cdd:cd20643  195 HA-DKCIQNIYRD---LRQKGKNeHEYPGILANLL-LQDK-LPIEDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQ 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 334 EKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTRPTKIDlgNDRIlnvEPGVTVAIPAYHFHH 413
Cdd:cd20643  269 EMLRAEVLAARQEAQGDMVKMLKSVPLLKAAIKETLRLHPVAVSLQRYITEDLVLQ--NYHI---PAGTLVQVGLYAMGR 343
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193912267 414 DEAYFPQPDEFRPERFDNGAISELtkRGclLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIE 477
Cdd:cd20643  344 DPTVFPKPEKYDPERWLSKDITHF--RN--LGFGFGPRQCLGRRIAETEMQLFLIHMLENFKIE 403
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
311-492 3.79e-18

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: 86.69  E-value: 3.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 311 GFET-SSAVLYHMLYTLgAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTrpTKid 389
Cdd:cd20677  248 GFDTiSTALQWSLLYLI-KYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFINEVFRHSSFVPFTIPHCT--TA-- 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 390 lgnDRILN---VEPGVTVAIPAYHFHHDEAYFPQPDEFRPERF--DNGAIS-ELTKRgcLLAFGDGPRICLGMRVGLLSV 463
Cdd:cd20677  323 ---DTTLNgyfIPKDTCVFINMYQVNHDETLWKDPDLFMPERFldENGQLNkSLVEK--VLIFGMGVRKCLGEDVARNEI 397
                        170       180       190
                 ....*....|....*....|....*....|.
gi 193912267 464 KMALLRILSQYKIEQT--KKLSLSSDSGLGM 492
Cdd:cd20677  398 FVFLTTILQQLKLEKPpgQKLDLTPVYGLTM 428
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
268-477 4.64e-18

cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; Cytochrome p450 27B1 (CYP27B1) is also called calcidiol 1-monooxygenase (EC 1.14.15.18), 25-hydroxyvitamin D(3) 1-alpha-hydroxylase (VD3 1A hydroxylase), 25-hydroxyvitamin D-1 alpha hydroxylase, 25-OHD-1 alpha-hydroxylase, 25-hydroxycholecalciferol 1-hydroxylase, or 25-hydroxycholecalciferol 1-monooxygenase. It catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D3) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D3 or calcitriol), and of 24,25-dihydroxyvitamin D3 (24,25(OH)(2)D3) to 1-alpha,24,25-trihydroxyvitamin D3 (1alpha,24,25(OH)(3)D3). It is also active with 25-hydroxy-24-oxo-vitamin D3, and has an important role in normal bone growth, calcium metabolism, and tissue differentiation. CYP27B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410741 [Multi-domain]  Cd Length: 430  Bit Score: 86.35  E-value: 4.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 268 AAKLRQSGSGGERSDYLAHLLQLQEkgASLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVD 347
Cdd:cd20648  205 EVAAKLPRGEAIEGKYLTYFLAREK--LPMKSIYGNVTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDN 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 348 KRISYEQLNALPYLDQCVYESMRMTSVIgfllkictrPTKIDLGNDRILNVE----PGVT-VAIPAYHFHHDEAYFPQPD 422
Cdd:cd20648  283 SVPSAADVARMPLLKAVVKEVLRLYPVI---------PGNARVIPDRDIQVGeyiiPKKTlITLCHYATSRDENQFPDPN 353
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 193912267 423 EFRPERFDNGaiSELTKRGCLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIE 477
Cdd:cd20648  354 SFRPERWLGK--GDTHHPYASLPFGFGKRSCIGRRIAELEVYLALARILTHFEVR 406
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
266-478 6.00e-18

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: 85.96  E-value: 6.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 266 RDAAKLRQSGSGGERSDYLAHLLQLQ-EKGASLDD--MVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLA 342
Cdd:cd20614  172 RLSQLVATARANGARTGLVAALIRARdDNGAGLSEqeLVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAA 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 343 ALDVDKRisYEQLNALPYLDQCVYESMRMTSVIGFLLKicTRPTKIDLGNDRIlnvEPGVTVAIPAYHFHHDEAYFPQPD 422
Cdd:cd20614  252 AGDVPRT--PAELRRFPLAEALFRETLRLHPPVPFVFR--RVLEEIELGGRRI---PAGTHLGIPLLLFSRDPELYPDPD 324
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193912267 423 EFRPERF--DNGAISELTkrgcLLAFGDGPRICLGMRVGLLSV---KMALLRILSQYKIEQ 478
Cdd:cd20614  325 RFRPERWlgRDRAPNPVE----LLQFGGGPHFCLGYHVACVELvqfIVALARELGAAGIRP 381
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
254-481 8.69e-18

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


Pssm-ID: 410738 [Multi-domain]  Cd Length: 419  Bit Score: 85.63  E-value: 8.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 254 TQAADDFYLKLTRDAAKLRQSGSGGERSDYLAHLLQLQEkgASLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQ 333
Cdd:cd20645  183 TEAWDNIFKTAKHCIDKRLQRYSQGPANDFLCDIYHDNE--LSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQ 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 334 EKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTRPTkiDLGnDRILnvePGVTVA-IPAYHFH 412
Cdd:cd20645  261 QKLLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTPSVPFTSRTLDKDT--VLG-DYLL---PKGTVLmINSQALG 334
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193912267 413 HDEAYFPQPDEFRPERF--DNGAISELTKrgclLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIEQTKK 481
Cdd:cd20645  335 SSEEYFEDGRQFKPERWlqEKHSINPFAH----VPFGIGKRMCIGRRLAELQLQLALCWIIQKYQIVATDN 401
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
282-476 5.29e-17

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: 83.09  E-value: 5.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 282 DYLAHLLQLQ-EKGASLDDMVGHAL--TVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNAL 358
Cdd:cd20678  219 DFLDILLFAKdENGKSLSDEDLRAEvdTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQM 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 359 PYLDQCVYESMRMTSVIGFLLKICTRPtkIDLGNDRILnvEPGVTVAIPAYHFHHDEAYFPQPDEFRPERF--DNgaiSE 436
Cdd:cd20678  299 PYTTMCIKEALRLYPPVPGISRELSKP--VTFPDGRSL--PAGITVSLSIYGLHHNPAVWPNPEVFDPLRFspEN---SS 371
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 193912267 437 LTKRGCLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKI 476
Cdd:cd20678  372 KRHSHAFLPFSAGPRNCIGQQFAMNEMKVAVALTLLRFEL 411
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
77-474 1.03e-16

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: 82.07  E-value: 1.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  77 VFL--TRQPQIL-VLDPQLAHEILVTNFSDFRdtvTSSYVTHSkdydkyvsRNPFF------SAGDEWKKHRVDAGAGLT 147
Cdd:cd20640   14 IFTysTGNKQFLyVSRPEMVKEINLCVSLDLG---KPSYLKKT--------LKPLFgggiltSNGPHWAHQRKIIAPEFF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 148 PNKLKQAYAIWEQTGEQLVSFIQSCIEERGSNIIETR--DLCYRYTAqamgDFIWGIDAGSLTGSAKETssFQRISTEWV 225
Cdd:cd20640   83 LDKVKGMVDLMVDSAQPLLSSWEERIDRAGGMAADIVvdEDLRAFSA----DVISRACFGSSYSKGKEI--FSKLRELQK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 226 ThaflgMTRLNRTTIAPIVRRLFRMRffTQAADDFYL---KLTRDAAKLRQSGSGGERSdylahLLQLQEKGASL----- 297
Cdd:cd20640  157 A-----VSKQSVLFSIPGLRHLPTKS--NRKIWELEGeirSLILEIVKEREEECDHEKD-----LLQAILEGARSscdkk 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 298 ----DDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAA-----LDVDkrisyeQLNALPYLDQCVYES 368
Cdd:cd20640  225 aeaeDFIVDNCKNIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVckggpPDAD------SLSRMKTVTMVIQET 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 369 MRMTSVIGFLLKICTRPTKidLGNdriLNVEPGVTVAIPAYHFHHD-EAYFPQPDEFRPERFDNGAISELTKRGCLLAFG 447
Cdd:cd20640  299 LRLYPPAAFVSREALRDMK--LGG---LVVPKGVNIWVPVSTLHLDpEIWGPDANEFNPERFSNGVAAACKPPHSYMPFG 373
                        410       420
                 ....*....|....*....|....*..
gi 193912267 448 DGPRICLGMRVGLLSVKMALLRILSQY 474
Cdd:cd20640  374 AGARTCLGQNFAMAELKVLVSLILSKF 400
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
174-481 1.17e-16

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: 82.27  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 174 EERGSNIIETRDLCYRYTAQAMGDFIWGIDAGSLTgsaketSSFQRISTEWVTHAFLGMTRLNRTTIAPIVRRLFR---- 249
Cdd:cd20647  108 EDDGETVTNVNDLFFKYSMEGVATILYECRLGCLE------NEIPKQTVEYIEALELMFSMFKTTMYAGAIPKWLRpfip 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 250 --MRFFTQAADD-FYLKLTRDAAKLRQSGSGGERSD-----YLAHLLQLQEkgASLDDMVGHALTVLMDGFETSSAVLYH 321
Cdd:cd20647  182 kpWEEFCRSWDGlFKFSQIHVDNRLREIQKQMDRGEevkggLLTYLLVSKE--LTLEEIYANMTEMLLAGVDTTSFTLSW 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 322 MLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVigflLKICTRPTKIDLGNDRILnVEPG 401
Cdd:cd20647  260 ATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPV----LPGNGRVTQDDLIVGGYL-IPKG 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 402 VTVAIPAYHFHHDEAYFPQPDEFRPERF-DNGAISELTKRGClLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIEQTK 480
Cdd:cd20647  335 TQLALCHYSTSYDEENFPRAEEFRPERWlRKDALDRVDNFGS-IPFGYGIRSCIGRRIAELEIHLALIQLLQNFEIKVSP 413

                 .
gi 193912267 481 K 481
Cdd:cd20647  414 Q 414
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
282-455 2.00e-16

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: 81.30  E-value: 2.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 282 DYLAHLLQLQEKGASLDDMVG--------HALTVLMD-GFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISY 352
Cdd:cd20652  208 FELCELEKAKKEGEDRDLFDGfytdeqlhHLLADLFGaGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTL 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 353 EQLNALPYLDQCVYESMRMTSVIGflLKI---CTRPTKidLGNDRIlnvePGVTVAIPAYHF-HHDEAYFPQPDEFRPER 428
Cdd:cd20652  288 EDLSSLPYLQACISESQRIRSVVP--LGIphgCTEDAV--LAGYRI----PKGSMIIPLLWAvHMDPNLWEEPEEFRPER 359
                        170       180
                 ....*....|....*....|....*....
gi 193912267 429 F--DNGAiseLTKRGCLLAFGDGPRICLG 455
Cdd:cd20652  360 FldTDGK---YLKPEAFIPFQTGKRMCLG 385
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
285-455 2.41e-16

