NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1488188862|ref|NP_001052|]
View 

thromboxane-A synthase isoform 1 [Homo sapiens]

Protein Classification

cytochrome P450( domain architecture ID 15335012)

cytochrome P450 catalyzes the oxidation of organic species by molecular oxygen, by the oxidative addition of atomic oxygen into an unactivated C-H or C-C bond; similar to Homo sapiens thromboxane-A synthase that catalyzes the conversion of prostaglandin H2 (PGH2) to thromboxane A2 (TXA2), a potent inducer of blood vessel constriction and platelet aggregation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
73-527 0e+00

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: 871.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  73 LYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSVADSVLFLRDKRWEEVRGALMSAFSPEKLNEMV 152
Cdd:cd20649     1 KYGPICGYYIGRRMFVVIAEPDMIKQVLVKDFNNFTNRMKANLITKPMSDSLLCLRDERWKRVRSILTPAFSAAKMKEMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 153 PLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFCIPRPILVLLLSF 232
Cdd:cd20649    81 PLINQACDVLLRNLKSYAESGNAFNIQRCYGCFTMDVVASVAFGTQVDSQKNPDDPFVKNCKRFFEFSFFRPILILFLAF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 233 PSIMVPLARILPNKNRDELNGFFNKLIRNVIALRDQQAAEERRRDFLQMVLDARHSASPMGVQDFDIVRDVFSSTGCKPN 312
Cdd:cd20649   161 PFIMIPLARILPNKSRDELNSFFTQCIRNMIAFRDQQSPEERRRDFLQLMLDARTSAKFLSVEHFDIVNDADESAYDGHP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 313 PS---RQHQPSPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCsLEEG 389
Cdd:cd20649   241 NSpanEQTKPSKQKRMLTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDYA-NVQE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 390 LPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTY 469
Cdd:cd20649   320 LPYLDMVIAETLRMYPPAFRFAREAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQRRHPFVY 399
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1488188862 470 LPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLESKSALGPKNGVY 527
Cdd:cd20649   400 LPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQACPETEIPLQLKSKSTLGPKNGVY 457
 
Name Accession Description Interval E-value
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
73-527 0e+00

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: 871.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  73 LYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSVADSVLFLRDKRWEEVRGALMSAFSPEKLNEMV 152
Cdd:cd20649     1 KYGPICGYYIGRRMFVVIAEPDMIKQVLVKDFNNFTNRMKANLITKPMSDSLLCLRDERWKRVRSILTPAFSAAKMKEMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 153 PLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFCIPRPILVLLLSF 232
Cdd:cd20649    81 PLINQACDVLLRNLKSYAESGNAFNIQRCYGCFTMDVVASVAFGTQVDSQKNPDDPFVKNCKRFFEFSFFRPILILFLAF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 233 PSIMVPLARILPNKNRDELNGFFNKLIRNVIALRDQQAAEERRRDFLQMVLDARHSASPMGVQDFDIVRDVFSSTGCKPN 312
Cdd:cd20649   161 PFIMIPLARILPNKSRDELNSFFTQCIRNMIAFRDQQSPEERRRDFLQLMLDARTSAKFLSVEHFDIVNDADESAYDGHP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 313 PS---RQHQPSPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCsLEEG 389
Cdd:cd20649   241 NSpanEQTKPSKQKRMLTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDYA-NVQE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 390 LPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTY 469
Cdd:cd20649   320 LPYLDMVIAETLRMYPPAFRFAREAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQRRHPFVY 399
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1488188862 470 LPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLESKSALGPKNGVY 527
Cdd:cd20649   400 LPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQACPETEIPLQLKSKSTLGPKNGVY 457
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
47-530 3.76e-94

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: 294.57  E-value: 3.76e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  47 PKPSPFIGNLTFFRQG--FWESQMELRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSVADS- 123
Cdd:pfam00067   4 PPPLPLFGNLLQLGRKgnLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRGPFl 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 124 ---VLFLRDKRWEEVRGALMSAF-SPEKLNeMVPLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPV 199
Cdd:pfam00067  84 gkgIVFANGPRWRQLRRFLTPTFtSFGKLS-FEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGERF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 200 DSWQAPEDP----FVKHCKRFFEFCIPRPILV--LLLSFPSimvPLARILpNKNRDELNGFFNKLIRNVIALRDQQaaEE 273
Cdd:pfam00067 163 GSLEDPKFLelvkAVQELSSLLSSPSPQLLDLfpILKYFPG---PHGRKL-KRARKKIKDLLDKLIEERRETLDSA--KK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 274 RRRDFLQMVLDARHSASPMGvqdfdivrdvfsstgckpnpsrqhqpspmarpLTVDEIVGQAFIFLIAGYEIITNTLSFA 353
Cdd:pfam00067 237 SPRDFLDALLLAKEEEDGSK--------------------------------LTDEELRATVLELFFAGTDTTSSTLSWA 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 354 TYLLATNPDCQEKLLREVDVFKEKHMAPEFCSLEEgLPYLDMVIAETLRMYPPA-FRFTREAAQDCEVLGQRIPAGAVLE 432
Cdd:pfam00067 285 LYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQN-MPYLDAVIKETLRLHPVVpLLLPREVTKDTVIPGYLIPKGTLVI 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 433 MAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPL 512
Cdd:pfam00067 364 VNLYALHRDPEVFPNPEEFDPERFLDENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPD 443
                         490
                  ....*....|....*...
gi 1488188862 513 QLESKSALGPKNGVYIKI 530
Cdd:pfam00067 444 IDETPGLLLPPKPYKLKF 461
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
59-501 1.14e-66

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: 220.92  E-value: 1.14e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  59 FRQGFWESQMELRKlYGPLCGYYLGRRMFIVISEPDMIKQVLV--ENFSNFTNRMASGLEFKSVADSVLFLRDKRWEEVR 136
Cdd:COG2124    17 FLRDPYPFYARLRE-YGPVFRVRLPGGGAWLVTRYEDVREVLRdpRTFSSDGGLPEVLRPLPLLGDSLLTLDGPEHTRLR 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 137 GALMSAFSPEKLNEMVPLISQACDLLLAHLkryaESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWqapeDPFVKHCKRF 216
Cdd:COG2124    96 RLVQPAFTPRRVAALRPRIREIADELLDRL----AARGPVDLVEEFARPLPVIVICELLGVPEEDR----DRLRRWSDAL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 217 FEFCIPRPILvlllsfpsimvPLARILpnKNRDELNGFFNKLIrnvialrdqqaaEERRR----DFLQMVLDARHsaspm 292
Cdd:COG2124   168 LDALGPLPPE-----------RRRRAR--RARAELDAYLRELI------------AERRAepgdDLLSALLAARD----- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 293 gvqdfdivrdvfssTGckpnpsrqhqpspmaRPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREvd 372
Cdd:COG2124   218 --------------DG---------------ERLSDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAE-- 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 373 vfkekhmapefcsleegLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFN 452
Cdd:COG2124   267 -----------------PELLPAAVEETLRLYPPVPLLPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFD 329
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1488188862 453 PERftaearqqhRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFR 501
Cdd:COG2124   330 PDR---------PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFP 369
PLN02290 PLN02290
cytokinin trans-hydroxylase
39-502 1.75e-32

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 130.70  E-value: 1.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  39 LEKLGLRHPKPSPFIGNLTFFRQGFWESQ-------------------MELRKLYGPLCGYYLGRRMFIVISEPDMIKQV 99
Cdd:PLN02290   39 MERQGVRGPKPRPLTGNILDVSALVSQSTskdmdsihhdivgrllphyVAWSKQYGKRFIYWNGTEPRLCLTETELIKEL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 100 LVEnFSNFTNRmaSGLEFKS----VADSVLFLRDKRWEEVRGALMSAFSPEKLNEMVPLISQACDLLLAHLKRYAESG-D 174
Cdd:PLN02290  119 LTK-YNTVTGK--SWLQQQGtkhfIGRGLLMANGADWYHQRHIAAPAFMGDRLKGYAGHMVECTKQMLQSLQKAVESGqT 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 175 AFDIQRCYCNYTTDVVASVAFGTPVDSWqapedpfvkhcKRFFEfciprpILVLLLSFPS-----IMVPLARILPNKNRD 249
Cdd:PLN02290  196 EVEIGEYMTRLTADIISRTEFDSSYEKG-----------KQIFH------LLTVLQRLCAqatrhLCFPGSRFFPSKYNR 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 250 E---LNGFFNKLIRNVIalrdqqaaeERRRDFLQMvldARHSASPMGVQDFdIVRDVFSSTGCKPNPSRQhqpspmarpL 326
Cdd:PLN02290  259 EiksLKGEVERLLMEII---------QSRRDCVEI---GRSSSYGDDLLGM-LLNEMEKKRSNGFNLNLQ---------L 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 327 TVDEIvgQAFIFliAGYEIITNTLSFATYLLATNPDCQEKLLREV-DVFKEKhmAPEFCSLEEgLPYLDMVIAETLRMYP 405
Cdd:PLN02290  317 IMDEC--KTFFF--AGHETTALLLTWTLMLLASNPTWQDKVRAEVaEVCGGE--TPSVDHLSK-LTLLNMVINESLRLYP 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 406 PAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHW-PSPETFNPERFTAEARQQHRPFtyLPFGAGPRSCLGVRL 484
Cdd:PLN02290  390 PATLLPRMAFEDIKLGDLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPFAPGRHF--IPFAAGPRNCIGQAF 467
                         490
                  ....*....|....*...
gi 1488188862 485 GLLEVKLTLLHVLHKFRF 502
Cdd:PLN02290  468 AMMEAKIILAMLISKFSF 485
 
Name Accession Description Interval E-value
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
73-527 0e+00

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: 871.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  73 LYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSVADSVLFLRDKRWEEVRGALMSAFSPEKLNEMV 152
Cdd:cd20649     1 KYGPICGYYIGRRMFVVIAEPDMIKQVLVKDFNNFTNRMKANLITKPMSDSLLCLRDERWKRVRSILTPAFSAAKMKEMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 153 PLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFCIPRPILVLLLSF 232
Cdd:cd20649    81 PLINQACDVLLRNLKSYAESGNAFNIQRCYGCFTMDVVASVAFGTQVDSQKNPDDPFVKNCKRFFEFSFFRPILILFLAF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 233 PSIMVPLARILPNKNRDELNGFFNKLIRNVIALRDQQAAEERRRDFLQMVLDARHSASPMGVQDFDIVRDVFSSTGCKPN 312
Cdd:cd20649   161 PFIMIPLARILPNKSRDELNSFFTQCIRNMIAFRDQQSPEERRRDFLQLMLDARTSAKFLSVEHFDIVNDADESAYDGHP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 313 PS---RQHQPSPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCsLEEG 389
Cdd:cd20649   241 NSpanEQTKPSKQKRMLTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDYA-NVQE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 390 LPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTY 469
Cdd:cd20649   320 LPYLDMVIAETLRMYPPAFRFAREAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQRRHPFVY 399
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1488188862 470 LPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLESKSALGPKNGVY 527
Cdd:cd20649   400 LPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQACPETEIPLQLKSKSTLGPKNGVY 457
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
74-527 0e+00

cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes vertebrate CYP3A subfamily enzymes and CYP5a1, and similar proteins. CYP5A1, also called thromboxane-A synthase, converts prostaglandin H2 into thromboxane A2, a biologically active metabolite of arachidonic acid. CYP3A enzymes are drug-metabolizing enzymes embedded in the endoplasmic reticulum, where they can catalyze a wide variety of biochemical reactions including hydroxylation, N-demethylation, O-dealkylation, S-oxidation, deamination, or epoxidation of substrates. The CYP3A-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410678 [Multi-domain]  Cd Length: 422  Bit Score: 572.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSVADSVLFLRDKRWEEVRGALMSAFSPEKLNEMVP 153
Cdd:cd11055     2 YGKVFGLYFGTIPVIVVSDPEMIKEILVKEFSNFTNRPLFILLDEPFDSSLLFLKGERWKRLRTTLSPTFSSGKLKLMVP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 154 LISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFCIPRPILVLLLSFP 233
Cdd:cd11055    82 IINDCCDELVEKLEKAAETGKPVDMKDLFQGFTLDVILSTAFGIDVDSQNNPDDPFLKAAKKIFRNSIIRLFLLLLLFPL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 234 SIMvpLARILPNKNRDELNGFFNKLIRNVIALRDQQAaEERRRDFLQMVLDARHSASPMGVqdfdivrdvfsstgckpnp 313
Cdd:cd11055   162 RLF--LFLLFPFVFGFKSFSFLEDVVKKIIEQRRKNK-SSRRKDLLQLMLDAQDSDEDVSK------------------- 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 314 srqhqpspmaRPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCSLEEgLPYL 393
Cdd:cd11055   220 ----------KKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSK-LKYL 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 394 DMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFG 473
Cdd:cd11055   289 DMVINETLRLYPPAFFISRECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKAKRHPYAYLPFG 368
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1488188862 474 AGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLESKSALGPKNGVY 527
Cdd:cd11055   369 AGPRNCIGMRFALLEVKLALVKILQKFRFVPCKETEIPLKLVGGATLSPKNGIY 422
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
74-527 3.85e-129

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: 383.43  E-value: 3.85e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMAS-GLEFKSVADSVLFLRDKRWEEVRGALMSAFSPEKLNEMV 152
Cdd:cd11056     2 GEPFVGIYLFRRPALLVRDPELIKQILVKDFAHFHDRGLYsDEKDDPLSANLFSLDGEKWKELRQKLTPAFTSGKLKNMF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 153 PLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFCIPRPI-LVLLLS 231
Cdd:cd11056    82 PLMVEVGDELVDYLKKQAEKGKELEIKDLMARYTTDVIASCAFGLDANSLNDPENEFREMGRRLFEPSRLRGLkFMLLFF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 232 FPSimvpLARILPNK-NRDELNGFFNKLIRNVIALRdqQAAEERRRDFLQMVLDARHSASPMGVQDFdivrdvfsstgck 310
Cdd:cd11056   162 FPK----LARLLRLKfFPKEVEDFFRKLVRDTIEYR--EKNNIVRNDFIDLLLELKKKGKIEDDKSE------------- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 311 pnpsrqhqpspmaRPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD-VFKEKHMAPEFCSLEEg 389
Cdd:cd11056   223 -------------KELTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDeVLEKHGGELTYEALQE- 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 390 LPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQR--IPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPF 467
Cdd:cd11056   289 MKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGTDvvIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKKKRHPY 368
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1488188862 468 TYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLESKSA-LGPKNGVY 527
Cdd:cd11056   369 TYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSSKTKIPLKLSPKSFvLSPKGGIW 429
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
74-529 3.35e-111

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: 337.08  E-value: 3.35e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLV-ENFSNFTNRMASGLEfKSVADSVLFLRDKRWEEVRGALMSAFSPEKLNEMV 152
Cdd:cd20650     2 YGKVWGIYDGRQPVLAITDPDMIKTVLVkECYSVFTNRRPFGPV-GFMKSAISIAEDEEWKRIRSLLSPTFTSGKLKEMF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 153 PLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFCIPRPILVLLLSF 232
Cdd:cd20650    81 PIIAQYGDVLVKNLRKEAEKGKPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLLKFDFLDPLFLSITVF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 233 PSimvpLARILPNKN-----RDELNgFFNKLIRNVIA--LRDQQaaeERRRDFLQMVLDARhsaspmgvqdfdivrdvfs 305
Cdd:cd20650   161 PF----LTPILEKLNisvfpKDVTN-FFYKSVKKIKEsrLDSTQ---KHRVDFLQLMIDSQ------------------- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 306 stgcKPNPSRQHqpspmaRPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCS 385
Cdd:cd20650   214 ----NSKETESH------KALSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDT 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 386 LEEgLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHR 465
Cdd:cd20650   284 VMQ-MEYLDMVVNETLRLFPIAGRLERVCKKDVEINGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDNID 362
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1488188862 466 PFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLESKSALGPKNGVYIK 529
Cdd:cd20650   363 PYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFKPCKETQIPLKLSLQGLLQPEKPIVLK 426
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
47-530 3.76e-94

