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Conserved domains on  [gi|1034571959|ref|XP_016872679|]
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vitamin D 25-hydroxylase isoform X1 [Homo sapiens]

Protein Classification

cytochrome P450 family protein( domain architecture ID 1750044)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cytochrome_P450 super family cl41757
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
17-442 0e+00

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.


The actual alignment was detected with superfamily member cd20661:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 436  Bit Score: 861.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  17 LFSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRYGRGWVDHRRLAVNSFRYFGYGQ 96
Cdd:cd20661    11 IHGQIFSLDLGGISTVVLNGYDAVKECLVHQSEIFADRPSLPLFMKLTNMGGLLNSKYGRGWTEHRKLAVNCFRYFGYGQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  97 KSFESKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNA 176
Cdd:cd20661    91 KSFESKISEECKFFLDAIDTYKGKPFDPKHLITNAVSNITNLIIFGERFTYEDTDFQHMIEIFSENVELAASAWVFLYNA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 177 FPWIGILPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENLIFSVGELIIAG 256
Cdd:cd20661   171 FPWIGILPFGKHQQLFRNAAEVYDFLLRLIERFSENRKPQSPRHFIDAYLDEMDQNKNDPESTFSMENLIFSVGELIIAG 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 257 TETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRG 336
Cdd:cd20661   251 TETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSKDAVVRG 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 337 YSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHL 416
Cdd:cd20661   331 YSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHL 410
                         410       420
                  ....*....|....*....|....*.
gi 1034571959 417 HFPHELVPDLKPRLGMTLQPQPYLIC 442
Cdd:cd20661   411 HFPHGLIPDLKPKLGMTLQPQPYLIC 436
 
Name Accession Description Interval E-value
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
17-442 0e+00

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: 861.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  17 LFSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRYGRGWVDHRRLAVNSFRYFGYGQ 96
Cdd:cd20661    11 IHGQIFSLDLGGISTVVLNGYDAVKECLVHQSEIFADRPSLPLFMKLTNMGGLLNSKYGRGWTEHRKLAVNCFRYFGYGQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  97 KSFESKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNA 176
Cdd:cd20661    91 KSFESKISEECKFFLDAIDTYKGKPFDPKHLITNAVSNITNLIIFGERFTYEDTDFQHMIEIFSENVELAASAWVFLYNA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 177 FPWIGILPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENLIFSVGELIIAG 256
Cdd:cd20661   171 FPWIGILPFGKHQQLFRNAAEVYDFLLRLIERFSENRKPQSPRHFIDAYLDEMDQNKNDPESTFSMENLIFSVGELIIAG 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 257 TETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRG 336
Cdd:cd20661   251 TETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSKDAVVRG 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 337 YSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHL 416
Cdd:cd20661   331 YSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHL 410
                         410       420
                  ....*....|....*....|....*.
gi 1034571959 417 HFPHELVPDLKPRLGMTLQPQPYLIC 442
Cdd:cd20661   411 HFPHGLIPDLKPKLGMTLQPQPYLIC 436
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
18-442 1.61e-124

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: 369.30  E-value: 1.61e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  18 FSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLF---MKMTKMGGLLNSRYGRgWVDHRRLAVNSFRYFGy 94
Cdd:pfam00067  33 YGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFatsRGPFLGKGIVFANGPR-WRQLRRFLTPTFTSFG- 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  95 gQKSFESKILEETKFFNDAIETYKGRP--FDFKQLITNAVSNITNLIIFGERF-TYEDTDFQHMIELFSENVELAASASV 171
Cdd:pfam00067 111 -KLSFEPRVEEEARDLVEKLRKTAGEPgvIDITDLLFRAALNVICSILFGERFgSLEDPKFLELVKAVQELSSLLSSPSP 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 172 FLYNAFPWIGILPfGKHQQLFRNAAVVY-DFLSRLIE--KASVNRKPQLPQHFVDAYLDEMDqgkNDPSSTFSKENLIFS 248
Cdd:pfam00067 190 QLLDLFPILKYFP-GPHGRKLKRARKKIkDLLDKLIEerRETLDSAKKSPRDFLDALLLAKE---EEDGSKLTDEELRAT 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 249 VGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHAT 328
Cdd:pfam00067 266 VLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKETLRLHPVVPLLLPREV 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 329 SEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFT 408
Cdd:pfam00067 346 TKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLA 425
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1034571959 409 ALLQRFHLHFPHEL-VPDLKPRLGMTLQPQPYLIC 442
Cdd:pfam00067 426 TLLQNFEVELPPGTdPPDIDETPGLLLPPKPYKLK 460
PTZ00404 PTZ00404
cytochrome P450; Provisional
18-446 6.91e-45

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 162.97  E-value: 6.91e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  18 FSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSrYGRGWVDHRRLAVNSFRyfgygqK 97
Cdd:PTZ00404   61 YGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHGTFYHGIVTS-SGEYWKRNREIVGKAMR------K 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  98 SFESKILEE-TKFFNDAIETYK-----GRPFDFKQLITNAVSNITNLIIFGERFTYEDT----DFQHMIELFSENVELAA 167
Cdd:PTZ00404  134 TNLKHIYDLlDDQVDVLIESMKkiessGETFEPRYYLTKFTMSAMFKYIFNEDISFDEDihngKLAELMGPMEQVFKDLG 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 168 SASVF--------LYnaFPWIgiLPFGKHQQLFRNaavvydFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDpsst 239
Cdd:PTZ00404  214 SGSLFdvieitqpLY--YQYL--EHTDKNFKKIKK------FIKEKYHEHLKTIDPEVPRDLLDLLIKEYGTNTDD---- 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 240 fSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNI 319
Cdd:PTZ00404  280 -DILSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPV 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 320 VPLGIFHATSEDAVV-RGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSgyfaKKEALVPFSLGRRHCLGEHL 398
Cdd:PTZ00404  359 SPFGLPRSTSNDIIIgGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPD----SNDAFMPFSIGPRNCVGQQF 434
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1034571959 399 ARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQPQPYLICAERR 446
Cdd:PTZ00404  435 AQDELYLAFSNIILNFKLKSIDGKKIDETEEYGLTLKPNKFKVLLEKR 482
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
21-435 6.92e-45

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: 160.83  E-value: 6.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRYGRGWVDHRRLAVNSFRyfgyGQ--KS 98
Cdd:COG2124    34 VFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVLRPLPLLGDSLLTLDGPEHTRLRRLVQPAFT----PRrvAA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  99 FESKILEETkffNDAIETYKGR-PFDFkqliTNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASasvflynaf 177
Cdd:COG2124   110 LRPRIREIA---DELLDRLAARgPVDL----VEEFARPLPVIVICELLGVPEEDRDRLRRWSDALLDALGP--------- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 178 pwigiLPFGKHQQLFRNAAVVYDFLSRLIEKasvnRKPQLPQHFVDAYLDEMDQGkndpsSTFSKENLIFSVGELIIAGT 257
Cdd:COG2124   174 -----LPPERRRRARRARAELDAYLRELIAE----RRAEPGDDLLSALLAARDDG-----ERLSDEELRDELLLLLLAGH 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 258 ETTTNVLRWAILFMALYPNIQGQVQKEIdlimgpngkpswddkckmPYTEAVLHEVLRFCNIVPLGIFHATsEDAVVRGY 337
Cdd:COG2124   240 ETTANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEETLRLYPPVPLLPRTAT-EDVELGGV 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 338 SIPKGTTVITNLYSVHFDEKYWRDPEVFHPERfldssgyfaKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHlH 417
Cdd:COG2124   301 TIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR---------PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFP-D 370
                         410       420
                  ....*....|....*....|
gi 1034571959 418 FphELVPD--LKPRLGMTLQ 435
Cdd:COG2124   371 L--RLAPPeeLRWRPSLTLR 388
 
Name Accession Description Interval E-value
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
17-442 0e+00

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: 861.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  17 LFSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRYGRGWVDHRRLAVNSFRYFGYGQ 96
Cdd:cd20661    11 IHGQIFSLDLGGISTVVLNGYDAVKECLVHQSEIFADRPSLPLFMKLTNMGGLLNSKYGRGWTEHRKLAVNCFRYFGYGQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  97 KSFESKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNA 176
Cdd:cd20661    91 KSFESKISEECKFFLDAIDTYKGKPFDPKHLITNAVSNITNLIIFGERFTYEDTDFQHMIEIFSENVELAASAWVFLYNA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 177 FPWIGILPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENLIFSVGELIIAG 256
Cdd:cd20661   171 FPWIGILPFGKHQQLFRNAAEVYDFLLRLIERFSENRKPQSPRHFIDAYLDEMDQNKNDPESTFSMENLIFSVGELIIAG 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 257 TETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRG 336
Cdd:cd20661   251 TETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSKDAVVRG 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 337 YSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHL 416
Cdd:cd20661   331 YSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHL 410
                         410       420
                  ....*....|....*....|....*.
gi 1034571959 417 HFPHELVPDLKPRLGMTLQPQPYLIC 442
Cdd:cd20661   411 HFPHGLIPDLKPKLGMTLQPQPYLIC 436
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
21-441 0e+00

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: 646.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRyGRGWVDHRRLAVNSFRYFGYGQKSFE 100
Cdd:cd11026     4 VFTVYLGSKPVVVLCGYEAVKEALVDQAEEFSGRPPVPLFDRVTKGYGVVFSN-GERWKQLRRFSLTTLRNFGMGKRSIE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 101 SKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAFPWI 180
Cdd:cd11026    83 ERIQEEAKFLVEAFRKTKGKPFDPTFLLSNAVSNVICSIVFGSRFDYEDKEFLKLLDLINENLRLLSSPWGQLYNMFPPL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 181 GILPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENLIFSVGELIIAGTETT 260
Cdd:cd11026   163 LKHLPGPHQKLFRNVEEIKSFIRELVEEHRETLDPSSPRDFIDCFLLKMEKEKDNPNSEFHEENLVMTVLDLFFAGTETT 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 261 TNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIP 340
Cdd:cd11026   243 STTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPLGVPHAVTRDTKFRGYTIP 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 341 KGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFP- 419
Cdd:cd11026   323 KGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGKFKKNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSLSSPv 402
                         410       420
                  ....*....|....*....|...
gi 1034571959 420 HELVPDLKPRL-GMTLQPQPYLI 441
Cdd:cd11026   403 GPKDPDLTPRFsGFTNSPRPYQL 425
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
18-441 9.43e-154

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: 442.31  E-value: 9.43e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  18 FSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRyGRGWVDHRRLAVNSFRYFGYGQK 97
Cdd:cd20662     1 YGNIFSLQLGSISSVIVTGLPLIKEALVTQEQNFMNRPETPLRERIFNKNGLIFSS-GQTWKEQRRFALMTLRNFGLGKK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  98 SFESKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAF 177
Cdd:cd20662    80 SLEERIQEECRHLVEAIREEKGNPFNPHFKINNAVSNIICSVTFGERFEYHDEWFQELLRLLDETVYLEGSPMSQLYNAF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 178 PWI-GILPfGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMdQGKNDPSSTFSKENLIFSVGELIIAG 256
Cdd:cd20662   160 PWImKYLP-GSHQTVFSNWKKLKLFVSDMIDKHREDWNPDEPRDFIDAYLKEM-AKYPDPTTSFNEENLICSTLDLFFAG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 257 TETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRG 336
Cdd:cd20662   238 TETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRMGNIIPLNVPREVAVDTKLAG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 337 YSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDsSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHL 416
Cdd:cd20662   318 FHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFLE-NGQFKKREAFLPFSMGKRACLGEQLARSELFIFFTSLLQKFTF 396
                         410       420
                  ....*....|....*....|....*
gi 1034571959 417 HFPHELVPDLKPRLGMTLQPQPYLI 441
Cdd:cd20662   397 KPPPNEKLSLKFRMGITLSPVPHRI 421
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
18-441 4.59e-150

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: 433.43  E-value: 4.59e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  18 FSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRYGRGWVDHRRLAVNSFRYFGYGQK 97
Cdd:cd20666     1 YGNIFSLFIGSQLVVVLNDFESVREALVQKAEVFSDRPSVPLVTILTKGKGIVFAPYGPVWRQQRKFSHSTLRHFGLGKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  98 SFESKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAF 177
Cdd:cd20666    81 SLEPKIIEEFRYVKAEMLKHGGDPFNPFPIVNNAVSNVICSMSFGRRFDYQDVEFKTMLGLMSRGLEISVNSAAILVNIC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 178 PWIGILPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQ-GKNDPSSTFSKENLIFSVGELIIAG 256
Cdd:cd20666   161 PWLYYLPFGPFRELRQIEKDITAFLKKIIADHRETLDPANPRDFIDMYLLHIEEeQKNNAESSFNEDYLFYIIGDLFIAG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 257 TETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRG 336
Cdd:cd20666   241 TDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLSIPHMASENTVLQG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 337 YSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHL 416
Cdd:cd20666   321 YTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLIKKEAFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTF 400
                         410       420
                  ....*....|....*....|....*.
gi 1034571959 417 HFPHELV-PDLKPRLGMTLQPQPYLI 441
Cdd:cd20666   401 LLPPNAPkPSMEGRFGLTLAPCPFNI 426
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
21-439 2.08e-146

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: 423.83  E-value: 2.08e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRyGRGWVDHRRLAVNSFRYFGYGQKSFE 100
Cdd:cd20664     4 IFTVQMGTKKVVVLAGYKTVKEALVNHAEAFGGRPIIPIFEDFNKGYGILFSN-GENWKEMRRFTLTTLRDFGMGKKTSE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 101 SKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAFPWI 180
Cdd:cd20664    83 DKILEEIPYLIEVFEKHKGKPFETTLSMNVAVSNIIASIVLGHRFEYTDPTLLRMVDRINENMKLTGSPSVQLYNMFPWL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 181 GILPfGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENLIFSVGELIIAGTETT 260
Cdd:cd20664   163 GPFP-GDINKLLRNTKELNDFLMETFMKHLDVLEPNDQRGFIDAFLVKQQEEEESSDSFFHDDNLTCSVGNLFGAGTDTT 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 261 TNVLRWAILFMALYPNIQGQVQKEIDLIMGPNgKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIP 340
Cdd:cd20664   242 GTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSR-QPQVEHRKNMPYTDAVIHEIQRFANIVPMNLPHATTRDVTFRGYFIP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 341 KGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFPH 420
Cdd:cd20664   321 KGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLDSQGKFVKRDAFMPFSAGRRVCIGETLAKMELFLFFTSLLQRFRFQPPP 400
                         410       420
                  ....*....|....*....|..
gi 1034571959 421 ---ELVPDLKPRLGMTLQPQPY 439
Cdd:cd20664   401 gvsEDDLDLTPGLGFTLNPLPH 422
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
18-439 1.58e-144

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


Pssm-ID: 410756 [Multi-domain]  Cd Length: 428  Bit Score: 419.10  E-value: 1.58e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  18 FSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKM---TKMGGLLNSRYGRGWVDHRRLAVNSFRYFGY 94
Cdd:cd20663     1 FGDVFSLQMAWKPVVVLNGLKAVREALVTCGEDTADRPPVPIFEHLgfgPKSQGVVLARYGPAWREQRRFSVSTLRNFGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  95 GQKSFESKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLY 174
Cdd:cd20663    81 GKKSLEQWVTEEAGHLCAAFTDQAGRPFNPNTLLNKAVCNVIASLIFARRFEYEDPRFIRLLKLLEESLKEESGFLPEVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 175 NAFPWIGILPfGKHQQLFRNAAVVYDFLSRLIEKASVNRKP-QLPQHFVDAYLDEMDQGKNDPSSTFSKENLIFSVGELI 253
Cdd:cd20663   161 NAFPVLLRIP-GLAGKVFPGQKAFLALLDELLTEHRTTWDPaQPPRDLTDAFLAEMEKAKGNPESSFNDENLRLVVADLF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 254 IAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAV 333
Cdd:cd20663   240 SAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQARMPYTNAVIHEVQRFGDIVPLGVPHMTSRDIE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 334 VRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQR 413
Cdd:cd20663   320 VQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQGHFVKPEAFMPFSAGRRACLGEPLARMELFLFFTCLLQR 399
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1034571959 414 FHLHfphelVPDLKPR------LGMTLQPQPY 439
Cdd:cd20663   400 FSFS-----VPAGQPRpsdhgvFAFLVSPSPY 426
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
20-441 1.16e-140

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: 409.29  E-value: 1.16e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  20 KIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMG-GLLNSRYGRGWVDHRRLAVNSFRYFGYGQKS 98
Cdd:cd11027     3 DVFSLYLGSRLVVVLNSGAAIKEALVKKSADFAGRPKLFTFDLFSRGGkDIAFGDYSPTWKLHRKLAHSALRLYASGGPR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  99 FESKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFlyNAFP 178
Cdd:cd11027    83 LEEKIAEEAEKLLKRLASQEGQPFDPKDELFLAVLNVICSITFGKRYKLDDPEFLRLLDLNDKFFELLGAGSLL--DIFP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 179 WIGILPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKN---DPSSTFSKENLIFSVGELIIA 255
Cdd:cd11027   161 FLKYFPNKALRELKELMKERDEILRKKLEEHKETFDPGNIRDLTDALIKAKKEAEDegdEDSGLLTDDHLVMTISDIFGA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 256 GTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVR 335
Cdd:cd11027   241 GTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVPLALPHKTTCDTTLR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 336 GYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKK-EALVPFSLGRRHCLGEHLARMEMFLFFTALLQRF 414
Cdd:cd11027   321 GYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENGKLVPKpESFLPFSAGRRVCLGESLAKAELFLFLARLLQKF 400
                         410       420
                  ....*....|....*....|....*...
gi 1034571959 415 HLHFPH-ELVPDLKPRLGMTLQPQPYLI 441
Cdd:cd11027   401 RFSPPEgEPPPELEGIPGLVLYPLPYKV 428
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
20-441 4.47e-131

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: 384.64  E-value: 4.47e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  20 KIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRYGRgWVDHRRLAVNSFRYFGYgQKSF 99
Cdd:cd20617     2 GIFTLWLGDVPTVVLSDPEIIKEAFVKNGDNFSDRPLLPSFEIISGGKGILFSNGDY-WKELRRFALSSLTKTKL-KKKM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 100 ESKILEETKFFNDAIETY--KGRPFDFKQLITNAVSNITNLIIFGERF-TYEDTDFQHMIELFSENVELAASASVFLYna 176
Cdd:cd20617    80 EELIEEEVNKLIESLKKHskSGEPFDPRPYFKKFVLNIINQFLFGKRFpDEDDGEFLKLVKPIEEIFKELGSGNPSDF-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 177 FPWIGILPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDqgKNDPSSTFSKENLIFSVGELIIAG 256
Cdd:cd20617   158 IPILLPFYFLYLKKLKKSYDKIKDFIEKIIEEHLKTIDPNNPRDLIDDELLLLL--KEGDSGLFDDDSIISTCLDLFLAG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 257 TETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRG 336
Cdd:cd20617   236 TDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGLPRVTTEDTEIGG 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 337 YSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYfAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHL 416
Cdd:cd20617   316 YFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDGN-KLSEQFIPFGIGKRNCVGENLARDELFLFFANLLLNFKF 394
                         410       420
                  ....*....|....*....|....*
gi 1034571959 417 HFPHELVPDLKPRLGMTLQPQPYLI 441
Cdd:cd20617   395 KSSDGLPIDEKEVFGLTLKPKPFKV 419
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
21-416 3.49e-129

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


Pssm-ID: 410758 [Multi-domain]  Cd Length: 425  Bit Score: 380.07  E-value: 3.49e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRyGRGWVDHRRLAVNSFRYFGYGQKSFE 100
Cdd:cd20665     4 VFTLYLGMKPTVVLHGYEAVKEALIDLGEEFSGRGRFPIFEKVNKGLGIVFSN-GERWKETRRFSLMTLRNFGMGKRSIE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 101 SKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAFP-W 179
Cdd:cd20665    83 DRVQEEARCLVEELRKTNGSPCDPTFILGCAPCNVICSIIFQNRFDYKDQDFLNLMEKLNENFKILSSPWLQVCNNFPaL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 180 IGILPfGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENLIFSVGELIIAGTET 259
Cdd:cd20665   163 LDYLP-GSHNKLLKNVAYIKSYILEKVKEHQESLDVNNPRDFIDCFLIKMEQEKHNQQSEFTLENLAVTVTDLFGAGTET 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 260 TTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSI 339
Cdd:cd20665   242 TSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRSPCMQDRSHMPYTDAVIHEIQRYIDLVPNNLPHAVTCDTKFRNYLI 321
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034571959 340 PKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHL 416
Cdd:cd20665   322 PKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDENGNFKKSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNL 398
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
18-442 1.61e-124

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: 369.30  E-value: 1.61e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  18 FSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLF---MKMTKMGGLLNSRYGRgWVDHRRLAVNSFRYFGy 94
Cdd:pfam00067  33 YGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFatsRGPFLGKGIVFANGPR-WRQLRRFLTPTFTSFG- 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  95 gQKSFESKILEETKFFNDAIETYKGRP--FDFKQLITNAVSNITNLIIFGERF-TYEDTDFQHMIELFSENVELAASASV 171
Cdd:pfam00067 111 -KLSFEPRVEEEARDLVEKLRKTAGEPgvIDITDLLFRAALNVICSILFGERFgSLEDPKFLELVKAVQELSSLLSSPSP 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 172 FLYNAFPWIGILPfGKHQQLFRNAAVVY-DFLSRLIE--KASVNRKPQLPQHFVDAYLDEMDqgkNDPSSTFSKENLIFS 248
Cdd:pfam00067 190 QLLDLFPILKYFP-GPHGRKLKRARKKIkDLLDKLIEerRETLDSAKKSPRDFLDALLLAKE---EEDGSKLTDEELRAT 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 249 VGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHAT 328
Cdd:pfam00067 266 VLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKETLRLHPVVPLLLPREV 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 329 SEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFT 408
Cdd:pfam00067 346 TKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLA 425
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1034571959 409 ALLQRFHLHFPHEL-VPDLKPRLGMTLQPQPYLIC 442
Cdd:pfam00067 426 TLLQNFEVELPPGTdPPDIDETPGLLLPPKPYKLK 460
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
18-439 3.45e-124

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: 367.16  E-value: 3.45e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  18 FSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRyGRGWVDHRRLAVNSFRYFGYGQK 97
Cdd:cd20669     1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRGDYPVFFNFTKGNGIAFSN-GERWKILRRFALQTLRNFGMGKR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  98 SFESKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAF 177
Cdd:cd20669    80 SIEERILEEAQFLLEELRKTKGAPFDPTFLLSRAVSNIICSVVFGSRFDYDDKRLLTILNLINDNFQIMSSPWGELYNIF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 178 PWIGILPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENLIFSVGELIIAGT 257
Cdd:cd20669   160 PSVMDWLPGPHQRIFQNFEKLRDFIAESVREHQESLDPNSPRDFIDCFLTKMAEEKQDPLSHFNMETLVMTTHNLLFGGT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 258 ETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGY 337
Cdd:cd20669   240 ETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFADIIPMSLPHAVTRDTNFRGF 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 338 SIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLH 417
Cdd:cd20669   320 LIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQ 399
                         410       420
                  ....*....|....*....|....*.
gi 1034571959 418 ---FPHELvpDLKPRL-GMTLQPQPY 439
Cdd:cd20669   400 plgAPEDI--DLTPLSsGLGNVPRPF 423
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
19-439 9.80e-124