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: 81.07  E-value: 2.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 285 AHLLQL-QEKGA-----SLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNAL 358
Cdd:cd11026  206 CFLLKMeKEKDNpnsefHEENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKM 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 359 PYLDQCVYESMRMTSVIGF-LLKICTRPTKidLGNDRIlnvePGVTVAIPAYH-FHHDEAYFPQPDEFRPERF--DNGai 434
Cdd:cd11026  286 PYTDAVIHEVQRFGDIVPLgVPHAVTRDTK--FRGYTI----PKGTTVIPNLTsVLRDPKQWETPEEFNPGHFldEQG-- 357
                        170       180
                 ....*....|....*....|.
gi 193912267 435 sELTKRGCLLAFGDGPRICLG 455
Cdd:cd11026  358 -KFKKNEAFMPFSAGKRVCLG 377
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
273-476 3.28e-16

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: 80.86  E-value: 3.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 273 QSGSGGE-RSDYLAHLL---QLqekgaSLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDK 348
Cdd:cd20646  208 RVDRGEPvEGEYLTYLLssgKL-----SPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDR 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 349 RISYEQLNALPYLDQCVYESMRMTSVIgfllkictrPtkidlGNDRILnVEPGVTVA---IPA--------YHFHHDEAY 417
Cdd:cd20646  283 IPTAEDIAKMPLLKAVIKETLRLYPVV---------P-----GNARVI-VEKEVVVGdylFPKntlfhlchYAVSHDETN 347
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 193912267 418 FPQPDEFRPERFDNGAISELTKRGClLAFGDGPRICLGMRVGLLSVKMALLRILSQYKI 476
Cdd:cd20646  348 FPEPERFKPERWLRDGGLKHHPFGS-IPFGYGVRACVGRRIAELEMYLALSRLIKRFEV 405
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
85-456 4.91e-16

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: 80.27  E-value: 4.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  85 ILVLDPQLAHEILVTNfsdfrDTVTSS----YVTHSKDYDKYVsrNPFFSAGDEWKKHR-VDAGAGLTPNKLKQAYAIWE 159
Cdd:cd11073   18 VVVSSPEAAREVLKTH-----DRVLSGrdvpDAVRALGHHKSS--IVWPPYGPRWRMLRkICTTELFSPKRLDATQPLRR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 160 QTGEQLVSFIQSCIEERGSniIETRDLCYRYTAQAMGDFIWGIDAGSLtgSAKETSSFQristEWVTHAflgMTRLNRTT 239
Cdd:cd11073   91 RKVRELVRYVREKAGSGEA--VDIGRAAFLTSLNLISNTLFSVDLVDP--DSESGSEFK----ELVREI---MELAGKPN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 240 IA---PIVRRL------FRMRFFTQAADDFYLKLTRDAAKLRQSGSG-GERSDYLAHLLQLQEKGASLDDmvGHALTVLM 309
Cdd:cd11073  160 VAdffPFLKFLdlqglrRRMAEHFGKLFDIFDGFIDERLAEREAGGDkKKDDDLLLLLDLELDSESELTR--NHIKALLL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 310 D----GFETSSAVL-YHMLYTLGaYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLL-KICT 383
Cdd:cd11073  238 DlfvaGTDTTSSTIeWAMAELLR-NPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLLLpRKAE 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 384 RPTKIdLGndriLNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFdngaiseLTKRGC-------LLAFGDGPRICLGM 456
Cdd:cd11073  317 EDVEV-MG----YTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERF-------LGSEIDfkgrdfeLIPFGSGRRICPGL 384
PLN02936 PLN02936
epsilon-ring hydroxylase
284-477 8.24e-16

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 79.84  E-value: 8.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 284 LAHLLQLQEKGASL---DDMvghaLTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDvDKRISYEQLNALPY 360
Cdd:PLN02936 264 LRFLLASREEVSSVqlrDDL----LSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQ-GRPPTYEDIKELKY 338
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 361 LDQCVYESMRMTSVIGFLLKictRPTKIDL--GNdriLNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFD--NGAISE 436
Cdd:PLN02936 339 LTRCINESMRLYPHPPVLIR---RAQVEDVlpGG---YKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDldGPVPNE 412
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 193912267 437 LTKRGCLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIE 477
Cdd:PLN02936 413 TNTDFRYIPFSGGPRKCVGDQFALLEAIVALAVLLQRLDLE 453
PLN02290 PLN02290
cytokinin trans-hydroxylase
82-476 2.01e-15

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 78.70  E-value: 2.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  82 QPQILVLDPQLAHEILVTnfsdfRDTVTSSYVTHSKDYDKYVSRNPFFSAGDEWKKHRVDAGAGLTPNKLKQAYAIWEQT 161
Cdd:PLN02290 104 EPRLCLTETELIKELLTK-----YNTVTGKSWLQQQGTKHFIGRGLLMANGADWYHQRHIAAPAFMGDRLKGYAGHMVEC 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 162 GEQLVSFIQSCIEErGSNIIETRDLCYRYTAqamgDFIWGIDAGSLTGSAKET----SSFQRISTEWVTHAFLGMTRLNR 237
Cdd:PLN02290 179 TKQMLQSLQKAVES-GQTEVEIGEYMTRLTA----DIISRTEFDSSYEKGKQIfhllTVLQRLCAQATRHLCFPGSRFFP 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 238 TTIAPIVRRLfRM---RFFTQAADDfylklTRDAAKLRQSGSGGErsDYLAHLLQLQEKGASldDMVGHALTVLMD---- 310
Cdd:PLN02290 254 SKYNREIKSL-KGeveRLLMEIIQS-----RRDCVEIGRSSSYGD--DLLGMLLNEMEKKRS--NGFNLNLQLIMDeckt 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 311 ----GFETSSAVLYHMLYTLGAYPEQQEKLRSEVlAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTRpt 386
Cdd:PLN02290 324 fffaGHETTALLLTWTLMLLASNPTWQDKVRAEV-AEVCGGETPSVDHLSKLTLLNMVINESLRLYPPATLLPRMAFE-- 400
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 387 KIDLGNdriLNVEPGVTVAIPAYHFHHDEAYF-PQPDEFRPERFdngAISELTKRGCLLAFGDGPRICLGMRVGLLSVKM 465
Cdd:PLN02290 401 DIKLGD---LHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRF---AGRPFAPGRHFIPFAAGPRNCIGQAFAMMEAKI 474
                        410
                 ....*....|.
gi 193912267 466 ALLRILSQYKI 476
Cdd:PLN02290 475 ILAMLISKFSF 485
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
305-492 2.68e-15

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: 78.03  E-value: 2.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 305 LTVLMD----GFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGF-LL 379
Cdd:cd20651  227 VMICLDlfiaGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLRIFTLVPIgIP 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 380 KICTRPTKidLGNDRIlnveP-GVTVAIPAYHFHHDEAYFPQPDEFRPERF--DNGaisELTKRGCLLAFGDGPRICLGM 456
Cdd:cd20651  307 HRALKDTT--LGGYRI----PkDTTILASLYSVHMDPEYWGDPEEFRPERFldEDG---KLLKDEWFLPFGAGKRRCLGE 377
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 193912267 457 RVGLLSVKMALLRILSQYKIEQTKKLSLSSDSGLGM 492
Cdd:cd20651  378 SLARNELFLFFTGLLQNFTFSPPNGSLPDLEGIPGG 413
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
311-492 2.97e-15

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: 77.75  E-value: 2.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 311 GFET-SSAVLYHMLYtLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTrpTKid 389
Cdd:cd20676  249 GFDTvTTALSWSLMY-LVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILETFRHSSFVPFTIPHCT--TR-- 323
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 390 lgnDRILN---VEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISELTKRGC--LLAFGDGPRICLGMRVGLLSVK 464
Cdd:cd20676  324 ---DTSLNgyyIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLTADGTEINKTESekVMLFGLGKRRCIGESIARWEVF 400
                        170       180       190
                 ....*....|....*....|....*....|
gi 193912267 465 MALLRILSQ--YKIEQTKKLSLSSDSGLGM 492
Cdd:cd20676  401 LFLAILLQQleFSVPPGVKVDMTPEYGLTM 430
PLN02966 PLN02966
cytochrome P450 83A1
296-493 5.92e-15

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 77.10  E-value: 5.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 296 SLDDMVGHALTVLMDGFETSSA-VLYHMLYtLGAYPEQQEKLRSEVLAALDVDKR--ISYEQLNALPYLDQCVYESMRMT 372
Cdd:PLN02966 286 TVDNVKAVILDIVVAGTDTAAAaVVWGMTY-LMKYPQVLKKAQAEVREYMKEKGStfVTEDDVKNLPYFRALVKETLRIE 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 373 SVIGFLL-KICTRPTKIdLGNDrilnVEPGVTVAIPAYHFHHDEA-YFPQPDEFRPERFDNGAISELTKRGCLLAFGDGP 450
Cdd:PLN02966 365 PVIPLLIpRACIQDTKI-AGYD----IPAGTTVNVNAWAVSRDEKeWGPNPDEFRPERFLEKEVDFKGTDYEFIPFGSGR 439
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 193912267 451 RICLGMRVG--LLSVKMALLRILSQYKIEQTKK---LSLSSDSGLGMY 493
Cdd:PLN02966 440 RMCPGMRLGaaMLEVPYANLLLNFNFKLPNGMKpddINMDVMTGLAMH 487
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
312-482 8.76e-14

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: 73.11  E-value: 8.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 312 FETSSAVLYHMLytlgAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSViGFLLKICTRPTKIdlg 391
Cdd:cd20635  231 FWTLAFILSHPS----VYKKVMEEISSVLGKAGKDKIKISEDDLKKMPYIKRCVLEAIRLRSP-GAITRKVVKPIKI--- 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 392 ndRILNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISELTKRGCLLAFGDGPRICLGMRVGLLSVKMALLRIL 471
Cdd:cd20635  303 --KNYTIPAGDMLMLSPYWAHRNPKYFPDPELFKPERWKKADLEKNVFLEGFVAFGGGRYQCPGRWFALMEIQMFVAMFL 380
                        170
                 ....*....|.
gi 193912267 472 SQYKIEQTKKL 482
Cdd:cd20635  381 YKYDFTLLDPV 391
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
276-455 1.35e-13

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: 72.74  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 276 SGGERSDYLAHLLQLQ-----EKGASLDDMVG----HALTVLMD----GFETSSAVLYHMLYTLGAYPEQQEKLRSEVLA 342
Cdd:cd20673  196 SSDSIRDLLDALLQAKmnaenNNAGPDQDSVGlsddHILMTVGDifgaGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQ 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 343 ALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLkictrPTK--ID--LGNdriLNVEPGVTVAIPAYHFHHDEAYF 418
Cdd:cd20673  276 NIGFSRTPTLSDRNHLPLLEATIREVLRIRPVAPLLI-----PHValQDssIGE---FTIPKGTRVVINLWALHHDEKEW 347
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 193912267 419 PQPDEFRPERFDNGAISEL-TKRGCLLAFGDGPRICLG 455
Cdd:cd20673  348 DQPDQFMPERFLDPTGSQLiSPSLSYLPFGAGPRVCLG 385
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
242-481 1.37e-13