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: 294.57  E-value: 3.76e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  47 PKPSPFIGNLTFFRQG--FWESQMELRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSVADS- 123
Cdd:pfam00067   4 PPPLPLFGNLLQLGRKgnLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRGPFl 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 124 ---VLFLRDKRWEEVRGALMSAF-SPEKLNeMVPLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPV 199
Cdd:pfam00067  84 gkgIVFANGPRWRQLRRFLTPTFtSFGKLS-FEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGERF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 200 DSWQAPEDP----FVKHCKRFFEFCIPRPILV--LLLSFPSimvPLARILpNKNRDELNGFFNKLIRNVIALRDQQaaEE 273
Cdd:pfam00067 163 GSLEDPKFLelvkAVQELSSLLSSPSPQLLDLfpILKYFPG---PHGRKL-KRARKKIKDLLDKLIEERRETLDSA--KK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 274 RRRDFLQMVLDARHSASPMGvqdfdivrdvfsstgckpnpsrqhqpspmarpLTVDEIVGQAFIFLIAGYEIITNTLSFA 353
Cdd:pfam00067 237 SPRDFLDALLLAKEEEDGSK--------------------------------LTDEELRATVLELFFAGTDTTSSTLSWA 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 354 TYLLATNPDCQEKLLREVDVFKEKHMAPEFCSLEEgLPYLDMVIAETLRMYPPA-FRFTREAAQDCEVLGQRIPAGAVLE 432
Cdd:pfam00067 285 LYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQN-MPYLDAVIKETLRLHPVVpLLLPREVTKDTVIPGYLIPKGTLVI 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 433 MAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPL 512
Cdd:pfam00067 364 VNLYALHRDPEVFPNPEEFDPERFLDENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPD 443
                         490
                  ....*....|....*...
gi 1488188862 513 QLESKSALGPKNGVYIKI 530
Cdd:pfam00067 444 IDETPGLLLPPKPYKLKF 461
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
75-528 8.87e-79

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: 253.60  E-value: 8.87e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  75 GPLCGYYLGRRMFIVISEPDMIKQVLvenfSNFTNrmasgLEfKS---------VADSVLFLRDKRWEEVRGALMSAFSP 145
Cdd:cd20628     1 GGVFRLWIGPKPYVVVTNPEDIEVIL----SSSKL-----IT-KSflydflkpwLGDGLLTSTGEKWRKRRKLLTPAFHF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 146 EKLNEMVPLISQACDLLLAHLKRYAEsGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEfCIPRPI 225
Cdd:cd20628    71 KILESFVEVFNENSKILVEKLKKKAG-GGEFDIFPYISLCTLDIICETAMGVKLNAQSNEDSEYVKAVKRILE-IILKRI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 226 LVLLLSFPSI--MVPLARILpNKNRDELNGFFNKLIRNVIALRDQQAAEE---------RRRDFLQMVLDARHSAspmgv 294
Cdd:cd20628   149 FSPWLRFDFIfrLTSLGKEQ-RKALKVLHDFTNKVIKERREELKAEKRNSeeddefgkkKRKAFLDLLLEAHEDG----- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 295 qdfdivrdvfsstgckpnpsrqhqpspmaRPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD-V 373
Cdd:cd20628   223 -----------------------------GPLTDEDIREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDeI 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 374 FKEKHMAPEFCSLEEgLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNP 453
Cdd:cd20628   274 FGDDDRRPTLEDLNK-MKYLERVIKETLRLYPSVPFIGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDP 352
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1488188862 454 ERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQvPLQLESKSALGPKNGVYI 528
Cdd:cd20628   353 DRFLPENSAKRHPYAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFRVLPVPPGE-DLKLIAEIVLRSKNGIRV 426
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
75-528 1.82e-73

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: 239.02  E-value: 1.82e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  75 GPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTnRMASGLEFKSVADSVLFLRD-KRWEEVRGALMSAFSPEKLNEMVP 153
Cdd:cd20620     1 GDVVRLRLGPRRVYLVTHPDHIQHVLVTNARNYV-KGGVYERLKLLLGNGLLTSEgDLWRRQRRLAQPAFHRRRIAAYAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 154 LISQACDLLLAHLKRYAESGdAFDIQRCYCNYTTDVVASVAFGTPVDSwQAPEdpfVKHCkrfFEFCIPRpilVLLLSFP 233
Cdd:cd20620    80 AMVEATAALLDRWEAGARRG-PVDVHAEMMRLTLRIVAKTLFGTDVEG-EADE---IGDA---LDVALEY---AARRMLS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 234 SIMVPLARILP-----NKNRDELNGFFNKLIRnvialrDQQAAEERRRDFLQMVLDARHSAspmgvqdfdivrdvfssTG 308
Cdd:cd20620   149 PFLLPLWLPTPanrrfRRARRRLDEVIYRLIA------ERRAAPADGGDLLSMLLAARDEE-----------------TG 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 309 ckpnpsrqhqpSPMARPLTVDEIVgqafIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD-VFKEKhmAPEFCSLE 387
Cdd:cd20620   206 -----------EPMSDQQLRDEVM----TLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDrVLGGR--PPTAEDLP 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 388 EgLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPF 467
Cdd:cd20620   269 Q-LPYTEMVLQESLRLYPPAWIIGREAVEDDEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREAARPRY 347
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1488188862 468 TYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVplQLESKSALGPKNGVYI 528
Cdd:cd20620   348 AYFPFGGGPRICIGNHFAMMEAVLLLATIAQRFRLRLVPGQPV--EPEPLITLRPKNGVRM 406
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
75-526 2.16e-73

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: 238.18  E-value: 2.16e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  75 GPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSV-ADSVLFLRDKRWEEVRGALMSAFSPEKLNEMVP 153
Cdd:cd00302     1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFlGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 154 LISQACDLLLAHLKRYAESGDAF--DIQRcycnYTTDVVASVAFGTPVDswqAPEDPFVKHCKRFFEFCIPRPILVLLLS 231
Cdd:cd00302    81 VIREIARELLDRLAAGGEVGDDVadLAQP----LALDVIARLLGGPDLG---EDLEELAELLEALLKLLGPRLLRPLPSP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 232 fpsimvplarilpnknrdelngffnklirnviALRDQQAAEERRRDFLQMVLDARHSASPMGVQDFDIVRDvfsstgckp 311
Cdd:cd00302   154 --------------------------------RLRRLRRARARLRDYLEELIARRRAEPADDLDLLLLADA--------- 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 312 npsrqhqpsPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHmapeFCSLEEGLP 391
Cdd:cd00302   193 ---------DDGGGLSDEEIVAELLTLLLAGHETTASLLAWALYLLARHPEVQERLRAEIDAVLGDG----TPEDLSKLP 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 392 YLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQhrPFTYLP 471
Cdd:cd00302   260 YLEAVVEETLRLYPPVPLLPRVATEDVELGGYTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPEREEP--RYAHLP 337
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1488188862 472 FGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLESKSaLGPKNGV 526
Cdd:cd00302   338 FGAGPHRCLGARLARLELKLALATLLRRFDFELVPDEELEWRPSLGT-LGPASLP 391
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
59-501 1.14e-66

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: 220.92  E-value: 1.14e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  59 FRQGFWESQMELRKlYGPLCGYYLGRRMFIVISEPDMIKQVLV--ENFSNFTNRMASGLEFKSVADSVLFLRDKRWEEVR 136
Cdd:COG2124    17 FLRDPYPFYARLRE-YGPVFRVRLPGGGAWLVTRYEDVREVLRdpRTFSSDGGLPEVLRPLPLLGDSLLTLDGPEHTRLR 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 137 GALMSAFSPEKLNEMVPLISQACDLLLAHLkryaESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWqapeDPFVKHCKRF 216
Cdd:COG2124    96 RLVQPAFTPRRVAALRPRIREIADELLDRL----AARGPVDLVEEFARPLPVIVICELLGVPEEDR----DRLRRWSDAL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 217 FEFCIPRPILvlllsfpsimvPLARILpnKNRDELNGFFNKLIrnvialrdqqaaEERRR----DFLQMVLDARHsaspm 292
Cdd:COG2124   168 LDALGPLPPE-----------RRRRAR--RARAELDAYLRELI------------AERRAepgdDLLSALLAARD----- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 293 gvqdfdivrdvfssTGckpnpsrqhqpspmaRPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREvd 372
Cdd:COG2124   218 --------------DG---------------ERLSDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAE-- 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 373 vfkekhmapefcsleegLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFN 452
Cdd:COG2124   267 -----------------PELLPAAVEETLRLYPPVPLLPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFD 329
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1488188862 453 PERftaearqqhRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFR 501
Cdd:COG2124   330 PDR---------PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFP 369
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
85-529 3.23e-66

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: 220.51  E-value: 3.23e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  85 RMFIVISEPDMIKQVLVENFSNFTNRMASGLEFksVADSVLFLRDKRWEEVRGALMSAFSPEKLNEMVPLISQACDLLLA 164
Cdd:cd20659    12 RPILVLNHPDTIKAVLKTSEPKDRDSYRFLKPW--LGDGLLLSNGKKWKRNRRLLTPAFHFDILKPYVPVYNECTDILLE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 165 HLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQ-APEDPFVKHCKRFFEFCIPRpILVLLLSFPSI--MVPLAR 241
Cdd:cd20659    90 KWSKLAETGESVEVFEDISLLTLDIILRCAFSYKSNCQQtGKNHPYVAAVHELSRLVMER-FLNPLLHFDWIyyLTPEGR 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 242 ILpNKNRDELNGFFNKLI---RNVIALRDQQAAEERRR-DFLQMVLDARHSaspmgvqdfdivrdvfSSTGckpnpsrqh 317
Cdd:cd20659   169 RF-KKACDYVHKFAEEIIkkrRKELEDNKDEALSKRKYlDFLDILLTARDE----------------DGKG--------- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 318 qpspmarpLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCSLEEgLPYLDMVI 397
Cdd:cd20659   223 --------LTDEEIRDEVDTFLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRDDIEWDDLSK-LPYLTMCI 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 398 AETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPR 477
Cdd:cd20659   294 KESLRLYPPVPFIARTLTKPITIDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIKKRDPFAFIPFSAGPR 373
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1488188862 478 SCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLEskSALGPKNGVYIK 529
Cdd:cd20659   374 NCIGQNFAMNEMKVVLARILRRFELSVDPNHPVEPKPG--LVLRSKNGIKLK 423
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
75-503 2.73e-64

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: 215.54  E-value: 2.73e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  75 GPLCGYYLGRRMFIVISEPDMIKQVLveNFSNFTNRmASGLEFKSVADSVLFLRDKRWEEVRGALMSAFSPEKLNEMVPL 154
Cdd:cd11057     1 GSPFRAWLGPRPFVITSDPEIVQVVL--NSPHCLNK-SFFYDFFRLGRGLFSAPYPIWKLQRKALNPSFNPKILLSFLPI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 155 ISQACDLLLAHLKRYAeSGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFCIPRPILVLLlsfps 234
Cdd:cd11057    78 FNEEAQKLVQRLDTYV-GGGEFDILPDLSRCTLEMICQTTLGSDVNDESDGNEEYLESYERLFELIAKRVLNPWL----- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 235 imvplarilpnknrdelngfFNKLIRNVIAL-RDQQAAEERRRDFLQMVLDARHSASPMGVQDFdivrdvfSSTGCKPNP 313
Cdd:cd11057   152 --------------------HPEFIYRLTGDyKEEQKARKILRAFSEKIIEKKLQEVELESNLD-------SEEDEENGR 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 314 SRQ---HQPSPMAR---PLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREV-DVFKEKHmapEFCSL 386
Cdd:cd11057   205 KPQifiDQLLELARngeEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEImEVFPDDG---QFITY 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 387 E--EGLPYLDMVIAETLRMYPPAFRFTREAAQDCEV-LGQRIPAGAVLEMAVGALHHDPEHW-PSPETFNPERFTAEARQ 462
Cdd:cd11057   282 EdlQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLsNGVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLPERSA 361
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1488188862 463 QHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQ 503
Cdd:cd11057   362 QRHPYAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRLK 402
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
74-526 3.63e-62

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: 210.07  E-value: 3.63e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLV-ENF---SNFTNRMASGLEFKSVADSVLFLRD-KRWEEVRGALMSAFSPEKL 148
Cdd:cd20613    11 YGPVFVFWILHRPIVVVSDPEAVKEVLItLNLpkpPRVYSRLAFLFGERFLGNGLVTEVDhEKWKKRRAILNPAFHRKYL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 149 NEMVPLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDPF---VKHCKRFFEFCIPRPI 225
Cdd:cd20613    91 KNLMDEFNESADLLVEKLSKKADGKTEVNMLDEFNRVTLDVIAKVAFGMDLNSIEDPDSPFpkaISLVLEGIQESFRNPL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 226 LVLLlsfpsimvPLARILPNKNRDELNgFFNKLIRNVIALR--DQQAAEERRRDFLQMVLDArhsaspmgvqdfdivrdv 303
Cdd:cd20613   171 LKYN--------PSKRKYRREVREAIK-FLRETGRECIEERleALKRGEEVPNDILTHILKA------------------ 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 304 fsstgCKPNPSrqhqpspmarpLTVDEIVGQaFI-FLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD-VFKEKHmap 381
Cdd:cd20613   224 -----SEEEPD-----------FDMEELLDD-FVtFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDeVLGSKQ--- 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 382 eFCSLEE--GLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAE 459
Cdd:cd20613   284 -YVEYEDlgKLEYLSQVLKETLRLYPPVPGTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPE 362
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1488188862 460 ARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPeTQvPLQLESKSALGPKNGV 526
Cdd:cd20613   363 APEKIPSYAYFPFSLGPRSCIGQQFAQIEAKVILAKLLQNFKFELVP-GQ-SFGILEEVTLRPKDGV 427
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
71-506 3.03e-61

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: 207.58  E-value: 3.03e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  71 RKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSVADSVLFLRDKRWEEVRGALMSAFSPEKLNE 150
Cdd:cd11052     8 IKQYGKNFLYWYGTDPRLYVTEPELIKELLSKKEGYFGKSPLQPGLKKLLGRGLVMSNGEKWAKHRRIANPAFHGEKLKG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 151 MVPLISQACDLLLAHLKRYAESGDA-FDIQRCYCNYTTDVVASVAFGTpvdSWQAPEDPFvKHCKRFFEFCIPrpilvll 229
Cdd:cd11052    88 MVPAMVESVSDMLERWKKQMGEEGEeVDVFEEFKALTADIISRTAFGS---SYEEGKEVF-KLLRELQKICAQ------- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 230 lSFPSIMVPLARILP---NKNRDELNGFFNKLIRNVIALRDQQAAEERRR----DFLQMVLDARHSASPmgvqdfdivrd 302
Cdd:cd11052   157 -ANRDVGIPGSRFLPtkgNKKIKKLDKEIEDSLLEIIKKREDSLKMGRGDdygdDLLGLLLEANQSDDQ----------- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 303 vfsstgckpnpsrqhqpspmARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREV-DVFKEKHMAP 381
Cdd:cd11052   225 --------------------NKNMTVQEIVDECKTFFFAGHETTALLLTWTTMLLAIHPEWQEKAREEVlEVCGKDKPPS 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 382 EFCSleeGLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPS-PETFNPERFTAE- 459
Cdd:cd11052   285 DSLS---KLKTVSMVINESLRLYPPAVFLTRKAKEDIKLGGLVIPKGTSIWIPVLALHHDEEIWGEdANEFNPERFADGv 361
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1488188862 460 ARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACP 506
Cdd:cd11052   362 AKAAKHPMAFLPFGLGPRNCIGQNFATMEAKIVLAMILQRFSFTLSP 408
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
71-506 4.57e-61