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: 366.16  E-value: 9.80e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  19 SKIFSLDLGGISTVVLNGYDVVKEclVHQSEIFADRPCLPlFMKMTKMG---GLLNSRyGRGWVDHRRLAVNSFRYFGYG 95
Cdd:cd20651     1 GDVVGLKLGKDKVVVVSGYEAVRE--VLSREEFDGRPDGF-FFRLRTFGkrlGITFTD-GPFWKEQRRFVLRHLRDFGFG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  96 QKSFESKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLyN 175
Cdd:cd20651    77 RRSMEEVIQEEAEELIDLLKKGEKGPIQMPDLFNVSVLNVLWAMVAGERYSLEDQKLRKLLELVHLLFRNFDMSGGLL-N 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 176 AFPWIG-ILP-FGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQgKNDPSSTFSKENLIFSVGELI 253
Cdd:cd20651   156 QFPWLRfIAPeFSGYNLLVELNQKLIEFLKEEIKEHKKTYDEDNPRDLIDAYLREMKK-KEPPSSSFTDDQLVMICLDLF 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 254 IAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAV 333
Cdd:cd20651   235 IAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLRIFTLVPIGIPHRALKDTT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 334 VRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQR 413
Cdd:cd20651   315 LGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKLLKDEWFLPFGAGKRRCLGESLARNELFLFFTGLLQN 394
                         410       420
                  ....*....|....*....|....*..
gi 1034571959 414 FHLHFPHELVPDLKPRL-GMTLQPQPY 439
Cdd:cd20651   395 FTFSPPNGSLPDLEGIPgGITLSPKPF 421
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
18-440 2.74e-118

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: 352.18  E-value: 2.74e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  18 FSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRyGRGWVDHRRLAVNSFRYFGYGQK 97
Cdd:cd20671     1 YGPVFTIHLGMQKTVVLTGYEAVKEALVGTGDEFADRPPIPIFQAIQHGNGVFFSS-GERWRTTRRFTVRSMKSLGMGKR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  98 SFESKILEETKFFNDAIETYKGRPFDFKQLITnAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAF 177
Cdd:cd20671    80 TIEDKILEELQFLNGQIDSFNGKPFPLRLLGW-APTNITFAMLFGRRFDYKDPTFVSLLDLIDEVMVLLGSPGLQLFNLY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 178 PWIGILpFGKHQQLFRNAAVVYDFLSRLIEKasvnRKPQLPQHFVDAYLDEM--DQGKNDPSST-FSKENLIFSVGELII 254
Cdd:cd20671   159 PVLGAF-LKLHKPILDKVEEVCMILRTLIEA----RRPTIDGNPLHSYIEALiqKQEEDDPKETlFHDANVLACTLDLVM 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 255 AGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPlGIFHATSEDAVV 334
Cdd:cd20671   234 AGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLP-HVPRCTAADTQF 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 335 RGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRF 414
Cdd:cd20671   313 KGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFLDAEGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKF 392
                         410       420
                  ....*....|....*....|....*....
gi 1034571959 415 HLHFPHELVP---DLKPRLGMTLQPQPYL 440
Cdd:cd20671   393 TFLPPPGVSPadlDATPAAAFTMRPQPQL 421
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
21-441 1.02e-111

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: 335.27  E-value: 1.02e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRyGRGWVDHRRLAVNSFRYFGYGQKSFE 100
Cdd:cd20667     4 IYTLWLGSTPIVVLSGFKAVKEGLVSHSEEFSGRPLTPFFRDLFGEKGIICTN-GLTWKQQRRFCMTTLRELGLGKQALE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 101 SKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAFPWI 180
Cdd:cd20667    83 SQIQHEAAELVKVFAQENGRPFDPQDPIVHATANVIGAVVFGHRFSSEDPIFLELIRAINLGLAFASTIWGRLYDAFPWL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 181 GILPFGKHQQLFRNAAVVYDFLSRLIeKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENLIFSVGELIIAGTETT 260
Cdd:cd20667   163 MRYLPGPHQKIFAYHDAVRSFIKKEV-IRHELRTNEAPQDFIDCYLAQITKTKDDPVSTFSEENMIQVVIDLFLGGTETT 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 261 TNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIP 340
Cdd:cd20667   242 ATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVSVGAVRQCVTSTTMHGYYVE 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 341 KGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFPh 420
Cdd:cd20667   322 KGTIILPNLASVLYDPECWETPHKFNPGHFLDKDGNFVMNEAFLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFQLP- 400
                         410       420
                  ....*....|....*....|...
gi 1034571959 421 ELVPDLKPR--LGMTLQPQPYLI 441
Cdd:cd20667   401 EGVQELNLEyvFGGTLQPQPYKI 423
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
18-430 3.70e-108

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: 326.50  E-value: 3.70e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  18 FSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRyGRGWVDHRRLAVNSFRYFGYGQK 97
Cdd:cd20670     1 YGPVFTVYMGPRPVVVLCGHEAVKEALVDQADEFSGRGELATIERNFQGHGVALAN-GERWRILRRFSLTILRNFGMGKR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  98 SFESKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAF 177
Cdd:cd20670    80 SIEERIQEEAGYLLEEFRKTKGAPIDPTFFLSRTVSNVISSVVFGSRFDYEDKQFLSLLRMINESFIEMSTPWAQLYDMY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 178 PwiGILPF--GKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENLIFSVGELIIA 255
Cdd:cd20670   160 S--GIMQYlpGRHNRIYYLIEELKDFIASRVKINEASLDPQNPRDFIDCFLIKMHQDKNNPHTEFNLKNLVLTTLNLFFA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 256 GTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVR 335
Cdd:cd20670   238 GTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQRLTDIVPLGVPHNVIRDTQFR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 336 GYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFH 415
Cdd:cd20670   318 GYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQGRFKKNEAFVPFSSGKRVCLGEAMARMELFLYFTSILQNFS 397
                         410
                  ....*....|....*....
gi 1034571959 416 lhfPHELVP----DLKPRL 430
Cdd:cd20670   398 ---LRSLVPpadiDITPKI 413
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
21-441 4.76e-108

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: 325.96  E-value: 4.76e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRyGRGWVDHRRLAVNSFRYFGYGQKSFE 100
Cdd:cd20672     4 VFTVHLGPRPVVMLCGTDAIREALVDQAEAFSGRGTIAVVDPIFQGYGVIFAN-GERWKTLRRFSLATMRDFGMGKRSVE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 101 SKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAFPwi 180
Cdd:cd20672    83 ERIQEEAQCLVEELRKSKGALLDPTFLFQSITANIICSIVFGERFDYKDPQFLRLLDLFYQTFSLISSFSSQVFELFS-- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 181 GILPF--GKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENLIFSVGELIIAGTE 258
Cdd:cd20672   161 GFLKYfpGAHRQIYKNLQEILDYIGHSVEKHRATLDPSAPRDFIDTYLLRMEKEKSNHHTEFHHQNLMISVLSLFFAGTE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 259 TTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYS 338
Cdd:cd20672   241 TTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPIGVPHRVTKDTLFRGYL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 339 IPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHF 418
Cdd:cd20672   321 LPKNTEVYPILSSALHDPQYFEQPDTFNPDHFLDANGALKKSEAFMPFSTGKRICLGEGIARNELFLFFTTILQNFSVAS 400
                         410       420
                  ....*....|....*....|....*..
gi 1034571959 419 PheLVP---DLKPR-LGMTLQPQPYLI 441
Cdd:cd20672   401 P--VAPediDLTPKeSGVGKIPPTYQI 425
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
18-439 1.69e-107

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: 324.44  E-value: 1.69e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  18 FSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRYGRGwVDHRRLAVNSFRYFGYGQK 97
Cdd:cd20668     1 YGPVFTIHLGPRRVVVLCGYDAVKEALVDQAEEFSGRGEQATFDWLFKGYGVAFSNGERA-KQLRRFSIATLRDFGVGKR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  98 SFESKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAF 177
Cdd:cd20668    80 GIEERIQEEAGFLIDALRGTGGAPIDPTFYLSRTVSNVISSIVFGDRFDYEDKEFLSLLRMMLGSFQFTATSTGQLYEMF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 178 PWI-GILPfGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENLIFSVGELIIAG 256
Cdd:cd20668   160 SSVmKHLP-GPQQQAFKELQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEKKNPNTEFYMKNLVMTTLNLFFAG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 257 TETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRG 336
Cdd:cd20668   239 TETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMGLARRVTKDTKFRD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 337 YSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHL 416
Cdd:cd20668   319 FFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDDKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRF 398
                         410       420
                  ....*....|....*....|....*
gi 1034571959 417 HFPHELVP-DLKPR-LGMTLQPQPY 439
Cdd:cd20668   399 KSPQSPEDiDVSPKhVGFATIPRNY 423
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
21-439 4.22e-103

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: 313.47  E-value: 4.22e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRYGRGWVDHRRLAVNSFRYFGYGQKS-- 98
Cdd:cd11028     4 VFQIRMGSRPVVVLNGLETIKQALVRQGEDFAGRPDFYSFQFISNGKSMAFSDYGPRWKLHRKLAQNALRTFSNARTHnp 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  99 FESKILEETKFfndAIETY-----KGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASvfL 173
Cdd:cd11028    84 LEEHVTEEAEE---LVTELtenngKPGPFDPRNEIYLSVGNVICAICFGKRYSRDDPEFLELVKSNDDFGAFVGAGN--P 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 174 YNAFPWIGILPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYL---DEMDQGKNdPSSTFSKENLIFSVG 250
Cdd:cd11028   159 VDVMPWLRYLTRRKLQKFKELLNRLNSFILKKVKEHLDTYDKGHIRDITDALIkasEEKPEEEK-PEVGLTDEHIISTVQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 251 ELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSE 330
Cdd:cd11028   238 DLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFILETMRHSSFVPFTIPHATTR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 331 DAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYF--AKKEALVPFSLGRRHCLGEHLARMEMFLFFT 408
Cdd:cd11028   318 DTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFLDDNGLLdkTKVDKFLPFGAGRRRCLGEELARMELFLFFA 397
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1034571959 409 ALLQRFHLHFPHELVPDLKPRLGMTLQPQPY 439
Cdd:cd11028   398 TLLQQCEFSVKPGEKLDLTPIYGLTMKPKPF 428
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
20-441 8.02e-99

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: 302.41  E-value: 8.02e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  20 KIFSLDLGGISTVVLNGYDVVKECLvhQSEIFADRPclPLFMKMTKMGG-LLNSRYGRGWVDHRRLAVNSFR-----YFG 93
Cdd:cd20652     2 SIFSLKMGSVYTVVLSDPKLIRDTF--RRDEFTGRA--PLYLTHGIMGGnGIICAEGDLWRDQRRFVHDWLRqfgmtKFG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  94 YGQKSFESKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFl 173
Cdd:cd20652    78 NGRAKMEKRIATGVHELIKHLKAESGQPVDPSPVLMHSLGNVINDLVFGFRYKEDDPTWRWLRFLQEEGTKLIGVAGPV- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 174 yNAFPWIGILPFGKHQQ--LFRNAAVVYDFLSRLIEKASVNRKPQLP-------QHFVDAYLDEMDQGKNDpSSTFSKEN 244
Cdd:cd20652   157 -NFLPFLRHLPSYKKAIefLVQGQAKTHAIYQKIIDEHKRRLKPENPrdaedfeLCELEKAKKEGEDRDLF-DGFYTDEQ 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 245 LIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGI 324
Cdd:cd20652   235 LHHLLADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSVVPLGI 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 325 FHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMF 404
Cdd:cd20652   315 PHGCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKYLKPEAFIPFQTGKRMCLGDELARMILF 394
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1034571959 405 LFFTALLQRFHLHFPHEL-VPDLKPRLGMTLQPQPYLI 441
Cdd:cd20652   395 LFTARILRKFRIALPDGQpVDSEGGNVGITLTPPPFKI 432
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
21-439 3.10e-95

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: 293.46  E-value: 3.10e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPclplfmKMTKMGGLlnSRYGRG---------WVDHRRLAVNSFRY 91
Cdd:cd20673     4 IYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGRP------RMVTTDLL--SRNGKDiafadysatWQLHRKLVHSAFAL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  92 FGYGQKSFESKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIElFSEN-VELAASAS 170
Cdd:cd20673    76 FGEGSQKLEKIICQEASSLCDTLATHNGESIDLSPPLFRAVTNVICLLCFNSSYKNGDPELETILN-YNEGiVDTVAKDS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 171 vfLYNAFPWIGILPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYL------DEMDQGKNDPSSTFSKEN 244
Cdd:cd20673   155 --LVDIFPWLQIFPNKDLEKLKQCVKIRDKLLQKKLEEHKEKFSSDSIRDLLDALLqakmnaENNNAGPDQDSVGLSDDH 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 245 LIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGI 324
Cdd:cd20673   233 ILMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIREVLRIRPVAPLLI 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 325 FHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEAL--VPFSLGRRHCLGEHLARME 402
Cdd:cd20673   313 PHVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLDPTGSQLISPSLsyLPFGAGPRVCLGEALARQE 392
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1034571959 403 MFLFFTALLQRFHLHFPHEL-VPDLKPRLGMTLQPQPY 439
Cdd:cd20673   393 LFLFMAWLLQRFDLEVPDGGqLPSLEGKFGVVLQIDPF 430
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
18-439 3.83e-87

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: 272.14  E-value: 3.83e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  18 FSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLF-MKMTKMGGLLNSRYGRGWVDHRRLAVNSFRyfGYGQ 96
Cdd:cd11065     1 YGPIISLKVGGQTIIVLNSPKAAKDLLEKRSAIYSSRPRMPMAgELMGWGMRLLLMPYGPRWRLHRRLFHQLLN--PSAV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  97 KSFESKILEETK-FFNDAIETykgrPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYN 175
Cdd:cd11065    79 RKYRPLQELESKqLLRDLLES----PDDFLDHIRRYAASIILRLAYGYRVPSYDDPLLRDAEEAMEGFSEAGSPGAYLVD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 176 AFPWIGILP--FG-----KHQQLFRNAAVVYDFLSRLIEKASVNRKPqlPQHFVDAYLDEMDQGkndpsSTFSKENLIFS 248
Cdd:cd11065   155 FFPFLRYLPswLGapwkrKARELRELTRRLYEGPFEAAKERMASGTA--TPSFVKDLLEELDKE-----GGLSEEEIKYL 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 249 VGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHAT 328
Cdd:cd11065   228 AGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPLGIPHAL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 329 SEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSG--YFAKKEALVPFSLGRRHCLGEHLARMEMFLF 406
Cdd:cd11065   308 TEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDPKgtPDPPDPPHFAFGFGRRICPGRHLAENSLFIA 387
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1034571959 407 FTALLQRFHLHFP-----HELVPDLKPRLGMTLQPQPY 439
Cdd:cd11065   388 IARLLWAFDIKKPkdeggKEIPDEPEFTDGLVSHPLPF 425
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
21-441 1.35e-86

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: 271.20  E-value: 1.35e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRP---CLPLFMKMTKMGglLNSRYGRGWVDHRRLAVNSFRYFGY--G 95
Cdd:cd20677     4 VFQIKLGMLPVVVVSGLETIKQVLLKQGESFAGRPdfyTFSLIANGKSMT--FSEKYGESWKLHKKIAKNALRTFSKeeA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  96 QKSFESKILEE------TKFFNDAIE-TYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELfseNVEL-AA 167
Cdd:cd20677    82 KSSTCSCLLEEhvcaeaSELVKTLVElSKEKGSFDPVSLITCAVANVVCALCFGKRYDHSDKEFLTIVEI---NNDLlKA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 168 SASVFLYNAFPWIGILPFG--KHQQLFRNAavVYDFLSRLIEKASVNRKPQLPQHFVDAyLDEMDQGKN--DPSSTFSKE 243
Cdd:cd20677   159 SGAGNLADFIPILRYLPSPslKALRKFISR--LNNFIAKSVQDHYATYDKNHIRDITDA-LIALCQERKaeDKSAVLSDE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 244 NLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLG 323
Cdd:cd20677   236 QIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFINEVFRHSSFVPFT 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 324 IFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKK--EALVPFSLGRRHCLGEHLARM 401
Cdd:cd20677   316 IPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQLNKSlvEKVLIFGMGVRKCLGEDVARN 395
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1034571959 402 EMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQPQPYLI 441
Cdd:cd20677   396 EIFVFLTTILQQLKLEKPPGQKLDLTPVYGLTMKPKPYRL 435
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
21-441 2.16e-81

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: 257.62  E-value: 2.16e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRYGRGWVDHRRLAVNSFRYFGYG----Q 96
Cdd:cd20675     4 VFQIRLGSRPVVVLNGERAIRQALVQQGTDFAGRPDFASFRVVSGGRSLAFGGYSERWKAHRRVAHSTVRAFSTRnprtR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  97 KSFESKILEETK-----FFNdaiETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMI---ELFSENVElAAS 168
Cdd:cd20675    84 KAFERHVLGEARelvalFLR---KSAGGAYFDPAPPLVVAVANVMSAVCFGKRYSHDDAEFRSLLgrnDQFGRTVG-AGS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 169 asvfLYNAFPWIGILP------FGKHQQLFRNaavVYDFLSrliEKASVNR---KPQLPQHFVDAYLDEMDQGKNDPS-S 238
Cdd:cd20675   160 ----LVDVMPWLQYFPnpvrtvFRNFKQLNRE---FYNFVL---DKVLQHRetlRGGAPRDMMDAFILALEKGKSGDSgV 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 239 TFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCN 318
Cdd:cd20675   230 GLDKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCIEDQPNLPYVMAFLYEAMRFSS 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 319 IVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEA--LVPFSLGRRHCLGE 396
Cdd:cd20675   310 FVPVTIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDENGFLNKDLAssVMIFSVGKRRCIGE 389
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1034571959 397 HLARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQPQPYLI 441
Cdd:cd20675   390 ELSKMQLFLFTSILAHQCNFTANPNEPLTMDFSYGLTLKPKPFTI 434
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
18-442 3.75e-80

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: 254.26  E-value: 3.75e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  18 FSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFmKMTKMGG--LLNSRYGRGWVDHRRLA----VNSFRy 91
Cdd:cd20674     1 YGPIYRLRLGLQDVVVLNSKRTIREALVRKWADFAGRPHSYTG-KLVSQGGqdLSLGDYSLLWKAHRKLTrsalQLGIR- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  92 fgygqKSFESKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTyEDTDFQHMIELFSENVELAASASV 171
Cdd:cd20674    79 -----NSLEPVVEQLTQELCERMRAQAGTPVDIQEEFSLLTCSIICCLTFGDKED-KDTLVQAFHDCVQELLKTWGHWSI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 172 FLYNAFPWIGILPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKND-PSSTFSKENLIFSVG 250
Cdd:cd20674   153 QALDSIPFLRFFPNPGLRRLKQAVENRDHIVESQLRQHKESLVAGQWRDMTDYMLQGLGQPRGEkGMGQLLEGHVHMAVV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 251 ELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSE 330
Cdd:cd20674   233 DLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRPVVPLALPHRTTR 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 331 DAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSgyfAKKEALVPFSLGRRHCLGEHLARMEMFLFFTAL 410
Cdd:cd20674   313 DSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEPG---AANRALLPFGCGARVCLGEPLARLELFVFLARL 389
                         410       420       430
                  ....*....|....*....|....*....|...
gi 1034571959 411 LQRFHLHFPH-ELVPDLKPRLGMTLQPQPYLIC 442
Cdd:cd20674   390 LQAFTLLPPSdGALPSLQPVAGINLKVQPFQVR 422
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
21-436 2.26e-69

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: 226.43  E-value: 2.26e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGL-LNSRYGRGWVDHRRLAVNSFRYFGY--GQK 97
Cdd:cd20676     4 VLQIQIGSRPVVVLSGLDTIRQALVKQGDDFKGRPDLYSFRFISDGQSLtFSTDSGPVWRARRKLAQNALKTFSIasSPT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  98 SFESKILEE---------TKFFNDAIETyKGRpFD-FKQLITnAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAA 167
Cdd:cd20676    84 SSSSCLLEEhvskeaeylVSKLQELMAE-KGS-FDpYRYIVV-SVANVICAMCFGKRYSHDDQELLSLVNLSDEFGEVAG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 168 SASvfLYNAFPWIGILPfGKHQQLFRNA-AVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSST--FSKEN 244
Cdd:cd20676   161 SGN--PADFIPILRYLP-NPAMKRFKDInKRFNSFLQKIVKEHYQTFDKDNIRDITDSLIEHCQDKKLDENANiqLSDEK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 245 LIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGI 324
Cdd:cd20676   238 IVNIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILETFRHSSFVPFTI 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 325 FHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKK---EALVPFSLGRRHCLGEHLARM 401
Cdd:cd20676   318 PHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLTADGTEINKtesEKVMLFGLGKRRCIGESIARW 397
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1034571959 402 EMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQP 436
Cdd:cd20676   398 EVFLFLAILLQQLEFSVPPGVKVDMTPEYGLTMKH 432
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
21-436 3.97e-64

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: 211.60  E-value: 3.97e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRYGRgWVDHRRLAVNSFRyfGYGQKSFE 100
Cdd:cd00302     3 VFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLTLDGPE-HRRLRRLLAPAFT--PRALAALR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 101 SKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFsenvelaasasvFLYNAFPWI 180
Cdd:cd00302    80 PVIREIARELLDRLAAGGEVGDDVADLAQPLALDVIARLLGGPDLGEDLEELAELLEAL------------LKLLGPRLL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 181 GILPFGKHQQLFRNAAVVYDFLSRLIEKasvnRKPQLPQHFVDAYLDEMDQGkndpsSTFSKENLIFSVGELIIAGTETT 260
Cdd:cd00302   148 RPLPSPRLRRLRRARARLRDYLEELIAR----RRAEPADDLDLLLLADADDG-----GGLSDEEIVAELLTLLLAGHETT 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 261 TNVLRWAILFMALYPNIQGQVQKEIDLIMGpngKPSWDDKCKMPYTEAVLHEVLRFCNIVPlGIFHATSEDAVVRGYSIP 340
Cdd:cd00302   219 ASLLAWALYLLARHPEVQERLRAEIDAVLG---DGTPEDLSKLPYLEAVVEETLRLYPPVP-LLPRVATEDVELGGYTIP 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 341 KGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGyfAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFPH 420
Cdd:cd00302   295 AGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPERE--EPRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFELVP 372
                         410
                  ....*....|....*.
gi 1034571959 421 ELVPDLKPRLGmTLQP 436
Cdd:cd00302   373 DEELEWRPSLG-TLGP 387
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
21-436 2.80e-61

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: 205.10  E-value: 2.80e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMG-GLLNSRYGRGWVDHRRLA---------VNSFR 90
Cdd:cd20618     3 LMYLRLGSVPTVVVSSPEMAKEVLKTQDAVFASRPRTAAGKIFSYNGqDIVFAPYGPHWRHLRKICtlelfsakrLESFQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  91 YFgygqKSFE-----SKILEETKffndaietyKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDF----QHMIELFSE 161
Cdd:cd20618    83 GV----RKEElshlvKSLLEESE---------SGKPVNLREHLSDLTLNNITRMLFGKRYFGESEKEseeaREFKELIDE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 162 NVELAASASVFLYnaFPWIGILPF-GKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQgkNDPSSTF 240
Cdd:cd20618   150 AFELAGAFNIGDY--IPWLRWLDLqGYEKRMKKLHAKLDRFLQKIIEEHREKRGESKKGGDDDDDLLLLLD--LDGEGKL 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 241 SKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIV 320
Cdd:cd20618   226 SDDNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPPG 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 321 PLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEA--LVPFSLGRRHCLGEHL 398
Cdd:cd20618   306 PLLLPHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIDDVKGQDfeLLPFGSGRRMCPGMPL 385
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1034571959 399 ArMEMFLFFTA-LLQRFHLHFPHEL--VPDLKPRLGMTLQP 436
Cdd:cd20618   386 G-LRMVQLTLAnLLHGFDWSLPGPKpeDIDMEEKFGLTVPR 425
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
21-438 4.79e-51