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: 72.72  E-value: 1.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 242 PIVRRLFRMRfftqaaDDFYLKLTRDAAKLRQS-GSGGERSDYLAHLLQLQEKGASLDD---------MVGHALTVLMDG 311
Cdd:cd20622  201 PSYRRAAKIK------DDFLQREIQAIARSLERkGDEGEVRSAVDHMVRRELAAAEKEGrkpdyysqvIHDELFGYLIAG 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 312 FETSSAVLYHMLYTLGAYPEQQEKLRSE---VLAALDVDKRI-SYEQLNA--LPYLDQCVYESMRMTSVIGFLLKICTRP 385
Cdd:cd20622  275 HDTTSTALSWGLKYLTANQDVQSKLRKAlysAHPEAVAEGRLpTAQEIAQarIPYLDAVIEEILRCANTAPILSREATVD 354
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 386 TKIdLGNdRIlnveP-GVTV----AIPAY---HFHHDEAYFPQ----------------PDEFRPER------------F 429
Cdd:cd20622  355 TQV-LGY-SI----PkGTNVfllnNGPSYlspPIEIDESRRSSssaakgkkagvwdskdIADFDPERwlvtdeetgetvF 428
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 193912267 430 DNGAiseltkrGCLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIEQTKK 481
Cdd:cd20622  429 DPSA-------GPTLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFELLPLPE 473
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
305-467 1.38e-13

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: 72.63  E-value: 1.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 305 LTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTR 384
Cdd:cd20655  234 LDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGPLLVRESTE 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 385 PTKIDlGNDrilnVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERF--DNGAISELTKRGC---LLAFGDGPRICLGMRVG 459
Cdd:cd20655  314 GCKIN-GYD----IPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFlaSSRSGQELDVRGQhfkLLPFGSGRRGCPGASLA 388

                 ....*...
gi 193912267 460 LLSVKMAL 467
Cdd:cd20655  389 YQVVGTAI 396
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
282-487 2.19e-13

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: 72.01  E-value: 2.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 282 DYLAHLLQLQEKGA-SLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDvDKRISYEQLNALPY 360
Cdd:cd20616  206 DFATELIFAQKRGElTAENVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLG-ERDIQNDDLQKLKV 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 361 LDQCVYESMRMTSVIGFLLKICTRPTKID-----LGNDRILNVEpgvtvaipayHFHHDEaYFPQPDEFRPERFDNGAIS 435
Cdd:cd20616  285 LENFINESMRYQPVVDFVMRKALEDDVIDgypvkKGTNIILNIG----------RMHRLE-FFPKPNEFTLENFEKNVPS 353
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193912267 436 ELtkrgcLLAFGDGPRICLGMRVGLLSVKMALLRILSQY-----------KIEQTKKLSLSSD 487
Cdd:cd20616  354 RY-----FQPFGFGPRSCVGKYIAMVMMKAILVTLLRRFqvctlqgrcveNIQKTNDLSLHPD 411
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
323-502 2.39e-13

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: 71.95  E-value: 2.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 323 LYTLGAYPEQQEKLRSEV---------LAALDVDKRISYEQLNALPYLDQCVYESMRMTSViGFLLKICTRPTKIDLGND 393
Cdd:cd20632  239 MYYLLRHPEALAAVRDEIdhvlqstgqELGPDFDIHLTREQLDSLVYLESAINESLRLSSA-SMNIRVVQEDFTLKLESD 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 394 RILNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERF--DNGAISELTKRG-----CLLAFGDGPRICLGMRVGLLSVKMA 466
Cdd:cd20632  318 GSVNLRKGDIVALYPQSLHMDPEIYEDPEVFKFDRFveDGKKKTTFYKRGqklkyYLMPFGSGSSKCPGRFFAVNEIKQF 397
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 193912267 467 LLRILSQYKIE----QTKKLSLSSDSGLG-MYLNGDVDLRY 502
Cdd:cd20632  398 LSLLLLYFDLElleeQKPPGLDNSRAGLGiLPPNSDVRFRY 438
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
244-455 4.06e-13

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: 71.19  E-value: 4.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 244 VRRLFRMrfFTQAADDFYLKLTRDAAKLRQSGSGGERSDYLAHLLQLQEKGASLDDMVG----HALTVLMDGF----ETS 315
Cdd:cd20675  174 VRTVFRN--FKQLNREFYNFVLDKVLQHRETLRGGAPRDMMDAFILALEKGKSGDSGVGldkeYVPSTVTDIFgasqDTL 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 316 SAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICT-RPTKIdLGndr 394
Cdd:cd20675  252 STALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCIEDQPNLPYVMAFLYEAMRFSSFVPVTIPHATtADTSI-LG--- 327
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193912267 395 iLNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERF--DNGAI-SELTKRgcLLAFGDGPRICLG 455
Cdd:cd20675  328 -YHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFldENGFLnKDLASS--VMIFSVGKRRCIG 388
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
128-490 8.74e-13

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: 70.25  E-value: 8.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 128 FFSAGDEWKKHRVDAGAG-LTPNKLKQAYAIWEQTGEQLVSFIQSCIEE--RGSNIIETRDLCYRYTAQAMGDFIWGIDA 204
Cdd:cd20644   59 FLLNGPEWRFDRLRLNPEvLSPAAVQRFLPMLDAVARDFSQALKKRVLQnaRGSLTLDVQPDLFRFTLEASNLALYGERL 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 205 GsLTGSAKETSSFQRIStewvthaflGMTRLNRTT-----IAPIVRRLFRMRFFT---QAADDFYLKLTRDAAKLRQSGS 276
Cdd:cd20644  139 G-LVGHSPSSASLRFIS---------AVEVMLKTTvpllfMPRSLSRWISPKLWKehfEAWDCIFQYADNCIQKIYQELA 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 277 GGERSDYLAHLLQLQEKGA-SLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQL 355
Cdd:cd20644  209 FGRPQHYTGIVAELLLQAElSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKAL 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 356 NALPYLDQCVYESMRMTSVIGFLLKICTRptKIDLGNDRIlnvEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAIS 435
Cdd:cd20644  289 TELPLLKAALKETLRLYPVGITVQRVPSS--DLVLQNYHI---PAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGS 363
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 193912267 436 ELTKRGclLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIEQTKKLSLSSDSGL 490
Cdd:cd20644  364 GRNFKH--LAFGFGMRQCLGRRLAEAEMLLLLMHVLKNFLVETLSQEDIKTVYSF 416
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
242-479 8.87e-13

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: 70.04  E-value: 8.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 242 PIVRRLFRMRFFTQAADDFYLKLTRDAAKL-----RQSGSGGERSDYLAHLLQLQEKGASLDDMVGHALTVLMDGFETSS 316
Cdd:cd11066  166 PILRYFPKMSKFRERADEYRNRRDKYLKKLlaklkEEIEDGTDKPCIVGNILKDKESKLTDAELQSICLTMVSAGLDTVP 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 317 AVLYHMLYTLG--AYPEQQEKLRSEVLAA--LDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLL-KICTRPTKIDlG 391
Cdd:cd11066  246 LNLNHLIGHLShpPGQEIQEKAYEEILEAygNDEDAWEDCAAEEKCPYVVALVKETLRYFTVLPLGLpRKTTKDIVYN-G 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 392 ndriLNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFdngaiseLTKRGCL------LAFGDGPRICLGMRVGLLSVKM 465
Cdd:cd11066  325 ----AVIPAGTILFMNAWAANHDPEHFGDPDEFIPERW-------LDASGDLipgpphFSFGAGSRMCAGSHLANRELYT 393
                        250
                 ....*....|....
gi 193912267 466 ALLRILSQYKIEQT 479
Cdd:cd11066  394 AICRLILLFRIGPK 407
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
314-472 9.82e-13

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: 69.81  E-value: 9.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 314 TSSAVLYHMLYtLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTRPTKIDLGnd 393
Cdd:cd20666  244 TTNTLLWCLLY-MSLYPEVQEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLSIPHMASENTVLQG-- 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 394 riLNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERF--DNGaisELTKRGCLLAFGDGPRICLGMRVGllsvKMALLRIL 471
Cdd:cd20666  321 --YTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFldENG---QLIKKEAFIPFGIGRRVCMGEQLA----KMELFLMF 391

                 .
gi 193912267 472 S 472
Cdd:cd20666  392 V 392
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
272-458 1.27e-12

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: 69.44  E-value: 1.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 272 RQSGSGGERSDYLAHLLQLQEKGASLDDMVGHA------LTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALD 345
Cdd:cd20671  190 RPTIDGNPLHSYIEALIQKQEEDDPKETLFHDAnvlactLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLG 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 346 VDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKiCTrPTKIDLGNDRIlnvePGVTVAIPAY-HFHHDEAYFPQPDEF 424
Cdd:cd20671  270 PGCLPNYEDRKALPYTSAVIHEVQRFITLLPHVPR-CT-AADTQFKGYLI----PKGTPVIPLLsSVLLDKTQWETPYQF 343
                        170       180       190
                 ....*....|....*....|....*....|....
gi 193912267 425 RPERFDNgAISELTKRGCLLAFGDGPRICLGMRV 458
Cdd:cd20671  344 NPNHFLD-AEGKFVKKEAFLPFSAGRRVCVGESL 376
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
77-481 4.22e-12

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 68.22  E-value: 4.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  77 VFLTRQPQ---ILVLDPQLAHEILVTNFSDF----RDTVTSSYVTHSKDYdkyvsrnPFFSAGDEWKKHRVDAGAGLTPN 149
Cdd:PLN02394  66 VFLLRMGQrnlVVVSSPELAKEVLHTQGVEFgsrtRNVVFDIFTGKGQDM-------VFTVYGDHWRKMRRIMTVPFFTN 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 150 K-LKQAYAIWEQTGEQLVSFIQSCIEERGSNIIETRDL---CYRYTAQAMGDfiwgidagsltgsaketSSFQriSTEwv 225
Cdd:PLN02394 139 KvVQQYRYGWEEEADLVVEDVRANPEAATEGVVIRRRLqlmMYNIMYRMMFD-----------------RRFE--SED-- 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 226 THAFLGMTRLN--RTTIA-----------PIVRRLF-------------RMRFFtqaaDDFYLKLTRDAAKLRQSGSGGE 279
Cdd:PLN02394 198 DPLFLKLKALNgeRSRLAqsfeynygdfiPILRPFLrgylkicqdvkerRLALF----KDYFVDERKKLMSAKGMDKEGL 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 280 RSDyLAHLLQLQEKGASLDDMVGHAL-TVLMDGFETSsavLYHM---LYTLGAYPEQQEKLRSEVLAALDVDKRISYEQL 355
Cdd:PLN02394 274 KCA-IDHILEAQKKGEINEDNVLYIVeNINVAAIETT---LWSIewgIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDT 349
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 356 NALPYLDQCVYESMRMTSVIGFLL-KICTRPTKIDlGNDrilnVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERF--DNG 432
Cdd:PLN02394 350 HKLPYLQAVVKETLRLHMAIPLLVpHMNLEDAKLG-GYD----IPAESKILVNAWWLANNPELWKNPEEFRPERFleEEA 424
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 193912267 433 AISELTKRGCLLAFGDGPRIC---------LGMRVGLLSVKMALLRILSQYKIEQTKK 481
Cdd:PLN02394 425 KVEANGNDFRFLPFGVGRRSCpgiilalpiLGIVLGRLVQNFELLPPPGQSKIDVSEK 482
PLN02738 PLN02738
carotene beta-ring hydroxylase
295-455 5.10e-12