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: 206.92  E-value: 4.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  71 RKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSVADSVLFLRDKRWEEVRGALMSAFSPEKLNE 150
Cdd:cd20639     8 RKIYGKTFLYWFGPTPRLTVADPELIREILLTRADHFDRYEAHPLVRQLEGDGLVSLRGEKWAHHRRVITPAFHMENLKR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 151 MVPLISQACDLLLAHLKRYAESGDAF--DIQRCYCNYTTDVVASVAFGTPVDSwqapedpfvkhCKRFFEFcIPRPILVL 228
Cdd:cd20639    88 LVPHVVKSVADMLDKWEAMAEAGGEGevDVAEWFQNLTEDVISRTAFGSSYED-----------GKAVFRL-QAQQMLLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 229 LLSFPSIMVPLARILPN-KNRD--ELNGFFNKLIRNVIALR----DQQAAEERRRDFLQMVLDARHSASpmgvqdfdivr 301
Cdd:cd20639   156 AEAFRKVYIPGYRFLPTkKNRKswRLDKEIRKSLLKLIERRqtaaDDEKDDEDSKDLLGLMISAKNARN----------- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 302 dvfsstgckpnpsrqhqpspmARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAP 381
Cdd:cd20639   225 ---------------------GEKMTVEEIIEECKTFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVP 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 382 EFCSLEEgLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHW-PSPETFNPERFTA-E 459
Cdd:cd20639   284 TKDHLPK-LKTLGMILNETLRLYPPAVATIRRAKKDVKLGGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADgV 362
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1488188862 460 ARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACP 506
Cdd:cd20639   363 ARAAKHPLAFIPFGLGPRTCVGQNLAILEAKLTLAVILQRFEFRLSP 409
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
88-511 9.17e-60

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: 203.66  E-value: 9.17e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  88 IVISEPDMIKQVLVENFSNFT-NRMASGLEFKSVADSVLFLRDKRWEEVRGALMSAFSPEKLNEMVPLIS----QACDLL 162
Cdd:cd11069    16 LLVTDPKALKHILVTNSYDFEkPPAFRRLLRRILGDGLLAAEGEEHKRQRKILNPAFSYRHVKELYPIFWskaeELVDKL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 163 LAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFciPRPILVLLLSFPSIMVPLARI 242
Cdd:cd11069    96 EEEIEESGDESISIDVLEWLSRATLDIIGLAGFGYDFDSLENPDNELAEAYRRLFEP--TLLGSLLFILLLFLPRWLVRI 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 243 LPNKNRDELN---GFFNKLIRNVIALRDQQAAEERR---RDFLQMVLDARHSASpmgvqdfdivrdvfsstgckpnpsrq 316
Cdd:cd11069   174 LPWKANREIRrakDVLRRLAREIIREKKAALLEGKDdsgKDILSILLRANDFAD-------------------------- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 317 hqpspmARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCSLE-EGLPYLDM 395
Cdd:cd11069   228 ------DERLSDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALPDPPDGDLSYDDlDRLPYLNA 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 396 VIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHW-PSPETFNPERF-----TAEARQQHRPFTY 469
Cdd:cd11069   302 VCRETLRLYPPVPLTSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWlepdgAASPGGAGSNYAL 381
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1488188862 470 LPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVP 511
Cdd:cd11069   382 LTFLHGPRSCIGKKFALAEMKVLLAALVSRFEFELDPDAEVE 423
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
75-503 5.12e-59

cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome P450 families 1 (CYP1) and 2 (CYP2), CYP17A1, and CYP21 in vertebrates, as well as insect and crustacean CYPs similar to CYP15A1 and CYP306A1. CYP1 and CYP2 enzymes are involved in the metabolism of endogenous and exogenous compounds such as hormones, xenobiotics, and drugs. CYP17A1 catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products, while CYP21 catalyzes the 21-hydroxylation of steroids such as progesterone and 17-alpha-hydroxyprogesterone (17-alpha-OH-progesterone) to form 11-deoxycorticosterone and 11-deoxycortisol, respectively. Members of this group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410710 [Multi-domain]  Cd Length: 419  Bit Score: 201.29  E-value: 5.12e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  75 GPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNR-MASGLEFKSVADSVLFLRDKRWEEVRGALMSAFSPEKL-NEMV 152
Cdd:cd20617     1 GGIFTLWLGDVPTVVLSDPEIIKEAFVKNGDNFSDRpLLPSFEIISGGKGILFSNGDYWKELRRFALSSLTKTKLkKKME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 153 PLISQACDLLLAHLKRYAESGDAFD----IQRCYCNyttdVVASVAFGTPVDSWQAPE-DPFVKHCKRFFEFcIPRPILV 227
Cdd:cd20617    81 ELIEEEVNKLIESLKKHSKSGEPFDprpyFKKFVLN----IINQFLFGKRFPDEDDGEfLKLVKPIEEIFKE-LGSGNPS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 228 LLLSFPSIMVPLARILPNKNRDELNGFFNKLIrnvialrdqqaaEERRRDFlqmvldarhsaspmgvqDFDIVRDVFSST 307
Cdd:cd20617   156 DFIPILLPFYFLYLKKLKKSYDKIKDFIEKII------------EEHLKTI-----------------DPNNPRDLIDDE 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 308 GCKPNPSRQHQPspmarpLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPefcSLE 387
Cdd:cd20617   207 LLLLLKEGDSGL------FDDDSIISTCLDLFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRV---TLS 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 388 E--GLPYLDMVIAETLRMYPPA-FRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTaEARQQH 464
Cdd:cd20617   278 DrsKLPYLNAVIKEVLRLRPILpLGLPRVTTEDTEIGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFL-ENDGNK 356
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1488188862 465 RPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQ 503
Cdd:cd20617   357 LSEQFIPFGIGKRNCVGENLARDELFLFFANLLLNFKFK 395
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
69-526 4.52e-58

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: 198.58  E-value: 4.52e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  69 ELRKLYGP---LCGYYLGRrmFIVISEPDMIKQVLVEN----FSNFTNRMASGLEFKSvadSVLFLRDKRWEEVRGALMS 141
Cdd:cd11053     6 RLRARYGDvftLRVPGLGP--VVVLSDPEAIKQIFTADpdvlHPGEGNSLLEPLLGPN---SLLLLDGDRHRRRRKLLMP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 142 AFSPEKLNEMVPLISQACDLLLAHLKRyaesGDAFDIQRCYCNYTTDVVASVAFGTPVDSwqaPEDPFVKHCKRFFEFcI 221
Cdd:cd11053    81 AFHGERLRAYGELIAEITEREIDRWPP----GQPFDLRELMQEITLEVILRVVFGVDDGE---RLQELRRLLPRLLDL-L 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 222 PRPilvlLLSFPSIMVPLARILPNKNRDELNGFFNKLIRNVIALRDQQAAEERRrDFLQMVLDARHSASpmgvqdfdivr 301
Cdd:cd11053   153 SSP----LASFPALQRDLGPWSPWGRFLRARRRIDALIYAEIAERRAEPDAERD-DILSLLLSARDEDG----------- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 302 dvfsstgckpnpsrqhqpspmaRPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAP 381
Cdd:cd11053   217 ----------------------QPLSDEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGDPDPE 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 382 EFcsleEGLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFtaeAR 461
Cdd:cd11053   275 DI----AKLPYLDAVIKETLRLYPVAPLVPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERF---LG 347
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1488188862 462 QQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLESKsALGPKNGV 526
Cdd:cd11053   348 RKPSPYEYLPFGGGVRRCIGAAFALLEMKVVLATLLRRFRLELTDPRPERPVRRGV-TLAPSRGV 411
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
65-533 1.12e-55

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: 192.78  E-value: 1.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  65 ESQMELRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVEnfSNFTNRMASGLEF-KSVADSVLFL---RDKRWEEVRGALM 140
Cdd:cd11068     3 QSLLRLADELGPIFKLTLPGRRVVVVSSHDLIAELCDE--SRFDKKVSGPLEElRDFAGDGLFTaytHEPNWGKAHRILM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 141 SAFSPEKLNEMVPLISQACDLLLAHLKRYAeSGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPE-DPFVKHCKRFFEF 219
Cdd:cd11068    81 PAFGPLAMRGYFPMMLDIAEQLVLKWERLG-PDEPIDVPDDMTRLTLDTIALCGFGYRFNSFYRDEpHPFVEAMVRALTE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 220 CIPRPilvlllSFPSIMVPLaRILPNKNRDELNGFFNKLIRNVIALRdQQAAEERRRDFLQMVLDARHSAspmgvqdfdi 299
Cdd:cd11068   160 AGRRA------NRPPILNKL-RRRAKRQFREDIALMRDLVDEIIAER-RANPDGSPDDLLNLMLNGKDPE---------- 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 300 vrdvfssTGckpnpsrqhqpspmaRPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD-VFkekh 378
Cdd:cd11068   222 -------TG---------------EKLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDeVL---- 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 379 mAPEFCSLEE--GLPYLDMVIAETLRMYPPAFRFTREAAQDcEVLGQR--IPAGAVLEMAVGALHHDPEHW-PSPETFNP 453
Cdd:cd11068   276 -GDDPPPYEQvaKLRYIRRVLDETLRLWPTAPAFARKPKED-TVLGGKypLKKGDPVLVLLPALHRDPSVWgEDAEEFRP 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 454 ERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPetqvPLQLESKSALGPK-NGVYIKIVS 532
Cdd:cd11068   354 ERFLPEEFRKLPPNAWKPFGNGQRACIGRQFALQEATLVLAMLLQRFDFEDDP----DYELDIKETLTLKpDGFRLKARP 429

                  .
gi 1488188862 533 R 533
Cdd:cd11068   430 R 430
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
82-500 1.50e-53

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: 186.76  E-value: 1.50e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  82 LGRRMFIVISEPDMIKQVLVENFSNFtNRMaSGLEfkSVADSV----LFLRDK-RWEEVRGALMSAFSPEKLNEMVPLIS 156
Cdd:cd11083     8 LGRQPVLVISDPELIREVLRRRPDEF-RRI-SSLE--SVFREMgingVFSAEGdAWRRQRRLVMPAFSPKHLRYFFPTLR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 157 QACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFefciprPILVLLLSFPsim 236
Cdd:cd11083    84 QITERLRERWERAAAEGEAVDVHKDLMRYTVDVTTSLAFGYDLNTLERGGDPLQEHLERVF------PMLNRRVNAP--- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 237 VPLARILP-------NKNRDELNGFFNKLI---RNVIALRDQQAaeERRRDFLQMVLDArhsaspmgvQDfdivrdvfss 306
Cdd:cd11083   155 FPYWRYLRlpadralDRALVEVRALVLDIIaaaRARLAANPALA--EAPETLLAMMLAE---------DD---------- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 307 tgckpnpsrqhqpsPMARpLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCSL 386
Cdd:cd11083   214 --------------PDAR-LTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPLLEA 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 387 EEGLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGA--VLEMAVGALhhDPEHWPSPETFNPERF--TAEARQ 462
Cdd:cd11083   279 LDRLPYLEAVARETLRLKPVAPLLFLEPNEDTVVGDIALPAGTpvFLLTRAAGL--DAEHFPDPEEFDPERWldGARAAE 356
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1488188862 463 QHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKF 500
Cdd:cd11083   357 PHDPSSLLPFGAGPRLCPGRSLALMEMKLVFAMLCRNF 394
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
136-507 2.38e-51

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: 180.85  E-value: 2.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 136 RGALMSAFSPEKLNEMVPLISQACDLLLAHLKRYAESGDAFDIQRcYCNYTT-DVVASVAFGTPVDSWQAPE-DPFVKhc 213
Cdd:cd11058    62 RRLLAHAFSEKALREQEPIIQRYVDLLVSRLRERAGSGTPVDMVK-WFNFTTfDIIGDLAFGESFGCLENGEyHPWVA-- 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 214 kRFFEFCIPRPILVLLLSFPSIMVPLARILPNKNRDELNGFFnKLIRNVIALRDQQAAEerRRDFLQMVLDARhsaspmg 293
Cdd:cd11058   139 -LIFDSIKALTIIQALRRYPWLLRLLRLLIPKSLRKKRKEHF-QYTREKVDRRLAKGTD--RPDFMSYILRNK------- 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 294 vqdfdivrdvfsstgckpnpsrqhqpsPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREV-D 372
Cdd:cd11058   208 ---------------------------DEKKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIrS 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 373 VFK-EKHMapEFCSLEEgLPYLDMVIAETLRMYPPA----FRFTREAAQDceVLGQRIPAGAVLEMAVGALHHDPEHWPS 447
Cdd:cd11058   261 AFSsEDDI--TLDSLAQ-LPYLNAVIQEALRLYPPVpaglPRVVPAGGAT--IDGQFVPGGTSVSVSQWAAYRSPRNFHD 335
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1488188862 448 PETFNPERFTAEARqqhRPFT------YLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPE 507
Cdd:cd11058   336 PDEFIPERWLGDPR---FEFDndkkeaFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLELDPE 398
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
71-507 1.15e-49

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: 176.56  E-value: 1.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  71 RKLYGPLCGYYLGRRMFIVISEPDMIKQVLvENFSNFTNRMasGLEF-------KSVADSVLFLRDKRWEEVRGALMSAF 143
Cdd:cd11054     1 HKKYGPIVREKLGGRDIVHLFDPDDIEKVF-RNEGKYPIRP--SLEPlekyrkkRGKPLGLLNSNGEEWHRLRSAVQKPL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 144 -SPEKLNEMVPLISQACDLLLAHLK--RYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDP----FVKHCKRF 216
Cdd:cd11054    78 lRPKSVASYLPAINEVADDFVERIRrlRDEDGEEVPDLEDELYKWSLESIGTVLFGKRLGCLDDNPDSdaqkLIEAVKDI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 217 FEfciprpiLVLLLSFpsiMVPLARILPNK-------NRDELNGFFNKLIRNVIA-LRDQQAAEERRRDFLQMVLDarhs 288
Cdd:cd11054   158 FE-------SSAKLMF---GPPLWKYFPTPawkkfvkAWDTIFDIASKYVDEALEeLKKKDEEDEEEDSLLEYLLS---- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 289 aspmgvqdfdivrdvfsstgcKPNpsrqhqpspmarpLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLL 368
Cdd:cd11054   224 ---------------------KPG-------------LSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLY 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 369 REVD-VFKEKHmAPEFCSLEEgLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPS 447
Cdd:cd11054   270 EEIRsVLPDGE-PITAEDLKK-MPYLKACIKESLRLYPVAPGNGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPD 347
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1488188862 448 PETFNPERF--TAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPE 507
Cdd:cd11054   348 PEEFIPERWlrDDSENKNIHPFASLPFGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEYHHE 409
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
71-530 1.21e-48

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: 173.14  E-value: 1.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  71 RKLYGPLCGYYL-GRRMfIVISEPDMIKQVLVENFSNFTNRMasgleFKSVAD-----SVLFLR--DKRWeeVRGALMSA 142
Cdd:cd11043     2 IKRYGPVFKTSLfGRPT-VVSADPEANRFILQNEGKLFVSWY-----PKSVRKllgksSLLTVSgeEHKR--LRGLLLSF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 143 FSPEKLNEMvpLISQACDLLLAHLKRYAESGDaFDIQRCYCNYTTDVVASVAFGTPVDSWQapeDPFVKHCKRFFEFcip 222
Cdd:cd11043    74 LGPEALKDR--LLGDIDELVRQHLDSWWRGKS-VVVLELAKKMTFELICKLLLGIDPEEVV---EELRKEFQAFLEG--- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 223 rpilvlLLSFPsIMVP---LARILpnKNRDELNGFFNKLIRnviALRDQQAAEERRRDFLQMVLDARhsaspmgvqdfdi 299
Cdd:cd11043   145 ------LLSFP-LNLPgttFHRAL--KARKRIRKELKKIIE---ERRAELEKASPKGDLLDVLLEEK------------- 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 300 vrdvfsSTGCKPnpsrqhqpspmarpLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHM 379
Cdd:cd11043   200 ------DEDGDS--------------LTDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLEEHEEIAKRKE 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 380 APEFCSLEE--GLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFt 457
Cdd:cd11043   260 EGEGLTWEDykSMKYTWQVINETLRLAPIVPGVFRKALQDVEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRW- 338
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1488188862 458 aEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLesksALGPKNGVYIKI 530
Cdd:cd11043   339 -EGKGKGVPYTFLPFGGGPRLCPGAELAKLEILVFLHHLVTRFRWEVVPDEKISRFP----LPRPPKGLPIRL 406
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
75-528 3.27e-47