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: 177.39  E-value: 4.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPlFMKMTKMGGLLNSRyGRGWVDHRRLAVNSFRyfgyGQK--S 98
Cdd:cd20620     3 VVRLRLGPRRVYLVTHPDHIQHVLVTNARNYVKGGVYE-RLKLLLGNGLLTSE-GDLWRRQRRLAQPAFH----RRRiaA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  99 FESKILEETKFFNDAIETYKGR-PFDFKQLITNAVSNITNLIIFGERFtyeDTDFQHMIELFSENVELAASAsvfLYNAF 177
Cdd:cd20620    77 YADAMVEATAALLDRWEAGARRgPVDVHAEMMRLTLRIVAKTLFGTDV---EGEADEIGDALDVALEYAARR---MLSPF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 178 PWIGILPFGKHQQLFRNAAVVYDFLSRLIEK--ASVNRKPQLPQHFVDAYLDEMDQGkndpsstFSKENLIFSVGELIIA 255
Cdd:cd20620   151 LLPLWLPTPANRRFRRARRRLDEVIYRLIAErrAAPADGGDLLSMLLAARDEETGEP-------MSDQQLRDEVMTLFLA 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 256 GTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATsEDAVVR 335
Cdd:cd20620   224 GHETTANALSWTWYLLAQHPEVAARLRAEVDRVLG-GRPPTAEDLPQLPYTEMVLQESLRLYPPAWIIGREAV-EDDEIG 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 336 GYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFH 415
Cdd:cd20620   302 GYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREAARPRYAYFPFGGGPRICIGNHFAMMEAVLLLATIAQRFR 381
                         410       420
                  ....*....|....*....|....*
gi 1034571959 416 LhfphELVP--DLKPRLGMTLQPQP 438
Cdd:cd20620   382 L----RLVPgqPVEPEPLITLRPKN 402
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
138-436 1.38e-50

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: 176.95  E-value: 1.38e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 138 LIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAFPWIGILPFGKHQQLFRNAAVVYDFLSRLIEKA-----SVN 212
Cdd:cd11054   129 TVLFGKRLGCLDDNPDSDAQKLIEAVKDIFESSAKLMFGPPLWKYFPTPAWKKFVKAWDTIFDIASKYVDEAleelkKKD 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 213 RKPQLPQHFVDAYLDEmdqgkndpsSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPN 292
Cdd:cd11054   209 EEDEEEDSLLEYLLSK---------PGLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDG 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 293 GKPSWDDKCKMPYTEAVLHEVLRfcnIVPLGIFHA--TSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERF 370
Cdd:cd11054   280 EPITAEDLKKMPYLKACIKESLR---LYPVAPGNGriLPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERW 356
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034571959 371 LDSSGYFAKKE--ALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFPHElvpDLKPRLGMTLQP 436
Cdd:cd11054   357 LRDDSENKNIHpfASLPFGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEYHHE---ELKVKTRLILVP 421
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
21-399 1.74e-50

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: 176.50  E-value: 1.74e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTkmGGLLN---SRYGRGWVDHRRLA---------VNS 88
Cdd:cd11072     5 LMLLRLGSVPTVVVSSPEAAKEVLKTHDLVFASRPKLLAARILS--YGGKDiafAPYGEYWRQMRKICvlellsakrVQS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  89 FRYFgygqksFEskilEETKFFNDAIETY--KGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFqhMIELFSENVELA 166
Cdd:cd11072    83 FRSI------RE----EEVSLLVKKIRESasSSSPVNLSELLFSLTNDIVCRAAFGRKYEGKDQDK--FKELVKEALELL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 167 ASASVFLYnaFPWIGILPF--GKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKEN 244
Cdd:cd11072   151 GGFSVGDY--FPSLGWIDLltGLDRKLEKVFKELDAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRLQKEGDLEFPLTRDN 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 245 LIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGI 324
Cdd:cd11072   229 IKAIILDMFLAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPPAPLLL 308
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034571959 325 FHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFakK----EaLVPFSLGRRHCLGEHLA 399
Cdd:cd11072   309 PRECREDCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLDSSIDF--KgqdfE-LIPFGAGRRICPGITFG 384
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
21-435 9.96e-48

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: 169.25  E-value: 9.96e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPcLPLFMKMTKMGG--LLNSRYGRGWVDHRRLAVNSFryfgygqks 98
Cdd:cd11073     7 IMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRD-VPDAVRALGHHKssIVWPPYGPRWRMLRKICTTEL--------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  99 FESKILEET------------KFFNDAIEtyKGRPFDFKQLITNAVSNITNLIIFGER-FTYEDTDFQHMIELFSENVEL 165
Cdd:cd11073    77 FSPKRLDATqplrrrkvrelvRYVREKAG--SGEAVDIGRAAFLTSLNLISNTLFSVDlVDPDSESGSEFKELVREIMEL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 166 AASASVFLYnaFPWIGIL-PFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSStFSKEN 244
Cdd:cd11073   155 AGKPNVADF--FPFLKFLdLQGLRRRMAEHFGKLFDIFDGFIDERLAEREAGGDKKKDDDLLLLLDLELDSESE-LTRNH 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 245 LIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGI 324
Cdd:cd11073   232 IKALLLDLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLLL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 325 FHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSG-YFAKKEALVPFSLGRRHCLGEHLA-RMe 402
Cdd:cd11073   312 PRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIdFKGRDFELIPFGSGRRICPGLPLAeRM- 390
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1034571959 403 MFLFFTALLQRFHLHFPHELVP---DLKPRLGMTLQ 435
Cdd:cd11073   391 VHLVLASLLHSFDWKLPDGMKPedlDMEEKFGLTLQ 426
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
21-415 2.57e-45

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: 162.80  E-value: 2.57e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLP----LFMKMTKMggLLNSRYGRGWVDHRR------LAVNSFR 90
Cdd:cd11075     5 IFTLRMGSRPLIVVASRELAHEALVQKGSSFASRPPANplrvLFSSNKHM--VNSSPYGPLWRTLRRnlvsevLSPSRLK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  91 YFGYGQKSFESKILEetKFFNDAIEtyKGRPFDFKQLITNAVSNITNLIIFGERFTyEDT--DFQHMIELFsenveLAAS 168
Cdd:cd11075    83 QFRPARRRALDNLVE--RLREEAKE--NPGPVNVRDHFRHALFSLLLYMCFGERLD-EETvrELERVQREL-----LLSF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 169 ASVFLYNAFPWIGILPF----GKHQQLFRNAAVVYDFL--SRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNdpsSTFSK 242
Cdd:cd11075   153 TDFDVRDFFPALTWLLNrrrwKKVLELRRRQEEVLLPLirARRKRRASGEADKDYTDFLLLDLLDLKEEGGE---RKLTD 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 243 ENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPL 322
Cdd:cd11075   230 EELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRHPPGHF 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 323 GIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGY-----FAKKEALVPFSLGRRHCLGEH 397
Cdd:cd11075   310 LLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGGEAadidtGSKEIKMMPFGAGRRICPGLG 389
                         410
                  ....*....|....*...
gi 1034571959 398 LARMEMFLFFTALLQRFH 415
Cdd:cd11075   390 LATLHLELFVARLVQEFE 407
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
20-436 3.30e-45

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: 162.37  E-value: 3.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  20 KIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPclPLFMKMTKMGGLLNSRYGRGWVDHRRLAVNSFRyfgygqksf 99
Cdd:cd11055     4 KVFGLYFGTIPVIVVSDPEMIKEILVKEFSNFTNRP--LFILLDEPFDSSLLFLKGERWKRLRTTLSPTFS--------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 100 ESKILEETKFFNDAI---------ETYKGRPFDFKQLITNAVSNITNLIIFG----ERFTYEDTDFQHMIELFSENVELA 166
Cdd:cd11055    73 SGKLKLMVPIINDCCdelveklekAAETGKPVDMKDLFQGFTLDVILSTAFGidvdSQNNPDDPFLKAAKKIFRNSIIRL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 167 ASASVFLYNAFPWIGILPFGKHQQLFRnaaVVYDFLSRLIE---KASVNRKPQLPQHFVDAyldeMDQGKNDPSSTFSKE 243
Cdd:cd11055   153 FLLLLLFPLRLFLFLLFPFVFGFKSFS---FLEDVVKKIIEqrrKNKSSRRKDLLQLMLDA----QDSDEDVSKKKLTDD 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 244 N-----LIFsvgelIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCn 318
Cdd:cd11055   226 EivaqsFIF-----LLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKYLDMVINETLRLY- 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 319 ivPLGIFH--ATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGE 396
Cdd:cd11055   300 --PPAFFIsrECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKAKRHPYAYLPFGAGPRNCIGM 377
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1034571959 397 HLARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQP 436
Cdd:cd11055   378 RFALLEVKLALVKILQKFRFVPCKETEIPLKLVGGATLSP 417
PTZ00404 PTZ00404
cytochrome P450; Provisional
18-446 6.91e-45

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 162.97  E-value: 6.91e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  18 FSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSrYGRGWVDHRRLAVNSFRyfgygqK 97
Cdd:PTZ00404   61 YGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHGTFYHGIVTS-SGEYWKRNREIVGKAMR------K 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  98 SFESKILEE-TKFFNDAIETYK-----GRPFDFKQLITNAVSNITNLIIFGERFTYEDT----DFQHMIELFSENVELAA 167
Cdd:PTZ00404  134 TNLKHIYDLlDDQVDVLIESMKkiessGETFEPRYYLTKFTMSAMFKYIFNEDISFDEDihngKLAELMGPMEQVFKDLG 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 168 SASVF--------LYnaFPWIgiLPFGKHQQLFRNaavvydFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDpsst 239
Cdd:PTZ00404  214 SGSLFdvieitqpLY--YQYL--EHTDKNFKKIKK------FIKEKYHEHLKTIDPEVPRDLLDLLIKEYGTNTDD---- 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 240 fSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNI 319
Cdd:PTZ00404  280 -DILSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPV 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 320 VPLGIFHATSEDAVV-RGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSgyfaKKEALVPFSLGRRHCLGEHL 398
Cdd:PTZ00404  359 SPFGLPRSTSNDIIIgGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPD----SNDAFMPFSIGPRNCVGQQF 434
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1034571959 399 ARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQPQPYLICAERR 446
Cdd:PTZ00404  435 AQDELYLAFSNIILNFKLKSIDGKKIDETEEYGLTLKPNKFKVLLEKR 482
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
21-435 6.92e-45

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: 160.83  E-value: 6.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRYGRGWVDHRRLAVNSFRyfgyGQ--KS 98
Cdd:COG2124    34 VFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVLRPLPLLGDSLLTLDGPEHTRLRRLVQPAFT----PRrvAA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  99 FESKILEETkffNDAIETYKGR-PFDFkqliTNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASasvflynaf 177
Cdd:COG2124   110 LRPRIREIA---DELLDRLAARgPVDL----VEEFARPLPVIVICELLGVPEEDRDRLRRWSDALLDALGP--------- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 178 pwigiLPFGKHQQLFRNAAVVYDFLSRLIEKasvnRKPQLPQHFVDAYLDEMDQGkndpsSTFSKENLIFSVGELIIAGT 257
Cdd:COG2124   174 -----LPPERRRRARRARAELDAYLRELIAE----RRAEPGDDLLSALLAARDDG-----ERLSDEELRDELLLLLLAGH 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 258 ETTTNVLRWAILFMALYPNIQGQVQKEIdlimgpngkpswddkckmPYTEAVLHEVLRFCNIVPLGIFHATsEDAVVRGY 337
Cdd:COG2124   240 ETTANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEETLRLYPPVPLLPRTAT-EDVELGGV 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 338 SIPKGTTVITNLYSVHFDEKYWRDPEVFHPERfldssgyfaKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHlH 417
Cdd:COG2124   301 TIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR---------PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFP-D 370
                         410       420
                  ....*....|....*....|
gi 1034571959 418 FphELVPD--LKPRLGMTLQ 435
Cdd:COG2124   371 L--RLAPPeeLRWRPSLTLR 388
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
21-434 1.06e-44

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: 161.63  E-value: 1.06e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKM---TKMGGLlnSRYGRGWVDHRRLAVnsfryfgygQK 97
Cdd:cd20654     3 IFTLRLGSHPTLVVSSWEMAKECFTTNDKAFSSRPKTAAAKLMgynYAMFGF--APYGPYWRELRKIAT---------LE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  98 SFESKILEETK---------FFNDAIETYKGR-------PFDFKQLITNAVSNITNLIIFGERF-----TYEDTDFQHMI 156
Cdd:cd20654    72 LLSNRRLEKLKhvrvsevdtSIKELYSLWSNNkkggggvLVEMKQWFADLTFNVILRMVVGKRYfggtaVEDDEEAERYK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 157 ELFSENVELAAsasVF-LYNAFPWIGILPFGKH-QQLFRNAAVVYDFLSRLIE----KASVNRKPQLPQHFVDAYLDEMD 230
Cdd:cd20654   152 KAIREFMRLAG---TFvVSDAIPFLGWLDFGGHeKAMKRTAKELDSILEEWLEehrqKRSSSGKSKNDEDDDDVMMLSIL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 231 QGKndPSSTFSKENLIFS-VGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpngKPSW---DDKCKMPYT 306
Cdd:cd20654   229 EDS--QISGYDADTVIKAtCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVG---KDRWveeSDIKNLVYL 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 307 EAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSsgyfaKKEA---- 382
Cdd:cd20654   304 QAIVKETLRLYPPGPLLGPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLTT-----HKDIdvrg 378
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034571959 383 ----LVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTL 434
Cdd:cd20654   379 qnfeLIPFGSGRRSCPGVSFGLQVMHLTLARLLHGFDIKTPSNEPVDMTEGPGLTN 434
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
68-438 5.47e-43

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: 156.53  E-value: 5.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  68 GLLNSRyGRGWVDHRRLAVNSF--RYFgygqKSFESKILEETKFFNDAIETY-KGRPFDFKQLITNAVSNI-------TN 137
Cdd:cd20628    48 GLLTST-GEKWRKRRKLLTPAFhfKIL----ESFVEVFNENSKILVEKLKKKaGGGEFDIFPYISLCTLDIicetamgVK 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 138 LIIFGErftyEDTDFQHMIELFSENVeLAASASVFLYnaFPWIGILpFGKHQQLFRNAAVVYDFLSRLIE--KASVNRKP 215
Cdd:cd20628   123 LNAQSN----EDSEYVKAVKRILEII-LKRIFSPWLR--FDFIFRL-TSLGKEQRKALKVLHDFTNKVIKerREELKAEK 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 216 QLPQH-----------FVDAYLDEMDQGKndpssTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKE 284
Cdd:cd20628   195 RNSEEddefgkkkrkaFLDLLLEAHEDGG-----PLTDEDIREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEE 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 285 IDLIMGPNG-KPSWDDKCKMPYTEAVLHEVLRFCNIVPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPE 363
Cdd:cd20628   270 LDEIFGDDDrRPTLEDLNKMKYLERVIKETLRLYPSVPF-IGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPE 348
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034571959 364 VFHPERFLDSSgyFAKKE--ALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHfPHELVPDLKPRLGMTLQPQP 438
Cdd:cd20628   349 KFDPDRFLPEN--SAKRHpyAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFRVL-PVPPGEDLKLIAEIVLRSKN 422
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
97-421 2.10e-42

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: 154.69  E-value: 2.10e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  97 KSFESKILEETKFFNDAIETYKGRP----FDFKQLITNAVSNITNLIIFGERF-TYEDTDFQHMIELFSENVELAAsasV 171
Cdd:cd11061    71 RGYEPRILSHVEQLCEQLDDRAGKPvswpVDMSDWFNYLSFDVMGDLAFGKSFgMLESGKDRYILDLLEKSMVRLG---V 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 172 FLYnaFPWIgiLPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVD--AYLdeMDQGKNDPSSTFSKENLifsV 249
Cdd:cd11061   148 LGH--APWL--RPLLLDLPLFPGATKARKRFLDFVRAQLKERLKAEEEKRPDifSYL--LEAKDPETGEGLDLEEL---V 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 250 GE---LIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCK-MPYTEAVLHEVLRFCNIVPLGIF 325
Cdd:cd11061   219 GEarlLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDDEIRLGPKLKsLPYLRACIDEALRLSPPVPSGLP 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 326 HAT-SEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAK-KEALVPFSLGRRHCLGEHLARMEM 403
Cdd:cd11061   299 RETpPGGLTIDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRPEELVRaRSAFIPFSIGPRGCIGKNLAYMEL 378
                         330
                  ....*....|....*...
gi 1034571959 404 FLFFTALLQRFHLHFPHE 421
Cdd:cd11061   379 RLVLARLLHRYDFRLAPG 396
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
159-436 6.69e-41

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: 150.75  E-value: 6.69e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 159 FSENVELAASASVFLYNAfPWIGILPFG-KHQQLFRNAA-VVYDFLSRLIEK--ASVNRKPQLPQHFVDAYLDEMDQGKN 234
Cdd:cd20613   151 FPKAISLVLEGIQESFRN-PLLKYNPSKrKYRREVREAIkFLRETGRECIEErlEALKRGEEVPNDILTHILKASEEEPD 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 235 dpsstFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVL 314
Cdd:cd20613   230 -----FDMEELLDDFVTFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKQYVEYEDLGKLEYLSQVLKETL 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 315 RFCNIVPlGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCL 394
Cdd:cd20613   305 RLYPPVP-GTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEAPEKIPSYAYFPFSLGPRSCI 383
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1034571959 395 GEHLARMEMFLFFTALLQRFHLhfphELVPD--LKPRLGMTLQP 436
Cdd:cd20613   384 GQQFAQIEAKVILAKLLQNFKF----ELVPGqsFGILEEVTLRP 423
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
79-416 8.60e-41

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: 150.48  E-value: 8.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  79 VDH-----RRLAVNSFryfgYGQKS---FESKILEETKFFNDAIETYK--GRPFDfkqlITNAVSNITNLII----FGER 144
Cdd:cd11062    50 VDHdlhrlRRKALSPF----FSKRSilrLEPLIQEKVDKLVSRLREAKgtGEPVN----LDDAFRALTADVIteyaFGRS 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 145 FTY-EDTDFQ-HMIELFSENVELAASASvflynAFPWIG----ILPFGKHQQLFRNAAVVYDFL---SRLIEKASVNRKP 215
Cdd:cd11062   122 YGYlDEPDFGpEFLDALRALAEMIHLLR-----HFPWLLkllrSLPESLLKRLNPGLAVFLDFQesiAKQVDEVLRQVSA 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 216 QLPQHFVDAYLDEMDqGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIM-GPNGK 294
Cdd:cd11062   197 GDPPSIVTSLFHALL-NSDLPPSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKTAMpDPDSP 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 295 PSWDDKCKMPYTEAVLHEVLRFCNIVPlgifH-----ATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPER 369
Cdd:cd11062   276 PSLAELEKLPYLTAVIKEGLRLSYGVP----TrlprvVPDEGLYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPER 351
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1034571959 370 FLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHL 416
Cdd:cd11062   352 WLGAAEKGKLDRYLVPFSKGSRSCLGINLAYAELYLALAALFRRFDL 398
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
21-442 2.29e-40

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: 149.39  E-value: 2.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFA-DRPCLPLFMKMtKMGGLLnSRYGRGWVDHRRLAVNSFRYFGYgqKSF 99
Cdd:cd11083     3 AYRFRLGRQPVLVISDPELIREVLRRRPDEFRrISSLESVFREM-GINGVF-SAEGDAWRRQRRLVMPAFSPKHL--RYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 100 ESKILEETKFFNDAIETY--KGRPFDFKQLITNAVSNITNLIIFGERF-TYEDTDfqHMIelfSENVELaasasVF---- 172
Cdd:cd11083    79 FPTLRQITERLRERWERAaaEGEAVDVHKDLMRYTVDVTTSLAFGYDLnTLERGG--DPL---QEHLER-----VFpmln 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 173 --LYNAFPWIGILPFGKHQQLFRNAAVVYDFLSRLIEKASV--NRKPQLPQHFVDayLDEMDQGKNDPSSTFSKENLIFS 248
Cdd:cd11083   149 rrVNAPFPYWRYLRLPADRALDRALVEVRALVLDIIAAARArlAANPALAEAPET--LLAMMLAEDDPDARLTDDEIYAN 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 249 VGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEID-LIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLgIFHA 327
Cdd:cd11083   227 VLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDaVLGGARVPPLLEALDRLPYLEAVARETLRLKPVAPL-LFLE 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 328 TSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLD--SSGYFAKKEALVPFSLGRRHCLGEHLARMEMFL 405
Cdd:cd11083   306 PNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDgaRAAEPHDPSSLLPFGAGPRLCPGRSLALMEMKL 385
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1034571959 406 FFTALLQRFHLHFPhELVPDLKPRLGMTLQPQPYLIC 442
Cdd:cd11083   386 VFAMLCRNFDIELP-EPAPAVGEEFAFTMSPEGLRVR 421
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
21-414 8.00e-39

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: 145.06  E-value: 8.00e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLP----LFMKMTKMGGllnSRYGRGWVDHRRLAV----NSFRYf 92
Cdd:cd20653     3 IFSLRFGSRLVVVVSSPSAAEECFTKNDIVLANRPRFLtgkhIGYNYTTVGS---APYGDHWRNLRRITTleifSSHRL- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  93 gygqKSFESKILEETKF-----FNDAIEtyKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMI----ELFSENV 163
Cdd:cd20653    79 ----NSFSSIRRDEIRRllkrlARDSKG--GFAKVELKPLFSELTFNNIMRMVAGKRYYGEDVSDAEEAklfrELVSEIF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 164 ELAASASVFLYnaFP---WIGILPFGKHqqlFRNAAVVYD-FLSRLIEKaSVNRKPQLPQHFVDAYLDemdQGKNDPSsT 239
Cdd:cd20653   153 ELSGAGNPADF--LPilrWFDFQGLEKR---VKKLAKRRDaFLQGLIDE-HRKNKESGKNTMIDHLLS---LQESQPE-Y 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 240 FSKE---NLIFSvgeLIIAGTETTTNVLRWAilfMAL---YPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEV 313
Cdd:cd20653   223 YTDEiikGLILV---MLLAGTDTSAVTLEWA---MSNllnHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISET 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 314 LRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFlDSSGYFAKKeaLVPFSLGRRHC 393
Cdd:cd20653   297 LRLYPAAPLLVPHESSEDCKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERF-EGEEREGYK--LIPFGLGRRAC 373
                         410       420
                  ....*....|....*....|.
gi 1034571959 394 LGEHLARMEMFLFFTALLQRF 414
Cdd:cd20653   374 PGAGLAQRVVGLALGSLIQCF 394
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
53-441 8.37e-39

cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect cytochrome P450s from families 313 (CYP313) and 318 (CYP318), and similar proteins. These proteins may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. Their specific function is yet unknown. They belong to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410680 [Multi-domain]  Cd Length: 427  Bit Score: 145.05  E-value: 8.37e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  53 DRPCLPLFMKMTKmgGLLNSRYGRgWVDHRRlAVNSfryfgygqkSFESKIL--------EETKFFNDAIETYKGRP-FD 123
Cdd:cd11057    33 NKSFFYDFFRLGR--GLFSAPYPI-WKLQRK-ALNP---------SFNPKILlsflpifnEEAQKLVQRLDTYVGGGeFD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 124 FKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAA--SASVFLYNAfpWIGILpFGKHQQLFRNAAVVYDF 201
Cdd:cd11057   100 ILPDLSRCTLEMICQTTLGSDVNDESDGNEEYLESYERLFELIAkrVLNPWLHPE--FIYRL-TGDYKEEQKARKILRAF 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 202 LSRLIEKA----------------SVNRKPQLpqhFVDAYLDEMDQGKNdpsstFSKENLIFSVGELIIAGTETTTNVLR 265
Cdd:cd11057   177 SEKIIEKKlqevelesnldseedeENGRKPQI---FIDQLLELARNGEE-----FTDEEIMDEIDTMIFAGNDTSATTVA 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 266 WAILFMALYPNIQGQVQKEIDLIMGPNGKP-SWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTT 344
Cdd:cd11057   249 YTLLLLAMHPEVQEKVYEEIMEVFPDDGQFiTYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLSNGVVIPKGTT 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 345 VITNLYSVHFDEKYW-RDPEVFHPERFL--DSSG---YfakkeALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHF 418
Cdd:cd11057   329 IVIDIFNMHRRKDIWgPDADQFDPDNFLpeRSAQrhpY-----AFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRLKT 403
                         410       420
                  ....*....|....*....|....
gi 1034571959 419 PHELvPDLKPRLGMTLQP-QPYLI 441
Cdd:cd11057   404 SLRL-EDLRFKFNITLKLaNGHLV 426
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
21-436 4.84e-38