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 68.40  E-value: 5.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 295 ASLDDMVGHAL-----TVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDvDKRISYEQLNALPYLDQCVYESM 369
Cdd:PLN02738 382 ASGDDVSSKQLrddlmTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLG-DRFPTIEDMKKLKYTTRVINESL 460
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 370 RMTSVIGFLLKictRPTKID-LGNDRIlnvEPGVTVAIPAYHFHHDEAYFPQPDEFRPERF--DNGAISELTKRGCLLAF 446
Cdd:PLN02738 461 RLYPQPPVLIR---RSLENDmLGGYPI---KRGEDIFISVWNLHRSPKHWDDAEKFNPERWplDGPNPNETNQNFSYLPF 534

                 ....*....
gi 193912267 447 GDGPRICLG 455
Cdd:PLN02738 535 GGGPRKCVG 543
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
243-477 6.37e-12

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: 67.10  E-value: 6.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 243 IVRRLFrmrFFTQAADDfyLKLTRDAAKLRQSGS--------GGERSDYLAHLLQLQEKgASLDDMVGHALTVLMD---- 310
Cdd:cd20624  119 IVRRLV---LGDSARDD--RELTDLLDALRRRANwaflrpriSRARERFRARLREYVER-AEPGSLVGELSRLPEGdevd 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 311 ----------GFETSSAVLYHMLYTLGAYPEQQEKLRSEvLAALDVDKrisyeqlnALPYLDQCVYESMRMTSVIGFLLK 380
Cdd:cd20624  193 pegqvpqwlfAFDAAGMALLRALALLAAHPEQAARAREE-AAVPPGPL--------ARPYLRACVLDAVRLWPTTPAVLR 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 381 ICTRPTKIdlgNDRIlnVEPGVTVAIPAYHFHHDEAYFPQPDEFRPER-FDNGAISELTkrgcLLAFGDGPRICLGMRVG 459
Cdd:cd20624  264 ESTEDTVW---GGRT--VPAGTGFLIFAPFFHRDDEALPFADRFVPEIwLDGRAQPDEG----LVPFSAGPARCPGENLV 334
                        250
                 ....*....|....*...
gi 193912267 460 LLSVKMALLRILSQYKIE 477
Cdd:cd20624  335 LLVASTALAALLRRAEID 352
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
283-455 7.89e-12

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: 67.13  E-value: 7.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 283 YLAHLLQLQEKGASL--DDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPY 360
Cdd:cd20662  207 YLKEMAKYPDPTTSFneENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPY 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 361 LDQCVYESMRMTSVIGF-LLKICTRPTKidLGNDRIlnvePGVTVAIPAY-HFHHDEAYFPQPDEFRPERF-DNGaisEL 437
Cdd:cd20662  287 TNAVIHEVQRMGNIIPLnVPREVAVDTK--LAGFHL----PKGTMILTNLtALHRDPKEWATPDTFNPGHFlENG---QF 357
                        170
                 ....*....|....*...
gi 193912267 438 TKRGCLLAFGDGPRICLG 455
Cdd:cd20662  358 KKREAFLPFSMGKRACLG 375
PLN02655 PLN02655
ent-kaurene oxidase
323-474 8.49e-12

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 67.07  E-value: 8.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 323 LYTLGAYPEQQEKLRSEVLAALDvDKRISYEQLNALPYLDQCVYESMRMTSVIGFLlkictrPTK-----IDLGNdriLN 397
Cdd:PLN02655 286 MYELAKNPDKQERLYREIREVCG-DERVTEEDLPNLPYLNAVFHETLRKYSPVPLL------PPRfvhedTTLGG---YD 355
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193912267 398 VEPGVTVAIPAYHFHHDEAYFPQPDEFRPERF--DNGAISELTKrgcLLAFGDGPRICLGMRVGLLSVKMALLRILSQY 474
Cdd:PLN02655 356 IPAGTQIAINIYGCNMDKKRWENPEEWDPERFlgEKYESADMYK---TMAFGAGKRVCAGSLQAMLIACMAIARLVQEF 431
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
279-455 8.66e-12

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: 67.09  E-value: 8.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 279 ERSDYLAHLlqlqekgaSLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNAL 358
Cdd:cd20669  214 EKQDPLSHF--------NMETLVMTTHNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARM 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 359 PYLDQCVYESMRMTSVIGF-LLKICTRPTkidlgNDRILNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERF--DNGais 435
Cdd:cd20669  286 PYTDAVIHEIQRFADIIPMsLPHAVTRDT-----NFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFldDNG--- 357
                        170       180
                 ....*....|....*....|
gi 193912267 436 ELTKRGCLLAFGDGPRICLG 455
Cdd:cd20669  358 SFKKNDAFMPFSAGKRICLG 377
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
305-474 1.09e-11

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 67.02  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 305 LTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKictR 384
Cdd:PLN03234 294 LDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKGYVSEEDIPNLPYLKAVIKESLRLEPVIPILLH---R 370
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 385 PTKID--LGNdriLNVEPGVTVAIPAYHFHHDEAYF-PQPDEFRPERFDN--GAISELTKRGCLLAFGDGPRICLGMRVG 459
Cdd:PLN03234 371 ETIADakIGG---YDIPAKTIIQVNAWAVSRDTAAWgDNPNEFIPERFMKehKGVDFKGQDFELLPFGSGRRMCPAMHLG 447
                        170
                 ....*....|....*
gi 193912267 460 LLSVKMALLRILSQY 474
Cdd:PLN03234 448 IAMVEIPFANLLYKF 462
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
272-487 1.16e-11

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: 66.58  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 272 RQSGSGGERSDYLAH--LLQLQ-EKGASLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDK 348
Cdd:cd11076  194 RAKRSNRARDDEDDVdvLLSLQgEEKLSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSR 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 349 RISYEQLNALPYLDQCVYESMRMTSViGFLL---KICTRPTKIDlGNdrilNVEPGVTVAIPAYHFHHDEAYFPQPDEFR 425
Cdd:cd11076  274 RVADSDVAKLPYLQAVVKETLRLHPP-GPLLswaRLAIHDVTVG-GH----VVPAGTTAMVNMWAITHDPHVWEDPLEFK 347
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193912267 426 PERF-DNGAISELTKRGC---LLAFGDGPRICLGMRVGLLSVKMALLRILSQYK--------IEQTKKLSLSSD 487
Cdd:cd11076  348 PERFvAAEGGADVSVLGSdlrLAPFGAGRRVCPGKALGLATVHLWVAQLLHEFEwlpddakpVDLSEVLKLSCE 421
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
336-497 1.38e-11

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: 66.21  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 336 LRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTRPTKIDLGNDRILNVEPGVTVAIpayHF---H 412
Cdd:cd20612  215 LRRPGAAHLAEIQALARENDEADATLRGYVLEALRLNPIAPGLYRRATTDTTVADGGGRTVSIKAGDRVFV---SLasaM 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 413 HDEAYFPQPDEFRPERFDNGAIseltkrgcllAFGDGPRICLGMRVGLLSVKMALLRILSQYKIE-------QTKKLsls 485
Cdd:cd20612  292 RDPRAFPDPERFRLDRPLESYI----------HFGHGPHQCLGEEIARAALTEMLRVVLRLPNLRrapgpqgELKKI--- 358
                        170
                 ....*....|..
gi 193912267 486 SDSGLGMYLNGD 497
Cdd:cd20612  359 PRGGFKAYLRED 370
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
314-481 3.09e-11

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: 65.35  E-value: 3.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 314 TSSAVLYhMLYTLGAYPEQQEKLRSEVlAAL--DVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTRPTKIDlg 391
Cdd:cd11082  236 STSSLVW-ALQLLADHPDVLAKVREEQ-ARLrpNDEPPLTLDLLEEMKYTRQVVKEVLRYRPPAPMVPHIAKKDFPLT-- 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 392 ndrilnvePGVTVA-----IPA-YHFHHDEayFPQPDEFRPERFDNGAISELTKRGCLLAFGDGPRICLGMR--VGLLSV 463
Cdd:cd11082  312 --------EDYTVPkgtivIPSiYDSCFQG--FPEPDKFDPDRFSPERQEDRKYKKNFLVFGAGPHQCVGQEyaINHLML 381
                        170
                 ....*....|....*...
gi 193912267 464 KMALLRILSQYKIEQTKK 481
Cdd:cd11082  382 FLALFSTLVDWKRHRTPG 399
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
251-494 3.54e-11

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: 65.22  E-value: 3.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 251 RFFTQAAD--DFYLKLTRDAAKLRQSGSGGERSD-YLAHLLQLQ---EKGASLDDMVGHALTVLMDGFETSSAVL-YHML 323
Cdd:cd20661  184 QLFRNAAEvyDFLLRLIERFSENRKPQSPRHFIDaYLDEMDQNKndpESTFSMENLIFSVGELIIAGTETTTNVLrWAIL 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 324 YtLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGF-LLKICTRPTKIdlgndRILNVEPGV 402
Cdd:cd20661  264 F-MALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPLgIFHATSKDAVV-----RGYSIPKGT 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 403 TVAIPAYHFHHDEAYFPQPDEFRPERFDNGAiSELTKRGCLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIEQTKKL 482
Cdd:cd20661  338 TVITNLYSVHFDEKYWSDPEVFHPERFLDSN-GQFAKKEAFVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHGL 416
                        250
                 ....*....|..
gi 193912267 483 SLSSDSGLGMYL 494
Cdd:cd20661  417 IPDLKPKLGMTL 428
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
305-490 4.52e-11

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 65.03  E-value: 4.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 305 LTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVlaaldvDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTR 384
Cdd:PLN02169 307 FSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEI------NTKFDNEDLEKLVYLHAALSESMRLYPPLPFNHKAPAK 380
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 385 PTKIDLGNdrilNVEPGVTVAIPAYHFHHDEAYFPQ-PDEFRPERF--DNGAISELTKRGcLLAFGDGPRICLGMRVGLL 461
Cdd:PLN02169 381 PDVLPSGH----KVDAESKIVICIYALGRMRSVWGEdALDFKPERWisDNGGLRHEPSYK-FMAFNSGPRTCLGKHLALL 455
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 193912267 462 SVKMALLRILSQY--------KIEQTKKLSLSSDSGL 490
Cdd:PLN02169 456 QMKIVALEIIKNYdfkvieghKIEAIPSILLRMKHGL 492
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
77-481 5.56e-11