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: 170.14  E-value: 3.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  75 GPLCGYYLGRRMFIVISEPDMIKQVLveNFSNFTNrmasglefKSVA---------DSVLFLRDKRWEEVRGALMSAFSP 145
Cdd:cd20660     1 GPIFRIWLGPKPIVVLYSAETVEVIL--SSSKHID--------KSFEydflhpwlgTGLLTSTGEKWHSRRKMLTPTFHF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 146 EKLNEMVPLISQACDLLLAHLKRYAeSGDAFD----IQRCycnyTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFCI 221
Cdd:cd20660    71 KILEDFLDVFNEQSEILVKKLKKEV-GKEEFDifpyITLC----ALDIICETAMGKSVNAQQNSDSEYVKAVYRMSELVQ 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 222 PRPILVLL-LSFPSIMVPLARiLPNKNRDELNGFFNKLIRNVIALR----DQQAAEE--------RRRDFLQMVLDARHS 288
Cdd:cd20660   146 KRQKNPWLwPDFIYSLTPDGR-EHKKCLKILHGFTNKVIQERKAELqkslEEEEEDDedadigkrKRLAFLDLLLEASEE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 289 ASPMGVQDfdiVRDvfsstgckpnpsrqhqpspmarplTVDeivgqafIFLIAGYEIITNTLSFATYLLATNPDCQEKLL 368
Cdd:cd20660   225 GTKLSDED---IRE------------------------EVD-------TFMFEGHDTTAAAINWALYLIGSHPEVQEKVH 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 369 REVD-VFKEKHMAPEFCSLEEgLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPS 447
Cdd:cd20660   271 EELDrIFGDSDRPATMDDLKE-MKYLECVIKEALRLFPSVPMFGRTLSEDIEIGGYTIPKGTTVLVLTYALHRDPRQFPD 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 448 PETFNPERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACpETQVPLQLESKSALGPKNGVY 527
Cdd:cd20660   350 PEKFDPDRFLPENSAGRHPYAYIPFSAGPRNCIGQKFALMEEKVVLSSILRNFRIESV-QKREDLKPAGELILRPVDGIR 428

                  .
gi 1488188862 528 I 528
Cdd:cd20660   429 V 429
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
64-507 6.71e-47

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


Pssm-ID: 410734 [Multi-domain]  Cd Length: 431  Bit Score: 169.17  E-value: 6.71e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  64 WESQmelrklYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSVADSVLFLRDKRWEEVRGALMSAF 143
Cdd:cd20641     7 WKSQ------YGETFLYWQGTTPRICISDHELAKQVLSDKFGFFGKSKARPEILKLSGKGLVFVNGDDWVRHRRVLNPAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 144 SPEKLNEMV-PLISQACDLLLAHLKRYAESGDA---FDIQRCYCNYTTDVVASVAFGTpvDSWQAPEdpfVKHCKRFFEF 219
Cdd:cd20641    81 SMDKLKSMTqVMADCTERMFQEWRKQRNNSETErieVEVSREFQDLTADIIATTAFGS--SYAEGIE---VFLSQLELQK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 220 CIPRPILvlllsfpSIMVPLARILP---NKNRDELNGFFNKLIRNVIALRDQQAAEERRRDFLQMVLDArhsaspmgvqd 296
Cdd:cd20641   156 CAAASLT-------NLYIPGTQYLPtprNLRVWKLEKKVRNSIKRIIDSRLTSEGKGYGDDLLGLMLEA----------- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 297 fdivrdvfsstgCKPNPSRQHQpspmARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREV--DVF 374
Cdd:cd20641   218 ------------ASSNEGGRRT----ERKMSIDEIIDECKTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVfrECG 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 375 KEKHMAPEFCSleeGLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPS-PETFNP 453
Cdd:cd20641   282 KDKIPDADTLS---KLKLMNMVLMETLRLYGPVINIARRASEDMKLGGLEIPKGTTIIIPIAKLHRDKEVWGSdADEFNP 358
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1488188862 454 ERFT-AEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPE 507
Cdd:cd20641   359 LRFAnGVSRAATHPNALLSFSLGPRACIGQNFAMIEAKTVLAMILQRFSFSLSPE 413
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
62-510 1.03e-45

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: 165.51  E-value: 1.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  62 GFWESQMElrklYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFT---------NRMASGLefkSVADSVLFLRDKRw 132
Cdd:cd11049     4 GFLSSLRA----HGDLVRIRLGPRPAYVVTSPELVRQVLVNDRVFDKggplfdrarPLLGNGL---ATCPGEDHRRQRR- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 133 eevrgaLMS-AFSPEKLNEMVPLISQACDlllAHLKRYaESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEdpfVK 211
Cdd:cd11049    76 ------LMQpAFHRSRIPAYAEVMREEAE---ALAGSW-RPGRVVDVDAEMHRLTLRVVARTLFSTDLGPEAAAE---LR 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 212 HC-KRFFEFCIPRPILvlllsfPSIMVPLARIlPNKNRDELNGFFNKLIRNVIAlrDQQAAEERRRDFLQMVLDARHSAS 290
Cdd:cd11049   143 QAlPVVLAGMLRRAVP------PKFLERLPTP-GNRRFDRALARLRELVDEIIA--EYRASGTDRDDLLSLLLAARDEEG 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 291 pmgvqdfdivrdvfsstgckpnpsrqhqpspmaRPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLRE 370
Cdd:cd11049   214 ---------------------------------RPLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAE 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 371 VD-VFKEKhmAPEFCSLEeGLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPE 449
Cdd:cd11049   261 LDaVLGGR--PATFEDLP-RLTYTRRVVTEALRLYPPVWLLTRRTTADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPE 337
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1488188862 450 TFNPERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQV 510
Cdd:cd11049   338 RFDPDRWLPGRAAAVPRGAFIPFGAGARKCIGDTFALTELTLALATIASRWRLRPVPGRPV 398
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
136-503 3.16e-45

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: 164.35  E-value: 3.16e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 136 RGALMSAFSPEKLNEMVPLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHckr 215
Cdd:cd11062    59 RKALSPFFSKRSILRLEPLIQEKVDKLVSRLREAKGTGEPVNLDDAFRALTADVITEYAFGRSYGYLDEPDFGPEFL--- 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 216 fFEFCIPRPILVLLLSFPSIMvPLARILPnknrdelngffnklirnVIALRDQQAAEERRRDFLQMVLD--ARHSASPMG 293
Cdd:cd11062   136 -DALRALAEMIHLLRHFPWLL-KLLRSLP-----------------ESLLKRLNPGLAVFLDFQESIAKqvDEVLRQVSA 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 294 VQDFDIVRDVFSSTgckpnpsrqHQPSPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD- 372
Cdd:cd11062   197 GDPPSIVTSLFHAL---------LNSDLPPSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKt 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 373 VFKEKHMAPEFCSLeEGLPYLDMVIAETLRMYPPAF-RFTREA-AQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPET 450
Cdd:cd11062   268 AMPDPDSPPSLAEL-EKLPYLTAVIKEGLRLSYGVPtRLPRVVpDEGLYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHE 346
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1488188862 451 FNPERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQ 503
Cdd:cd11062   347 FRPERWLGAAEKGKLDRYLVPFSKGSRSCLGINLAYAELYLALAALFRRFDLE 399
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
74-516 6.19e-45

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: 163.53  E-value: 6.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNR--MASGLEF----KSVAdsvlfLRD--KRWEEVRGALMSAF-- 143
Cdd:cd11027     1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKKSADFAGRpkLFTFDLFsrggKDIA-----FGDysPTWKLHRKLAHSALrl 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 144 ---SPEKLNEMvplISQACDLLLAHLKryAESGDAFDIQRCYCNYTTDVVASVAFGTPVDswqaPEDP----FVKHCKRF 216
Cdd:cd11027    76 yasGGPRLEEK---IAEEAEKLLKRLA--SQEGQPFDPKDELFLAVLNVICSITFGKRYK----LDDPeflrLLDLNDKF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 217 FEfciprpilVLLLSFPSIMVPLARILPNKN-------RDELNGFFNKLIRNVIALRDqqaaEERRRDFLQMVLDARHSA 289
Cdd:cd11027   147 FE--------LLGAGSLLDIFPFLKYFPNKAlrelkelMKERDEILRKKLEEHKETFD----PGNIRDLTDALIKAKKEA 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 290 SPMGVQDfdivrdvfsstgckpnpsrqhqpspmARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLR 369
Cdd:cd11027   215 EDEGDED--------------------------SGLLTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHA 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 370 EVDVFKEKHMAPEfcsLE--EGLPYLDMVIAETLRMYPPA-FRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWP 446
Cdd:cd11027   269 ELDDVIGRDRLPT---LSdrKRLPYLEATIAEVLRLSSVVpLALPHKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWD 345
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1488188862 447 SPETFNPERFTAEARQQH-RPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQaCPETQVPLQLES 516
Cdd:cd11027   346 DPDEFRPERFLDENGKLVpKPESFLPFSAGRRVCLGESLAKAELFLFLARLLQKFRFS-PPEGEPPPELEG 415
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
88-501 6.42e-45

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: 164.04  E-value: 6.42e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  88 IVISEPDMIKQVL-VENFSNFTNRMASGLEFksVADSVLFLRDKRWEEVRGALMSAFSpEKLNEMV--PLISQA---CDL 161
Cdd:cd11070    15 ILVTKPEYLTQIFrRRDDFPKPGNQYKIPAF--YGPNVISSEGEDWKRYRKIVAPAFN-ERNNALVweESIRQAqrlIRY 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 162 LLAHLKRyaESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFCIPRpilvLLLSFPSIMVPLAR 241
Cdd:cd11070    92 LLEEQPS--AKGGGVDVRDLLQRLALNVIGEVGFGFDLPALDEEESSLHDTLNAIKLAIFPP----LFLNFPFLDRLPWV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 242 ILPnknrdelngffnklirnvialRDQQAAEERRRdFLQMVLDARHSASPMGVQDFDIVRDVFSSTGckpnpsrqhQPSP 321
Cdd:cd11070   166 LFP---------------------SRKRAFKDVDE-FLSELLDEVEAELSADSKGKQGTESVVASRL---------KRAR 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 322 MARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD-VFKEKHMAPEFCSLEEGLPYLDMVIAET 400
Cdd:cd11070   215 RSGGLTEKELLGNLFIFFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDsVLGDEPDDWDYEEDFPKLPYLLAVIYET 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 401 LRMYPPA---FRFTREAAQDCEVLGQR--IPAGAVLEMAVGALHHDPEHW-PSPETFNPERF-------TAEARQQHRPF 467
Cdd:cd11070   295 LRLYPPVqllNRKTTEPVVVITGLGQEivIPKGTYVGYNAYATHRDPTIWgPDADEFDPERWgstsgeiGAATRFTPARG 374
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1488188862 468 TYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFR 501
Cdd:cd11070   375 AFIPFSAGPRACLGRKFALVEFVAALAELFRQYE 408
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
117-503 2.01e-44

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: 162.01  E-value: 2.01e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 117 FKSVADSVLFLRDKrweEV----RGALMSAFSPEKLNEMVPLISQACDLLLAHLKR--YAESGDAFDIQRcYCNYTT-DV 189
Cdd:cd11061    38 LSPSASLTFTTRDK---AEharrRRVWSHAFSDKALRGYEPRILSHVEQLCEQLDDraGKPVSWPVDMSD-WFNYLSfDV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 190 VASVAFGTPVDSWQAPEDpfvkhckRFFEFCIPRPILVL-LLSFPSIMVPLARILP-----NKNRDELNGFFNKLIRNVI 263
Cdd:cd11061   114 MGDLAFGKSFGMLESGKD-------RYILDLLEKSMVRLgVLGHAPWLRPLLLDLPlfpgaTKARKRFLDFVRAQLKERL 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 264 alrdqQAAEERRRDFLQMVLDARHSASPmgvqdfdivrdvfsstgckpnpsrqhqpspmaRPLTVDEIVGQAFIFLIAGY 343
Cdd:cd11061   187 -----KAEEEKRPDIFSYLLEAKDPETG--------------------------------EGLDLEELVGEARLLIVAGS 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 344 EIITNTLSFATYLLATNPDCQEKLLREVD-VFKEKHMAPEFCSLEeGLPYLDMVIAETLRMYPPAFRFT-REA-AQDCEV 420
Cdd:cd11061   230 DTTATALSAIFYYLARNPEAYEKLRAELDsTFPSDDEIRLGPKLK-SLPYLRACIDEALRLSPPVPSGLpRETpPGGLTI 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 421 LGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAE---ARQQHRPFTylPFGAGPRSCLGVRLGLLEVKLTLLHVL 497
Cdd:cd11061   309 DGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRpeeLVRARSAFI--PFSIGPRGCIGKNLAYMELRLVLARLL 386

                  ....*.
gi 1488188862 498 HKFRFQ 503
Cdd:cd11061   387 HRYDFR 392
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
74-527 5.98e-44

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: 161.38  E-value: 5.98e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSVADSVLFLRD-KRWEEVRGALMSAFSPEKLNEMV 152
Cdd:cd11046    10 YGPIYKLAFGPKSFLVISDPAIAKHVLRSNAFSYDKKGLLAEILEPIMGKGLIPADgEIWKKRRRALVPALHKDYLEMMV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 153 PLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSwQAPEDPFVKHCKR-FFEFCIPR--PILVLL 229
Cdd:cd11046    90 RVFGRCSERLMEKLDAAAETGESVDMEEEFSSLTLDIIGLAVFNYDFGS-VTEESPVIKAVYLpLVEAEHRSvwEPPYWD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 230 LSFPSIMVPLARILpNKNRDELNGFFNKLIRNVIALRDQQAAEERRRDFLQmvldarhsaspmgVQDFDIVRDVFSSTGc 309
Cdd:cd11046   169 IPAALFIVPRQRKF-LRDLKLLNDTLDDLIRKRKEMRQEEDIELQQEDYLN-------------EDDPSLLRFLVDMRD- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 310 kpnpsrqhqPSPMARPLTvDEIVgqafIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD-VFKEKHmAPEFCSLEE 388
Cdd:cd11046   234 ---------EDVDSKQLR-DDLM----TMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDaVLGDRL-PPTYEDLKK 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 389 gLPYLDMVIAETLRMYPPAFRFTREAAQDcEVLGQ---RIPAGAVLEMAVGALHHDPEHWPSPETFNPERF----TAEAR 461
Cdd:cd11046   299 -LKYTRRVLNESLRLYPQPPVLIRRAVED-DKLPGggvKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFldpfINPPN 376
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1488188862 462 QQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQ-ACPETQVplQLESKSALGPKNGVY 527
Cdd:cd11046   377 EVIDDFAFLPFGGGPRKCLGDQFALLEATVALAMLLRRFDFElDVGPRHV--GMTTGATIHTKNGLK 441
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
75-500 1.14e-43

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: 160.41  E-value: 1.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  75 GPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNR--MASGLEFKSVADSVLFLR-DKRWEEVRG-ALMSAFSPEKLNE 150
Cdd:cd20618     1 GPLMYLRLGSVPTVVVSSPEMAKEVLKTQDAVFASRprTAAGKIFSYNGQDIVFAPyGPHWRHLRKiCTLELFSAKRLES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 151 MVPLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEfciprpILVLLL 230
Cdd:cd20618    81 FQGVRKEELSHLVKSLLEESESGKPVNLREHLSDLTLNNITRMLFGKRYFGESEKESEEAREFKELID------EAFELA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 231 SFPSI--MVPLARILP----NKNRDELNGFFNKLIRNVIalrdqqaaEERRRDflqmvldaRHSASPMGVQDFDIVrdvf 304
Cdd:cd20618   155 GAFNIgdYIPWLRWLDlqgyEKRMKKLHAKLDRFLQKII--------EEHREK--------RGESKKGGDDDDDLL---- 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 305 sstgckpnpsrQHQPSPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD--VFKEKHMape 382
Cdd:cd20618   215 -----------LLLDLDGEGKLSDDNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDsvVGRERLV--- 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 383 fcslEE----GLPYLDMVIAETLRMYPPA-FRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERF- 456
Cdd:cd20618   281 ----EEsdlpKLPYLQAVVKETLRLHPPGpLLLPHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFl 356
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1488188862 457 ---TAEARQQHrpFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKF 500
Cdd:cd20618   357 esdIDDVKGQD--FELLPFGSGRRMCPGMPLGLRMVQLTLANLLHGF 401
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
71-509 1.47e-43