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: 143.01  E-value: 4.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMG-GLLNSRYGRGWVDHRRLAVNSFryfgYGQKSF 99
Cdd:cd20656     4 IISVWIGSTLNVVVSSSELAKEVLKEKDQQLADRHRTRSAARFSRNGqDLIWADYGPHYVKVRKLCTLEL----FTPKRL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 100 ES--KILEE------TKFFNDAIET-YKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVE--LAAS 168
Cdd:cd20656    80 ESlrPIREDevtamvESIFNDCMSPeNEGKPVVLRKYLSAVAFNNITRLAFGKRFVNAEGVMDEQGVEFKAIVSngLKLG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 169 ASVFLYNAFPWIGILpFGKHQQLFRNAAVVYDFLSRLI--EKASVNRKPQLPQHFVDAYLDEMDQgkndpsSTFSKENLI 246
Cdd:cd20656   160 ASLTMAEHIPWLRWM-FPLSEKAFAKHGARRDRLTKAImeEHTLARQKSGGGQQHFVALLTLKEQ------YDLSEDTVI 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 247 FSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFH 326
Cdd:cd20656   233 GLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLHPPTPLMLPH 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 327 ATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFL----DSSGYFAKkeaLVPFSLGRRHCLGEHLARME 402
Cdd:cd20656   313 KASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLeedvDIKGHDFR---LLPFGAGRRVCPGAQLGINL 389
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1034571959 403 MFLFFTALLQrfhlHFPHELVPDLKP-RLGMTLQP 436
Cdd:cd20656   390 VTLMLGHLLH----HFSWTPPEGTPPeEIDMTENP 420
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
21-436 9.38e-38

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: 141.95  E-value: 9.38e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGI-STVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLnsrygrgWVD------HRRLAVNSFRyfg 93
Cdd:cd11053    14 VFTLRVPGLgPVVVLSDPEAIKQIFTADPDVLHPGEGNSLLEPLLGPNSLL-------LLDgdrhrrRRKLLMPAFH--- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  94 yGQ--KSFESKILEETkffNDAIETYK-GRPFDFKQLITNAVSNITNLIIFGErftYEDTDFQHMIELFSENVELAASAS 170
Cdd:cd11053    84 -GErlRAYGELIAEIT---EREIDRWPpGQPFDLRELMQEITLEVILRVVFGV---DDGERLQELRRLLPRLLDLLSSPL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 171 VFLYNAFP-WIGILPFGKHQqlfRNAAVVYDFLSRLIEKASvnRKPQLPQHFVdayLDEMDQGKNDPSSTFSKENLIFSV 249
Cdd:cd11053   157 ASFPALQRdLGPWSPWGRFL---RARRRIDALIYAEIAERR--AEPDAERDDI---LSLLLSARDEDGQPLSDEELRDEL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 250 GELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDlimGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLgIFHATS 329
Cdd:cd11053   229 MTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELD---ALGGDPDPEDIAKLPYLDAVIKETLRLYPVAPL-VPRRVK 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 330 EDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSgyFAKKEALvPFSLGRRHCLGEHLARMEMFLFFTA 409
Cdd:cd11053   305 EPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGRK--PSPYEYL-PFGGGVRRCIGAAFALLEMKVVLAT 381
                         410       420       430
                  ....*....|....*....|....*....|
gi 1034571959 410 LLQRFHLhfphELV--PDLKPRL-GMTLQP 436
Cdd:cd11053   382 LLRRFRL----ELTdpRPERPVRrGVTLAP 407
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
68-438 3.52e-37

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: 140.85  E-value: 3.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  68 GLLNSrYGRGWVDHRRLAVNSFRYfgygQ--KSFESKILEETKFFNDAIETYKGRPFDFKQLITNAV-------SNITNL 138
Cdd:cd20621    50 GLLFS-EGEEWKKQRKLLSNSFHF----EklKSRLPMINEITKEKIKKLDNQNVNIIQFLQKITGEVvirsffgEEAKDL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 139 IIFGERFTYEDTD-FQHMIELFSENVELAASASVFLYNAFpwiGILPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQL 217
Cdd:cd20621   125 KINGKEIQVELVEiLIESFLYRFSSPYFQLKRLIFGRKSW---KLFPTKKEKKLQKRVKELRQFIEKIIQNRIKQIKKNK 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 218 PQHFVDAYLDEMDQGKNDPSST-FSKENLI--FSVgeLIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGK 294
Cdd:cd20621   202 DEIKDIIIDLDLYLLQKKKLEQeITKEEIIqqFIT--FFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDD 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 295 PSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSS 374
Cdd:cd20621   280 ITFEDLQKLNYLNAFIKEVLRLYNPAPFLFPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLNQN 359
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034571959 375 GYFAKKEALVPFSLGRRHCLGEHLARMEMflffTALLQRFHLHFPHELVPDLKPRLGMTLQPQP 438
Cdd:cd20621   360 NIEDNPFVFIPFSAGPRNCIGQHLALMEA----KIILIYILKNFEIEIIPNPKLKLIFKLLYEP 419
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
255-437 4.09e-37

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: 140.38  E-value: 4.09e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 255 AGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLgIFHATSEDAVV 334
Cdd:cd20659   238 AGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRDDIEWDDLSKLPYLTMCIKESLRLYPPVPF-IARTLTKPITI 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 335 RGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSgyfAKKE---ALVPFSLGRRHCLGEHLARMEMFLFFTALL 411
Cdd:cd20659   317 DGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPEN---IKKRdpfAFIPFSAGPRNCIGQNFAMNEMKVVLARIL 393
                         170       180
                  ....*....|....*....|....*...
gi 1034571959 412 QRFHLhfphELVPD--LKPRLGMTLQPQ 437
Cdd:cd20659   394 RRFEL----SVDPNhpVEPKPGLVLRSK 417
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
82-420 4.65e-37

cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of fungal cytochrome P450s including: Nectria haematococca cytochrome P450 57A1 (CYP57A1), also called pisatin demethylase, which detoxifies the phytoalexin pisatin; Penicillium aethiopicum P450 monooxygenase gsfF, also called griseofulvin synthesis protein F, which catalyzes the coupling of orcinol and phloroglucinol rings in griseophenone B to form desmethyl-dehydrogriseofulvin A during the biosynthesis of griseofulvin, a spirocyclic fungal natural product used to treat dermatophyte infections; and Penicillium aethiopicum P450 monooxygenase vrtE, also called viridicatumtoxin synthesis protein E, which catalyzes hydroxylation at C5 of the polyketide backbone during the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP57A1-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410683 [Multi-domain]  Cd Length: 425  Bit Score: 140.41  E-value: 4.65e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  82 RRLAVNSFrYFGYGQKSFESKILEETKFFNDAIETY--KGRPFDFKQLIT----NAVSNITnliiFGERFTY--EDTDFQ 153
Cdd:cd11060    60 LRRKVASG-YSMSSLLSLEPFVDECIDLLVDLLDEKavSGKEVDLGKWLQyfafDVIGEIT----FGKPFGFleAGTDVD 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 154 HMIElfseNVElAASASVFLYNAFPWIG----ILPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQH--FVDAYLD 227
Cdd:cd11060   135 GYIA----SID-KLLPYFAVVGQIPWLDrlllKNPLGPKRKDKTGFGPLMRFALEAVAERLAEDAESAKGRkdMLDSFLE 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 228 EmdqGKNDPSStFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDlIMGPNGKPS----WDDKCKM 303
Cdd:cd11060   210 A---GLKDPEK-VTDREVVAEALSNILAGSDTTAIALRAILYYLLKNPRVYAKLRAEID-AAVAEGKLSspitFAEAQKL 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 304 PYTEAVLHEVLRFCNIVPLGIF-HATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSGyfAKKE 381
Cdd:cd11060   285 PYLQAVIKEALRLHPPVGLPLErVVPPGGATICGRFIPGGTIVGVNPWVIHRDKEVFgEDADVFRPERWLEADE--EQRR 362
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1034571959 382 ----ALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFPH 420
Cdd:cd11060   363 mmdrADLTFGAGSRTCLGKNIALLELYKVIPELLRRFDFELVD 405
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
17-443 9.43e-37

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 140.98  E-value: 9.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  17 LFSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLN-SRYGRGWVDHRRLA-VNSFRYFGY 94
Cdd:PLN03234   60 LYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTARPLLKGQQTMSYQGRELGfGQYTAYYREMRKMCmVNLFSPNRV 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  95 GqkSFESKILEETKFFNDAIetYKGR----PFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASas 170
Cdd:PLN03234  140 A--SFRPVREEECQRMMDKI--YKAAdqsgTVDLSELLLSFTNCVVCRQAFGKRYNEYGTEMKRFIDILYETQALLGT-- 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 171 VFLYNAFPWIGILP--FGKHQQLFRNAAVVYDFLSRLI-EKASVNRKPQLPQHFVDAYldeMDQGKNDPSS-TFSKENLI 246
Cdd:PLN03234  214 LFFSDLFPYFGFLDnlTGLSARLKKAFKELDTYLQELLdETLDPNRPKQETESFIDLL---MQIYKDQPFSiKFTHENVK 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 247 FSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFH 326
Cdd:PLN03234  291 AMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKGYVSEEDIPNLPYLKAVIKESLRLEPVIPILLHR 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 327 ATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRD-PEVFHPERFLDSS---GYFAKKEALVPFSLGRRHCLGEHLARME 402
Cdd:PLN03234  371 ETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDnPNEFIPERFMKEHkgvDFKGQDFELLPFGSGRRMCPAMHLGIAM 450
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1034571959 403 MFLFFTALLQRFHLHFPHELVP-DLKPRL--GMTLQPQPYLICA 443
Cdd:PLN03234  451 VEIPFANLLYKFDWSLPKGIKPeDIKMDVmtGLAMHKKEHLVLA 494
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
141-425 1.21e-36

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: 138.87  E-value: 1.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 141 FGERFT-YEDTDFQHMIELFSENVELAASASVFLYnaFPWIG-----ILPFGKHQQLFRNAAVVYDFLSRLIEKASvNRK 214
Cdd:cd11058   121 FGESFGcLENGEYHPWVALIFDSIKALTIIQALRR--YPWLLrllrlLIPKSLRKKRKEHFQYTREKVDRRLAKGT-DRP 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 215 pqlpqHFVDAYLDEMDQGKndpssTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEI--------D 286
Cdd:cd11058   198 -----DFMSYILRNKDEKK-----GLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIrsafssedD 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 287 LIMgpngkpswdDKC-KMPYTEAVLHEVLRFCNIVPLGIFHAT-SEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEV 364
Cdd:cd11058   268 ITL---------DSLaQLPYLNAVIQEALRLYPPVPAGLPRVVpAGGATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDE 338
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034571959 365 FHPERFLDSSGYFA---KKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLhfphELVPD 425
Cdd:cd11058   339 FIPERWLGDPRFEFdndKKEAFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNFDL----ELDPE 398
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
15-433 2.07e-36

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: 139.04  E-value: 2.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  15 FLLFSKIFSLDLGGISTVVLNGYDVVKECLvhQSEIFAdRPCLPLFMK--MTKMGGLLNSRYGRGWVDHRRLAVNSFRyf 92
Cdd:cd11046     7 FLEYGPIYKLAFGPKSFLVISDPAIAKHVL--RSNAFS-YDKKGLLAEilEPIMGKGLIPADGEIWKKRRRALVPALH-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  93 gygqksfeSKILEET-KFFNDAIETY---------KGRPFDFKQLITNAVSNITNLIIFGERF---TYEDTDFQHMIELF 159
Cdd:cd11046    82 --------KDYLEMMvRVFGRCSERLmekldaaaeTGESVDMEEEFSSLTLDIIGLAVFNYDFgsvTEESPVIKAVYLPL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 160 SEnvelAASASVFL--YNAFPWIG-ILPFGKHQQlfRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDE-------- 228
Cdd:cd11046   154 VE----AEHRSVWEppYWDIPAALfIVPRQRKFL--RDLKLLNDTLDDLIRKRKEMRQEEDIELQQEDYLNEddpsllrf 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 229 -MDQGKNDPSSTFSKENLIfsvgELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTE 307
Cdd:cd11046   228 lVDMRDEDVDSKQLRDDLM----TMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTR 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 308 AVLHEVLRFCNIVPLGIFHATSEDAVVRG-YSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKE----A 382
Cdd:cd11046   304 RVLNESLRLYPQPPVLIRRAVEDDKLPGGgVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPNEViddfA 383
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034571959 383 LVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLhfphELVPDlKPRLGMT 433
Cdd:cd11046   384 FLPFGGGPRKCLGDQFALLEATVALAMLLRRFDF----ELDVG-PRHVGMT 429
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
131-417 2.71e-36

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: 138.20  E-value: 2.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 131 AVSNITNLIiFGERFTYEDTDFQHMIELFSENVELAASASvFLYNAFPWIGILPFGKHQQLFRNA-AVVYDFLSRLIEKA 209
Cdd:cd11059   111 AMDVVSHLL-FGESFGTLLLGDKDSRERELLRRLLASLAP-WLRWLPRYLPLATSRLIIGIYFRAfDEIEEWALDLCARA 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 210 SvnRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEI-DLI 288
Cdd:cd11059   189 E--SSLAESSDSESLTVLLLEKLKGLKKQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELaGLP 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 289 MGPNGKPSWDDKCKMPYTEAVLHEVLRFCN--------IVPLGifhatseDAVVRGYSIPKGTTVITNLYSVHFDEKYWR 360
Cdd:cd11059   267 GPFRGPPDLEDLDKLPYLNAVIRETLRLYPpipgslprVVPEG-------GATIGGYYIPGGTIVSTQAYSLHRDPEVFP 339
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034571959 361 DPEVFHPERFLDSSG--YFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLH 417
Cdd:cd11059   340 DPEEFDPERWLDPSGetAREMKRAFWPFGSGSRMCIGMNLALMEMKLALAAIYRNYRTS 398
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
19-435 8.08e-36

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: 137.08  E-value: 8.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  19 SKIFSLDLGGISTVVLNGYDVVKECLVHQSeiFADRPclplfMKMTKMGgLLNSR------YGRGWVDHRRLAvnSFRYF 92
Cdd:cd11076     3 KRLMAFSLGETRVVITSHPETAREILNSPA--FADRP-----VKESAYE-LMFNRaigfapYGEYWRNLRRIA--SNHLF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  93 GYGQ-KSFE---SKILEE-TKFFNDAIETyKGRPFDFKQLITNAVSNITNLIiFGER--FTYEDTDFQHMIELFSENVEL 165
Cdd:cd11076    73 SPRRiAASEpqrQAIAAQmVKAIAKEMER-SGEVAVRKHLQRASLNNIMGSV-FGRRydFEAGNEEAEELGEMVREGYEL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 166 AAsasVF-LYNAFPWIGILPFGKHQQLFRN-AAVVYDFLSRLIE--KASVNRKPQLPQHFVDAYLDEmdqgknDPSSTFS 241
Cdd:cd11076   151 LG---AFnWSDHLPWLRWLDLQGIRRRCSAlVPRVNTFVGKIIEehRAKRSNRARDDEDDVDVLLSL------QGEEKLS 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 242 KENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVP 321
Cdd:cd11076   222 DSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDVAKLPYLQAVVKETLRLHPPGP 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 322 LGIFHATS-EDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGY-----FAKKEALVPFSLGRRHCLG 395
Cdd:cd11076   302 LLSWARLAiHDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVAAEGGadvsvLGSDLRLAPFGAGRRVCPG 381
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1034571959 396 EHLARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQ 435
Cdd:cd11076   382 KALGLATVHLWVAQLLHEFEWLPDDAKPVDLSEVLKLSCE 421
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
21-438 1.07e-35

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: 136.64  E-value: 1.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFadRPCLPLFMKMTkMGGllNSRYGRGWVDHRRLAvnsfRYFGygqKSFE 100
Cdd:cd11044    24 VFKTHLLGRPTVFVIGAEAVRFILSGEGKLV--RYGWPRSVRRL-LGE--NSLSLQDGEEHRRRR----KLLA---PAFS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 101 SKILEE-----TKFFNDAIETYKGRPF-----DFKQLITNavsnITNLIIFGERFTYEDTDFQHMIELFSENVelaasas 170
Cdd:cd11044    92 REALESyvptiQAIVQSYLRKWLKAGEvalypELRRLTFD----VAARLLLGLDPEVEAEALSQDFETWTDGL------- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 171 vflyNAFPWIgiLPFGKhqqlFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAyLDEMDQGKNDPSSTFSKENLIFSVG 250
Cdd:cd11044   161 ----FSLPVP--LPFTP----FGRAIRARNKLLARLEQAIRERQEEENAEAKDA-LGLLLEAKDEDGEPLSMDELKDQAL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 251 ELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLiMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGiFHATSE 330
Cdd:cd11044   230 LLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDA-LGLEEPLTLESLKKMPYLDQVIKEVLRLVPPVGGG-FRKVLE 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 331 DAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKE-ALVPFSLGRRHCLGEHLARMEMFLFFTA 409
Cdd:cd11044   308 DFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPARSEDKKKPfSLIPFGGGPRECLGKEFAQLEMKILASE 387
                         410       420
                  ....*....|....*....|....*....
gi 1034571959 410 LLQRFHLhfphELVPDLKPRLGMTLQPQP 438
Cdd:cd11044   388 LLRNYDW----ELLPNQDLEPVVVPTPRP 412
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
183-437 1.13e-35

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: 136.16  E-value: 1.13e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 183 LPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQH-FVDAYLDEMDQGKNDPSSTFSKENLIFsvgeLIIAGTETTT 261
Cdd:cd11043   152 LPGTTFHRALKARKRIRKELKKIIEERRAELEKASPKGdLLDVLLEEKDEDGDSLTDEEILDNILT----LLFAGHETTS 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 262 NVLRWAILFMALYPNIQGQVQKEIDLI---MGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPlGIFHATSEDAVVRGYS 338
Cdd:cd11043   228 TTLTLAVKFLAENPKVLQELLEEHEEIakrKEEGEGLTWEDYKSMKYTWQVINETLRLAPIVP-GVFRKALQDVEYKGYT 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 339 IPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKkeALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLhf 418
Cdd:cd11043   307 IPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGKGVPY--TFLPFGGGPRLCPGAELAKLEILVFLHHLVTRFRW-- 382
                         250
                  ....*....|....*....
gi 1034571959 419 phELVPDLKPRLGMTLQPQ 437
Cdd:cd11043   383 --EVVPDEKISRFPLPRPP 399
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
42-416 1.84e-35

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: 136.30  E-value: 1.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  42 ECLVHQSE----IFADRPclpLFMKMTKMGGLLN-------SRYGRGWVDHRRLAVNSFRYFGYGQKSfeSKILEETKFF 110
Cdd:cd11070    14 NILVTKPEyltqIFRRRD---DFPKPGNQYKIPAfygpnviSSEGEDWKRYRKIVAPAFNERNNALVW--EESIRQAQRL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 111 NDAIE----TYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSEnVELAASASVFLYNAF-PWIGILPF 185
Cdd:cd11070    89 IRYLLeeqpSAKGGGVDVRDLLQRLALNVIGEVGFGFDLPALDEEESSLHDTLNA-IKLAIFPPLFLNFPFlDRLPWVLF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 186 GKHQQLFRNaavVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKE----NLIFsvgeLIIAGTETTT 261
Cdd:cd11070   168 PSRKRAFKD---VDEFLSELLDEVEAELSADSKGKQGTESVVASRLKRARRSGGLTEKellgNLFI----FFIAGHETTA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 262 NVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSW--DDKCKMPYTEAVLHEVLRFCNIVPLgIFHATSEDAVVRGYS- 338
Cdd:cd11070   241 NTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDWDyeEDFPKLPYLLAVIYETLRLYPPVQL-LNRKTTEPVVVITGLg 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 339 ----IPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSG------YFAK-KEALVPFSLGRRHCLGEHLARMEMFLF 406
Cdd:cd11070   320 qeivIPKGTYVGYNAYATHRDPTIWgPDADEFDPERWGSTSGeigaatRFTPaRGAFIPFSAGPRACLGRKFALVEFVAA 399
                         410
                  ....*....|
gi 1034571959 407 FTALLQRFHL 416
Cdd:cd11070   400 LAELFRQYEW 409
PLN02183 PLN02183
ferulate 5-hydroxylase
21-443 2.51e-35

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 136.90  E-value: 2.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMT-KMGGLLNSRYGRGWVDHRRLAVNSFryfgYGQKSF 99
Cdd:PLN02183   71 LFHMRMGYLHMVAVSSPEVARQVLQVQDSVFSNRPANIAISYLTyDRADMAFAHYGPFWRQMRKLCVMKL----FSRKRA 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 100 ES--KILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSEnvelaasasvfLYNAF 177
Cdd:PLN02183  147 ESwaSVRDEVDSMVRSVSSNIGKPVNIGELIFTLTRNITYRAAFGSSSNEGQDEFIKILQEFSK-----------LFGAF 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 178 ------PWIG-ILPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFV-----------------DAYLDEMDQGK 233
Cdd:PLN02183  216 nvadfiPWLGwIDPQGLNKRLVKARKSLDGFIDDIIDDHIQKRKNQNADNDSeeaetdmvddllafyseEAKVNESDDLQ 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 234 NdpSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEV 313
Cdd:PLN02183  296 N--SIKLTRDNIKAIIMDVMFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGLNRRVEESDLEKLTYLKCTLKET 373
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 314 LRFCNIVPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSS--GYFAKKEALVPFSLGRR 391
Cdd:PLN02183  374 LRLHPPIPL-LLHETAEDAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFLKPGvpDFKGSHFEFIPFGSGRR 452
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034571959 392 HCLGEHLARMEMFLFFTALLQRFHLHFPHELVP---DLKPRLGMTLQ--------PQPYLICA 443
Cdd:PLN02183  453 SCPGMQLGLYALDLAVAHLLHCFTWELPDGMKPselDMNDVFGLTAPratrlvavPTYRLQCP 515
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
21-442 3.61e-35