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: 64.42  E-value: 5.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  77 VFLTRQPQ---ILVLDPQLAHEILVTNFSDF----RDTVTSSYVTHSKDYdkyvsrnPFFSAGDEWKKHRVDAGAGLTPN 149
Cdd:cd11074    6 IFLLRMGQrnlVVVSSPELAKEVLHTQGVEFgsrtRNVVFDIFTGKGQDM-------VFTVYGEHWRKMRRIMTVPFFTN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 150 KLKQAYA-IWEQTGEQLVSFIQSCIEERGSNIIETRDL---CYRYTAQAMGDfiwgidagsltgsaketssfQRISTEwV 225
Cdd:cd11074   79 KVVQQYRyGWEEEAARVVEDVKKNPEAATEGIVIRRRLqlmMYNNMYRIMFD--------------------RRFESE-D 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 226 THAFLGMTRLN--RTTIA-----------PIVRRLFRMRF-FTQAADDFYLKLTRD-----AAKLRQSGSGGERSDYLA- 285
Cdd:cd11074  138 DPLFVKLKALNgeRSRLAqsfeynygdfiPILRPFLRGYLkICKEVKERRLQLFKDyfvdeRKKLGSTKSTKNEGLKCAi 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 286 -HLLQLQEKGASLDDMVGHAL-TVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQ 363
Cdd:cd11074  218 dHILDAQKKGEINEDNVLYIVeNINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQA 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 364 CVYESMRMTSVIGFLL-KICTRPTKIDlGNDriLNVEPGVTVAipAYHFHHDEAYFPQPDEFRPERFDNGAiSELTKRGC 442
Cdd:cd11074  298 VVKETLRLRMAIPLLVpHMNLHDAKLG-GYD--IPAESKILVN--AWWLANNPAHWKKPEEFRPERFLEEE-SKVEANGN 371
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 193912267 443 ---LLAFGDGPRIC---------LGMRVGLLSVKMALLRILSQYKIEQTKK 481
Cdd:cd11074  372 dfrYLPFGVGRRSCpgiilalpiLGITIGRLVQNFELLPPPGQSKIDTSEK 422
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
205-467 1.19e-10

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: 63.39  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 205 GSLTGSAKETSSFQRISTEWVTHAFLGmtrlNRTTIAPIVRRLF------RMRFFTQAADDFYLKLTRDAaklRQSGSGG 278
Cdd:cd20653  132 GEDVSDAEEAKLFRELVSEIFELSGAG----NPADFLPILRWFDfqglekRVKKLAKRRDAFLQGLIDEH---RKNKESG 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 279 ERSdYLAHLLQLQEKGASL--DDMV-GHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQL 355
Cdd:cd20653  205 KNT-MIDHLLSLQESQPEYytDEIIkGLILVMLLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDL 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 356 NALPYLDQCVYESMRMTSVIGFLLKIC-TRPTKIDlGNDrilnVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGaI 434
Cdd:cd20653  284 PKLPYLQNIISETLRLYPAAPLLVPHEsSEDCKIG-GYD----IPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFEGE-E 357
                        250       260       270
                 ....*....|....*....|....*....|...
gi 193912267 435 SELTKrgcLLAFGDGPRICLGMRVGLLSVKMAL 467
Cdd:cd20653  358 REGYK---LIPFGLGRRACPGAGLAQRVVGLAL 387
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
97-460 1.41e-10

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: 63.01  E-value: 1.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  97 LVTNFSD----FRDTVT-SSYVTHSKDYDKYVSRNPFFSA------GDEWKKHRVDAGAGLTPNKLKQayaiWEQTGEQL 165
Cdd:cd11078   23 VVSRYEDvkavLRDPQTfSSAGGLTPESPLWPEAGFAPTPslvnedPPRHTRLRRLVSRAFTPRRIAA----LEPRIREL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 166 V-SFIQSCIEERGSNIIEtrDLCYRYTAQAMGDFIwGIDAgsltgsaketSSFQRIStEWvTHAFLGMTRlNRTTIAPIV 244
Cdd:cd11078   99 AaELLDRLAEDGRADFVA--DFAAPLPALVIAELL-GVPE----------EDMERFR-RW-ADAFALVTW-GRPSEEEQV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 245 RRLfrmrfftQAADDFYLKLTRDAAKLRQSgsggERSDYLAHLLQLQEK-GASLDD--MVGHALTVLMDGFETSSAVLYH 321
Cdd:cd11078  163 EAA-------AAVGELWAYFADLVAERRRE----PRDDLISDLLAAADGdGERLTDeeLVAFLFLLLVAGHETTTNLLGN 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 322 MLYTLGAYPEQQEKLRSEvlAALdvdkrisyeqlnalpyLDQCVYESMRMTSVIGFLLKICTRPTKIDlgndrilnvepG 401
Cdd:cd11078  232 AVKLLLEHPDQWRRLRAD--PSL----------------IPNAVEETLRYDSPVQGLRRTATRDVEIG-----------G 282
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193912267 402 VTvaIPAYHF--------HHDEAYFPQPDEFRPERfdngaiselTKRGCLLAFGDGPRICLG-------MRVGL 460
Cdd:cd11078  283 VT--IPAGARvlllfgsaNRDERVFPDPDRFDIDR---------PNARKHLTFGHGIHFCLGaalarmeARIAL 345
PLN02183 PLN02183
ferulate 5-hydroxylase
305-471 1.41e-10

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 63.33  E-value: 1.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 305 LTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTR 384
Cdd:PLN02183 310 MDVMFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGLNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAE 389
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 385 PTKIDLgndriLNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISELtkRGC---LLAFGDGPRICLGMRVGLL 461
Cdd:PLN02183 390 DAEVAG-----YFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFLKPGVPDF--KGShfeFIPFGSGRRSCPGMQLGLY 462
                        170
                 ....*....|
gi 193912267 462 SVKMALLRIL 471
Cdd:PLN02183 463 ALDLAVAHLL 472
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
280-475 1.61e-10

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: 62.62  E-value: 1.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 280 RSDYLAHLLQLQEKGASLDDM--VGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSE---VLAALDvdkrisyeq 354
Cdd:cd11032  177 RDDLISRLVEAEVDGERLTDEeiVGFAILLLIAGHETTTNLLGNAVLCLDEDPEVAARLRADpslIPGAIE--------- 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 355 lnalpyldqcvyESMRMTSVIGFLLKICTRPTKIDlgndrilnvepGVTvaIPAYHF--------HHDEAYFPQPDEFRP 426
Cdd:cd11032  248 ------------EVLRYRPPVQRTARVTTEDVELG-----------GVT--IPAGQLviawlasaNRDERQFEDPDTFDI 302
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 193912267 427 ERFDNGAiseltkrgclLAFGDGPRICLGMRVGLLSVKMALLRILSQYK 475
Cdd:cd11032  303 DRNPNPH----------LSFGHGIHFCLGAPLARLEARIALEALLDRFP 341
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
83-471 1.75e-10

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 63.30  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  83 PQILVLDPQLAHEILVTnfsdfRDTVTSSYV-THSKDYDKY----VSRNPFfsaGDEWKK-HRVDAGAGLTPNKLKQAYA 156
Cdd:PLN03112  76 DAITTDDPELIREILLR-----QDDVFASRPrTLAAVHLAYgcgdVALAPL---GPHWKRmRRICMEHLLTTKRLESFAK 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 157 IWEQTGEQLVSFIQSciEERGSNIIETRDLCYRYTAQAMGDFIWGI-DAGSLTGSAKETSSFQRISTEwvthAFLGMTRL 235
Cdd:PLN03112 148 HRAEEARHLIQDVWE--AAQTGKPVNLREVLGAFSMNNVTRMLLGKqYFGAESAGPKEAMEFMHITHE----LFRLLGVI 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 236 NRTTIAPIVRRL------FRMRFFTQAADDFYLKLTRDAAKLRQS-GSGGERSDYLAHLLQLQ-EKGAS-LDDMVGHALT 306
Cdd:PLN03112 222 YLGDYLPAWRWLdpygceKKMREVEKRVDEFHDKIIDEHRRARSGkLPGGKDMDFVDVLLSLPgENGKEhMDDVEIKALM 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 307 VLMDGFET-SSAVL--YHMLYTLgAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLL-KIC 382
Cdd:PLN03112 302 QDMIAAATdTSAVTneWAMAEVI-KNPRVLRKIQEELDSVVGRNRMVQESDLVHLNYLRCVVRETFRMHPAGPFLIpHES 380
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 383 TRPTKIDlGNDrilnVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERF-----DNGAISELTKRGcLLAFGDGPRICLGMR 457
Cdd:PLN03112 381 LRATTIN-GYY----IPAKTRVFINTHGLGRNTKIWDDVEEFRPERHwpaegSRVEISHGPDFK-ILPFSAGKRKCPGAP 454
                        410
                 ....*....|....
gi 193912267 458 VGLLSVKMALLRIL 471
Cdd:PLN03112 455 LGVTMVLMALARLF 468
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
89-467 2.05e-10

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 62.87  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267  89 DPQLAHEILVTNFSDF-RDTVTSSYVthskdyDKYVSRNPFFSAGDEWKKHRVDAGAGLTPNKLKQ-AYAIWEQTGEQLV 166
Cdd:PLN03195  82 DPVNVEHVLKTNFANYpKGEVYHSYM------EVLLGDGIFNVDGELWRKQRKTASFEFASKNLRDfSTVVFREYSLKLS 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 167 SFI-QSCIEERgsnIIETRDLCYRYTAQAMGDFIWGIDAGSLTGSAKETSSFQRIST--EWVTHAFlgmtrlnrttIAPI 243
Cdd:PLN03195 156 SILsQASFANQ---VVDMQDLFMRMTLDSICKVGFGVEIGTLSPSLPENPFAQAFDTanIIVTLRF----------IDPL 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 244 --VRRLFRM---RFFTQAA---DDF-YLKLTRDAAKLRQSGSGGE--RSDYLAHLLQLQEKG------ASLDDMVghaLT 306
Cdd:PLN03195 223 wkLKKFLNIgseALLSKSIkvvDDFtYSVIRRRKAEMDEARKSGKkvKHDILSRFIELGEDPdsnftdKSLRDIV---LN 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 307 VLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEvLAALDVDKR---------------------ISYEQLNALPYLDQCV 365
Cdd:PLN03195 300 FVIAGRDTTATTLSWFVYMIMMNPHVAEKLYSE-LKALEKERAkeedpedsqsfnqrvtqfaglLTYDSLGKLQYLHAVI 378
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 366 YESMRMTSVI-----GFLlkictrptkidlgNDRIL----NVEPGVTVAIPAYHFHHDEAYF-PQPDEFRPER-FDNGAI 434
Cdd:PLN03195 379 TETLRLYPAVpqdpkGIL-------------EDDVLpdgtKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERwIKDGVF 445
                        410       420       430
                 ....*....|....*....|....*....|...
gi 193912267 435 SELTKRGcLLAFGDGPRICLGMRVGLLSVKMAL 467
Cdd:PLN03195 446 QNASPFK-FTAFQAGPRICLGKDSAYLQMKMAL 477
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
253-492 4.35e-10