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: 159.88  E-value: 1.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  71 RKLYGPLCGYYLGRRMFIVISEPDMIKQV--LVENFSNFTNRMASGLEfKSVADSVLFLRDKRWEEVRGALMSAFSPEKL 148
Cdd:cd20640     8 RKQYGPIFTYSTGNKQFLYVSRPEMVKEInlCVSLDLGKPSYLKKTLK-PLFGGGILTSNGPHWAHQRKIIAPEFFLDKV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 149 NEMVPLISQACDLLLAHLKRY--AESGDAFDIQ-----RcycNYTTDVVASVAFGTpvdSWQAPEDPFVKhcKRFFEFCI 221
Cdd:cd20640    87 KGMVDLMVDSAQPLLSSWEERidRAGGMAADIVvdedlR---AFSADVISRACFGS---SYSKGKEIFSK--LRELQKAV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 222 PRPiLVLLLsfpsimVPLARILP---NKNRDELNGFFNKLIRNVIALRDQQAAEERrrDFLQMVLDArhsaspmgvqdfd 298
Cdd:cd20640   159 SKQ-SVLFS------IPGLRHLPtksNRKIWELEGEIRSLILEIVKEREEECDHEK--DLLQAILEG------------- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 299 ivrdvfSSTGCKPNPSRQhqpspmarpltvDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREV-DVFKEK 377
Cdd:cd20640   217 ------ARSSCDKKAEAE------------DFIVDNCKNIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVlEVCKGG 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 378 hmAPEFCSLEEgLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHW-PSPETFNPERF 456
Cdd:cd20640   279 --PPDADSLSR-MKTVTMVIQETLRLYPPAAFVSREALRDMKLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERF 355
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1488188862 457 T-AEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQ 509
Cdd:cd20640   356 SnGVAAACKPPHSYMPFGAGARTCLGQNFAMAELKVLVSLILSKFSFTLSPEYQ 409
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
68-503 4.61e-43

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: 158.19  E-value: 4.61e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  68 MELRKLYGPLCgyylgrrmfiVISEPDMIKQVLVENFSNFTNRMASGLEFKSVADSVLFLRDKRWEEVRGALMSAFSPEK 147
Cdd:cd11051     3 LDLWPFAPPLL----------VVTDPELAEQITQVTNLPKPPPLRKFLTPLTGGSSLISMEGEEWKRLRKRFNPGFSPQH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 148 LNEMVPLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSwQAPEDPFVKHckrffefciprpILV 227
Cdd:cd11051    73 LMTLVPTILDEVEIFAAILRELAESGEVFSLEELTTNLTFDVIGRVTLDIDLHA-QTGDNSLLTA------------LRL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 228 LLLSFPSIMVPLARILPNKNRdelngffnKLIRNVIALRDqqaaeerrrdFLQMVLDARHSaspmgvqdfdivrdvfsst 307
Cdd:cd11051   140 LLALYRSLLNPFKRLNPLRPL--------RRWRNGRRLDR----------YLKPEVRKRFE------------------- 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 308 gckpnpsrqhqpspmarpltVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD-VF-KEKHMAPEFC- 384
Cdd:cd11051   183 --------------------LERAIDQIKTFLFAGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHDeVFgPDPSAAAELLr 242
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 385 ---SLEEGLPYLDMVIAETLRMYPPA--FRFTREAAQDCEVLGQRIP-AGAVLEMAVGALHHDPEHWPSPETFNPERFTA 458
Cdd:cd11051   243 egpELLNQLPYTTAVIKETLRLFPPAgtARRGPPGVGLTDRDGKEYPtDGCIVYVCHHAIHRDPEYWPRPDEFIPERWLV 322
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1488188862 459 EARQQHRPFT--YLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQ 503
Cdd:cd11051   323 DEGHELYPPKsaWRPFERGPRNCIGQELAMLELKIILAMTVRRFDFE 369
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
55-506 1.06e-42

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: 157.44  E-value: 1.06e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  55 NLTFFRQG--FWESQmelRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFtnRMASGLEFKSV-ADSVLFLRD-K 130
Cdd:cd11044     3 TLEFLRDPedFIQSR---YQKYGPVFKTHLLGRPTVFVIGAEAVRFILSGEGKLV--RYGWPRSVRRLlGENSLSLQDgE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 131 RWEEVRGALMSAFSPEKLNEMVPLISqacDLLLAHLKRYAESGdAFDIQRCYCNYTTDVVASVAFG--TPVDSWQAPEDp 208
Cdd:cd11044    78 EHRRRRKLLAPAFSREALESYVPTIQ---AIVQSYLRKWLKAG-EVALYPELRRLTFDVAARLLLGldPEVEAEALSQD- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 209 FVKHCKRFFEFCIPRPilvlllsfpsiMVPLARILpnKNRDELNGFFNKLIRnviaLRDQQAAEERRrDFLQMVLDARHS 288
Cdd:cd11044   153 FETWTDGLFSLPVPLP-----------FTPFGRAI--RARNKLLARLEQAIR----ERQEEENAEAK-DALGLLLEAKDE 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 289 aspmgvqdfdivrdvfsstgckpnpsrqhqpspMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLL 368
Cdd:cd11044   215 ---------------------------------DGEPLSMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLR 261
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 369 REvdvfKEKHMAPEFCSLE--EGLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWP 446
Cdd:cd11044   262 QE----QDALGLEEPLTLEslKKMPYLDQVIKEVLRLVPPVGGGFRKVLEDFELGGYQIPKGWLVYYSIRDTHRDPELYP 337
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1488188862 447 SPETFNPERFTAEARQQHR-PFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACP 506
Cdd:cd11044   338 DPERFDPERFSPARSEDKKkPFSLIPFGGGPRECLGKEFAQLEMKILASELLRNYDWELLP 398
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
74-510 1.16e-42

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: 157.79  E-value: 1.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMasglefKSVADSVLFLRDKR----------WEEVRGALMS-A 142
Cdd:cd11075     2 YGPIFTLRMGSRPLIVVASRELAHEALVQKGSSFASRP------PANPLRVLFSSNKHmvnsspygplWRTLRRNLVSeV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 143 FSPEKLNEMVPLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTT-DVVASVAFGTPVDswqapeDPFVKHCKRffefcI 221
Cdd:cd11075    76 LSPSRLKQFRPARRRALDNLVERLREEAKENPGPVNVRDHFRHALfSLLLYMCFGERLD------EETVRELER-----V 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 222 PRPILVLLLSF-PSIMVPLARILPNKNRDelngffnkliRNVIALRdqqaaeERRRDFLQMVLDARHSASPMGVQDFDIV 300
Cdd:cd11075   145 QRELLLSFTDFdVRDFFPALTWLLNRRRW----------KKVLELR------RRQEEVLLPLIRARRKRRASGEADKDYT 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 301 RDVFSSTGCKPNPSRQhqpspmaRPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD-------V 373
Cdd:cd11075   209 DFLLLDLLDLKEEGGE-------RKLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKevvgdeaV 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 374 FKEKHMapefcsleEGLPYLDMVIAETLRMYPPA-FRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFN 452
Cdd:cd11075   282 VTEEDL--------PKMPYLKAVVLETLRRHPPGhFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFK 353
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1488188862 453 PERF-----TAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQV 510
Cdd:cd11075   354 PERFlaggeAADIDTGSKEIKMMPFGAGRRICPGLGLATLHLELFVARLVQEFEWKLVEGEEV 416
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
65-525 1.75e-42

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: 156.71  E-value: 1.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  65 ESQMELRKLYGPLC-GYYLGRRMfIVISEPDMIKQVLVENFSNFTNRMASGLEFKSVADSVLFLRDkrWEEVRGA---LM 140
Cdd:cd11045     1 EFARQRYRRYGPVSwTGMLGLRV-VALLGPDANQLVLRNRDKAFSSKQGWDPVIGPFFHRGLMLLD--FDEHRAHrriMQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 141 SAFSPEKL----NEMVPLISQAcdllLAHLKryaeSGDAFDIQRCYCNYTTDVVASVAFGtpvdswqAPEDPFVKHCKRF 216
Cdd:cd11045    78 QAFTRSALagylDRMTPGIERA----LARWP----TGAGFQFYPAIKELTLDLATRVFLG-------VDLGPEADKVNKA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 217 FEFCIPRPILVLLLSFPSimVPLARILpnKNRDELNGFFNKLIrnvialrdqqaAEERRR---DFLQMVLdarHSASPMG 293
Cdd:cd11045   143 FIDTVRASTAIIRTPIPG--TRWWRGL--RGRRYLEEYFRRRI-----------PERRAGggdDLFSALC---RAEDEDG 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 294 VQdfdivrdvfsstgckpnpsrqhqpspmarpLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD- 372
Cdd:cd11045   205 DR------------------------------FSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLa 254
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 373 VFKEkhmAPEFCSLEEgLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFN 452
Cdd:cd11045   255 LGKG---TLDYEDLGQ-LEVTDWVFKEALRLVPPVPTLPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFD 330
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1488188862 453 PERFTAE--ARQQHRpFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLESKSAlgPKNG 525
Cdd:cd11045   331 PERFSPEraEDKVHR-YAWAPFGGGAHKCIGLHFAGMEVKAILHQMLRRFRWWSVPGYYPPWWQSPLPA--PKDG 402
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
136-502 1.84e-42

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


Pssm-ID: 410682 [Multi-domain]  Cd Length: 422  Bit Score: 156.69  E-value: 1.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 136 RGALMSAFSPE--KLNEMVPLISQACDLLLAHLKRYAESG---DAFDIQRCYcnyTTDVVASVAFGTPVDSwqapeDPFV 210
Cdd:cd11059    59 RRLLSGVYSKSslLRAAMEPIIRERVLPLIDRIAKEAGKSgsvDVYPLFTAL---AMDVVSHLLFGESFGT-----LLLG 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 211 KHCKRFFEFciprpILVLLLSFPSIMVPLARilpnknrdelngFFNKLIRNVIALRDQQAAEERRRDFLQMVLDARhSAS 290
Cdd:cd11059   131 DKDSREREL-----LRRLLASLAPWLRWLPR------------YLPLATSRLIIGIYFRAFDEIEEWALDLCARAE-SSL 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 291 PMGVQDFDIVRDVFSSTGckpnpsrqhqpSPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLRE 370
Cdd:cd11059   193 AESSDSESLTVLLLEKLK-----------GLKKQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREE 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 371 V-DVFKEKHMAPEFCSLEEgLPYLDMVIAETLRMYPPA-FRFTREAAQDCEVL-GQRIPAGAVLEMAVGALHHDPEHWPS 447
Cdd:cd11059   262 LaGLPGPFRGPPDLEDLDK-LPYLNAVIRETLRLYPPIpGSLPRVVPEGGATIgGYYIPGGTIVSTQAYSLHRDPEVFPD 340
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1488188862 448 PETFNPERF----TAEARQQHRPFtyLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRF 502
Cdd:cd11059   341 PEEFDPERWldpsGETAREMKRAF--WPFGSGSRMCIGMNLALMEMKLALAAIYRNYRT 397
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
88-503 2.05e-42

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: 156.59  E-value: 2.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  88 IVISEPDMIKQVLvenfsNFTNR-------MASGLEFKSVADsvLF-LRDKRW-EEVRGALMSAFSPEKLNEMVPLISQA 158
Cdd:cd11060    11 VSISDPEAIKTIY-----GTRSPytksdwyKAFRPKDPRKDN--LFsERDEKRhAALRRKVASGYSMSSLLSLEPFVDEC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 159 CDLLLAHLKRYAESGDAFDIQRcYCNYTT-DVVASVAFGTPVDswqapedpFVKHCKRFFEFCIP----RPILVLLLSFP 233
Cdd:cd11060    84 IDLLVDLLDEKAVSGKEVDLGK-WLQYFAfDVIGEITFGKPFG--------FLEAGTDVDGYIASidklLPYFAVVGQIP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 234 SIMVPLARILPNKNRDELNGF--FNKLIRNVIALRDQQAAEER--RRDFLQMVLDARHSaspmgvqdfdivrdvfsstgc 309
Cdd:cd11060   155 WLDRLLLKNPLGPKRKDKTGFgpLMRFALEAVAERLAEDAESAkgRKDMLDSFLEAGLK--------------------- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 310 KPNPsrqhqpspmarpLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCSLEE- 388
Cdd:cd11060   214 DPEK------------VTDREVVAEALSNILAGSDTTAIALRAILYYLLKNPRVYAKLRAEIDAAVAEGKLSSPITFAEa 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 389 -GLPYLDMVIAETLRMYPP-AFRFTREA-AQDCEVLGQRIPAGAVLEMAVGALHHDPEHW-PSPETFNPERF---TAEAR 461
Cdd:cd11060   282 qKLPYLQAVIKEALRLHPPvGLPLERVVpPGGATICGRFIPGGTIVGVNPWVIHRDKEVFgEDADVFRPERWleaDEEQR 361
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1488188862 462 QQHRPfTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQ 503
Cdd:cd11060   362 RMMDR-ADLTFGAGSRTCLGKNIALLELYKVIPELLRRFDFE 402
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
74-500 2.31e-41

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: 153.77  E-value: 2.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRmasgleFKSVADSVLF--LRD-------KRWEEVRGALMS-AF 143
Cdd:cd11072     2 YGPLMLLRLGSVPTVVVSSPEAAKEVLKTHDLVFASR------PKLLAARILSygGKDiafapygEYWRQMRKICVLeLL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 144 SPEKLNEMVPLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGtpvdswqapeDPFVKHCKRFFEFCIpR 223
Cdd:cd11072    76 SAKRVQSFRSIREEEVSLLVKKIRESASSSSPVNLSELLFSLTNDIVCRAAFG----------RKYEGKDQDKFKELV-K 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 224 PILVLLLSFP-SIMVPLARILpnknrDELNGFFNKLIRNvialrdqqaaeeRRR--DFLQMVLDARHSASPMGVQDFDIV 300
Cdd:cd11072   145 EALELLGGFSvGDYFPSLGWI-----DLLTGLDRKLEKV------------FKEldAFLEKIIDEHLDKKRSKDEDDDDD 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 301 RDVFSstgckpnpsRQHQPSPMARPLTVDEIvgQAFIF--LIAGYEIITNTLSFA-TYLLAtNPDCQEKLLREV-DVFKE 376
Cdd:cd11072   208 DLLDL---------RLQKEGDLEFPLTRDNI--KAIILdmFLAGTDTSATTLEWAmTELIR-NPRVMKKAQEEVrEVVGG 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 377 KHMAPEfcSLEEGLPYLDMVIAETLRMYPPA-FRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPER 455
Cdd:cd11072   276 KGKVTE--EDLEKLKYLKAVIKETLRLHPPApLLLPRECREDCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPER 353
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1488188862 456 F---TAEARQQHrpFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKF 500
Cdd:cd11072   354 FldsSIDFKGQD--FELIPFGAGRRICPGITFGLANVELALANLLYHF 399
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
72-506 8.16e-41