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: 135.42  E-value: 3.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  21 IFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRP------CLPL---------------FMK---MTKmggLLNSRygr 76
Cdd:cd20655     3 LLHLRIGSVPCVVVSSASVAKEILKTHDLNFSSRPvpaaaeSLLYgssgfafapygdywkFMKklcMTE---LLGPR--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  77 gwvdhrrlAVNSFRYFGYGQ-KSFESKILEETKffndaietyKGRPFDF-KQLI--TNavsNITNLIIFGERFTYEDTDF 152
Cdd:cd20655    77 --------ALERFRPIRAQElERFLRRLLDKAE---------KGESVDIgKELMklTN---NIICRMIMGRSCSEENGEA 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 153 QHMIELFSENVELAA--SASVFLYNAFPWiGILPFGKhqqlfRNAAVVYDF---LSRLI---EKASVNRKPQLPQHFVDA 224
Cdd:cd20655   137 EEVRKLVKESAELAGkfNASDFIWPLKKL-DLQGFGK-----RIMDVSNRFdelLERIIkehEEKRKKRKEGGSKDLLDI 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 225 YLDEMdqgkNDPSSTF--SKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCK 302
Cdd:cd20655   211 LLDAY----EDENAEYkiTRNHIKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPN 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 303 MPYTEAVLHEVLRFCNIVPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEA 382
Cdd:cd20655   287 LPYLQAVVKETLRLHPPGPL-LVRESTEGCKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLASSRSGQELDV 365
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034571959 383 ------LVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQPQPYLIC 442
Cdd:cd20655   366 rgqhfkLLPFGSGRRGCPGASLAYQVVGTAIAAMVQCFDWKVGDGEKVNMEEASGLTLPRAHPLKC 431
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
175-446 1.18e-34

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: 133.85  E-value: 1.18e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 175 NAFPWIGILPFGKHQQLFRNAAVVYDFLSRLIEKasvnRKpQLPQHFVDAYLDEMDQGKnDPSST--FSKENLIFSVGEL 252
Cdd:cd11068   165 NRPPILNKLRRRAKRQFREDIALMRDLVDEIIAE----RR-ANPDGSPDDLLNLMLNGK-DPETGekLSDENIRYQMITF 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 253 IIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPnGKPSWDDKCKMPYTEAVLHEVLRFCNIVPlGIFHATSEDA 332
Cdd:cd11068   239 LIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGD-DPPPYEQVAKLRYIRRVLDETLRLWPTAP-AFARKPKEDT 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 333 VVRG-YSIPKGTTVITNLYSVHFDEK-YWRDPEVFHPERFLDssGYFAK--KEALVPFSLGRRHCLGEHLARMEMFLFFT 408
Cdd:cd11068   317 VLGGkYPLKKGDPVLVLLPALHRDPSvWGEDAEEFRPERFLP--EEFRKlpPNAWKPFGNGQRACIGRQFALQEATLVLA 394
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034571959 409 ALLQRFHLHFPHELVPDLKPRLgmTLQPQPYLICAERR 446
Cdd:cd11068   395 MLLQRFDFEDDPDYELDIKETL--TLKPDGFRLKARPR 430
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
207-437 1.20e-34

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: 133.54  E-value: 1.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 207 EKASVNRKPQLPqhFVDAYLDEMDQGKNdpsstFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEID 286
Cdd:cd20660   202 EDADIGKRKRLA--FLDLLLEASEEGTK-----LSDEDIREEVDTFMFEGHDTTAAAINWALYLIGSHPEVQEKVHEELD 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 287 LIMG-PNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVF 365
Cdd:cd20660   275 RIFGdSDRPATMDDLKEMKYLECVIKEALRLFPSVPM-FGRTLSEDIEIGGYTIPKGTTVLVLTYALHRDPRQFPDPEKF 353
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034571959 366 HPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHfPHELVPDLKPRLGMTLQPQ 437
Cdd:cd20660   354 DPDRFLPENSAGRHPYAYIPFSAGPRNCIGQKFALMEEKVVLSSILRNFRIE-SVQKREDLKPAGELILRPV 424
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
165-427 2.13e-32

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: 127.77  E-value: 2.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 165 LAASASVFLYNAF------PWIGILPFGKHQQLFRNAAVVYDFLSRLIE--KASVNRKPQlpqhfvdayldemDQGK--- 233
Cdd:cd11069   150 FEPTLLGSLLFILllflprWLVRILPWKANREIRRAKDVLRRLAREIIRekKAALLEGKD-------------DSGKdil 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 234 ------NDPSST--FSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEI-DLIMG-PNGKPSWDDKCKM 303
Cdd:cd11069   217 sillraNDFADDerLSDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIrAALPDpPDGDLSYDDLDRL 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 304 PYTEAVLHEVLRFCNIVPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSGYFAKKEA 382
Cdd:cd11069   297 PYLNAVCRETLRLYPPVPL-TSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWLEPDGAASPGGA 375
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034571959 383 -----LVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLhfphELVPDLK 427
Cdd:cd11069   376 gsnyaLLTFLHGPRSCIGKKFALAEMKVLLAALVSRFEF----ELDPDAE 421
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
107-417 8.17e-32

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: 125.73  E-value: 8.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 107 TKFFNDAIEtyKGRPFDFKQLITNAVSNITNLIIFG---ERFTYEDTDFQHMIELFSENvELAASASVFLYNAFP----W 179
Cdd:cd11056    92 VDYLKKQAE--KGKELEIKDLMARYTTDVIASCAFGldaNSLNDPENEFREMGRRLFEP-SRLRGLKFMLLFFFPklarL 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 180 IGILPFGKHqqlfrnaavVYDFLSRLI-------EKASVNRKPQLpQHFVDAYLDEmDQGKNDPSSTFSKENLIFSVGEL 252
Cdd:cd11056   169 LRLKFFPKE---------VEDFFRKLVrdtieyrEKNNIVRNDFI-DLLLELKKKG-KIEDDKSEKELTDEELAAQAFVF 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 253 IIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIM-GPNGKPSWDDKCKMPYTEAVLHEVLRfcnIVPLGIFHA--TS 329
Cdd:cd11056   238 FLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLeKHGGELTYEALQEMKYLDQVVNETLR---KYPPLPFLDrvCT 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 330 EDAVVRG--YSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFF 407
Cdd:cd11056   315 KDYTLPGtdVVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGL 394
                         330
                  ....*....|
gi 1034571959 408 TALLQRFHLH 417
Cdd:cd11056   395 VHLLSNFRVE 404
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
20-428 1.27e-31

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: 125.50  E-value: 1.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  20 KIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMK-MTKMGGLL------NSRYGRgwvdhRRLAVNSfryf 92
Cdd:cd11066     3 PVFQIRLGNKRIVVVNSFASVRDLWIKNSSALNSRPTFYTFHKvVSSTQGFTigtspwDESCKR-----RRKAAAS---- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  93 GYGQKSFESKI----LEETKFFNDAIETYKG--RPFDFKQLITNAVSNITNLIIFGERFtyedtDFQHMIELFSENVELA 166
Cdd:cd11066    74 ALNRPAVQSYApiidLESKSFIRELLRDSAEgkGDIDPLIYFQRFSLNLSLTLNYGIRL-----DCVDDDSLLLEIIEVE 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 167 ASASVF------LYNAFPWIGILP----FGKHQQLFRNAAVVY--DFLSRLIEKAS-VNRKPQLpqhfvdayldemdQGK 233
Cdd:cd11066   149 SAISKFrstssnLQDYIPILRYFPkmskFRERADEYRNRRDKYlkKLLAKLKEEIEdGTDKPCI-------------VGN 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 234 N--DPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMA--LYPNIQGQVQKEIdLIMGPNGKPSWDD-----KCkmP 304
Cdd:cd11066   216 IlkDKESKLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLShpPGQEIQEKAYEEI-LEAYGNDEDAWEDcaaeeKC--P 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 305 YTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALV 384
Cdd:cd11066   293 YVVALVKETLRYFTVLPLGLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIPGPPHF 372
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1034571959 385 PFSLGRRHCLGEHLARMEMFLFFTALLQRFHLH-FPHELVPDLKP 428
Cdd:cd11066   373 SFGAGSRMCAGSHLANRELYTAICRLILLFRIGpKDEEEPMELDP 417
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
235-414 1.70e-31

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 125.86  E-value: 1.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 235 DPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKP---SWDDKCKMPYTEAVLH 311
Cdd:PLN02987  258 ASDDGFSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEHEKIRAMKSDSyslEWSDYKSMPFTQCVVN 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 312 EVLRFCNIVPlGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRR 391
Cdd:PLN02987  338 ETLRVANIIG-GIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGTTVPSNVFTPFGGGPR 416
                         170       180
                  ....*....|....*....|...
gi 1034571959 392 HCLGEHLARMEMFLFFTALLQRF 414
Cdd:PLN02987  417 LCPGYELARVALSVFLHRLVTRF 439
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
177-431 3.21e-31

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: 124.39  E-value: 3.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 177 FP-WI-GILPFGKHqqlFRNA-AVVYDFLSRLIEKASVNRKPQLP--QHFVDAYLDEM-DQGKNDPSSTFSkenlifSVG 250
Cdd:cd20646   169 LPkWTrPYLPFWKR---YVDAwDTIFSFGKKLIDKKMEEIEERVDrgEPVEGEYLTYLlSSGKLSPKEVYG------SLT 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 251 ELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSE 330
Cdd:cd20646   240 ELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARVIVEK 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 331 DAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTAL 410
Cdd:cd20646   320 EVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRDGGLKHHPFGSIPFGYGVRACVGRRIAELEMYLALSRL 399
                         250       260
                  ....*....|....*....|.
gi 1034571959 411 LQRFhlhfphELVPDlkPRLG 431
Cdd:cd20646   400 IKRF------EVRPD--PSGG 412
PLN02966 PLN02966
cytochrome P450 83A1
18-425 4.94e-31

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 124.86  E-value: 4.94e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  18 FSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPclPL----FMKMTKMGGLLNsRYGRGWVDHRRLAVNSFrYFG 93
Cdd:PLN02966   62 YGPILSYRIGSRTMVVISSAELAKELLKTQDVNFADRP--PHrgheFISYGRRDMALN-HYTPYYREIRKMGMNHL-FSP 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  94 YGQKSFESKILEETKFFNDAIETY--KGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASasV 171
Cdd:PLN02966  138 TRVATFKHVREEEARRMMDKINKAadKSEVVDISELMLTFTNSVVCRQAFGKKYNEDGEEMKRFIKILYGTQSVLGK--I 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 172 FLYNAFPWIGILpfgkhqqlfrnaavvyDFLSRLIE--KASVNRKPQLPQHFVDAYLDE--------------MDQGKND 235
Cdd:PLN02966  216 FFSDFFPYCGFL----------------DDLSGLTAymKECFERQDTYIQEVVNETLDPkrvkpetesmidllMEIYKEQ 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 236 P-SSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKP--SWDDKCKMPYTEAVLHE 312
Cdd:PLN02966  280 PfASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEKGSTfvTEDDVKNLPYFRALVKE 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 313 VLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSGYFAKKE-ALVPFSLGR 390
Cdd:PLN02966  360 TLRIEPVIPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPERFLEKEVDFKGTDyEFIPFGSGR 439
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1034571959 391 RHCLGEHLARMEMFLFFTALLQRFHLHFPHELVPD 425
Cdd:PLN02966  440 RMCPGMRLGAAMLEVPYANLLLNFNFKLPNGMKPD 474
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
18-419 5.96e-31

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: 123.35  E-value: 5.96e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  18 FSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMG-GLLNSRYGRGWVDHRRLAVNSFryfgygq 96
Cdd:cd11074     3 FGDIFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDIFTGKGqDMVFTVYGEHWRKMRRIMTVPF------- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  97 ksFESKILEETKF-----FNDAIETYKGRPfdfkQLITNAV----------SNITNLIIFGERFTYEDTD-FQHMIELFS 160
Cdd:cd11074    76 --FTNKVVQQYRYgweeeAARVVEDVKKNP----EAATEGIvirrrlqlmmYNNMYRIMFDRRFESEDDPlFVKLKALNG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 161 ENVELAASasvFLYNAFPWIGIL-PF------------GKHQQLFRNAavvydFLSRLIEKASVNR-KPQLPQHFVDAYL 226
Cdd:cd11074   150 ERSRLAQS---FEYNYGDFIPILrPFlrgylkickevkERRLQLFKDY-----FVDERKKLGSTKStKNEGLKCAIDHIL 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 227 DEMDQGKndpsstFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYT 306
Cdd:cd11074   222 DAQKKGE------INEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYL 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 307 EAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSgyfAKKEA---- 382
Cdd:cd11074   296 QAVVKETLRLRMAIPLLVPHMNLHDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEE---SKVEAngnd 372
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1034571959 383 --LVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFP 419
Cdd:cd11074   373 frYLPFGVGRRSCPGIILALPILGITIGRLVQNFELLPP 411
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
18-419 1.08e-30

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 123.69  E-value: 1.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  18 FSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMG-GLLNSRYGRGWVDHRRLAVNSFryfgygq 96
Cdd:PLN02394   63 YGDVFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDIFTGKGqDMVFTVYGDHWRKMRRIMTVPF------- 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  97 ksFESKILEETKFFNDA-----IETYKGRP------FDFKQLITNAVSNITNLIIFGERF-TYEDTDFQHMIELFSENVE 164
Cdd:PLN02394  136 --FTNKVVQQYRYGWEEeadlvVEDVRANPeaategVVIRRRLQLMMYNIMYRMMFDRRFeSEDDPLFLKLKALNGERSR 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 165 LAASasvFLYNAFPWIGIL-PF------------GKHQQLFRNAAVvyDFLSRLIEKASVNRKPQlpQHFVDAYLDEMDQ 231
Cdd:PLN02394  214 LAQS---FEYNYGDFIPILrPFlrgylkicqdvkERRLALFKDYFV--DERKKLMSAKGMDKEGL--KCAIDHILEAQKK 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 232 GKndpsstFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLH 311
Cdd:PLN02394  287 GE------INEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDTHKLPYLQAVVK 360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 312 EVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGyfaKKEA------LVP 385
Cdd:PLN02394  361 ETLRLHMAIPLLVPHMNLEDAKLGGYDIPAESKILVNAWWLANNPELWKNPEEFRPERFLEEEA---KVEAngndfrFLP 437
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1034571959 386 FSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFP 419
Cdd:PLN02394  438 FGVGRRSCPGIILALPILGIVLGRLVQNFELLPP 471
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
252-438 1.20e-30

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: 122.37  E-value: 1.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 252 LIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLgIFHATSED 331
Cdd:cd11049   228 LLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLG-GRPATFEDLPRLTYTRRVVTEALRLYPPVWL-LTRRTTAD 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 332 AVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALL 411
Cdd:cd11049   306 VELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVPRGAFIPFGAGARKCIGDTFALTELTLALATIA 385
                         170       180
                  ....*....|....*....|....*....
gi 1034571959 412 QRFHLHfpheLVPDLK--PRLGMTLQPQP 438
Cdd:cd11049   386 SRWRLR----PVPGRPvrPRPLATLRPRR 410
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
118-435 1.37e-30

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


Pssm-ID: 410750 [Multi-domain]  Cd Length: 438  Bit Score: 122.53  E-value: 1.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 118 KGRPFDFKQLITNAVSNITNLIIFGERFTYEDTD-----FQHMIelfsenVELAASASVFLYNAF-PWIGIL-PFGKHQQ 190
Cdd:cd20657   102 KGEPVVLGEMLNVCMANMLGRVMLSKRVFAAKAGakaneFKEMV------VELMTVAGVFNIGDFiPSLAWMdLQGVEKK 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 191 LFRNAAVVYDFLSRLIE--KASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENLIFSvgeLIIAGTETTTNVLRWAI 268
Cdd:cd20657   176 MKRLHKRFDALLTKILEehKATAQERKGKPDFLDFVLLENDDNGEGERLTDTNIKALLLN---LFTAGTDTSSSTVEWAL 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 269 LFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITN 348
Cdd:cd20657   253 AELIRHPDILKKAQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPSTPLNLPRIASEACEVDGYYIPKGTRLLVN 332
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 349 LYSVHFDEKYWRDPEVFHPERFLdsSGYFAKKEA------LVPFSLGRRHCLGEHL-ARMEMFLFFTaLLQRFHLHFPHE 421
Cdd:cd20657   333 IWAIGRDPDVWENPLEFKPERFL--PGRNAKVDVrgndfeLIPFGAGRRICAGTRMgIRMVEYILAT-LVHSFDWKLPAG 409
                         330
                  ....*....|....*..
gi 1034571959 422 LVPD---LKPRLGMTLQ 435
Cdd:cd20657   410 QTPEelnMEEAFGLALQ 426
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
17-437 1.53e-30

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: 122.06  E-value: 1.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  17 LFSKIFSLDLGGISTVVLNGYDVVKECLVHqSEIFADRPCLPLFMKMTKMGGLLNSRyGRGWVDHRRLAVNSFryFGYGQ 96
Cdd:cd11052    10 QYGKNFLYWYGTDPRLYVTEPELIKELLSK-KEGYFGKSPLQPGLKKLLGRGLVMSN-GEKWAKHRRIANPAF--HGEKL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  97 KSFESKILEETKFFNDAIETYKGR---PFDFKQLITNAVSNITNLIIFGErfTYED--TDFQHMIELfsenVELAASASV 171
Cdd:cd11052    86 KGMVPAMVESVSDMLERWKKQMGEegeEVDVFEEFKALTADIISRTAFGS--SYEEgkEVFKLLREL----QKICAQANR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 172 FLYnaFPWIGILPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDpsstfSKENLIFSVGE 251
Cdd:cd11052   160 DVG--IPGSRFLPTKGNKKIKKLDKEIEDSLLEIIKKREDSLKMGRGDDYGDDLLGLLLEANQS-----DDQNKNMTVQE 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 252 LI-------IAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGI 324
Cdd:cd11052   233 IVdecktffFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCG-KDKPPSDSLSKLKTVSMVINESLRLYPPAVFLT 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 325 FHAtSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLD-SSGYFAKKEALVPFSLGRRHCLGEHLARME 402
Cdd:cd11052   312 RKA-KEDIKLGGLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFADgVAKAAKHPMAFLPFGLGPRNCIGQNFATME 390
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1034571959 403 MFLFFTALLQRFHLHfpheLVPDLK--PRLGMTLQPQ 437
Cdd:cd11052   391 AKIVLAMILQRFSFT----LSPTYRhaPTVVLTLRPQ 423
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
201-432 3.46e-30

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: 121.41  E-value: 3.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 201 FLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQ 280
Cdd:cd20680   200 EMKAEEDKTGDSDGESPSKKKRKAFLDMLLSVTDEEGNKLSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRK 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 281 VQKEIDLIMGPNGKP-SWDDKCKMPYTEAVLHEVLRFCNIVPLgiFHAT-SEDAVVRGYSIPKGTTVITNLYSVHFDEKY 358
Cdd:cd20680   280 VHKELDEVFGKSDRPvTMEDLKKLRYLECVIKESLRLFPSVPL--FARSlCEDCEIRGFKVPKGVNAVIIPYALHRDPRY 357
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 359 WRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHL---HFPHELVPD----LKPRLG 431
Cdd:cd20680   358 FPEPEEFRPERFFPENSSGRHPYAYIPFSAGPRNCIGQRFALMEEKVVLSCILRHFWVeanQKREELGLVgeliLRPQNG 437

                  .
gi 1034571959 432 M 432
Cdd:cd20680   438 I 438
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
237-416 4.24e-30

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: 121.18  E-value: 4.24e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 237 SSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRF 316
Cdd:cd20647   230 SKELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRL 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 317 CNIVPlGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLdssgyfaKKEAL--------VPFSL 388
Cdd:cd20647   310 FPVLP-GNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWL-------RKDALdrvdnfgsIPFGY 381
                         170       180
                  ....*....|....*....|....*...
gi 1034571959 389 GRRHCLGEHLARMEMFLFFTALLQRFHL 416
Cdd:cd20647   382 GIRSCIGRRIAELEIHLALIQLLQNFEI 409
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
252-441 4.91e-30

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: 120.78  E-value: 4.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 252 LIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMG-PNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSE 330
Cdd:cd11042   220 LLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGdGDDPLTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKP 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 331 DAV-VRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKE--ALVPFSLGRRHCLGEHLARMEMFLFF 407
Cdd:cd11042   300 FEVeGGGYVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAEDSKGGkfAYLPFGAGRHRCIGENFAYLQIKTIL 379
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034571959 408 TALLQRFHLHFPHELVPDLKPRLGMTLQPQPYLI 441
Cdd:cd11042   380 STLLRNFDFELVDSPFPEPDYTTMVVWPKGPARV 413
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
198-437 7.54e-30

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: 120.21  E-value: 7.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 198 VYDFLSRLIEKASVNRKPQLPQHFVDaYLDEMDQGKNDPSSTFSK---------ENLIFsvgelIIAGTETTTNVLRWAI 268
Cdd:cd20650   179 VTNFFYKSVKKIKESRLDSTQKHRVD-FLQLMIDSQNSKETESHKalsdleilaQSIIF-----IFAGYETTSSTLSFLL 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 269 LFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRfcnIVPLG--IFHATSEDAVVRGYSIPKGTTVI 346
Cdd:cd20650   253 YELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLR---LFPIAgrLERVCKKDVEINGVFIPKGTVVM 329
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 347 TNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFPHELVPDL 426
Cdd:cd20650   330 IPTYALHRDPQYWPEPEEFRPERFSKKNKDNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFKPCKETQIPL 409
                         250
                  ....*....|.
gi 1034571959 427 KPRLGMTLQPQ 437
Cdd:cd20650   410 KLSLQGLLQPE 420
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
118-435 2.24e-29

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 119.96  E-value: 2.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 118 KGRPFDFKQLITNAVSNITNLIIFGERF----TYEDTDFQHMIelfsenVELAASASVFLYNAF-PWIGILPFGKHQQLF 192
Cdd:PLN00110  165 RGEPVVVPEMLTFSMANMIGQVILSRRVfetkGSESNEFKDMV------VELMTTAGYFNIGDFiPSIAWMDIQGIERGM 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 193 RNAAVVYD-FLSRLIEK--ASVNRKPQLPQhFVDAYldeMDQGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAIL 269
Cdd:PLN00110  239 KHLHKKFDkLLTRMIEEhtASAHERKGNPD-FLDVV---MANQENSTGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLA 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 270 FMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNL 349
Cdd:PLN00110  315 EMLKNPSILKRAHEEMDQVIGRNRRLVESDLPKLPYLQAICKESFRKHPSTPLNLPRVSTQACEVNGYYIPKNTRLSVNI 394
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 350 YSVHFDEKYWRDPEVFHPERFLdsSGYFAKKEA------LVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFPHELV 423
Cdd:PLN00110  395 WAIGRDPDVWENPEEFRPERFL--SEKNAKIDPrgndfeLIPFGAGRRICAGTRMGIVLVEYILGTLVHSFDWKLPDGVE 472
                         330
                  ....*....|..
gi 1034571959 424 PDLKPRLGMTLQ 435
Cdd:PLN00110  473 LNMDEAFGLALQ 484
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
24-434 3.51e-29