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: 61.45  E-value: 4.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 253 FTQAADDFYLKLTRDAAKLRQSgsggERSDYLAHLLQLQEKGASL--DDMVGHALTVLMDGFET-SSAVLYHMLYtLGAY 329
Cdd:cd11035  146 RAAAAQAVLDYLTPLIAERRAN----PGDDLISAILNAEIDGRPLtdDELLGLCFLLFLAGLDTvASALGFIFRH-LARH 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 330 PEQQEKLRSE---VLAALDvdkrisyeqlnalpyldqcvyESMRMTSVIgFLLKICTRPTKIDlGndriLNVEPGVTVAI 406
Cdd:cd11035  221 PEDRRRLREDpelIPAAVE---------------------ELLRRYPLV-NVARIVTRDVEFH-G----VQLKAGDMVLL 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 407 PAYHFHHDEAYFPQPDEFRPERFDNGAiseltkrgclLAFGDGPRICLGMRVGLLSVKMAL---LRILSQYKIEQTKKLS 483
Cdd:cd11035  274 PLALANRDPREFPDPDTVDFDRKPNRH----------LAFGAGPHRCLGSHLARLELRIALeewLKRIPDFRLAPGAQPT 343

                 ....*....
gi 193912267 484 LSSDSGLGM 492
Cdd:cd11035  344 YHGGSVMGL 352
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
311-467 7.23e-10

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: 60.90  E-value: 7.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 311 GFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLL-KICTRPTKID 389
Cdd:cd20657  240 GTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPSTPLNLpRIASEACEVD 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 390 lGndriLNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISELTKRGC---LLAFGDGPRICLGMRVGLLSVKMA 466
Cdd:cd20657  320 -G----YYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPGRNAKVDVRGNdfeLIPFGAGRRICAGTRMGIRMVEYI 394

                 .
gi 193912267 467 L 467
Cdd:cd20657  395 L 395
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
242-474 8.94e-10

cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the meta-hydroxylation step in the phenylpropanoid biosynthetic pathway. CYP98A3, also called p-coumaroylshikimate/quinate 3'-hydroxylase, catalyzes 3'-hydroxylation of p-coumaric esters of shikimic/quinic acids to form lignin monomers. CYP98A8, also called p-coumarate 3-hydroxylase, acts redundantly with CYP98A9 as tricoumaroylspermidine meta-hydroxylase. CYP98 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410749 [Multi-domain]  Cd Length: 432  Bit Score: 60.58  E-value: 8.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 242 PIVRRLFRMR---FFTQAA--DDFYLKLTRDAAKLRQSGSGGERsdYLAHLLQLQEK-GASLDDMVGHALTVLMDGFETS 315
Cdd:cd20656  169 PWLRWMFPLSekaFAKHGArrDRLTKAIMEEHTLARQKSGGGQQ--HFVALLTLKEQyDLSEDTVIGLLWDMITAGMDTT 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 316 SAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLL-KICTRPTKIDlGNDr 394
Cdd:cd20656  247 AISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLHPPTPLMLpHKASENVKIG-GYD- 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 395 ilnVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISELTKRGCLLAFGDGPRICLGMRVGLLSVKMALLRILSQY 474
Cdd:cd20656  325 ---IPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVDIKGHDFRLLPFGAGRRVCPGAQLGINLVTLMLGHLLHHF 401
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
255-471 1.72e-09

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: 59.49  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 255 QAADDFYLKLTRDAAKLRQSGsggeRSDYLAHLLQLQEKGASL--DDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQ 332
Cdd:cd20625  159 AAAAELAAYFRDLIARRRADP----GDDLISALVAAEEDGDRLseDELVANCILLLVAGHETTVNLIGNGLLALLRHPEQ 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 333 QEKLRSE-VLAAldvdkrisyeqlNAlpyldqcVYESMRMTSVIGFLLKICTRPtkIDLGNDRIlnvEPG--VTVAIPAY 409
Cdd:cd20625  235 LALLRADpELIP------------AA-------VEELLRYDSPVQLTARVALED--VEIGGQTI---PAGdrVLLLLGAA 290
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193912267 410 HfhHDEAYFPQPDEFRPERFDNGAiseltkrgclLAFGDGPRICLGMRVGLLSVKMALLRIL 471
Cdd:cd20625  291 N--RDPAVFPDPDRFDITRAPNRH----------LAFGAGIHFCLGAPLARLEAEIALRALL 340
PLN00168 PLN00168
Cytochrome P450; Provisional
243-461 1.78e-09

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 59.96  E-value: 1.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 243 IVRRLFRMRFFTQAA-----DDFYLKL--TRDAAKLRQSGSGGERSD-------YLAHLLQL---QEKGASL--DDMVGH 303
Cdd:PLN00168 231 VTKHLFRGRLQKALAlrrrqKELFVPLidARREYKNHLGQGGEPPKKettfehsYVDTLLDIrlpEDGDRALtdDEIVNL 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 304 ALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKR-ISYEQLNALPYLDQCVYESMRMTSVIGFLLkic 382
Cdd:PLN00168 311 CSEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDDQEeVSEEDVHKMPYLKAVVLEGLRKHPPAHFVL--- 387
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 383 trPTK----IDLGNDRIlnvEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISE-----LTKRGCLLAFGDGPRIC 453
Cdd:PLN00168 388 --PHKaaedMEVGGYLI---PKGATVNFMVAEMGRDEREWERPMEFVPERFLAGGDGEgvdvtGSREIRMMPFGVGRRIC 462

                 ....*...
gi 193912267 454 LGMRVGLL 461
Cdd:PLN00168 463 AGLGIAML 470
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
304-455 1.80e-09

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: 59.79  E-value: 1.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 304 ALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKicT 383
Cdd:cd20672  231 VLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPIGVP--H 308
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193912267 384 RPTKIDLGNDRIL----NVEPGVTVAIpayhfhHDEAYFPQPDEFRPERF--DNGAiseLTKRGCLLAFGDGPRICLG 455
Cdd:cd20672  309 RVTKDTLFRGYLLpkntEVYPILSSAL------HDPQYFEQPDTFNPDHFldANGA---LKKSEAFMPFSTGKRICLG 377
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
283-484 2.08e-09

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: 59.47  E-value: 2.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 283 YLAHLLQLQEKGASL---DDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALP 359
Cdd:cd20667  206 YLAQITKTKDDPVSTfseENMIQVVIDLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLP 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 360 YLDQCVYESMRMTSVIGF-LLKICTRPTKIdLGndriLNVEPGvTVAIPAYH-FHHDEAYFPQPDEFRPERFdngaiseL 437
Cdd:cd20667  286 YTNAVIHEVQRLSNVVSVgAVRQCVTSTTM-HG----YYVEKG-TIILPNLAsVLYDPECWETPHKFNPGHF-------L 352
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 193912267 438 TKRG------CLLAFGDGPRICLG---MRVGLLSVKMALLRILSQYKIEQTKKLSL 484
Cdd:cd20667  353 DKDGnfvmneAFLPFSAGHRVCLGeqlARMELFIFFTTLLRTFNFQLPEGVQELNL 408
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
270-476 2.38e-09

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: 59.55  E-value: 2.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 270 KLRQSGSGGERSDYLAHLLQLQEKGASLD----DMVGHA--LTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAA 343
Cdd:cd20654  206 KRSSSGKSKNDEDDDDVMMLSILEDSQISgydaDTVIKAtcLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTH 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 344 LDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKictRPTKID--LGNdriLNVEPGVTVAIPAYHFHHDEAYFPQP 421
Cdd:cd20654  286 VGKDRWVEESDIKNLVYLQAIVKETLRLYPPGPLLGP---REATEDctVGG---YHVPKGTRLLVNVWKIQRDPNVWSDP 359
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 193912267 422 DEFRPERFDNGAiSELTKRGC---LLAFGDGPRICLGMRVGLLSVKMALLRILSQYKI 476
Cdd:cd20654  360 LEFKPERFLTTH-KDIDVRGQnfeLIPFGSGRRSCPGVSFGLQVMHLTLARLLHGFDI 416
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
282-469 4.53e-09

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: 58.35  E-value: 4.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 282 DYLAHLLQLQEKGASLDD--MVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRsevlaaldvdkrisyEQLNALP 359
Cdd:cd11031  187 DLLSALVAARDDDDRLSEeeLVTLAVGLLVAGHETTASQIGNGVLLLLRHPEQLARLR---------------ADPELVP 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 360 yldQCVYESMRMTSVI--GFLLKICTRPtkIDLGNDRIlnvEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAisel 437
Cdd:cd11031  252 ---AAVEELLRYIPLGagGGFPRYATED--VELGGVTI---RAGEAVLVSLNAANRDPEVFPDPDRLDLDREPNPH---- 319
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 193912267 438 tkrgclLAFGDGPRICLGM---RVGLLSVKMALLR 469
Cdd:cd11031  320 ------LAFGHGPHHCLGAplaRLELQVALGALLR 348
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
282-455 4.55e-09

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: 58.31  E-value: 4.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 282 DYLAHLLQLQEKGASL--DDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEvlAALdvdkrisyeqlnalp 359
Cdd:cd11029  192 DLLSALVAARDEGDRLseEELVSTVFLLLVAGHETTVNLIGNGVLALLTHPDQLALLRAD--PEL--------------- 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 360 yLDQCVYESMRMTS-VIGFLLKICTRPTKIDlgndrilnvepGVTvaIPAYHF--------HHDEAYFPQPDEFRPERFD 430
Cdd:cd11029  255 -WPAAVEELLRYDGpVALATLRFATEDVEVG-----------GVT--IPAGEPvlvslaaaNRDPARFPDPDRLDITRDA 320
                        170       180
                 ....*....|....*....|....*
gi 193912267 431 NGaiseltkrgcLLAFGDGPRICLG 455
Cdd:cd11029  321 NG----------HLAFGHGIHYCLG 335
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
296-476 1.60e-08

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: 56.86  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 296 SLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVI 375
Cdd:cd20670  223 NLKNLVLTTLNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQRLTDIV 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 376 GF-LLKICTRPTKIdlgndRILNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERF--DNGaisELTKRGCLLAFGDGPRI 452
Cdd:cd20670  303 PLgVPHNVIRDTQF-----RGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFldEQG---RFKKNEAFVPFSSGKRV 374
                        170       180
                 ....*....|....*....|....
gi 193912267 453 CLGMRVGLLSVKMALLRILSQYKI 476
Cdd:cd20670  375 CLGEAMARMELFLYFTSILQNFSL 398
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
296-482 1.71e-08

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: 56.73  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 296 SLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVI 375
Cdd:cd20668  223 YMKNLVMTTLNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVI 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 376 GflLKICTRPTKIDLGNDRILnvePGVTVAIPAY-HFHHDEAYFPQPDEFRPERF--DNGaisELTKRGCLLAFGDGPRI 452
Cdd:cd20668  303 P--MGLARRVTKDTKFRDFFL---PKGTEVFPMLgSVLKDPKFFSNPKDFNPQHFldDKG---QFKKSDAFVPFSIGKRY 374
                        170       180       190
                 ....*....|....*....|....*....|
gi 193912267 453 CLGMRVGLLSVKMALLRILSQYKIEQTKKL 482
Cdd:cd20668  375 CFGEGLARMELFLFFTTIMQNFRFKSPQSP 404
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
281-433 2.28e-08