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: 152.43  E-value: 8.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  72 KLYGPLCGYYLGRRMFIVISEPDMIKQVLvENFSNFTNRMASGLeFKSVADSVLFLRDKRWEEVRGALMSAFSPEKLNEM 151
Cdd:cd20642     9 KTYGKNSFTWFGPIPRVIIMDPELIKEVL-NKVYDFQKPKTNPL-TKLLATGLASYEGDKWAKHRKIINPAFHLEKLKNM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 152 VPLISQACDLLLAHLKRYAESGDAF--DIQRCYCNYTTDVVASVAFGtpvDSWqapedpfvKHCKRFFEFCIpRPILVLL 229
Cdd:cd20642    87 LPAFYLSCSEMISKWEKLVSSKGSCelDVWPELQNLTSDVISRTAFG---SSY--------EEGKKIFELQK-EQGELII 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 230 LSFPSIMVPLARILP---NKNRDELNGFFNKLIRNVIALRDQ--QAAEERRRDFLQMVLDARHsaspmgvqdfdivrdvf 304
Cdd:cd20642   155 QALRKVYIPGWRFLPtkrNRRMKEIEKEIRSSLRGIINKREKamKAGEATNDDLLGILLESNH----------------- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 305 sstgckpNPSRQHQPSPMArpLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREV-DVFKEKHmaPEF 383
Cdd:cd20642   218 -------KEIKEQGNKNGG--MSTEDVIEECKLFYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVlQVFGNNK--PDF 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 384 csleEGLPYL---DMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHW-PSPETFNPERFT-- 457
Cdd:cd20642   287 ----EGLNHLkvvTMILYEVLRLYPPVIQLTRAIHKDTKLGDLTLPAGVQVSLPILLVHRDPELWgDDAKEFNPERFAeg 362
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1488188862 458 -AEARQQHrpFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACP 506
Cdd:cd20642   363 iSKATKGQ--VSYFPFGWGPRICIGQNFALLEAKMALALILQRFSFELSP 410
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
82-530 1.32e-38

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: 146.25  E-value: 1.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  82 LGRRMFIVISEPDMIKQVLVENFSNFTnrMASGLEFKSVAD-SVLFLRDKRWEEVRGALMSAFSPEKLNEMVPLISQACD 160
Cdd:cd20621    10 LGSKPLISLVDPEYIKEFLQNHHYYKK--KFGPLGIDRLFGkGLLFSEGEEWKKQRKLLSNSFHFEKLKSRLPMINEITK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 161 LLLAHLKryaesGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQ----APEDPFVKHCKRFFEFCIPRPILVLLLSFpsIM 236
Cdd:cd20621    88 EKIKKLD-----NQNVNIIQFLQKITGEVVIRSFFGEEAKDLKingkEIQVELVEILIESFLYRFSSPYFQLKRLI--FG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 237 VPLARILPNKNRDELNG---FFNKLIRNVIALRDQQaaeerrrdfLQMvldarhsaspMGVQDFDIVRDVFSSTGCKPNP 313
Cdd:cd20621   161 RKSWKLFPTKKEKKLQKrvkELRQFIEKIIQNRIKQ---------IKK----------NKDEIKDIIIDLDLYLLQKKKL 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 314 SRQhqpspmarpLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVdvfkeKHMAPEFCSLEE----G 389
Cdd:cd20621   222 EQE---------ITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEI-----KSVVGNDDDITFedlqK 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 390 LPYLDMVIAETLRMYPPAFR-FTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFT 468
Cdd:cd20621   288 LNYLNAFIKEVLRLYNPAPFlFPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLNQNNIEDNPFV 367
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1488188862 469 YLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPEtqVPLQLESKSALGPKNGVYIKI 530
Cdd:cd20621   368 FIPFSAGPRNCIGQHLALMEAKIILIYILKNFEIEIIPN--PKLKLIFKLLYEPVNDLLLKL 427
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
74-485 2.84e-37

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: 142.72  E-value: 2.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNR--MASGLEFKSVADSVLFLR-DKRWEEVRGALMSAFSPEKLNE 150
Cdd:cd11065     1 YGPIISLKVGGQTIIVLNSPKAAKDLLEKRSAIYSSRprMPMAGELMGWGMRLLLMPyGPRWRLHRRLFHQLLNPSAVRK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 151 MVPLISQ-ACDLLlahlKRYAESGDAFD--IQRcycnYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFCIPrPILV 227
Cdd:cd11065    81 YRPLQELeSKQLL----RDLLESPDDFLdhIRR----YAASIILRLAYGYRVPSYDDPLLRDAEEAMEGFSEAGS-PGAY 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 228 LLLSFPSIM-VPLARILPNKN-----RDELNGFFNKLIRNVialRDQQAAEERRRDFLQMVLDARHSASPMgvqdfdivr 301
Cdd:cd11065   152 LVDFFPFLRyLPSWLGAPWKRkarelRELTRRLYEGPFEAA---KERMASGTATPSFVKDLLEELDKEGGL--------- 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 302 dvfsstgckpnpsrqhqpspmarplTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAP 381
Cdd:cd11065   220 -------------------------SEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLP 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 382 EFcSLEEGLPYLDMVIAETLRMYPPA-FRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEA 460
Cdd:cd11065   275 TF-EDRPNLPYVNAIVKEVLRWRPVApLGIPHALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDP 353
                         410       420
                  ....*....|....*....|....*....
gi 1488188862 461 rqQHRPFTYLP----FGAGPRSCLGVRLG 485
Cdd:cd11065   354 --KGTPDPPDPphfaFGFGRRICPGRHLA 380
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
79-506 8.88e-37

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: 141.19  E-value: 8.88e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  79 GYYLGRRMFIVISEPDMIKQVLVENFSNFtnrmASGLEFKSVADSVL----FLRD-KRWEEVRGALMSAFSPEKLNE-MV 152
Cdd:cd11064     5 GPWPGGPDGIVTADPANVEHILKTNFDNY----PKGPEFRDLFFDLLgdgiFNVDgELWKFQRKTASHEFSSRALREfME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 153 PL----ISQACDLLLAHLkryAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSW--QAPEDPFVKHCKRFFEFCIPRPIL 226
Cdd:cd11064    81 SVvrekVEKLLVPLLDHA---AESGKVVDLQDVLQRFTFDVICKIAFGVDPGSLspSLPEVPFAKAFDDASEAVAKRFIV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 227 VL----LLSFpsIMVPLARILpNKNRDELNGFFNKLIRNVIA-LRDQQAAEERRRDFLQMVLDARHSASPmgVQDFDIVR 301
Cdd:cd11064   158 PPwlwkLKRW--LNIGSEKKL-REAIRVIDDFVYEVISRRREeLNSREEENNVREDLLSRFLASEEEEGE--PVSDKFLR 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 302 DVFSStgckpnpsrqhqpspmarpltvdeivgqafiFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD-----VFKE 376
Cdd:cd11064   233 DIVLN-------------------------------FILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKsklpkLTTD 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 377 KHMAPEFCSLEEgLPYLDMVIAETLRMYPPAFRFTREAAQDcEVL--GQRIPAGAVLEMAVGALHHDPEHW-PSPETFNP 453
Cdd:cd11064   282 ESRVPTYEELKK-LVYLHAALSESLRLYPPVPFDSKEAVND-DVLpdGTFVKKGTRIVYSIYAMGRMESIWgEDALEFKP 359
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1488188862 454 ERFTAEAR--QQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACP 506
Cdd:cd11064   360 ERWLDEDGglRPESPYKFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVVP 414
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
223-503 1.40e-35

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: 137.73  E-value: 1.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 223 RPILVLLLSFPsimVPLARILpNKNRDELNGFFNKLIRNvialRdQQAAEERRRDFLQMVLDARhsaspmgvqdfdiVRD 302
Cdd:cd11042   147 TPIAFFFPPLP---LPSFRRR-DRARAKLKEIFSEIIQK----R-RKSPDKDEDDMLQTLMDAK-------------YKD 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 303 VfsstgckpnpsrqhqpspmaRPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD-VFKEKHMAP 381
Cdd:cd11042   205 G--------------------RPLTDDEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKeVLGDGDDPL 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 382 EFCSLEEgLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQ--RIPAGAVLEMAVGALHHDPEHWPSPETFNPERF--- 456
Cdd:cd11042   265 TYDVLKE-MPLLHACIKETLRLHPPIHSLMRKARKPFEVEGGgyVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFlkg 343
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1488188862 457 TAEARQQHrPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQ 503
Cdd:cd11042   344 RAEDSKGG-KFAYLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDFE 389
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
338-528 1.66e-35

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: 137.97  E-value: 1.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 338 FLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD-VFKEKHMAPEFCSLEEgLPYLDMVIAETLRMYPPAFRFTREAAQ 416
Cdd:cd20680   251 FMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDeVFGKSDRPVTMEDLKK-LRYLECVIKESLRLFPSVPLFARSLCE 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 417 DCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHV 496
Cdd:cd20680   330 DCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSGRHPYAYIPFSAGPRNCIGQRFALMEEKVVLSCI 409
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1488188862 497 LHKFRFQACpETQVPLQLESKSALGPKNGVYI 528
Cdd:cd20680   410 LRHFWVEAN-QKREELGLVGELILRPQNGIWI 440
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
71-500 1.95e-34

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: 134.58  E-value: 1.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  71 RKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRM--ASGLEFKSVADSVLFL-RDKRWEEVRGALMS-AFSPE 146
Cdd:cd11073     1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDvpDAVRALGHHKSSIVWPpYGPRWRMLRKICTTeLFSPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 147 KLNEMVPLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDswqapeDPFVKHCKRFFEfcIPRPIL 226
Cdd:cd11073    81 RLDATQPLRRRKVRELVRYVREKAGSGEAVDIGRAAFLTSLNLISNTLFSVDLV------DPDSESGSEFKE--LVREIM 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 227 VLLLS------FPSimvpLARILPNKNRDELNGFFNKLIrnvialrdqqaaeerrrDFLQMVLDAR---HSASPMGVQDF 297
Cdd:cd11073   153 ELAGKpnvadfFPF----LKFLDLQGLRRRMAEHFGKLF-----------------DIFDGFIDERlaeREAGGDKKKDD 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 298 DIVRDVFSStgckpnpsrQHQPSPMARpltvDEIVGQAFIFLIAGYEIITNTLSFA-TYLLaTNPDCQEKLLREVD---- 372
Cdd:cd11073   212 DLLLLLDLE---------LDSESELTR----NHIKALLLDLFVAGTDTTSSTIEWAmAELL-RNPEKMAKARAELDevig 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 373 ---VFKEKHMApefcsleeGLPYLDMVIAETLRMYPPA-FRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSP 448
Cdd:cd11073   278 kdkIVEESDIS--------KLPYLQAVVKETLRLHPPApLLLPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDP 349
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1488188862 449 ETFNPERF---TAEARQQHrpFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKF 500
Cdd:cd11073   350 LEFKPERFlgsEIDFKGRD--FELIPFGSGRRICPGLPLAERMVHLVLASLLHSF 402
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
340-510 6.72e-34

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: 133.51  E-value: 6.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 340 IAGYEIITNTLSFATYLLATNPDCQEKLLREVD--VFKEKHmapefcsLEEG----LPYLDMVIAETLRMYPPA-FRFTR 412
Cdd:cd20654   251 LGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDthVGKDRW-------VEESdiknLVYLQAIVKETLRLYPPGpLLGPR 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 413 EAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERF-TAEA----RQQHrpFTYLPFGAGPRSCLGVRLGLL 487
Cdd:cd20654   324 EATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFlTTHKdidvRGQN--FELIPFGSGRRSCPGVSFGLQ 401
                         170       180
                  ....*....|....*....|...
gi 1488188862 488 EVKLTLLHVLHKFRFQACPETQV 510
Cdd:cd20654   402 VMHLTLARLLHGFDIKTPSNEPV 424
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
74-517 3.60e-33

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: 131.29  E-value: 3.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNR--MAS---------GLEFksvADSvlflrDKRWEEVRGALMSA 142
Cdd:cd20673     1 YGPIYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGRprMVTtdllsrngkDIAF---ADY-----SATWQLHRKLVHSA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 143 FS-----PEKLNEMV-PLISQACDLLLAHlkryaeSGDAFDIQRCYCNYTTDVVASVAFGTpvdSWQaPEDPFVKHCKRF 216
Cdd:cd20673    73 FAlfgegSQKLEKIIcQEASSLCDTLATH------NGESIDLSPPLFRAVTNVICLLCFNS---SYK-NGDPELETILNY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 217 FEF---CIPRPILVlllsfpsIMVPLARILPNKNRDelngffnkLIRNVIALRD---QQAAEERR--------RDFLQMV 282
Cdd:cd20673   143 NEGivdTVAKDSLV-------DIFPWLQIFPNKDLE--------KLKQCVKIRDkllQKKLEEHKekfssdsiRDLLDAL 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 283 LDARHSASpmgvqdfdivrdvfsstgcKPNPSRQHQPSPMARP---LTVDEIVGqafifliAGYEIITNTLSFATYLLAT 359
Cdd:cd20673   208 LQAKMNAE-------------------NNNAGPDQDSVGLSDDhilMTVGDIFG-------AGVETTTTVLKWIIAFLLH 261
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 360 NPDCQEKLLREVDVFKEKHMAPEFcSLEEGLPYLDMVIAETLRMYPPA-FRFTREAAQDCEVLGQRIPAGAVLEMAVGAL 438
Cdd:cd20673   262 NPEVQKKIQEEIDQNIGFSRTPTL-SDRNHLPLLEATIREVLRIRPVApLLIPHVALQDSSIGEFTIPKGTRVVINLWAL 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 439 HHDPEHWPSPETFNPERFTAEARQQHR--PFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQaCPETQVPLQLES 516
Cdd:cd20673   341 HHDEKEWDQPDQFMPERFLDPTGSQLIspSLSYLPFGAGPRVCLGEALARQELFLFMAWLLQRFDLE-VPDGGQLPSLEG 419

                  .
gi 1488188862 517 K 517
Cdd:cd20673   420 K 420
PLN02290 PLN02290
cytokinin trans-hydroxylase
39-502 1.75e-32

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 130.70  E-value: 1.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  39 LEKLGLRHPKPSPFIGNLTFFRQGFWESQ-------------------MELRKLYGPLCGYYLGRRMFIVISEPDMIKQV 99
Cdd:PLN02290   39 MERQGVRGPKPRPLTGNILDVSALVSQSTskdmdsihhdivgrllphyVAWSKQYGKRFIYWNGTEPRLCLTETELIKEL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 100 LVEnFSNFTNRmaSGLEFKS----VADSVLFLRDKRWEEVRGALMSAFSPEKLNEMVPLISQACDLLLAHLKRYAESG-D 174
Cdd:PLN02290  119 LTK-YNTVTGK--SWLQQQGtkhfIGRGLLMANGADWYHQRHIAAPAFMGDRLKGYAGHMVECTKQMLQSLQKAVESGqT 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 175 AFDIQRCYCNYTTDVVASVAFGTPVDSWqapedpfvkhcKRFFEfciprpILVLLLSFPS-----IMVPLARILPNKNRD 249
Cdd:PLN02290  196 EVEIGEYMTRLTADIISRTEFDSSYEKG-----------KQIFH------LLTVLQRLCAqatrhLCFPGSRFFPSKYNR 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 250 E---LNGFFNKLIRNVIalrdqqaaeERRRDFLQMvldARHSASPMGVQDFdIVRDVFSSTGCKPNPSRQhqpspmarpL 326
Cdd:PLN02290  259 EiksLKGEVERLLMEII---------QSRRDCVEI---GRSSSYGDDLLGM-LLNEMEKKRSNGFNLNLQ---------L 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 327 TVDEIvgQAFIFliAGYEIITNTLSFATYLLATNPDCQEKLLREV-DVFKEKhmAPEFCSLEEgLPYLDMVIAETLRMYP 405
Cdd:PLN02290  317 IMDEC--KTFFF--AGHETTALLLTWTLMLLASNPTWQDKVRAEVaEVCGGE--TPSVDHLSK-LTLLNMVINESLRLYP 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 406 PAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHW-PSPETFNPERFTAEARQQHRPFtyLPFGAGPRSCLGVRL 484
Cdd:PLN02290  390 PATLLPRMAFEDIKLGDLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPFAPGRHF--IPFAAGPRNCIGQAF 467
                         490
                  ....*....|....*...
gi 1488188862 485 GLLEVKLTLLHVLHKFRF 502
Cdd:PLN02290  468 AMMEAKIILAMLISKFSF 485
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
82-526 1.91e-32