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 119.54  E-value: 3.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  24 LDLGGISTVVLNGYDVVKECLVHQSEIFADRP-CLPLFMKMTKMGGLLNSRYGRGWVDHRRLAVNSF----RYfgygqKS 98
Cdd:PLN03112   70 LRLGSVDAITTDDPELIREILLRQDDVFASRPrTLAAVHLAYGCGDVALAPLGPHWKRMRRICMEHLlttkRL-----ES 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  99 FESKILEETKFFNDAI--ETYKGRPFDFKQLITNAVSNITNLIIFGERF-------TYEDTDFQHMI-ELFSenvelaAS 168
Cdd:PLN03112  145 FAKHRAEEARHLIQDVweAAQTGKPVNLREVLGAFSMNNVTRMLLGKQYfgaesagPKEAMEFMHIThELFR------LL 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 169 ASVFLYNAFP-WIGILPFGKHQQLFRNAAVVYDFLSRLIEK----ASVNRKPQLPQHFVDAYLDEmdQGKNDPSSTFSKE 243
Cdd:PLN03112  219 GVIYLGDYLPaWRWLDPYGCEKKMREVEKRVDEFHDKIIDEhrraRSGKLPGGKDMDFVDVLLSL--PGENGKEHMDDVE 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 244 nLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLG 323
Cdd:PLN03112  297 -IKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVGRNRMVQESDLVHLNYLRCVVRETFRMHPAGPFL 375
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 324 IFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGyfAKKEA-------LVPFSLGRRHCLGE 396
Cdd:PLN03112  376 IPHESLRATTINGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERHWPAEG--SRVEIshgpdfkILPFSAGKRKCPGA 453
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1034571959 397 HLARMEMFLFFTALLQRFHLHFPHELVP---DLKPRLGMTL 434
Cdd:PLN03112  454 PLGVTMVLMALARLFHCFDWSPPDGLRPediDTQEVYGMTM 494
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
185-436 1.24e-28

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: 116.50  E-value: 1.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 185 FGKHQQLFRNA------AVVYDFLSRLIEKASVNRKPQLPQHFVDAY--LDEMDQGKNDPsstfsKE--NLIFSVgelII 254
Cdd:cd11063   155 LGKLLWLLRDKkfreacKVVHRFVDPYVDKALARKEESKDEESSDRYvfLDELAKETRDP-----KElrDQLLNI---LL 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 255 AGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVV 334
Cdd:cd11063   227 AGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPVPLNSRVAVRDTTLP 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 335 RG--------YSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSGyfaKKEALVPFSLGRRHCLGEHLARMEMFL 405
Cdd:cd11063   307 RGggpdgkspIFVPKGTRVLYSVYAMHRRKDIWgPDAEEFRPERWEDLKR---PGWEYLPFNGGPRICLGQQFALTEASY 383
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034571959 406 FFTALLQRFHlHFPHELVPDLKPRLGMTLQP 436
Cdd:cd11063   384 VLVRLLQTFD-RIESRDVRPPEERLTLTLSN 413
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
170-430 5.59e-28

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: 115.07  E-value: 5.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 170 SVFLYNAFpwigILPFGKHQQLFRNAA-VVYDFLSRLIE--KASVNRKPQLPQHFVDAYLDEMD---QGKNDPSSTFSKE 243
Cdd:cd20678   163 NFFYHNDF----IYKLSPHGRRFRRACqLAHQHTDKVIQqrKEQLQDEGELEKIKKKRHLDFLDillFAKDENGKSLSDE 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 244 NLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPlG 323
Cdd:cd20678   239 DLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVP-G 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 324 IFHATSED-AVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARME 402
Cdd:cd20678   318 ISRELSKPvTFPDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSSKRHSHAFLPFSAGPRNCIGQQFAMNE 397
                         250       260
                  ....*....|....*....|....*...
gi 1034571959 403 MFLFFTALLQRFHLHFPHELVPDLKPRL 430
Cdd:cd20678   398 MKVAVALTLLRFELLPDPTRIPIPIPQL 425
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
228-438 5.83e-28

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: 114.72  E-value: 5.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 228 EMDQGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLImgPNGKPSWDDKCKMPYTE 307
Cdd:cd11045   195 ALCRAEDEDGDRFSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLAL--GKGTLDYEDLGQLEVTD 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 308 AVLHEVLRFCNIVPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAK-KEALVPF 386
Cdd:cd11045   273 WVFKEALRLVPPVPT-LPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEDKVhRYAWAPF 351
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034571959 387 SLGRRHCLGEHLARMEMFLFFTALLQRFHLhfphELVPDLKPRLGMTLQPQP 438
Cdd:cd11045   352 GGGAHKCIGLHFAGMEVKAILHQMLRRFRW----WSVPGYYPPWWQSPLPAP 399
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
68-435 6.17e-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: 115.00  E-value: 6.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  68 GLLNSRyGRGWVDHRRLAVNSF---RYFGYGQKSFESKILEETKFFNDAIETyKGRPFDFKQLITNAVSNITNLIIFGer 144
Cdd:cd11064    50 GIFNVD-GELWKFQRKTASHEFssrALREFMESVVREKVEKLLVPLLDHAAE-SGKVVDLQDVLQRFTFDVICKIAFG-- 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 145 FTYEDTDFQHMIELFSENVElAASASVFLYNAFP--------WIGIlpfGKHQQLFRNAAVVYDFLSRLI-----EKASV 211
Cdd:cd11064   126 VDPGSLSPSLPEVPFAKAFD-DASEAVAKRFIVPpwlwklkrWLNI---GSEKKLREAIRVIDDFVYEVIsrrreELNSR 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 212 NRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENLIfsvgELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEID--LIM 289
Cdd:cd11064   202 EEENNVREDLLSRFLASEEEEGEPVSDKFLRDIVL----NFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKskLPK 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 290 GPNGK---PSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVF 365
Cdd:cd11064   278 LTTDEsrvPTYEELKKLVYLHAALSESLRLYPPVPFDSKEAVNDDVLPDGTFVKKGTRIVYSIYAMGRMESIWgEDALEF 357
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034571959 366 HPERFLDSSGYFAKKEAL--VPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLhfphELVP--DLKPRLGMTLQ 435
Cdd:cd11064   358 KPERWLDEDGGLRPESPYkfPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDF----KVVPghKVEPKMSLTLH 427
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
255-437 6.85e-28

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: 114.85  E-value: 6.85e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 255 AGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRfcnIVPLGIF--HATSEDA 332
Cdd:cd20639   243 AGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDHLPKLKTLGMILNETLR---LYPPAVAtiRRAKKDV 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 333 VVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSGYFAKKE-ALVPFSLGRRHCLGEHLARMEMFLFFTAL 410
Cdd:cd20639   320 KLGGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADGVARAAKHPlAFIPFGLGPRTCVGQNLAILEAKLTLAVI 399
                         170       180
                  ....*....|....*....|....*....
gi 1034571959 411 LQRFHLHfpheLVPDL--KPRLGMTLQPQ 437
Cdd:cd20639   400 LQRFEFR----LSPSYahAPTVLMLLQPQ 424
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
219-416 8.26e-28

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


Pssm-ID: 410738 [Multi-domain]  Cd Length: 419  Bit Score: 114.52  E-value: 8.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 219 QHFVDAYLDEMDQGKNDP-------SSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGP 291
Cdd:cd20645   194 KHCIDKRLQRYSQGPANDflcdiyhDNELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPA 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 292 NGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFL 371
Cdd:cd20645   274 NQTPRAEDLKNMPYLKACLKESMRLTPSVPF-TSRTLDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWL 352
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034571959 372 DssgyfaKKEAL-----VPFSLGRRHCLGEHLARMEMFLFFTALLQRFHL 416
Cdd:cd20645   353 Q------EKHSInpfahVPFGIGKRMCIGRRLAELQLQLALCWIIQKYQI 396
PLN02687 PLN02687
flavonoid 3'-monooxygenase
252-435 1.43e-27

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 114.91  E-value: 1.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 252 LIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSED 331
Cdd:PLN02687  305 LFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEE 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 332 AVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFL---DSSGYFAKKE--ALVPFSLGRRHCLGEHLArMEMFLF 406
Cdd:PLN02687  385 CEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLpggEHAGVDVKGSdfELIPFGAGRRICAGLSWG-LRMVTL 463
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1034571959 407 FTA-LLQRFHLHFPHELVPD---LKPRLGMTLQ 435
Cdd:PLN02687  464 LTAtLVHAFDWELADGQTPDklnMEEAYGLTLQ 496
PLN02655 PLN02655
ent-kaurene oxidase
235-395 3.66e-27

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 113.30  E-value: 3.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 235 DPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNgKPSWDDKCKMPYTEAVLHEVL 314
Cdd:PLN02655  253 SEATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYREIREVCGDE-RVTEEDLPNLPYLNAVFHETL 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 315 RFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCL 394
Cdd:PLN02655  332 RKYSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLGEKYESADMYKTMAFGAGKRVCA 411

                  .
gi 1034571959 395 G 395
Cdd:PLN02655  412 G 412
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
126-434 1.27e-25

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: 108.22  E-value: 1.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 126 QLITNAVSNItnliIFGERFTYEDTDFQHMIELFSENVELaasasvFLYNaFPWIgilpfgkhqqLFRNAAVVYDFLSRL 205
Cdd:cd11040   130 DVLTRATTEA----LFGPKLPELDPDLVEDFWTFDRGLPK------LLLG-LPRL----------LARKAYAARDRLLKA 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 206 IEKASVNRKPQLPQ----------HFVDAYLDEMDQGKNDPSstfskenlifsvgeLIIAGTETTTNVLRWAILFMALYP 275
Cdd:cd11040   189 LEKYYQAAREERDDgselirarakVLREAGLSEEDIARAELA--------------LLWAINANTIPAAFWLLAHILSDP 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 276 NIQGQVQKEIDLIMGPNGKPSW-----DDKCKMPYTEAVLHEVLRFCNIvPLGIFHATSEDAVVRGYSIPKGTTVITNLY 350
Cdd:cd11040   255 ELLERIREEIEPAVTPDSGTNAildltDLLTSCPLLDSTYLETLRLHSS-STSVRLVTEDTVLGGGYLLRKGSLVMIPPR 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 351 SVHFDEKYW-RDPEVFHPERFLD---SSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHfPHELVPDL 426
Cdd:cd11040   334 LLHMDPEIWgPDPEEFDPERFLKkdgDKKGRGLPGAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFDVE-PVGGGDWK 412

                  ....*...
gi 1034571959 427 KPRLGMTL 434
Cdd:cd11040   413 VPGMDESP 420
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
118-437 1.64e-25

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: 108.54  E-value: 1.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 118 KGRPFDFKQLITNAVSNITNLIIFGERFT-------------------------------YEDTDFQHMIELFSENVELA 166
Cdd:cd20622   105 KGRPFSAKEDIHHAALDAIWAFAFGINFDasqtrpqlelleaedstilpagldepvefpeAPLPDELEAVLDLADSVEKS 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 167 ASASV-----FLYNAFPWIgilpfgkhqqlFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQ------GKND 235
Cdd:cd20622   185 IKSPFpklshWFYRNQPSY-----------RRAAKIKDDFLQREIQAIARSLERKGDEGEVRSAVDHMVRrelaaaEKEG 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 236 PSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGP----NGKPSWDD--KCKMPYTEAV 309
Cdd:cd20622   254 RKPDYYSQVIHDELFGYLIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAHPEavaeGRLPTAQEiaQARIPYLDAV 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 310 LHEVLRFCNIVPLGIFHATsEDAVVRGYSIPKGTTVITNLY-------SVHFDE--------------KYW--RDPEVFH 366
Cdd:cd20622   334 IEEILRCANTAPILSREAT-VDTQVLGYSIPKGTNVFLLNNgpsylspPIEIDEsrrssssaakgkkaGVWdsKDIADFD 412
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 367 PERFLDSSGYFAKKE------ALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHfphelvpDLKPRL-------GMT 433
Cdd:cd20622   413 PERWLVTDEETGETVfdpsagPTLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFELL-------PLPEALsgyeaidGLT 485

                  ....
gi 1034571959 434 LQPQ 437
Cdd:cd20622   486 RMPK 489
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
241-433 3.07e-25

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


Pssm-ID: 410741 [Multi-domain]  Cd Length: 430  Bit Score: 107.15  E-value: 3.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 241 SKENL----IFS-VGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLR 315
Cdd:cd20648   226 AREKLpmksIYGnVTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLR 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 316 FCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFL---DSSGYFAKkealVPFSLGRRH 392
Cdd:cd20648   306 LYPVIPGNARVIPDRDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLgkgDTHHPYAS----LPFGFGKRS 381
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034571959 393 CLGEHLARMEMFLfftaLLQRFHLHFPHELVPDLKPRLGMT 433
Cdd:cd20648   382 CIGRRIAELEVYL----ALARILTHFEVRPEPGGSPVKPMT 418
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
245-437 3.78e-25

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: 106.76  E-value: 3.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 245 LIFSVGELI-------IAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFC 317
Cdd:cd20641   229 RKMSIDEIIdecktffFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDADTLSKLKLMNMVLMETLRLY 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 318 NIVPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSGYFAKK-EALVPFSLGRRHCLG 395
Cdd:cd20641   309 GPVIN-IARRASEDMKLGGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGVSRAATHpNALLSFSLGPRACIG 387
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034571959 396 EHLARMEMFLFFTALLQRFHLHFPHELVPdlKPRLGMTLQPQ 437
Cdd:cd20641   388 QNFAMIEAKTVLAMILQRFSFSLSPEYVH--APADHLTLQPQ 427
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
240-422 1.39e-24

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


Pssm-ID: 410723 [Multi-domain]  Cd Length: 373  Bit Score: 104.43  E-value: 1.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 240 FSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpngkpswddkckmpyteaVLHEVLRFCNI 319
Cdd:cd20630   199 LSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAEPELLRN------------------ALEEVLRWDNF 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 320 VPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERfldssgyfaKKEALVPFSLGRRHCLGEHLA 399
Cdd:cd20630   261 GKMGTARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRR---------DPNANIAFGYGPHFCIGAALA 331
                         170       180
                  ....*....|....*....|...
gi 1034571959 400 RMEMFLFFTALLQRFhlhFPHEL 422
Cdd:cd20630   332 RLELELAVSTLLRRF---PEMEL 351
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
200-419 2.41e-24

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: 104.29  E-value: 2.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 200 DFLSRLIEKAsVNRKPQLPqhfVDAYLDEMDQGkndpssTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQG 279
Cdd:cd20615   181 AFNLKIYNRA-RQRGQSTP---IVKLYEAVEKG------DITFEELLQTLDEMLFANLDVTTGVLSWNLVFLAANPAVQE 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 280 QVQKEIdLIMGPNGKPSWDDKC--KMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSV-HFDE 356
Cdd:cd20615   251 KLREEI-SAAREQSGYPMEDYIlsTDTLLAYCVLESLRLRPLLAFSVPESSPTDKIIGGYRIPANTPVVVDTYALnINNP 329
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034571959 357 KYWRDPEVFHPERFLDSSGYFAKKeALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFP 419
Cdd:cd20615   330 FWGPDGEAYRPERFLGISPTDLRY-NFWRFGFGPRKCLGQHVADVILKALLAHLLEQYELKLP 391
PLN02971 PLN02971
tryptophan N-hydroxylase
121-419 3.90e-24

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 105.12  E-value: 3.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 121 PFDFKQLITNAVSNITNLIIFGERFTYEDT---------DFQHMIELFSEnveLAASASVFLYNAFPWIGILPFGKHQQL 191
Cdd:PLN02971  197 PVDLRFVTRHYCGNAIKRLMFGTRTFSEKTepdggptleDIEHMDAMFEG---LGFTFAFCISDYLPMLTGLDLNGHEKI 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 192 FRNAAVVYD-----FLSRLIEKASVNRKPQLpQHFVDAYLDEMDQGKNdpsSTFSKENLIFSVGELIIAGTETTTNVLRW 266
Cdd:PLN02971  274 MRESSAIMDkyhdpIIDERIKMWREGKRTQI-EDFLDIFISIKDEAGQ---PLLTADEIKPTIKELVMAAPDNPSNAVEW 349
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 267 AILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVI 346
Cdd:PLN02971  350 AMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVL 429
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034571959 347 TNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKE---ALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFP 419
Cdd:PLN02971  430 LSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTEndlRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLA 505
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
101-414 5.52e-24

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: 103.10  E-value: 5.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 101 SKILEETKFFNDAIETY--KGRPFDFKQLITNAVSNITNLIIFGERFtyedtDFQHMIELFSENVELAASASVFLYNAFP 178
Cdd:cd11051    78 PTILDEVEIFAAILRELaeSGEVFSLEELTTNLTFDVIGRVTLDIDL-----HAQTGDNSLLTALRLLLALYRSLLNPFK 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 179 WIGILpfgKHQQLFRNAAVVYDFLSRLIEKAsvnrkpqlpqhfvdayldemdqgkndpsstFSKENLIFSVGELIIAGTE 258
Cdd:cd11051   153 RLNPL---RPLRRWRNGRRLDRYLKPEVRKR------------------------------FELERAIDQIKTFLFAGHD 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 259 TTTNVLRWAilFMAL--YPNIQGQVQKEIDLIMGPNGKPSW-----DDKC--KMPYTEAVLHEVLRfcnIVPLGI----- 324
Cdd:cd11051   200 TTSSTLCWA--FYLLskHPEVLAKVRAEHDEVFGPDPSAAAellreGPELlnQLPYTTAVIKETLR---LFPPAGtarrg 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 325 ---FHATSEDavvrGYSIP-KGTTVITNLYSVHFDEKYWRDPEVFHPERFL--DSSGYFAKKEALVPFSLGRRHCLGEHL 398
Cdd:cd11051   275 ppgVGLTDRD----GKEYPtDGCIVYVCHHAIHRDPEYWPRPDEFIPERWLvdEGHELYPPKSAWRPFERGPRNCIGQEL 350
                         330
                  ....*....|....*.
gi 1034571959 399 ARMEMFLFFTALLQRF 414
Cdd:cd11051   351 AMLELKIILAMTVRRF 366
PLN02738 PLN02738
carotene beta-ring hydroxylase
221-433 2.50e-23

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 102.68  E-value: 2.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 221 FVDAYLDEMD--------QGKNDPSSTFSKENLIfsvgELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpN 292
Cdd:PLN02738  364 FHEEYMNERDpsilhfllASGDDVSSKQLRDDLM----TMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLG-D 438
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 293 GKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDaVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERF-L 371
Cdd:PLN02738  439 RFPTIEDMKKLKYTTRVINESLRLYPQPPVLIRRSLEND-MLGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWpL 517
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034571959 372 DSSGYFAKKE--ALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLhfphELVPDLKPrLGMT 433
Cdd:PLN02738  518 DGPNPNETNQnfSYLPFGGGPRKCVGDMFASFENVVATAMLVRRFDF----QLAPGAPP-VKMT 576
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
26-446 5.15e-23

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


Pssm-ID: 410751 [Multi-domain]  Cd Length: 444  Bit Score: 100.90  E-value: 5.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  26 LGGISTVVLNGYDVVKECLVHQSEIFADRPclpLFMKMTKM-GGLLN---SRYGRGWVDHRRLAVN------SFRYFgYG 95
Cdd:cd20658     8 LGNTHVIPVTCPKIAREILRKQDAVFASRP---LTYATEIIsGGYKTtviSPYGEQWKKMRKVLTTelmspkRHQWL-HG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  96 QKSFESKILEeTKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTD--------FQHMIELFSE-NVELA 166
Cdd:cd20658    84 KRTEEADNLV-AYVYNMCKKSNGGGLVNVRDAARHYCGNVIRKLMFGTRYFGKGMEdggpgleeVEHMDAIFTAlKCLYA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 167 ASASVFLynafPWIGILPFGKHQQLFRNA-AVVYDFLSRLIE---KASVNRKPQLPQHFVDAYLDEMDQGKNdpsSTFSK 242
Cdd:cd20658   163 FSISDYL----PFLRGLDLDGHEKIVREAmRIIRKYHDPIIDeriKQWREGKKKEEEDWLDVFITLKDENGN---PLLTP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 243 ENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPL 322
Cdd:cd20658   236 DEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQESDIPNLNYVKACAREAFRLHPVAPF 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 323 GIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEA---LVPFSLGRRHCLGEHLA 399
Cdd:cd20658   316 NVPHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSEVTLTEPdlrFISFSTGRRGCPGVKLG 395
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1034571959 400 RMEMFLFFTALLQRFHLHFPHELVP-DLKPRLGMTLQPQPYLICAERR 446
Cdd:cd20658   396 TAMTVMLLARLLQGFTWTLPPNVSSvDLSESKDDLFMAKPLVLVAKPR 443
PLN02936 PLN02936
epsilon-ring hydroxylase
237-433 5.41e-23

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 101.02  E-value: 5.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 237 SSTFSKENLIfsvgELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpNGKPSWDDKCKMPYTEAVLHEVLRF 316
Cdd:PLN02936  275 SSVQLRDDLL----SMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQ-GRPPTYEDIKELKYLTRCINESMRL 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 317 CNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERF-LD-------SSGYfakkeALVPFSL 388
Cdd:PLN02936  350 YPHPPVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFdLDgpvpnetNTDF-----RYIPFSG 424
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034571959 389 GRRHCLGEHLARMEMFLFFTALLQRFHLhfphELVPDLKprLGMT 433
Cdd:PLN02936  425 GPRKCVGDQFALLEAIVALAVLLQRLDL----ELVPDQD--IVMT 463
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
192-430 9.16e-22

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: 97.07  E-value: 9.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 192 FRNA-AVVYDFLSRLIEKasvnRKPQLPQHFVDAYLDEMDQGKN------------DPSSTFSKENLIFSVGELIIAGTE 258
Cdd:cd20679   183 FRRAcRLVHDFTDAVIQE----RRRTLPSQGVDDFLKAKAKSKTldfidvlllskdEDGKELSDEDIRAEADTFMFEGHD 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 259 TTTNVLRWAILFMALYPNIQGQVQKEI-DLIMGPNGKP-SWDDKCKMPYTEAVLHEVLRFCNIVPLgIFHATSEDAVVR- 335
Cdd:cd20679   259 TTASGLSWILYNLARHPEYQERCRQEVqELLKDREPEEiEWDDLAQLPFLTMCIKESLRLHPPVTA-ISRCCTQDIVLPd 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 336 GYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFH 415
Cdd:cd20679   338 GRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGRSPLAFIPFSAGPRNCIGQTFAMAEMKVVLALTLLRFR 417
                         250
                  ....*....|....*
gi 1034571959 416 LhFPHELVPDLKPRL 430
Cdd:cd20679   418 V-LPDDKEPRRKPEL 431
PLN00168 PLN00168
Cytochrome P450; Provisional
11-414 1.16e-21