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: 56.11  E-value: 2.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 281 SDYLAHLLQLQEKGASLDDMVGHAL--TVLMDGFETSSAVLYHMLYTLGAYPEQ-QEKLRSEVLAALDVDKRISYEQLNA 357
Cdd:cd11071  205 ANAGLEVLDEAEKLGLSREEAVHNLlfMLGFNAFGGFSALLPSLLARLGLAGEElHARLAEEIRSALGSEGGLTLAALEK 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 358 LPYLDQCVYESMRMTSVIGFllkICTRPTKidlgnDRILNVEPGvTVAIP------AYHF--HHDEAYFPQPDEFRPERF 429
Cdd:cd11071  285 MPLLKSVVYETLRLHPPVPL---QYGRARK-----DFVIESHDA-SYKIKkgellvGYQPlaTRDPKVFDNPDEFVPDRF 355

                 ....
gi 193912267 430 DNGA 433
Cdd:cd11071  356 MGEE 359
PLN02500 PLN02500
cytochrome P450 90B1
262-455 2.56e-08

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 56.41  E-value: 2.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 262 LKLTRDAAKLRQSGSGGERSDYLAHLLQlqEKGASLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVL 341
Cdd:PLN02500 244 RKMEERIEKLKEEDESVEEDDLLGWVLK--HSNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEHL 321
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 342 AALDVDKRISYEQLNALPY----LDQCVY-ESMRMTSVIGFLLKICTRPTKIDlGND-----RILNVEPGVtvaipayhf 411
Cdd:PLN02500 322 EIARAKKQSGESELNWEDYkkmeFTQCVInETLRLGNVVRFLHRKALKDVRYK-GYDipsgwKVLPVIAAV--------- 391
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 193912267 412 HHDEAYFPQPDEFRPERFDN------GAISELTKRGCLLAFGDGPRICLG 455
Cdd:PLN02500 392 HLDSSLYDQPQLFNPWRWQQnnnrggSSGSSSATTNNFMPFGGGPRLCAG 441
PLN02687 PLN02687
flavonoid 3'-monooxygenase
249-465 2.64e-08

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 56.36  E-value: 2.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 249 RMRFFTQAADDFYLKLTRDAAKLRQSGsGGERSDYLAHLLQLQEK------GASLDDMVGHALTVLM--DGFETSSAVLY 320
Cdd:PLN02687 240 KMKRLHRRFDAMMNGIIEEHKAAGQTG-SEEHKDLLSTLLALKREqqadgeGGRITDTEIKALLLNLftAGTDTTSSTVE 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 321 HMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRM-TSVIGFLLKICTRPTKIDlGndriLNVE 399
Cdd:PLN02687 319 WAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLhPSTPLSLPRMAAEECEIN-G----YHIP 393
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 400 PGVTVAIPAYHFHHDEAYFPQPDEFRPERF-DNGAISELTKRGC---LLAFGDGPRICLGMRVGLLSVKM 465
Cdd:PLN02687 394 KGATLLVNVWAIARDPEQWPDPLEFRPDRFlPGGEHAGVDVKGSdfeLIPFGAGRRICAGLSWGLRMVTL 463
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
229-472 2.93e-08

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: 55.81  E-value: 2.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 229 FLGMTRLNRTTIAPIVRRLFRMRFFTQAADDFyLKLTRDAAKLRQSGSGGERSDYLAHLLQLQEKGASLDD--MVGHALT 306
Cdd:cd11034  119 LLGLPDEDGERLRDWVHAILHDEDPEEGAAAF-AELFGHLRDLIAERRANPRDDLISRLIEGEIDGKPLSDgeVIGFLTL 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 307 VLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAaldvdkrisyeqlnalpyLDQCVYESMRMTSVIGFLLKICTRPT 386
Cdd:cd11034  198 LLLGGTDTTSSALSGALLWLAQHPEDRRRLIADPSL------------------IPNAVEEFLRFYSPVAGLARTVTQEV 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 387 kiDLGNDRIlnvEPG--VTVAIPAYhfHHDEAYFPQPDEFRPERFDNGAiseltkrgclLAFGDGPRICLGMRVGLLSVK 464
Cdd:cd11034  260 --EVGGCRL---KPGdrVLLAFASA--NRDEEKFEDPDRIDIDRTPNRH----------LAFGSGVHRCLGSHLARVEAR 322

                 ....*...
gi 193912267 465 MALLRILS 472
Cdd:cd11034  323 VALTEVLK 330
PLN02774 PLN02774
brassinosteroid-6-oxidase
263-478 2.93e-08

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 55.94  E-value: 2.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 263 KLTRDAAKLRQSgSGGERSDYLAHLLQLQEKGASLDD--MVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEV 340
Cdd:PLN02774 227 RMLRQLIQERRA-SGETHTDMLGYLMRKEGNRYKLTDeeIIDQIITILYSGYETVSTTSMMAVKYLHDHPKALQELRKEH 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 341 LA---ALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLkictRPTKIDLGNDRILnVEPGVTVAIPAYHFHHDEAY 417
Cdd:PLN02774 306 LAireRKRPEDPIDWNDYKSMRFTRAVIFETSRLATIVNGVL----RKTTQDMELNGYV-IPKGWRIYVYTREINYDPFL 380
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193912267 418 FPQPDEFRPERF-DNGaiseLTKRGCLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIEQ 478
Cdd:PLN02774 381 YPDPMTFNPWRWlDKS----LESHNYFFLFGGGTRLCPGKELGIVEISTFLHYFVTRYRWEE 438
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
305-500 4.22e-08

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 55.63  E-value: 4.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 305 LTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAALDVDKRISYEQLNALPYLDQCVYESMRM-TSVIGFLLKICT 383
Cdd:PLN00110 295 LNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRRLVESDLPKLPYLQAICKESFRKhPSTPLNLPRVST 374
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 384 RPTKIDLgndriLNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISELTKRGC---LLAFGDGPRICLGMRVGL 460
Cdd:PLN00110 375 QACEVNG-----YYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEKNAKIDPRGNdfeLIPFGAGRRICAGTRMGI 449
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 193912267 461 LSVKMALLRILSQYKIEQTKKLSLSSDSGLGMYLNGDVDL 500
Cdd:PLN00110 450 VLVEYILGTLVHSFDWKLPDGVELNMDEAFGLALQKAVPL 489
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
240-474 8.43e-08

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 54.60  E-value: 8.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 240 IAPIVRRLFRMRffTQAADDFYLKLTRdaaKLRQSGSGGER-SDYLAHLLQlQEKGASLDDMVGHALTVLMDGFETSSAV 318
Cdd:PLN02987 213 FSTTYRRAIQAR--TKVAEALTLVVMK---RRKEEEEGAEKkKDMLAALLA-SDDGFSDEEIVDFLVALLVAGYETTSTI 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 319 LYHMLYTLGAYPEQQEKLRSE---VLAALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLkictRPTKIDLgNDRI 395
Cdd:PLN02987 287 MTLAVKFLTETPLALAQLKEEhekIRAMKSDSYSLEWSDYKSMPFTQCVVNETLRVANIIGGIF----RRAMTDI-EVKG 361
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193912267 396 LNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISELTKrGCLLAFGDGPRICLGMRVGLLSVKMALLRILSQY 474
Cdd:PLN02987 362 YTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGTTVPS-NVFTPFGGGPRLCPGYELARVALSVFLHRLVTRF 439
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
297-477 1.77e-07

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 53.54  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 297 LDDMVghaLTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVLAAL-DVDKRISYEQLNALPYLDQCVYESMRMTSVI 375
Cdd:PLN02426 294 LRDIV---VSFLLAGRDTVASALTSFFWLLSKHPEVASAIREEADRVMgPNQEAASFEEMKEMHYLHAALYESMRLFPPV 370
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 376 GFLLKICTrptkidlgNDRILN----VEPGVTVAIPAYHF-HHDEAYFPQPDEFRPERF-DNGA-ISELTKRgcLLAFGD 448
Cdd:PLN02426 371 QFDSKFAA--------EDDVLPdgtfVAKGTRVTYHPYAMgRMERIWGPDCLEFKPERWlKNGVfVPENPFK--YPVFQA 440
                        170       180
                 ....*....|....*....|....*....
gi 193912267 449 GPRICLGMRVGLLSVKMALLRILSQYKIE 477
Cdd:PLN02426 441 GLRVCLGKEMALMEMKSVAVAVVRRFDIE 469
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
311-455 4.29e-07

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: 52.12  E-value: 4.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 311 GFETSSAVLYHMLYTLGAYPEQQEKLRSEVlaaldvDKRIS-----YEQLNALPYLDQCVYESMRMTSVIGFLLKictRP 385
Cdd:cd20664  237 GTDTTGTTLRWGLLLMMKYPEIQKKVQEEI------DRVIGsrqpqVEHRKNMPYTDAVIHEIQRFANIVPMNLP---HA 307
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 386 TKIDLgNDRILNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAiSELTKRGCLLAFGDGPRICLG 455
Cdd:cd20664  308 TTRDV-TFRGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLDSQ-GKFVKRDAFMPFSAGRRVCIG 375
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
296-471 6.69e-07

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: 51.37  E-value: 6.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 296 SLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEVlaaldvdkrisyeqlnALpyLDQCVYESMRMTSVI 375
Cdd:cd11033  206 TDEEFASFFILLAVAGNETTRNSISGGVLALAEHPDQWERLRADP----------------SL--LPTAVEEILRWASPV 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 376 GFLLKICTRPTkiDLGNDRIlnvEPG--VTVAIPAYHFhhDEAYFPQPDEFRPERFDNGaiseltkrgcLLAFGDGPRIC 453
Cdd:cd11033  268 IHFRRTATRDT--ELGGQRI---RAGdkVVLWYASANR--DEEVFDDPDRFDITRSPNP----------HLAFGGGPHFC 330
                        170
                 ....*....|....*...
gi 193912267 454 LGMRVGLLSVKMALLRIL 471
Cdd:cd11033  331 LGAHLARLELRVLFEELL 348
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
314-477 7.35e-07

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: 51.60  E-value: 7.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 314 TSSAVLYHMLYTLgAYPEQQEKLRSEVLAAL----------DVDKRISYEQLNALPYLDQCVYESMRMTsVIGFLLKICT 383
Cdd:cd20633  240 TGPASFWLLLYLL-KHPEAMKAVREEVEQVLketgqevkpgGPLINLTRDMLLKTPVLDSAVEETLRLT-AAPVLIRAVV 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 384 RPTKIDLGNDRILNVEPGVTVAIPAYHFHH-DEAYFPQPDEFRPERF---DNGAISELTKRG-----CLLAFGDGPRICL 454
Cdd:cd20633  318 QDMTLKMANGREYALRKGDRLALFPYLAVQmDPEIHPEPHTFKYDRFlnpDGGKKKDFYKNGkklkyYNMPWGAGVSICP 397
                        170       180
                 ....*....|....*....|...
gi 193912267 455 GMRVGLLSVKMALLRILSQYKIE 477
Cdd:cd20633  398 GRFFAVNEMKQFVFLMLTYFDLE 420
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
279-456 8.64e-07