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: 128.83  E-value: 1.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  82 LGRRMfIVISEPDMIKQVLVENFSNFTNrmasGLEFKSVADSVL----FLRD-KRWEEVRGALMSAFSPEKLNEmVPLIS 156
Cdd:cd11063    10 LGTRV-IFTIEPENIKAVLATQFKDFGL----GERRRDAFKPLLgdgiFTSDgEEWKHSRALLRPQFSRDQISD-LELFE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 157 QACDLLLAHLKRYaesGDAFDIQRCYCNYTTDVVASVAFGTPVDS-----WQAPEDPFVKHCKRFFEFCIPRpilvllls 231
Cdd:cd11063    84 RHVQNLIKLLPRD---GSTVDLQDLFFRLTLDSATEFLFGESVDSlkpggDSPPAARFAEAFDYAQKYLAKR-------- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 232 fpSIMVPLARILPNK----NRDELNGFFNKLIRNVIALRDQQAAEERRRDFLqmVLD--ARHSASPMGVQDfdivrdvfs 305
Cdd:cd11063   153 --LRLGKLLWLLRDKkfreACKVVHRFVDPYVDKALARKEESKDEESSDRYV--FLDelAKETRDPKELRD--------- 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 306 stgckpnpsrqhqpspmarpltvdeivgQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREV-DVFKEKHmAPEFC 384
Cdd:cd11063   220 ----------------------------QLLNILLAGRDTTASLLSFLFYELARHPEVWAKLREEVlSLFGPEP-TPTYE 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 385 SLEEgLPYLDMVIAETLRMYPPAFRFTREAAQDCeVL-------GQR---IPAGAVLEMAVGALHHDPEHW-PSPETFNP 453
Cdd:cd11063   271 DLKN-MKYLRAVINETLRLYPPVPLNSRVAVRDT-TLprgggpdGKSpifVPKGTRVLYSVYAMHRRKDIWgPDAEEFRP 348
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1488188862 454 ERFTAEARQqhrPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKF-RFQACPETqvPLQLESKSALGPKNGV 526
Cdd:cd11063   349 ERWEDLKRP---GWEYLPFNGGPRICLGQQFALTEASYVLVRLLQTFdRIESRDVR--PPEERLTLTLSNANGV 417
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
74-530 4.19e-32

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: 127.91  E-value: 4.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNR-------MAS-GLEFKSVADSVLFLRDKRwEEVRGALMSAFSp 145
Cdd:cd20674     1 YGPIYRLRLGLQDVVVLNSKRTIREALVRKWADFAGRphsytgkLVSqGGQDLSLGDYSLLWKAHR-KLTRSALQLGIR- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 146 eklNEMVPLISQACDLLLAHLKRYAesGDAFDIQRCYCNYTTDVVASVAFGTPVDswqapEDPFVkhckRFFEFCIPRpi 225
Cdd:cd20674    79 ---NSLEPVVEQLTQELCERMRAQA--GTPVDIQEEFSLLTCSIICCLTFGDKED-----KDTLV----QAFHDCVQE-- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 226 LVLLLSFPSI----MVPLARILPNKnrdelngffnklirnviALRDQQAAEERRRDFLQMVLDaRHSASPMGVQDFDIVR 301
Cdd:cd20674   143 LLKTWGHWSIqaldSIPFLRFFPNP-----------------GLRRLKQAVENRDHIVESQLR-QHKESLVAGQWRDMTD 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 302 DVFSSTGckpnpsRQHQPSPMArPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDvfkeKHMAP 381
Cdd:cd20674   205 YMLQGLG------QPRGEKGMG-QLLEGHVHMAVVDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELD----RVLGP 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 382 EFCSLEEG---LPYLDMVIAETLRMYPPA-FRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFT 457
Cdd:cd20674   274 GASPSYKDrarLPLLNATIAEVLRLRPVVpLALPHRTTRDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFL 353
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1488188862 458 AEARQQHRpftYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPlqlesksALGPKNGVYIKI 530
Cdd:cd20674   354 EPGAANRA---LLPFGCGARVCLGEPLARLELFVFLARLLQAFTLLPPSDGALP-------SLQPVAGINLKV 416
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
338-529 1.25e-31

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: 126.62  E-value: 1.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 338 FLIAGYEIITNTLSFATYLLATNPDCQEK-------LLREVDVFKEKHMAPefcsleegLPYLDMVIAETLRMYPPAFRF 410
Cdd:cd20678   247 FMFEGHDTTASGISWILYCLALHPEHQQRcreeireILGDGDSITWEHLDQ--------MPYTTMCIKEALRLYPPVPGI 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 411 TREAAQ-----DcevlGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCLGVRLG 485
Cdd:cd20678   319 SRELSKpvtfpD----GRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSSKRHSHAFLPFSAGPRNCIGQQFA 394
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1488188862 486 LLEVK----LTLLhvlhkfRFQACPETQVPLQLESKSALGPKNGVYIK 529
Cdd:cd20678   395 MNEMKvavaLTLL------RFELLPDPTRIPIPIPQLVLKSKNGIHLY 436
PLN02738 PLN02738
carotene beta-ring hydroxylase
61-533 5.24e-31

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 127.34  E-value: 5.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  61 QGFWESQMELRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNR-MASGLEFksVADSVLFLRDKR-WEEVRGA 138
Cdd:PLN02738  151 EAFFIPLYELFLTYGGIFRLTFGPKSFLIVSDPSIAKHILRDNSKAYSKGiLAEILEF--VMGKGLIPADGEiWRVRRRA 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 139 LMSAFSPEKLNEMVPLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQapedpfvkhckrfFE 218
Cdd:PLN02738  229 IVPALHQKYVAAMISLFGQASDRLCQKLDAAASDGEDVEMESLFSRLTLDIIGKAVFNYDFDSLS-------------ND 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 219 FCIPRPILVLLLS--------FPSIMVPLAR-ILPNKNR-DELNGFFNKLIRNVIALRDQQAAEErrrdflqmvlDARHS 288
Cdd:PLN02738  296 TGIVEAVYTVLREaedrsvspIPVWEIPIWKdISPRQRKvAEALKLINDTLDDLIAICKRMVEEE----------ELQFH 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 289 ASPMGVQDFDIVRDVFSSTgcKPNPSRQHQPSPMArpltvdeivgqafiFLIAGYEIITNTLSFATYLLATNPDCQEKLL 368
Cdd:PLN02738  366 EEYMNERDPSILHFLLASG--DDVSSKQLRDDLMT--------------MLIAGHETSAAVLTWTFYLLSKEPSVVAKLQ 429
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 369 REVDVFkekhMAPEFCSLEE--GLPYLDMVIAETLRMYPPAFRFTREAAQDcEVLGQ-RIPAGAVLEMAVGALHHDPEHW 445
Cdd:PLN02738  430 EEVDSV----LGDRFPTIEDmkKLKYTTRVINESLRLYPQPPVLIRRSLEN-DMLGGyPIKRGEDIFISVWNLHRSPKHW 504
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 446 PSPETFNPERFTAEA---RQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQvPLQLESKSALGP 522
Cdd:PLN02738  505 DDAEKFNPERWPLDGpnpNETNQNFSYLPFGGGPRKCVGDMFASFENVVATAMLVRRFDFQLAPGAP-PVKMTTGATIHT 583
                         490
                  ....*....|.
gi 1488188862 523 KNGVYIKIVSR 533
Cdd:PLN02738  584 TEGLKMTVTRR 594
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
326-511 5.63e-31

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: 125.19  E-value: 5.63e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 326 LTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREV-DVFKEKHmaPEFCSLEE--GLPYLDMVIAETLR 402
Cdd:cd20679   240 LSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVqELLKDRE--PEEIEWDDlaQLPFLTMCIKESLR 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 403 MYPPAFRFTREAAQDCEVLGQR-IPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCLG 481
Cdd:cd20679   318 LHPPVTAISRCCTQDIVLPDGRvIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGRSPLAFIPFSAGPRNCIG 397
                         170       180       190
                  ....*....|....*....|....*....|
gi 1488188862 482 VRLGLLEVKLTLLHVLHKFRFqaCPETQVP 511
Cdd:cd20679   398 QTFAMAEMKVVLALTLLRFRV--LPDDKEP 425
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
74-511 1.18e-30

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


Pssm-ID: 410652 [Multi-domain]  Cd Length: 425  Bit Score: 123.82  E-value: 1.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLeFKSVADS--VLFLRDKRWEEVRG-ALMS--AFSPEKL 148
Cdd:cd11026     1 YGPVFTVYLGSKPVVVLCGYEAVKEALVDQAEEFSGRPPVPL-FDRVTKGygVVFSNGERWKQLRRfSLTTlrNFGMGKR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 149 nEMVPLISQACDLLLAHLKRYaeSGDAFDIQRCYCNYTTDVVASVAFGTPVDSwqapEDPF----VKHCKRFFEFCIpRP 224
Cdd:cd11026    80 -SIEERIQEEAKFLVEAFRKT--KGKPFDPTFLLSNAVSNVICSIVFGSRFDY----EDKEflklLDLINENLRLLS-SP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 225 ILVLLLSFPSIMvplaRILPnknrdelnGFFNKLIRNVIALRD--QQAAEERRRDflqmvLDArhsASPmgvQDFdIvrD 302
Cdd:cd11026   152 WGQLYNMFPPLL----KHLP--------GPHQKLFRNVEEIKSfiRELVEEHRET-----LDP---SSP---RDF-I--D 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 303 VFSS--TGCKPNPSRqhqpspmarPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMA 380
Cdd:cd11026   206 CFLLkmEKEKDNPNS---------EFHEENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRT 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 381 PefcSLE--EGLPYLDMVIAETLRM---YPPAFrfTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPER 455
Cdd:cd11026   277 P---SLEdrAKMPYTDAVIHEVQRFgdiVPLGV--PHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGH 351
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1488188862 456 FTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVP 511
Cdd:cd11026   352 FLDEQGKFKKNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSLSSPVGPKDP 407
PLN02183 PLN02183
ferulate 5-hydroxylase
47-521 1.46e-30

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 124.96  E-value: 1.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  47 PKPSPFIGNLTFFRQGFWESQMELRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMA----SGLEFKSvAD 122
Cdd:PLN02183   41 PKGLPIIGNMLMMDQLTHRGLANLAKQYGGLFHMRMGYLHMVAVSSPEVARQVLQVQDSVFSNRPAniaiSYLTYDR-AD 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 123 SVLFLRDKRWEEVRG-ALMSAFSpEKLNEMVPLISQACDLLLahlKRYAES-GDAFDIQRCYCNYTTDVVASVAFGTPVD 200
Cdd:PLN02183  120 MAFAHYGPFWRQMRKlCVMKLFS-RKRAESWASVRDEVDSMV---RSVSSNiGKPVNIGELIFTLTRNITYRAAFGSSSN 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 201 SWQapeDPFVKHCKRFFEfciprpiLVLLLSFPSIMVPLARILPN-------KNRDELNGFFNKLIRNVIALRDQQAAEE 273
Cdd:PLN02183  196 EGQ---DEFIKILQEFSK-------LFGAFNVADFIPWLGWIDPQglnkrlvKARKSLDGFIDDIIDDHIQKRKNQNADN 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 274 RRRDFlqmvldarhsaspmgvqDFDIVRDV--FSSTGCKPNPSRQHQPspmARPLTVDEIVGQAFIFLIAGYEIITNTLS 351
Cdd:PLN02183  266 DSEEA-----------------ETDMVDDLlaFYSEEAKVNESDDLQN---SIKLTRDNIKAIIMDVMFGGTETVASAIE 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 352 FATYLLATNPDCQEKLLREV-DVFKEKHMAPEfcSLEEGLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAV 430
Cdd:PLN02183  326 WAMAELMKSPEDLKRVQQELaDVVGLNRRVEE--SDLEKLTYLKCTLKETLRLHPPIPLLLHETAEDAEVAGYFIPKRSR 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 431 LEMAVGALHHDPEHWPSPETFNPERF----TAEARQQHrpFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQaCP 506
Cdd:PLN02183  404 VMINAWAIGRDKNSWEDPDTFKPSRFlkpgVPDFKGSH--FEFIPFGSGRRSCPGMQLGLYALDLAVAHLLHCFTWE-LP 480
                         490
                  ....*....|....*
gi 1488188862 507 ETQVPLQLESKSALG 521
Cdd:PLN02183  481 DGMKPSELDMNDVFG 495
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
338-513 1.46e-30

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: 123.48  E-value: 1.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 338 FLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPefcSLEE--GLPYLDMVIAETLRMYPPA-FRFTREA 414
Cdd:cd20651   233 LFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLP---TLDDrsKLPYTEAVILEVLRIFTLVpIGIPHRA 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 415 AQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLL 494
Cdd:cd20651   310 LKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKLLKDEWFLPFGAGKRRCLGESLARNELFLFFT 389
                         170
                  ....*....|....*....
gi 1488188862 495 HVLHKFRFQACPETQVPLQ 513
Cdd:cd20651   390 GLLQNFTFSPPNGSLPDLE 408
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
74-522 2.69e-29

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: 119.90  E-value: 2.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSVA-DSVLFLRDKRWEEVRG-ALMS----AFSPEK 147
Cdd:cd20662     1 YGNIFSLQLGSISSVIVTGLPLIKEALVTQEQNFMNRPETPLRERIFNkNGLIFSSGQTWKEQRRfALMTlrnfGLGKKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 148 LNEMvplISQACDLLLAHLKryAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSwqapEDPFVKHCKRFFEFCI---PRP 224
Cdd:cd20662    81 LEER---IQEECRHLVEAIR--EEKGNPFNPHFKINNAVSNIICSVTFGERFEY----HDEWFQELLRLLDETVyleGSP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 225 ILVLLLSFPSIMvplarilpnknrDELNGFFNKLIRNvialrdqqaaEERRRDFL-QMVLDARHSASPMGVQDFdivRDV 303
Cdd:cd20662   152 MSQLYNAFPWIM------------KYLPGSHQTVFSN----------WKKLKLFVsDMIDKHREDWNPDEPRDF---IDA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 304 FSSTGCKPnpsrqhqPSPMARpLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPef 383
Cdd:cd20662   207 YLKEMAKY-------PDPTTS-FNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQP-- 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 384 cSLE--EGLPYLDMVIAETLRM---YPpaFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTA 458
Cdd:cd20662   277 -SLAdrESMPYTNAVIHEVQRMgniIP--LNVPREVAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFLE 353
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1488188862 459 EARQQHRPfTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLESKSALGP 522
Cdd:cd20662   354 NGQFKKRE-AFLPFSMGKRACLGEQLARSELFIFFTSLLQKFTFKPPPNEKLSLKFRMGITLSP 416
PTZ00404 PTZ00404
cytochrome P450; Provisional
34-510 7.37e-29

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 119.44  E-value: 7.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  34 SAFSRLEKLGLRHPKPSPFIGNLTFFRQGFWESQMELRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMAS 113
Cdd:PTZ00404   21 KKYKKIHKNELKGPIPIPILGNLHQLGNLPHRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKI 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 114 -GLEFKSVADSVLFLRDKRWEEVRGALMSAFSPEKLNEMVPLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVAS 192
Cdd:PTZ00404  101 pSIKHGTFYHGIVTSSGEYWKRNREIVGKAMRKTNLKHIYDLLDDQVDVLIESMKKIESSGETFEPRYYLTKFTMSAMFK 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 193 VAFGTPV----DSWQAPEDPFVKHCKRFFEFC----------IPRPILVLLL-----SFPSIMvplarilpnknrdelng 253
Cdd:PTZ00404  181 YIFNEDIsfdeDIHNGKLAELMGPMEQVFKDLgsgslfdvieITQPLYYQYLehtdkNFKKIK----------------- 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 254 ffnKLIRNVIALRDQQAAEERRRDFLQMVLDARHSASpmgvqDFDIVrdvfsstgckpnpsrqhqpspmarpltvdEIVG 333
Cdd:PTZ00404  244 ---KFIKEKYHEHLKTIDPEVPRDLLDLLIKEYGTNT-----DDDIL-----------------------------SILA 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 334 QAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREV-DVFKEKHMApeFCSLEEGLPYLDMVIAETLRMYPPA-FRFT 411
Cdd:PTZ00404  287 TILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIkSTVNGRNKV--LLSDRQSTPYTVAIIKETLRYKPVSpFGLP 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 412 REAAQDCEVL-GQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTaearQQHRPFTYLPFGAGPRSCLGVRLGLLEVK 490
Cdd:PTZ00404  365 RSTSNDIIIGgGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFL----NPDSNDAFMPFSIGPRNCVGQQFAQDELY 440
                         490       500
                  ....*....|....*....|
gi 1488188862 491 LTLLHVLHKFRFQACPETQV 510
Cdd:PTZ00404  441 LAFSNIILNFKLKSIDGKKI 460
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
330-507 2.09e-28