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 97.33  E-value: 1.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  11 LNVVFLLFSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLL-NSRYGRGWVDHRRLAV--- 86
Cdd:PLN00168   63 LRRLIARYGPVVSLRVGSRLSVFVADRRLAHAALVERGAALADRPAVASSRLLGESDNTItRSSYGPVWRLLRRNLVaet 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  87 ---NSFRYFGYGQKSFESKILEetKFFNDAIETYKGRPFDFKQLitnAVSNITNLIIFGERFtyeDTDFQHMIELFSENV 163
Cdd:PLN00168  143 lhpSRVRLFAPARAWVRRVLVD--KLRREAEDAAAPRVVETFQY---AMFCLLVLMCFGERL---DEPAVRAIAAAQRDW 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 164 ELAASASVFLYNAFPWIGILPF-GKHQQLFRNAAVVYDFLSRLIEkASVNRKPQLPQH---------FVDAYLDEMDQGK 233
Cdd:PLN00168  215 LLYVSKKMSVFAFFPAVTKHLFrGRLQKALALRRRQKELFVPLID-ARREYKNHLGQGgeppkkettFEHSYVDTLLDIR 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 234 --NDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPN-GKPSWDDKCKMPYTEAVL 310
Cdd:PLN00168  294 lpEDGDRALTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDDqEEVSEEDVHKMPYLKAVV 373
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 311 HEVLRfcnIVPLGIF---HATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFL--------DSSGyfAK 379
Cdd:PLN00168  374 LEGLR---KHPPAHFvlpHKAAEDMEVGGYLIPKGATVNFMVAEMGRDEREWERPMEFVPERFLaggdgegvDVTG--SR 448
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1034571959 380 KEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRF 414
Cdd:PLN00168  449 EIRMMPFGVGRRICAGLGIAMLHLEYFVANMVREF 483
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
231-437 3.17e-21

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: 95.42  E-value: 3.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 231 QGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpNGKPSWDDKCKMPYTEAVL 310
Cdd:cd20642   221 KEQGNKNGGMSTEDVIEECKLFYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFG-NNKPDFEGLNHLKVVTMIL 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 311 HEVLRfcnIVPLGIF--HATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSGYFAKKE-ALVPF 386
Cdd:cd20642   300 YEVLR---LYPPVIQltRAIHKDTKLGDLTLPAGVQVSLPILLVHRDPELWgDDAKEFNPERFAEGISKATKGQvSYFPF 376
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034571959 387 SLGRRHCLGEHLARMEMFLFFTALLQRFHLhfphELVPDLK--PRLGMTLQPQ 437
Cdd:cd20642   377 GWGPRICIGQNFALLEAKMALALILQRFSF----ELSPSYVhaPYTVLTLQPQ 425
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
99-438 3.81e-21

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


Pssm-ID: 410667 [Multi-domain]  Cd Length: 441  Bit Score: 95.05  E-value: 3.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  99 FESKILEETkffNDAIETYKG-----RPFDFKQLITNAVSNITNLIIFGERFTYeDTDFQHMIELFSENVELAASASVFL 173
Cdd:cd11041    83 LLPDLQEEL---RAALDEELGsctewTEVNLYDTVLRIVARVSARVFVGPPLCR-NEEWLDLTINYTIDVFAAAAALRLF 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 174 YNAF-PWIG-ILPFGKHQQLFRNAAVVydFLSRLIEKASVNRKPQLPQHFVDA--YLdeMDQGKNDPSSTFskENLIFSV 249
Cdd:cd11041   159 PPFLrPLVApFLPEPRRLRRLLRRARP--LIIPEIERRRKLKKGPKEDKPNDLlqWL--IEAAKGEGERTP--YDLADRQ 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 250 GELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKpsWDDKC--KMPYTEAVLHEVLRFCNIVPLGIF-H 326
Cdd:cd11041   233 LALSFAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGG--WTKAAlnKLKKLDSFMKESQRLNPLSLVSLRrK 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 327 ATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERF--LDSSGYFAKKEALV-------PFSLGRRHCLGEH 397
Cdd:cd11041   311 VLKDVTLSDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFyrLREQPGQEKKHQFVstspdflGFGHGRHACPGRF 390
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1034571959 398 LARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQPQP 438
Cdd:cd11041   391 FASNEIKLILAHLLLNYDFKLPEGGERPKNIWFGEFIMPDP 431
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
177-416 4.72e-21

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: 94.73  E-value: 4.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 177 FPWIgilpFGKHQqlfRNAAVVYDFLSRLIEKasvnRKPQLPQhfVDAYLDEMD--------QGKNDpsstFSKENLIFS 248
Cdd:cd20616   166 ISWL----YKKYE---KAVKDLKDAIEILIEQ----KRRRIST--AEKLEDHMDfatelifaQKRGE----LTAENVNQC 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 249 VGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHAT 328
Cdd:cd20616   229 VLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLG-ERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRKAL 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 329 SEDaVVRGYSIPKGTTVITNLYSVHFDEkYWRDPEVFHPERFLDS--SGYFAkkealvPFSLGRRHCLGEHLARMEMFLF 406
Cdd:cd20616   308 EDD-VIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENFEKNvpSRYFQ------PFGFGPRSCVGKYIAMVMMKAI 379
                         250
                  ....*....|
gi 1034571959 407 FTALLQRFHL 416
Cdd:cd20616   380 LVTLLRRFQV 389
PLN02302 PLN02302
ent-kaurenoic acid oxidase
255-416 2.67e-20

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 93.24  E-value: 2.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 255 AGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMG---PNGKP-SWDDKCKMPYTEAVLHEVLRFCNIVPLgIFHATSE 330
Cdd:PLN02302  298 AGHESSGHLTMWATIFLQEHPEVLQKAKAEQEEIAKkrpPGQKGlTLKDVRKMEYLSQVIDETLRLINISLT-VFREAKT 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 331 DAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFldsSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTAL 410
Cdd:PLN02302  377 DVEVNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRW---DNYTPKAGTFLPFGLGSRLCPGNDLAKLEISIFLHHF 453

                  ....*.
gi 1034571959 411 LQRFHL 416
Cdd:PLN02302  454 LLGYRL 459
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
171-414 4.74e-20

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: 92.21  E-value: 4.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 171 VFLYNAFPWI-----GILPFGKHQ-------QLFRNAAVVY----------DFLsRLIEKASVNRKPQLPQHF---VDAY 225
Cdd:cd20649   154 LILFLAFPFImiplaRILPNKSRDelnsfftQCIRNMIAFRdqqspeerrrDFL-QLMLDARTSAKFLSVEHFdivNDAD 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 226 LD-------EMDQGKNDPSSTFSKENLIFSVGE---LIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKP 295
Cdd:cd20649   233 ESaydghpnSPANEQTKPSKQKRMLTEDEIVGQafiFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMV 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 296 SWDDKCKMPYTEAVLHEVLRfcnIVPLGIFHA--TSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDS 373
Cdd:cd20649   313 DYANVQELPYLDMVIAETLR---MYPPAFRFAreAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAE 389
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1034571959 374 sgyfAKKE----ALVPFSLGRRHCLGEHLARMEMFLFFTALLQRF 414
Cdd:cd20649   390 ----AKQRrhpfVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRF 430
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
243-437 6.94e-20

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: 91.32  E-value: 6.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 243 ENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIdlimGPNGKPSWDDKCKM----PYTEAVLHEVLRFcN 318
Cdd:cd20643   233 EDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEV----LAARQEAQGDMVKMlksvPLLKAAIKETLRL-H 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 319 IVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDS-SGYFAKkealVPFSLGRRHCLGEH 397
Cdd:cd20643   308 PVAVSLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKdITHFRN----LGFGFGPRQCLGRR 383
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1034571959 398 LARMEMFLFFTALLQRFHLHFPHElvPDLKPRLGMTLQPQ 437
Cdd:cd20643   384 IAETEMQLFLIHMLENFKIETQRL--VEVKTTFDLILVPE 421
PLN02290 PLN02290
cytokinin trans-hydroxylase
68-438 9.80e-20

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 91.41  E-value: 9.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  68 GLLNSRyGRGWVDHRRLAVNSFryFGYGQKSFESKILEETKFFNDAIETYKGRP---FDFKQLITNAVSNITNLIIFGER 144
Cdd:PLN02290  143 GLLMAN-GADWYHQRHIAAPAF--MGDRLKGYAGHMVECTKQMLQSLQKAVESGqteVEIGEYMTRLTADIISRTEFDSS 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 145 FTYEDTDFQHMIELFSenveLAASASVFLYnaFPWIGILPFGKHQQLFRNAAVVYDFLSRLIEK----ASVNRKPQLPQH 220
Cdd:PLN02290  220 YEKGKQIFHLLTVLQR----LCAQATRHLC--FPGSRFFPSKYNREIKSLKGEVERLLMEIIQSrrdcVEIGRSSSYGDD 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 221 FVDAYLDEMDQGKNDPSSTfskeNLIFSVGE---LIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNgKPSW 297
Cdd:PLN02290  294 LLGMLLNEMEKKRSNGFNL----NLQLIMDEcktFFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGE-TPSV 368
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 298 DDKCKMPYTEAVLHEVLRF---CNIVPLGIFhatsEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFldS 373
Cdd:PLN02290  369 DHLSKLTLLNMVINESLRLyppATLLPRMAF----EDIKLGDLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRF--A 442
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034571959 374 SGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFPHE------LVPDLKPRLGMTLQPQP 438
Cdd:PLN02290  443 GRPFAPGRHFIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSFTISDNyrhapvVVLTIKPKYGVQVCLKP 513
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
252-430 1.68e-19

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: 89.58  E-value: 1.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 252 LIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLImgPNgkpswddkckmpyteaVLHEVLRFCNIVPLgIFHATSED 331
Cdd:cd11032   206 LLIAGHETTTNLLGNAVLCLDEDPEVAARLRADPSLI--PG----------------AIEEVLRYRPPVQR-TARVTTED 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 332 AVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERflDSSGYFAkkealvpFSLGRRHCLGEHLARMEMFLFFTALL 411
Cdd:cd11032   267 VELGGVTIPAGQLVIAWLASANRDERQFEDPDTFDIDR--NPNPHLS-------FGHGIHFCLGAPLARLEARIALEALL 337
                         170       180
                  ....*....|....*....|
gi 1034571959 412 QRfhlhFPH-ELVPDLKPRL 430
Cdd:cd11032   338 DR----FPRiRVDPDVPLEL 353
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
179-414 6.04e-19

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: 88.19  E-value: 6.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 179 WIGI---LPFGKHQQLFrNAAVV--YDFLSRLIEKASVNRKPQLPQHFVDAYLDEmdqgkndpsSTFSKENLIFSVGELI 253
Cdd:cd11038   154 DLGLafgLEVKDHLPRI-EAAVEelYDYADALIEARRAEPGDDLISTLVAAEQDG---------DRLSDEELRNLIVALL 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 254 IAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLImgpngkpswddkckmpytEAVLHEVLRFCNIVPLGIFHATsEDAV 333
Cdd:cd11038   224 FAGVDTTRNQLGLAMLTFAEHPDQWRALREDPELA------------------PAAVEEVLRWCPTTTWATREAV-EDVE 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 334 VRGYSIPKGTTVITNLYSVHfdekywRDPEVFHPERFlDSSgyfAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQR 413
Cdd:cd11038   285 YNGVTIPAGTVVHLCSHAAN------RDPRVFDADRF-DIT---AKRAPHLGFGGGVHHCLGAFLARAELAEALTVLARR 354

                  .
gi 1034571959 414 F 414
Cdd:cd11038   355 L 355
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
252-417 2.95e-18

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 86.91  E-value: 2.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 252 LIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKP---SWDDKCKMPYTEAVLHEVLRFCNIVPLgIFHAT 328
Cdd:PLN02196  272 VIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRKDKEEGeslTWEDTKKMPLTSRVIQETLRVASILSF-TFREA 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 329 SEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSsgyfAKKEALVPFSLGRRHCLGEHLARMEMFLFFT 408
Cdd:PLN02196  351 VEDVEYEGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRFEVA----PKPNTFMPFGNGTHSCPGNELAKLEISVLIH 426

                  ....*....
gi 1034571959 409 ALLQRFHLH 417
Cdd:PLN02196  427 HLTTKYRWS 435
PLN02500 PLN02500
cytochrome P450 90B1
238-415 4.92e-18

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 86.07  E-value: 4.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 238 STFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKE---IDLIMGPNG--KPSWDDKCKMPYTEAVLHE 312
Cdd:PLN02500  273 SNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEhleIARAKKQSGesELNWEDYKKMEFTQCVINE 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 313 VLRFCNIVPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLD-------SSGYFAKKEALVP 385
Cdd:PLN02500  353 TLRLGNVVRF-LHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQnnnrggsSGSSSATTNNFMP 431
                         170       180       190
                  ....*....|....*....|....*....|
gi 1034571959 386 FSLGRRHCLGEHLARMEMFLFFTALLQRFH 415
Cdd:PLN02500  432 FGGGPRLCAGSELAKLEMAVFIHHLVLNFN 461
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
204-414 7.08e-18

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 85.56  E-value: 7.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 204 RLIEKASVNRKPQLPQHFVDAYLDEmdqGKNDPSSTFSKENLIfsvgELIIAGTETTTNVLRWAILFMALYP-------- 275
Cdd:PLN03141  218 RRAMKNKEEDETGIPKDVVDVLLRD---GSDELTDDLISDNMI----DMMIPGEDSVPVLMTLAVKFLSDCPvalqqlte 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 276 -NIQGQVQKEIdlimgpNGKP-SWDDKCKMPYTEAVLHEVLRFCNIVpLGIFHATSEDAVVRGYSIPKGTTVITNLYSVH 353
Cdd:PLN03141  291 eNMKLKRLKAD------TGEPlYWTDYMSLPFTQNVITETLRMGNII-NGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVH 363
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034571959 354 FDEKYWRDPEVFHPERFLDSSgyfAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRF 414
Cdd:PLN03141  364 LDEENYDNPYQFNPWRWQEKD---MNNSSFTPFGGGQRLCPGLDLARLEASIFLHHLVTRF 421
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
226-428 6.74e-17

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: 82.10  E-value: 6.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 226 LDEMDQGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCkmPY 305
Cdd:cd20614   190 VAALIRARDDNGAGLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAAGDVPRTPAELRRF--PL 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 306 TEAVLHEVLRFCNIVPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDssgyfaKKEALVP 385
Cdd:cd20614   268 AEALFRETLRLHPPVPF-VFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWLG------RDRAPNP 340
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034571959 386 -----FSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFPHELVPDLKP 428
Cdd:cd20614   341 vellqFGGGPHFCLGYHVACVELVQFIVALARELGAAGIRPLLVGVLP 388
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
235-432 7.41e-17

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


Pssm-ID: 410657 [Multi-domain]  Cd Length: 380  Bit Score: 81.84  E-value: 7.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 235 DPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLImgpngkpswddkckmpytEAVLHEVL 314
Cdd:cd11031   197 DDDDRLSEEELVTLAVGLLVAGHETTASQIGNGVLLLLRHPEQLARLRADPELV------------------PAAVEELL 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 315 RFcniVPL----GIFHATSEDAVVRGYSIPKGTTVITNLYSVHfdekywRDPEVF-HPERFLdssgyFAKKEAL-VPFSL 388
Cdd:cd11031   259 RY---IPLgaggGFPRYATEDVELGGVTIRAGEAVLVSLNAAN------RDPEVFpDPDRLD-----LDREPNPhLAFGH 324
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1034571959 389 GRRHCLGEHLARMEMFLFFTALLQRF---HLHFPHElvpDLKPRLGM 432
Cdd:cd11031   325 GPHHCLGAPLARLELQVALGALLRRLpglRLAVPEE---ELRWREGL 368
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
219-425 9.60e-17

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: 81.91  E-value: 9.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 219 QHFVDAYLDEMDQGKNDPSStFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKP-SW 297
Cdd:cd11082   196 HEILEEIKEAEEEGEPPPPH-SSDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDEPPlTL 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 298 DDKCKMPYTEAVLHEVLRFCNIVPLgIFHATSEDAVV-RGYSIPKGTTVITNLYSVHFDEkyWRDPEVFHPERFLDSSG- 375
Cdd:cd11082   275 DLLEEMKYTRQVVKEVLRYRPPAPM-VPHIAKKDFPLtEDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPERQe 351
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034571959 376 -YFAKKEALVpFSLGRRHCLGEHLARMEMFLfFTALLQRfHLHFPHELVPD 425
Cdd:cd11082   352 dRKYKKNFLV-FGAGPHQCVGQEYAINHLML-FLALFST-LVDWKRHRTPG 399
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
214-412 1.07e-16

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: 81.78  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 214 KPQLPQHFVDAY--LDEMDQGKNDPsstFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGP 291
Cdd:cd20638   201 REDTEQQCKDALqlLIEHSRRNGEP---LNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQEKGLL 277
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 292 NGKPSWDDKCKM------PYTEAVLHEVLRFCNIVPLGiFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVF 365
Cdd:cd20638   278 STKPNENKELSMevleqlKYTGCVIKETLRLSPPVPGG-FRVALKTFELNGYQIPKGWNVIYSICDTHDVADIFPNKDEF 356
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1034571959 366 HPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQ 412
Cdd:cd20638   357 NPDRFMSPLPEDSSRFSFIPFGGGSRSCVGKEFAKVLLKIFTVELAR 403
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
251-437 1.12e-16

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: 81.81  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 251 ELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRfcnIVPLGIF--HAT 328
Cdd:cd20644   239 ELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALTELPLLKAALKETLR---LYPVGITvqRVP 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 329 SEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALvPFSLGRRHCLGEHLARMEMFLFFT 408
Cdd:cd20644   316 SSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGSGRNFKHL-AFGFGMRQCLGRRLAEAEMLLLLM 394
                         170       180
                  ....*....|....*....|....*....
gi 1034571959 409 ALLQRFHLHFPHElvPDLKPRLGMTLQPQ 437
Cdd:cd20644   395 HVLKNFLVETLSQ--EDIKTVYSFILRPE 421
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
240-415 2.30e-16

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: 80.34  E-value: 2.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 240 FSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLImgpngkPSWddkckmpyteavLHEVLRFCNI 319
Cdd:cd11078   205 LTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLRADPSLI------PNA------------VEETLRYDSP 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 320 VPlGIFHATSEDAVVRGYSIPKGTTVITNLYSVHfdekywRDPEVF-HPERF-LDSSGyfAKKeaLVPFSLGRRHCLGEH 397
Cdd:cd11078   267 VQ-GLRRTATRDVEIGGVTIPAGARVLLLFGSAN------RDERVFpDPDRFdIDRPN--ARK--HLTFGHGIHFCLGAA 335
                         170
                  ....*....|....*...
gi 1034571959 398 LARMEMFLFFTALLQRFH 415
Cdd:cd11078   336 LARMEARIALEELLRRLP 353
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
193-414 9.26e-16

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


Pssm-ID: 410656 [Multi-domain]  Cd Length: 381  Bit Score: 78.33  E-value: 9.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 193 RNAAVVYDFLSRLIEkasvnRKPQLPQhfvDAYLDEM--DQGKNDPsstFSKENLIFSVGELIIAGTETTTNVLRWAILF 270
Cdd:cd11030   166 AAGAELRAYLDELVA-----RKRREPG---DDLLSRLvaEHGAPGE---LTDEELVGIAVLLLVAGHETTANMIALGTLA 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 271 MALYPNIQGQVQKEIDLImgpngkPSWDDkckmpyteavlhEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLY 350
Cdd:cd11030   235 LLEHPEQLAALRADPSLV------PGAVE------------ELLRYLSIVQDGLPRVATEDVEIGGVTIRAGEGVIVSLP 296
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034571959 351 SVHfdekywRDPEVF-HPERF---LDSSGYFAkkealvpFSLGRRHCLGEHLARMEMFLFFTALLQRF 414
Cdd:cd11030   297 AAN------RDPAVFpDPDRLditRPARRHLA-------FGHGVHQCLGQNLARLELEIALPTLFRRF 351
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
255-437 1.11e-15

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: 78.61  E-value: 1.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 255 AGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpNGKPSWDDKCKMPYTEAVLHEVLRfcnIVPLGIFHA--TSEDA 332
Cdd:cd20640   241 AGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCK-GGPPDADSLSRMKTVTMVIQETLR---LYPPAAFVSreALRDM 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 333 VVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDS-SGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTAL 410
Cdd:cd20640   317 KLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSNGvAAACKPPHSYMPFGAGARTCLGQNFAMAELKVLVSLI 396
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034571959 411 LQRFHL----HFPHElvpdlkPRLGMTLQPQ 437
Cdd:cd20640   397 LSKFSFtlspEYQHS------PAFRLIVEPE 421
PLN03018 PLN03018
homomethionine N-hydroxylase
17-446 1.22e-15

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 78.90  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  17 LFSKIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKM----TKMGgllNSRYGRGWVDHRRLAVNSFRYF 92
Cdd:PLN03018   74 LKTDIACFNFAGTHTITINSDEIAREAFRERDADLADRPQLSIMETIgdnyKSMG---TSPYGEQFMKMKKVITTEIMSV 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  93 GYGQKSFESKILEETKFFNDAIETY-KGRPFDFKQLITNAVSNITNLIIFGERFTYEDTdfqhmieLFSENVELAASASV 171
Cdd:PLN03018  151 KTLNMLEAARTIEADNLIAYIHSMYqRSETVDVRELSRVYGYAVTMRMLFGRRHVTKEN-------VFSDDGRLGKAEKH 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 172 FLYNAFPWIGILPF-----------------GKHQQLFRNAAVVYDFLSRLI-EKASVNRK---PQLPQHFVDAYLDEMD 230
Cdd:PLN03018  224 HLEVIFNTLNCLPGfspvdyverwlrgwnidGQEERAKVNVNLVRSYNNPIIdERVELWREkggKAAVEDWLDTFITLKD 303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 231 QGKNdpsSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVL 310
Cdd:PLN03018  304 QNGK---YLVTPDEIKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGKDRLVQESDIPNLNYLKACC 380
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 311 HEVLRF---CNIVPLgifHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGyFAKKEALV--- 384
Cdd:PLN03018  381 RETFRIhpsAHYVPP---HVARQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHLQGDG-ITKEVTLVete 456
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034571959 385 ----PFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFPHELVP-DLKPRLGMTLQPQPYLICAERR 446
Cdd:PLN03018  457 mrfvSFSTGRRGCVGVKVGTIMMVMMLARFLQGFNWKLHQDFGPlSLEEDDASLLMAKPLLLSVEPR 523
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
252-414 1.38e-15

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: 77.73  E-value: 1.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 252 LIIAGTETTTNVLrwAILFMAL--YPNIQGQVQKEIDLImgpngkpswddkckmpytEAVLHEVLRFCNIVpLGIFHATS 329
Cdd:cd20629   200 LLPAGSDTTYRAL--ANLLTLLlqHPEQLERVRRDRSLI------------------PAAIEEGLRWEPPV-ASVPRMAL 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 330 EDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERfldssgyfAKKEALVpFSLGRRHCLGEHLARMEMFLFFTA 409
Cdd:cd20629   259 RDVELDGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDIDR--------KPKPHLV-FGGGAHRCLGEHLARVELREALNA 329

                  ....*
gi 1034571959 410 LLQRF 414
Cdd:cd20629   330 LLDRL 334
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
198-424 1.44e-15

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: 77.96  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 198 VYDFLSRLIEkasvnRKPQLPQhfvDAYLDEMDQGkNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPni 277
Cdd:cd11029   174 LVDYLAELVA-----RKRAEPG---DDLLSALVAA-RDEGDRLSEEELVSTVFLLLVAGHETTVNLIGNGVLALLTHP-- 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 278 qGQ---VQKEIDLImgpngkpswddkckmpytEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHF 354
Cdd:cd11029   243 -DQlalLRADPELW------------------PAAVEELLRYDGPVALATLRFATEDVEVGGVTIPAGEPVLVSLAAANR 303
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034571959 355 DEKYWRDPEVFHPERflDSSGYFAkkealvpFSLGRRHCLGEHLARMEMFLFFTALLQRF-HLHF---PHELVP 424
Cdd:cd11029   304 DPARFPDPDRLDITR--DANGHLA-------FGHGIHYCLGAPLARLEAEIALGALLTRFpDLRLavpPDELRW 368
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
266-417 1.01e-13