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: 51.15  E-value: 8.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 279 ERSDYLAHLLQLQEKGASLDDMVGHALTVLM--DGFETSSAVLYHMLYTLGAYPEQQEKLR---SEVLAALDvdkrisye 353
Cdd:cd20629  170 PGDDLISRLLRAEVEGEKLDDEEIISFLRLLlpAGSDTTYRALANLLTLLLQHPEQLERVRrdrSLIPAAIE-------- 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 354 qlnalpyldqcvyESMRMTSVIGFLLKICTRPTKIDlgndrilnvepGVTvaIPAYHF--------HHDEAYFPQPDEFR 425
Cdd:cd20629  242 -------------EGLRWEPPVASVPRMALRDVELD-----------GVT--IPAGSLldlsvgsaNRDEDVYPDPDVFD 295
                        170       180       190
                 ....*....|....*....|....*....|.
gi 193912267 426 PERfdngaiseltKRGCLLAFGDGPRICLGM 456
Cdd:cd20629  296 IDR----------KPKPHLVFGGGAHRCLGE 316
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
311-469 9.64e-07

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: 51.04  E-value: 9.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 311 GFETSSAVLYHMLYTLGAYPEQQEKLRSE---VLAALDvdkrisyeqlnalpyldqcvyESMRMTSVIGFLLKICTRPTK 387
Cdd:cd11037  214 GLDTTISAIGNALWLLARHPDQWERLRADpslAPNAFE---------------------EAVRLESPVQTFSRTTTRDTE 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 388 IDlgndrilnvepGVTvaIPA----YHF----HHDEAYFPQPDEFRPERFDNGAiseltkrgclLAFGDGPRICLGMRVG 459
Cdd:cd11037  273 LA-----------GVT--IPAgsrvLVFlgsaNRDPRKWDDPDRFDITRNPSGH----------VGFGHGVHACVGQHLA 329
                        170
                 ....*....|...
gi 193912267 460 LL---SVKMALLR 469
Cdd:cd11037  330 RLegeALLTALAR 342
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
269-455 1.33e-06

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: 50.58  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 269 AKLRQSGSGGERSDYLAHLLQLQEKGA---SLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSEV----L 341
Cdd:cd20638  197 AKIQREDTEQQCKDALQLLIEHSRRNGeplNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELqekgL 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 342 AALDV--DKRISYEQLNALPYLDQCVYESMRMTSVI--GFLLKICTrptkIDLGNDRIlnvePGVTVAIPAYHFHHDEA- 416
Cdd:cd20638  277 LSTKPneNKELSMEVLEQLKYTGCVIKETLRLSPPVpgGFRVALKT----FELNGYQI----PKGWNVIYSICDTHDVAd 348
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 193912267 417 YFPQPDEFRPERFDNGAIsELTKRGCLLAFGDGPRICLG 455
Cdd:cd20638  349 IFPNKDEFNPDRFMSPLP-EDSSRFSFIPFGGGSRSCVG 386
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
264-475 2.27e-06

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 49.93  E-value: 2.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 264 LTRDAAKLRQSGSggERSDYLAHLLQLQEkGASLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYP--------EQQEK 335
Cdd:PLN02196 232 LAKILSKRRQNGS--SHNDLLGSFMGDKE-GLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPsvleavteEQMAI 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 336 LRSEvlaalDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLkictRPTKIDLGNDRILnVEPGVTVaIPAY-HFHHD 414
Cdd:PLN02196 309 RKDK-----EEGESLTWEDTKKMPLTSRVIQETLRVASILSFTF----REAVEDVEYEGYL-IPKGWKV-LPLFrNIHHS 377
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193912267 415 EAYFPQPDEFRPERFDNGAiseltKRGCLLAFGDGPRICLGMRVGLLSVKMALLRILSQYK 475
Cdd:PLN02196 378 ADIFSDPGKFDPSRFEVAP-----KPNTFMPFGNGTHSCPGNELAKLEISVLIHHLTTKYR 433
PLN02302 PLN02302
ent-kaurenoic acid oxidase
270-477 3.24e-06

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 49.71  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 270 KLRQSGSGGERSDYLAHLL-QLQEKGASLDD--MVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSE----VLA 342
Cdd:PLN02302 255 NSRKQNISPRKKDMLDLLLdAEDENGRKLDDeeIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEVLQKAKAEqeeiAKK 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 343 ALDVDKRISYEQLNALPYLDQCVYESMRMT--SVIGFllkictRPTKIDLGNDRILnVEPGVTVAIPAYHFHHDEAYFPQ 420
Cdd:PLN02302 335 RPPGQKGLTLKDVRKMEYLSQVIDETLRLIniSLTVF------REAKTDVEVNGYT-IPKGWKVLAWFRQVHMDPEVYPN 407
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 193912267 421 PDEFRPERFDNgaisELTKRGCLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIE 477
Cdd:PLN02302 408 PKEFDPSRWDN----YTPKAGTFLPFGLGSRLCPGNDLAKLEISIFLHHFLLGYRLE 460
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
255-490 9.82e-06

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: 47.74  E-value: 9.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 255 QAADDFYLKLTRDAAKLRQSGSGGErSDYLAHLLQLQEKGASLDD--MVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQ 332
Cdd:cd11079  138 EVAEEFDGIIRDLLADRRAAPRDAD-DDVTARLLRERVDGRPLTDeeIVSILRNWTVGELGTIAACVGVLVHYLARHPEL 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 333 QEKLR---SEVLAALDvdkrisyeqlnalpyldqcvyESMRM-TSVIGFLlKICTRPTKIdlGNDRILNVEPgvtVAIPA 408
Cdd:cd11079  217 QARLRanpALLPAAID---------------------EILRLdDPFVANR-RITTRDVEL--GGRTIPAGSR---VTLNW 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 409 YHFHHDEAYFPQPDEFRPERfdnGAISELTkrgcllaFGDGPRICLGMRVGLLsvkmaLLRILSQYKIEQTKKLSLSSDS 488
Cdd:cd11079  270 ASANRDERVFGDPDEFDPDR---HAADNLV-------YGRGIHVCPGAPLARL-----ELRILLEELLAQTEAITLAAGG 334

                 ..
gi 193912267 489 GL 490
Cdd:cd11079  335 PP 336
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
319-491 1.46e-05

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: 47.37  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 319 LYHMLYTlgayPEQQEKLRSEVLAAL--------DVDKRISY--EQLNALPYLDQCVYESMRMTSViGFLLKICTRPTKI 388
Cdd:cd20631  251 LFYLLRC----PEAMKAATKEVKRTLektgqkvsDGGNPIVLtrEQLDDMPVLGSIIKEALRLSSA-SLNIRVAKEDFTL 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 389 DLGNDRILNVEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISELTK--------RGCLLAFGDGPRICLGMRVGL 460
Cdd:cd20631  326 HLDSGESYAIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGKEKTTfykngrklKYYYMPFGSGTSKCPGRFFAI 405
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 193912267 461 LSVKMALLRILSQYKIE----QTKKLSL-SSDSGLG 491
Cdd:cd20631  406 NEIKQFLSLMLCYFDMElldgNAKCPPLdQSRAGLG 441
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
280-455 1.47e-05

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: 47.36  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 280 RSDYLAHLLQLQEKGASLDD--MVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRsevlaaldvdkrisyeqlnA 357
Cdd:cd11038  193 GDDLISTLVAAEQDGDRLSDeeLRNLIVALLFAGVDTTRNQLGLAMLTFAEHPDQWRALR-------------------E 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 358 LPYL-DQCVYESMRMTSVIGFLLKICTRptkidlgndrilNVE-PGVTvaIPAYHFHH--DEAYFPQPDEFRPERFDNGA 433
Cdd:cd11038  254 DPELaPAAVEEVLRWCPTTTWATREAVE------------DVEyNGVT--IPAGTVVHlcSHAANRDPRVFDADRFDITA 319
                        170       180
                 ....*....|....*....|..
gi 193912267 434 iseltKRGCLLAFGDGPRICLG 455
Cdd:cd11038  320 -----KRAPHLGFGGGVHHCLG 336
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
280-500 4.22e-05

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: 45.93  E-value: 4.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 280 RSDYLAHLLQLQEKGASLDD--MVGHALTVLMDGFETSSAVLYHMLYTLGAYPEQQEKLRSevlaaldvDKRIsyeqlna 357
Cdd:cd11080  172 GSDLISILCTAEYEGEALSDedIKALILNVLLAATEPADKTLALMIYHLLNNPEQLAAVRA--------DRSL------- 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 358 lpyLDQCVYESMRMTSVIGFLLKICTRPTKIdlGNDRIlnvEPGVTVAIPAYHFHHDEAYFPQPDEFRPERFDNGAISEL 437
Cdd:cd11080  237 ---VPRAIAETLRYHPPVQLIPRQASQDVVV--SGMEI---KKGTTVFCLIGAANRDPAAFEDPDTFNIHREDLGIRSAF 308
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193912267 438 TKRGCLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIEQTKKLSLSSDSGLgmYLNGDVDL 500
Cdd:cd11080  309 SGAADHLAFGSGRHFCVGAALAKREIEIVANQVLDALPNIRLEPGFEYAESGL--YTRGPVSL 369
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
255-477 2.05e-04

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: 43.68  E-value: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 255 QAADDFYLKLTRDAAKLRQSGSGGERSDYLAHLLQLQE---KGASLDDMVGHALTVLMDGFETSSAVLYHMLYTLGAYPE 331
Cdd:cd20637  179 RARDSLQKSLEKAIREKLQGTQGKDYADALDILIESAKehgKELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPG 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 332 QQEKLRSEVLA------ALDVDKRISYEQLNALPYLDQCVYESMRMTSVIGFLLKICTRPTKIDLgndriLNVEPGVTVA 405
Cdd:cd20637  259 VLEKLREELRSngilhnGCLCEGTLRLDTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFELDG-----FQIPKGWSVL 333
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193912267 406 IPAYHFHHDEAYFPQPDEFRPERFDNGAISELTKRGCLLAFGDGPRICLGMRVGLLSVKMALLRILSQYKIE 477
Cdd:cd20637  334 YSIRDTHDTAPVFKDVDAFDPDRFGQERSEDKDGRFHYLPFGGGVRTCLGKQLAKLFLKVLAVELASTSRFE 405
PLN02648 PLN02648
allene oxide synthase
281-429 2.69e-03

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 40.30  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 281 SDYLAHLLQLQEK-GASLDDMVgHALtVLMDGFETS---SAVLYHMLYTLG-AYPEQQEKLRSEVLAALDV-DKRISYEQ 354
Cdd:PLN02648 252 RASATEALDLAEKfGISREEAL-HNL-LFVLGFNAFggfKIFFPALLKWVGrAGEELQARLAEEVRSAVKAgGGGVTFAA 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193912267 355 LNALPYLDQCVYESMRMTS-------------VI-----GFLLKictrptKIDLgndrILNVEPGVTvaipayhfhHDEA 416
Cdd:PLN02648 330 LEKMPLVKSVVYEALRIEPpvpfqygraredfVIeshdaAFEIK------KGEM----LFGYQPLVT---------RDPK 390
                        170
                 ....*....|...
gi 193912267 417 YFPQPDEFRPERF 429
Cdd:PLN02648 391 VFDRPEEFVPDRF 403
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
412-435 3.30e-03

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: 39.82  E-value: 3.30e-03
                         10        20
                 ....*....|....*....|....
gi 193912267 412 HHDEAYFPQPDEFRPERFDNGAIS 435
Cdd:cd11067  311 NHDPRLWEDPDRFRPERFLGWEGD 334
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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