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: 72.34  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 266 WAILFMALYPNIQGQVQKEIDLIMGPNGKPSW----DDKCKMPYTEAVLHEVLRFCNivPLGIFHATSEDAVVRGYSIPK 341
Cdd:cd20635   232 WTLAFILSHPSVYKKVMEEISSVLGKAGKDKIkiseDDLKKMPYIKRCVLEAIRLRS--PGAITRKVVKPIKIKNYTIPA 309
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034571959 342 GTTVITNLYSVHFDEKYWRDPEVFHPERFLDSS-GYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLH 417
Cdd:cd20635   310 GDMLMLSPYWAHRNPKYFPDPELFKPERWKKADlEKNVFLEGFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKYDFT 386
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
252-414 1.23e-13

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: 71.81  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 252 LIIAGTETTTNVLRWAILFMALYPniqGQVQKeidLIMGPngkpswddkckmPYTEAVLHEVLRFCNIVPLGIFHATsED 331
Cdd:cd20625   209 LLVAGHETTVNLIGNGLLALLRHP---EQLAL---LRADP------------ELIPAAVEELLRYDSPVQLTARVAL-ED 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 332 AVVRGYSIPKGTTVITNLYSVHfdekywRDPEVF-HPERF-LDSSGyfakkEALVPFSLGRRHCLGEHLARMEMFLFFTA 409
Cdd:cd20625   270 VEIGGQTIPAGDRVLLLLGAAN------RDPAVFpDPDRFdITRAP-----NRHLAFGAGIHFCLGAPLARLEAEIALRA 338

                  ....*
gi 1034571959 410 LLQRF 414
Cdd:cd20625   339 LLRRF 343
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
250-413 1.24e-13

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: 72.18  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 250 GELI---IAGTETTtNVLR------WAILFMAL----YPNIQGQVQKEIDlimgpngkpswddkckmPYTEAVLHEVLRF 316
Cdd:cd11067   214 GELLperVAAVELL-NLLRptvavaRFVTFAALalheHPEWRERLRSGDE-----------------DYAEAFVQEVRRF 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 317 CNIVPL--GIfhaTSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYfakKEALVP-----FSLG 389
Cdd:cd11067   276 YPFFPFvgAR---ARRDFEWQGYRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERFLGWEGD---PFDFIPqgggdHATG 349
                         170       180
                  ....*....|....*....|....*..
gi 1034571959 390 RRhCLGEHL--ARMEMFL-FFTALLQR 413
Cdd:cd11067   350 HR-CPGEWItiALMKEALrLLARRDYY 375
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
253-417 2.60e-13

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 71.65  E-value: 2.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 253 IIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGK-PSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSED 331
Cdd:PLN02426  302 LLAGRDTVASALTSFFWLLSKHPEVASAIREEADRVMGPNQEaASFEEMKEMHYLHAALYESMRLFPPVQFDSKFAAEDD 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 332 AVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSGYFAKKEALVP-FSLGRRHCLGEHLARMEMFLFFTA 409
Cdd:PLN02426  382 VLPDGTFVAKGTRVTYHPYAMGRMERIWgPDCLEFKPERWLKNGVFVPENPFKYPvFQAGLRVCLGKEMALMEMKSVAVA 461

                  ....*...
gi 1034571959 410 LLQRFHLH 417
Cdd:PLN02426  462 VVRRFDIE 469
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
183-434 5.12e-13

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 70.58  E-value: 5.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 183 LPFGKHQQLFRNAAVVYDFLSRLIE--KASV-NRKPQLPQHFVDAYLDEMDQGKnDPSSTFSKENLIFSVGELIIAGTET 259
Cdd:PLN03195  229 LNIGSEALLSKSIKVVDDFTYSVIRrrKAEMdEARKSGKKVKHDILSRFIELGE-DPDSNFTDKSLRDIVLNFVIAGRDT 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 260 TTNVLRWAILFMALYPNIQGQVQKEIDLI-------MGPNGKPS-------------WDDKCKMPYTEAVLHEVLRFCNI 319
Cdd:PLN03195  308 TATTLSWFVYMIMMNPHVAEKLYSELKALekerakeEDPEDSQSfnqrvtqfaglltYDSLGKLQYLHAVITETLRLYPA 387
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 320 VPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLdSSGYF--AKKEALVPFSLGRRHCLGE 396
Cdd:PLN03195  388 VPQDPKGILEDDVLPDGTKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERWI-KDGVFqnASPFKFTAFQAGPRICLGK 466
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034571959 397 HLARMEMFLfFTALLQRFhlhFPHELVP--DLKPRLGMTL 434
Cdd:PLN03195  467 DSAYLQMKM-ALALLCRF---FKFQLVPghPVKYRMMTIL 502
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
252-414 1.34e-12

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: 68.71  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 252 LIIAGTETTTNVLRWAILFMALYPniqGQVQKeidLIMGPNGKPSwddkckmpyteAVlHEVLRFcnIVPLGIF--HATs 329
Cdd:cd11033   217 LAVAGNETTRNSISGGVLALAEHP---DQWER---LRADPSLLPT-----------AV-EEILRW--ASPVIHFrrTAT- 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 330 EDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERfldssgyfaKKEALVPFSLGRRHCLGEHLARMEMFLFFTA 409
Cdd:cd11033   276 RDTELGGQRIRAGDKVVLWYASANRDEEVFDDPDRFDITR---------SPNPHLAFGGGPHFCLGAHLARLELRVLFEE 346

                  ....*
gi 1034571959 410 LLQRF 414
Cdd:cd11033   347 LLDRV 351
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
202-417 1.76e-12

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


Pssm-ID: 410720 [Multi-domain]  Cd Length: 394  Bit Score: 68.69  E-value: 1.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 202 LSRLIEKASVNRKPQLPQHFVdaYLDEMDQGkNDPSSTFSKENLIFSvgeliIAGTETTTNVLRWAILFMALYPNIQGQV 281
Cdd:cd20627   168 MESVLKKVIKERKGKNFSQHV--FIDSLLQG-NLSEQQVLEDSMIFS-----LAGCVITANLCTWAIYFLTTSEEVQKKL 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 282 QKEIDLIMGpNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRgYSIPKGTTVITNLYSVHFDEKYWRD 361
Cdd:cd20627   240 YKEVDQVLG-KGPITLEKIEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQ-HIIPKETLVLYALGVVLQDNTTWPL 317
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034571959 362 PEVFHPERFLDSSgyFAKKEALVPFSlGRRHCLGEHLARMEMFLFFTALLQRFHLH 417
Cdd:cd20627   318 PYRFDPDRFDDES--VMKSFSLLGFS-GSQECPELRFAYMVATVLLSVLVRKLRLL 370
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
244-415 1.07e-11

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: 66.13  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 244 NLIFSVGeliIAGTETTTNVLRWAILFMALY-PNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPL 322
Cdd:cd11071   228 NLLFMLG---FNAFGGFSALLPSLLARLGLAgEELHARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPPVPL 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 323 gIFHATSEDAVV----RGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGyfaKKEALVPFSLGR-------- 390
Cdd:cd11071   305 -QYGRARKDFVIeshdASYKIKKGELLVGYQPLATRDPKVFDNPDEFVPDRFMGEEG---KLLKHLIWSNGPeteeptpd 380
                         170       180
                  ....*....|....*....|....*.
gi 1034571959 391 -RHCLGEHLARMEMFLFFTALLQRFH 415
Cdd:cd11071   381 nKQCPGKDLVVLLARLFVAELFLRYD 406
PLN02774 PLN02774
brassinosteroid-6-oxidase
241-414 1.80e-11

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 65.95  E-value: 1.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 241 SKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKE---IDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFC 317
Cdd:PLN02774  261 TDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKALQELRKEhlaIRERKRPEDPIDWNDYKSMRFTRAVIFETSRLA 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 318 NIVPlGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSgyFAKKEALVPFSLGRRHCLGEH 397
Cdd:PLN02774  341 TIVN-GVLRKTTQDMELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWLDKS--LESHNYFFLFGGGTRLCPGKE 417
                         170
                  ....*....|....*..
gi 1034571959 398 LARMEMFLFFTALLQRF 414
Cdd:PLN02774  418 LGIVEISTFLHYFVTRY 434
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
164-400 1.97e-11

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


Pssm-ID: 410729 [Multi-domain]  Cd Length: 431  Bit Score: 65.63  E-value: 1.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 164 ELAASASVFLYNAFPWIGILPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKE 243
Cdd:cd20636   151 YLAKTFEQLVENLFSLPLDVPFSGLRKGIKARDILHEYMEKAIEEKLQRQQAAEYCDALDYMIHSARENGKELTMQELKE 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 244 NLIfsvgELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEID---LIMGPNGKP---SWDDKCKMPYTEAVLHEVLRFC 317
Cdd:cd20636   231 SAV----ELIFAAFSTTASASTSLVLLLLQHPSAIEKIRQELVshgLIDQCQCCPgalSLEKLSRLRYLDCVVKEVLRLL 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 318 NIVPLGIFHA--TSEdavVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERF-----LDSSGYFakkeALVPFSLGR 390
Cdd:cd20636   307 PPVSGGYRTAlqTFE---LDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFgvereESKSGRF----NYIPFGGGV 379
                         250
                  ....*....|
gi 1034571959 391 RHCLGEHLAR 400
Cdd:cd20636   380 RSCIGKELAQ 389
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
145-435 3.53e-11

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: 64.87  E-value: 3.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 145 FTYEDTDFQHMIELFSENVElaasasvflyNAFPWIGILPFGKhqqlFRNAAVVYDFLSRLIEKAsVNRKPQLPQ--HFV 222
Cdd:cd20637   141 FRVSEEELSHLFSVFQQFVE----------NVFSLPLDLPFSG----YRRGIRARDSLQKSLEKA-IREKLQGTQgkDYA 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 223 DAyLDEMDQGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEID----LIMGP--NGKPS 296
Cdd:cd20637   206 DA-LDILIESAKEHGKELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREELRsngiLHNGClcEGTLR 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 297 WDDKCKMPYTEAVLHEVLRFCNIVPLGiFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERF-----L 371
Cdd:cd20637   285 LDTISSLKYLDCVIKEVLRLFTPVSGG-YRTALQTFELDGFQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRFgqersE 363
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 372 DSSGYFakkeALVPFSLGRRHCLGEHLARMEMFLFFTAL--LQRFHLH---FPH-ELVPDLKPRLGMTLQ 435
Cdd:cd20637   364 DKDGRF----HYLPFGGGVRTCLGKQLAKLFLKVLAVELasTSRFELAtrtFPRmTTVPVVHPVDGLRVK 429
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
249-413 4.42e-11

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: 64.14  E-value: 4.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 249 VGELIIAGTETTTNVLRWAILFMALYPNiQGQVQKEidlimgpngKPSwddkcKMPyteAVLHEVLRFCNivPLGIFH-A 327
Cdd:cd11037   207 MRDYLSAGLDTTISAIGNALWLLARHPD-QWERLRA---------DPS-----LAP---NAFEEAVRLES--PVQTFSrT 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 328 TSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERflDSSGYfakkealVPFSLGRRHCLGEHLARMEMFLFF 407
Cdd:cd11037   267 TTRDTELAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITR--NPSGH-------VGFGHGVHACVGQHLARLEGEALL 337

                  ....*.
gi 1034571959 408 TALLQR 413
Cdd:cd11037   338 TALARR 343
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
240-403 6.12e-11

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: 63.65  E-value: 6.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 240 FSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLImgpngkpswddkckmpytEAVLHEVLRFCNI 319
Cdd:cd11080   189 LSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPEQLAAVRADRSLV------------------PRAIAETLRYHPP 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 320 VPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERF-LDSSGYFAKKEALVPFSLGRRHCLGEHL 398
Cdd:cd11080   251 VQL-IPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHREdLGIRSAFSGAADHLAFGSGRHFCVGAAL 329

                  ....*
gi 1034571959 399 ARMEM 403
Cdd:cd11080   330 AKREI 334
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
171-403 1.65e-10

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 62.72  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 171 VFLYNAFPWIGIlpfGKHQQLFRNAAVVYDFLSRLI---EKASVNRKPQLPQHfVDA--YLDEMDQGKND---PSSTFSK 242
Cdd:PLN02169  227 VILWRLQNWIGI---GLERKMRTALATVNRMFAKIIssrRKEEISRAETEPYS-KDAltYYMNVDTSKYKllkPKKDKFI 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 243 ENLIFSvgeLIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIdlimgpNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPL 322
Cdd:PLN02169  303 RDVIFS---LVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEI------NTKFDNEDLEKLVYLHAALSESMRLYPPLPF 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 323 GIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSGYFAKKEA--LVPFSLGRRHCLGEHLA 399
Cdd:PLN02169  374 NHKAPAKPDVLPSGHKVDAESKIVICIYALGRMRSVWgEDALDFKPERWISDNGGLRHEPSykFMAFNSGPRTCLGKHLA 453

                  ....
gi 1034571959 400 RMEM 403
Cdd:PLN02169  454 LLQM 457
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
263-439 1.81e-10

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: 62.09  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 263 VLRwAILFMALYPNIQGQVQKEIdliMGPNGKPSWddkckmPYTEAVLHEVLRFCNIVPLgIFHATSEDAVVRGYSIPKG 342
Cdd:cd20624   211 LLR-ALALLAAHPEQAARAREEA---AVPPGPLAR------PYLRACVLDAVRLWPTTPA-VLRESTEDTVWGGRTVPAG 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 343 TTVITnlysvhFDEKYWRDPEV------FHPERFLDssGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRfhl 416
Cdd:cd20624   280 TGFLI------FAPFFHRDDEAlpfadrFVPEIWLD--GRAQPDEGLVPFSAGPARCPGENLVLLVASTALAALLRR--- 348
                         170       180
                  ....*....|....*....|...
gi 1034571959 417 hfpHELVPDLKPRLGmTLQPQPY 439
Cdd:cd20624   349 ---AEIDPLESPRSG-PGEPLPG 367
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
96-413 1.67e-08

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


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 56.19  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959  96 QKSFESKILEETKFFNDAIETYKGRPF-----------DFKQL-ITNAVSNITNLIIFGERFTYEDTDFQHMIELFSEnv 163
Cdd:cd20612    62 QRELMRKALYSPDLAKDVVFFYELQTRallvessrlggSGGQVdIVRDVANLVPARFCADLFGLPLKTKENPRGGYTE-- 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 164 elaASASVFLYNAFPWI-GILPFGKHQQLFRNAAVVYDFLSRLIEKAsvnrkpqlpqhfVDAYLdemdqgkndpsstfsK 242
Cdd:cd20612   140 ---AELYRALAAIFAYIfFDLDPAKSFQLRRAAQAAAARLGALLDAA------------VADEV---------------R 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 243 ENLIFsvgeLIIAGTETTTNVLRWAILFMALYPNiqgqvQKEIDLIMGPNGKPSWDDKCKMPYteaVLhEVLRFCNIVPl 322
Cdd:cd20612   190 DNVLG----TAVGGVPTQSQAFAQILDFYLRRPG-----AAHLAEIQALARENDEADATLRGY---VL-EALRLNPIAP- 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 323 GIFHATSEDAVV-----RGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSsgYFAkkealvpFSLGRRHCLGEH 397
Cdd:cd20612   256 GLYRRATTDTTVadgggRTVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDRPLES--YIH-------FGHGPHQCLGEE 326
                         330
                  ....*....|....*.
gi 1034571959 398 LARMEMFLFFTALLQR 413
Cdd:cd20612   327 IARAALTEMLRVVLRL 342
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
252-414 2.82e-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: 55.42  E-value: 2.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 252 LIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLImgpngkpswddkckmpyTEAVlHEVLRFCNIVpLGIFHATSED 331
Cdd:cd11034   198 LLLGGTDTTSSALSGALLWLAQHPEDRRRLIADPSLI-----------------PNAV-EEFLRFYSPV-AGLARTVTQE 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 332 AVVRGYSIPKGTTVITNLYSVHfdekywRDPEVF-HPERF-LDSsgyFAKKEalVPFSLGRRHCLGEHLARMEMFLFFTA 409
Cdd:cd11034   259 VEVGGCRLKPGDRVLLAFASAN------RDEEKFeDPDRIdIDR---TPNRH--LAFGSGVHRCLGSHLARVEARVALTE 327

                  ....*
gi 1034571959 410 LLQRF 414
Cdd:cd11034   328 VLKRI 332
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
252-433 4.54e-08

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: 54.90  E-value: 4.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 252 LIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMgpngkpswddkckmpyteAVLHEVLRFCNIVPLGifHATSED 331
Cdd:cd11035   198 LFLAGLDTVASALGFIFRHLARHPEDRRRLREDPELIP------------------AAVEELLRRYPLVNVA--RIVTRD 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 332 AVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERfldssgyfaKKEALVPFSLGRRHCLGEHLARMEMFLFftalL 411
Cdd:cd11035   258 VEFHGVQLKAGDMVLLPLALANRDPREFPDPDTVDFDR---------KPNRHLAFGAGPHRCLGSHLARLELRIA----L 324
                         170       180
                  ....*....|....*....|...
gi 1034571959 412 QRFHLHFPH-ELVPDLKPRLGMT 433
Cdd:cd11035   325 EEWLKRIPDfRLAPGAQPTYHGG 347
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
266-436 1.54e-07

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: 53.46  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 266 WAILFMALYPNIQGQVQKEIDLIMGPNGK---PSWD------DKCKMPYTEAVLHEVLRFC----NI-VPLGIFHATSED 331
Cdd:cd20632   237 WAMYYLLRHPEALAAVRDEIDHVLQSTGQelgPDFDihltreQLDSLVYLESAINESLRLSsasmNIrVVQEDFTLKLES 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 332 AvvRGYSIPKGTTVItnLY--SVHFDEKYWRDPEVFHPERFLDSSG---YFAK-----KEALVPFSLGRRHCLGEHLARM 401
Cdd:cd20632   317 D--GSVNLRKGDIVA--LYpqSLHMDPEIYEDPEVFKFDRFVEDGKkktTFYKrgqklKYYLMPFGSGSSKCPGRFFAVN 392
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034571959 402 EMFLFFTALLqrfhLHFPHELVPDLKP------RLGMTLQP 436
Cdd:cd20632   393 EIKQFLSLLL----LYFDLELLEEQKPpgldnsRAGLGILP 429
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
266-436 4.09e-06

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


Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 48.91  E-value: 4.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 266 WAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCK----------MPYTEAVLHEVLRFCNiVPLGIFHATSEDAVV- 334
Cdd:cd20631   249 WSLFYLLRCPEAMKAATKEVKRTLEKTGQKVSDGGNPivltreqlddMPVLGSIIKEALRLSS-ASLNIRVAKEDFTLHl 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 335 ---RGYSIPKGTTVItnLYS--VHFDEKYWRDPEVFHPERFLDSSG----YFAK-----KEALVPFSLGRRHCLGEHLAR 400
Cdd:cd20631   328 dsgESYAIRKDDIIA--LYPqlLHLDPEIYEDPLTFKYDRYLDENGkektTFYKngrklKYYYMPFGSGTSKCPGRFFAI 405
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1034571959 401 MEMFLFFTALLQRF--HLHFPHELVPDL-KPRLGM-TLQP 436
Cdd:cd20631   406 NEIKQFLSLMLCYFdmELLDGNAKCPPLdQSRAGLgILPP 445
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
308-414 2.13e-05

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


Pssm-ID: 410662 [Multi-domain]  Cd Length: 340  Bit Score: 46.33  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 308 AVLHEVLRFCNIVplgifHATS----EDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGyfakkeal 383
Cdd:cd11036   223 AAVAETLRYDPPV-----RLERrfaaEDLELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGRPTARSA-------- 289
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1034571959 384 vPFSLGRRHCLGEHLARMEMFLFFTALLQRF 414
Cdd:cd11036   290 -HFGLGRHACLGAALARAAAAAALRALAARF 319
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
266-437 3.74e-05

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


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 45.91  E-value: 3.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 266 WAILFMALYPNIQGQVQKEIDLIMGPNGKP-------SWDDKCKMPYTEAVLHEVLRFcNIVPLgIFHATSEDAVV---- 334
Cdd:cd20634   243 WLLLFLLKHPEAMAAVRGEIQRIKHQRGQPvsqtltiNQELLDNTPVFDSVLSETLRL-TAAPF-ITREVLQDMKLrlad 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 335 -RGYSIPKGTTVITNLY-SVHFDEKYWRDPEVFHPERFLDSSGY----FAKKEALV-----PFSLGRRHCLGEHLARMEM 403
Cdd:cd20634   321 gQEYNLRRGDRLCLFPFlSPQMDPEIHQEPEVFKYDRFLNADGTekkdFYKNGKRLkyynmPWGAGDNVCIGRHFAVNSI 400
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034571959 404 FLFFTALLQRFHLHF--PHELVPDLKP-RLGM-TLQPQ 437
Cdd:cd20634   401 KQFVFLILTHFDVELkdPEAEIPEFDPsRYGFgLLQPE 438
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
266-436 7.98e-05

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: 44.67  E-value: 7.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 266 WAILFMALYPNIQGQVQKEIDLIMGPNGK------PSWDDKCKM----PYTEAVLHEVLRFcNIVPLgIFHATSEDAVV- 334
Cdd:cd20633   246 WLLLYLLKHPEAMKAVREEVEQVLKETGQevkpggPLINLTRDMllktPVLDSAVEETLRL-TAAPV-LIRAVVQDMTLk 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 335 ----RGYSIPKGTTVITNLY-SVHFDEKYWRDPEVFHPERFLDSSGYFAK---------KEALVPFSLGRRHCLGEHLAR 400
Cdd:cd20633   324 mangREYALRKGDRLALFPYlAVQMDPEIHPEPHTFKYDRFLNPDGGKKKdfykngkklKYYNMPWGAGVSICPGRFFAV 403
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1034571959 401 MEMFLFFTALLQRFHLHF--PHELVPDLKP-RLGM-TLQP 436
Cdd:cd20633   404 NEMKQFVFLMLTYFDLELvnPDEEIPSIDPsRWGFgTMQP 443
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
307-413 1.06e-04

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: 44.27  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 307 EAVLHEVLR-------FCNIvplgifhaTSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERfldssgyfaK 379
Cdd:cd11079   228 PAAIDEILRlddpfvaNRRI--------TTRDVELGGRTIPAGSRVTLNWASANRDERVFGDPDEFDPDR---------H 290
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034571959 380 KEALVPFSLGRRHCLGEHLARMEMFLFFTALLQR 413
Cdd:cd11079   291 AADNLVYGRGIHVCPGAPLARLELRILLEELLAQ 324
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
312-403 7.15e-04

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


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 41.72  E-value: 7.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571959 312 EVLRFcnIVPLGIF-HATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHperfldssgYFAKKEALVPFSLGR 390
Cdd:cd11039   252 EGLRW--ISPIGMSpRRVAEDFEIRGVTLPAGDRVFLMFGSANRDEARFENPDRFD---------VFRPKSPHVSFGAGP 320
                          90
                  ....*....|...
gi 1034571959 391 RHCLGEHLARMEM 403
Cdd:cd11039   321 HFCAGAWASRQMV 333
 
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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