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: 118.17  E-value: 2.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 330 EIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLRE-VDVFKEKHMAPEFCSLEE----GLPYLDMVIAETLRMY 404
Cdd:cd20622   262 VIHDELFGYLIAGHDTTSTALSWGLKYLTANQDVQSKLRKAlYSAHPEAVAEGRLPTAQEiaqaRIPYLDAVIEEILRCA 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 405 PPAFRFTREAAQDCEVLGQRIPAGA-VLEMAVG------ALHHDPE-------------HWPSPET---FNPERFTAEAR 461
Cdd:cd20622   342 NTAPILSREATVDTQVLGYSIPKGTnVFLLNNGpsylspPIEIDESrrssssaakgkkaGVWDSKDiadFDPERWLVTDE 421
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1488188862 462 QQH------RPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPE 507
Cdd:cd20622   422 ETGetvfdpSAGPTLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFELLPLPE 473
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
75-493 3.31e-28

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


Pssm-ID: 410748 [Multi-domain]  Cd Length: 433  Bit Score: 116.93  E-value: 3.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  75 GPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSVADSVLFLR---DKRWEEVRGALMS-AFSPEKLNE 150
Cdd:cd20655     1 GPLLHLRIGSVPCVVVSSASVAKEILKTHDLNFSSRPVPAAAESLLYGSSGFAFapyGDYWKFMKKLCMTeLLGPRALER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 151 MVPLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGT--PVDSWQAPE-----------------DPFVK 211
Cdd:cd20655    81 FRPIRAQELERFLRRLLDKAEKGESVDIGKELMKLTNNIICRMIMGRscSEENGEAEEvrklvkesaelagkfnaSDFIW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 212 HCKRFFEFCIPRPILVLLLSFPSImvpLARILpnKNRDElngffnklirnviALRDQQaaEERRRDFLQMVLDARHsasp 291
Cdd:cd20655   161 PLKKLDLQGFGKRIMDVSNRFDEL---LERII--KEHEE-------------KRKKRK--EGGSKDLLDILLDAYE---- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 292 mgvqdfdivrdvfsstgckpNPSRQHQpspmarpLTVDEIvgQAFI--FLIAGYEIITNTLSFATYLLATNPDCQEKLLR 369
Cdd:cd20655   217 --------------------DENAEYK-------ITRNHI--KAFIldLFIAGTDTSAATTEWAMAELINNPEVLEKARE 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 370 EVD-VFKEKHMAPEfcSLEEGLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSP 448
Cdd:cd20655   268 EIDsVVGKTRLVQE--SDLPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKINGYDIPEKTTLFVNVYAIMRDPNYWEDP 345
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1488188862 449 ETFNPERFTA--------EARQQHrpFTYLPFGAGPRSCLGVRLGLLEVKLTL 493
Cdd:cd20655   346 LEFKPERFLAssrsgqelDVRGQH--FKLLPFGSGRRGCPGASLAYQVVGTAI 396
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
74-520 2.11e-27

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: 114.32  E-value: 2.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNR--MASgLEFKSVADSVLFLRD-KRWEEVRGALMSA---FSPEK 147
Cdd:cd11028     1 YGDVFQIRMGSRPVVVLNGLETIKQALVRQGEDFAGRpdFYS-FQFISNGKSMAFSDYgPRWKLHRKLAQNAlrtFSNAR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 148 ----LNEMVpliSQACDLLLAHLKRYAESGDAFDIQrcycNYTTDVVASV----AFGTPVDSwqapEDP----FVKHCKR 215
Cdd:cd11028    80 thnpLEEHV---TEEAEELVTELTENNGKPGPFDPR----NEIYLSVGNVicaiCFGKRYSR----DDPefleLVKSNDD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 216 FFEF---CIPRPILvlllsfpsimvPLARILPN---KNRDELNGFFNKLIRNVIalrdqqaaEERRRDFLQM----VLDA 285
Cdd:cd11028   149 FGAFvgaGNPVDVM-----------PWLRYLTRrklQKFKELLNRLNSFILKKV--------KEHLDTYDKGhirdITDA 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 286 RHSAS---PMGVQDFDIVRDvfsstgckpnpsrQHQPSpmarplTVDEIVGqafifliAGYEIITNTLSFATYLLATNPD 362
Cdd:cd11028   210 LIKASeekPEEEKPEVGLTD-------------EHIIS------TVQDLFG-------AGFDTISTTLQWSLLYMIRYPE 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 363 CQEKLLREVDVFKEKHMAPEFCSLEEgLPYLDMVIAETLR---MYPpaFRFTREAAQDCEVLGQRIPAGAVLEMAVGALH 439
Cdd:cd11028   264 IQEKVQAELDRVIGRERLPRLSDRPN-LPYTEAFILETMRhssFVP--FTIPHATTRDTTLNGYFIPKGTVVFVNLWSVN 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 440 HDPEHWPSPETFNPERFTAEARQQHRPFT--YLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPEtqVPLQLESK 517
Cdd:cd11028   341 HDEKLWPDPSVFRPERFLDDNGLLDKTKVdkFLPFGAGRRRCLGEELARMELFLFFATLLQQCEFSVKPG--EKLDLTPI 418

                  ...
gi 1488188862 518 SAL 520
Cdd:cd11028   419 YGL 421
PLN02936 PLN02936
epsilon-ring hydroxylase
74-533 2.77e-27

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 114.89  E-value: 2.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLvenfSNFTNRMASGLefksVADSVLFL--------RDKRWEEVRGALMSAFSP 145
Cdd:PLN02936   49 YGPVYRLAAGPRNFVVVSDPAIAKHVL----RNYGSKYAKGL----VAEVSEFLfgsgfaiaEGELWTARRRAVVPSLHR 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 146 EKLNEMVPLISQAC-DLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQApEDPFVKHCKRFFEFCIPRP 224
Cdd:PLN02936  121 RYLSVMVDRVFCKCaERLVEKLEPVALSGEAVNMEAKFSQLTLDVIGLSVFNYNFDSLTT-DSPVIQAVYTALKEAETRS 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 225 ILVLllsfPSIMVPLARILPNKNRDELNGFfnKLIRNVIA-----LRDQQAAEERRRDFLQMVLDARHSaspmgvqdfdI 299
Cdd:PLN02936  200 TDLL----PYWKVDFLCKISPRQIKAEKAV--TVIRETVEdlvdkCKEIVEAEGEVIEGEEYVNDSDPS----------V 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 300 VRDVFSStgckpnpsRQHQPSPMARpltvDEIVGqafiFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD-VFKEKh 378
Cdd:PLN02936  264 LRFLLAS--------REEVSSVQLR----DDLLS----MLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDrVLQGR- 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 379 mAPEFCSLEEgLPYLDMVIAETLRMYPPAFRFTREAAQDcEVL--GQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERF 456
Cdd:PLN02936  327 -PPTYEDIKE-LKYLTRCINESMRLYPHPPVLIRRAQVE-DVLpgGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERF 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 457 TAEARQQHRP---FTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVplQLESKSALGPKNGVYIKIVSR 533
Cdd:PLN02936  404 DLDGPVPNETntdFRYIPFSGGPRKCVGDQFALLEAIVALAVLLQRLDLELVPDQDI--VMTTGATIHTTNGLYMTVSRR 481
PLN02655 PLN02655
ent-kaurene oxidase
51-481 3.17e-26

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 111.37  E-value: 3.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  51 PFIGNL----------TFFRqgfWEsqmelrKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNR-MASGLEFKS 119
Cdd:PLN02655    8 PVIGNLlqlkekkphrTFTK---WS------EIYGPIYTIRTGASSVVVLNSTEVAKEAMVTKFSSISTRkLSKALTVLT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 120 VADSVLFLRD--KRWEEVRGALMSA---FSPEK----LNEMvpLISQACDLLLAHLKRYAESgdAFDIQRCYCNYTTDVV 190
Cdd:PLN02655   79 RDKSMVATSDygDFHKMVKRYVMNNllgANAQKrfrdTRDM--LIENMLSGLHALVKDDPHS--PVNFRDVFENELFGLS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 191 ASVAFGTPVDSWQAPEdpfvkhckrfFEFCIPR----PILVLLLSFPSIMV------PLARILPNKNrdelngfFNKLIR 260
Cdd:PLN02655  155 LIQALGEDVESVYVEE----------LGTEISKeeifDVLVHDMMMCAIEVdwrdffPYLSWIPNKS-------FETRVQ 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 261 NVialrdqqaaeERRRDFLQMVLDARHSASPMGVQDFDIVRDVFSSTgckpnpsrqhqpspmARPLTVDEIVGQAFIFLI 340
Cdd:PLN02655  218 TT----------EFRRTAVMKALIKQQKKRIARGEERDCYLDFLLSE---------------ATHLTDEQLMMLVWEPII 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 341 AGYEIITNTLSFATYLLATNPDCQEKLLREV------DVFKEKHMaPEfcsleegLPYLDMVIAETLRMYPPA----FRF 410
Cdd:PLN02655  273 EAADTTLVTTEWAMYELAKNPDKQERLYREIrevcgdERVTEEDL-PN-------LPYLNAVFHETLRKYSPVpllpPRF 344
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1488188862 411 TREaaqDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCLG 481
Cdd:PLN02655  345 VHE---DTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLGEKYESADMYKTMAFGAGKRVCAG 412
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
329-493 1.19e-25

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: 109.23  E-value: 1.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 329 DEIV-GQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD-VFKEKHMapefcsLEEG----LPYLDMVIAETLR 402
Cdd:cd20653   225 DEIIkGLILVMLLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDtQVGQDRL------IEESdlpkLPYLQNIISETLR 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 403 MYPPA-FRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRpftYLPFGAGPRSCLG 481
Cdd:cd20653   299 LYPAApLLVPHESSEDCKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFEGEEREGYK---LIPFGLGRRACPG 375
                         170
                  ....*....|..
gi 1488188862 482 VRLGLLEVKLTL 493
Cdd:cd20653   376 AGLAQRVVGLAL 387
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
322-509 1.19e-25

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: 109.24  E-value: 1.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 322 MARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCSLEEgLPYLDMVIAETL 401
Cdd:cd20647   229 VSKELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPK-LPLIRALLKETL 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 402 RMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFT-AEARQQHRPFTYLPFGAGPRSCL 480
Cdd:cd20647   308 RLFPVLPGNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLrKDALDRVDNFGSIPFGYGIRSCI 387
                         170       180
                  ....*....|....*....|....*....
gi 1488188862 481 GVRLGLLEVKLTLLHVLHKFRFQACPETQ 509
Cdd:cd20647   388 GRRIAELEIHLALIQLLQNFEIKVSPQTT 416
PLN02966 PLN02966
cytochrome P450 83A1
47-503 1.76e-25

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 109.84  E-value: 1.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  47 PKPSPFIGNLTFFR----QGFWESQMelrKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMA-SGLEFKSVA 121
Cdd:PLN02966   34 PSPLPVIGNLLQLQklnpQRFFAGWA---KKYGPILSYRIGSRTMVVISSAELAKELLKTQDVNFADRPPhRGHEFISYG 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 122 --DSVLFLRDKRWEEVRGALMS-AFSPEKLNEMVPLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTP 198
Cdd:PLN02966  111 rrDMALNHYTPYYREIRKMGMNhLFSPTRVATFKHVREEEARRMMDKINKAADKSEVVDISELMLTFTNSVVCRQAFGKK 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 199 VDswqapEDPfvKHCKRFFEFcIPRPILVLLLSFPSIMVPLARILpnknrDELNGFFNKLirnvialrdqQAAEERRRDF 278
Cdd:PLN02966  191 YN-----EDG--EEMKRFIKI-LYGTQSVLGKIFFSDFFPYCGFL-----DDLSGLTAYM----------KECFERQDTY 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 279 LQMVLDAR---HSASPMGVQDFDIVRDVFsstgckpnpsrqhQPSPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATY 355
Cdd:PLN02966  248 IQEVVNETldpKRVKPETESMIDLLMEIY-------------KEQPFASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 356 LLATNPDCQEKLLREV-DVFKEKHMApeFCSLEE--GLPYLDMVIAETLRMYPP-AFRFTREAAQDCEVLGQRIPAGAVL 431
Cdd:PLN02966  315 YLMKYPQVLKKAQAEVrEYMKEKGST--FVTEDDvkNLPYFRALVKETLRIEPViPLLIPRACIQDTKIAGYDIPAGTTV 392
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1488188862 432 EMAVGALHHDPEHW-PSPETFNPERF-TAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQ 503
Cdd:PLN02966  393 NVNAWAVSRDEKEWgPNPDEFRPERFlEKEVDFKGTDYEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFK 466
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
326-508 2.15e-25

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: 108.59  E-value: 2.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 326 LTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREV-DVFKEKHM--APEFCSLeeglPYLDMVIAETLR 402
Cdd:cd20646   229 LSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEViSVCPGDRIptAEDIAKM----PLLKAVIKETLR 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 403 MYP--PA-FRFTREaaQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSC 479
Cdd:cd20646   305 LYPvvPGnARVIVE--KEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRDGGLKHHPFGSIPFGYGVRAC 382
                         170       180
                  ....*....|....*....|....*....
gi 1488188862 480 LGVRLGLLEVKLTLLHVLHKFRFQACPET 508
Cdd:cd20646   383 VGRRIAELEMYLALSRLIKRFEVRPDPSG 411
PLN02687 PLN02687
flavonoid 3'-monooxygenase
47-521 2.18e-24

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 106.43  E-value: 2.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  47 PKPSPFIGNLTFFRQGFWESQMELRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMA-SGLEFKSV--ADS 123
Cdd:PLN02687   39 PRGWPVLGNLPQLGPKPHHTMAALAKTYGPLFRLRFGFVDVVVAASASVAAQFLRTHDANFSNRPPnSGAEHMAYnyQDL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 124 VLFLRDKRWEEVRG-ALMSAFSPEKLNEMVPLISQACDLLLAHLKRYAES-----GDAFDIqrcyCnyTTDVVASVAFGT 197
Cdd:PLN02687  119 VFAPYGPRWRALRKiCAVHLFSAKALDDFRHVREEEVALLVRELARQHGTapvnlGQLVNV----C--TTNALGRAMVGR 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 198 PVdsWQAPEDPFVKhckrffEFcipRPILVLLLSFPSIM-----VPLARILpnknrdELNGFFNKLIRnvialrdqqaAE 272
Cdd:PLN02687  193 RV--FAGDGDEKAR------EF---KEMVVELMQLAGVFnvgdfVPALRWL------DLQGVVGKMKR----------LH 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 273 ERRRDFLQMVL-DARHSASPMGVQDFDIVRDVFSSTgckpnpsRQHQPSPMARPLTVDEIVGQAFIFLIAGYEIITNTLS 351
Cdd:PLN02687  246 RRFDAMMNGIIeEHKAAGQTGSEEHKDLLSTLLALK-------REQQADGEGGRITDTEIKALLLNLFTAGTDTTSSTVE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 352 FATYLLATNPDCQEKLLREVDVFKEKHMAPEFCSLEEgLPYLDMVIAETLRMYPPA-FRFTREAAQDCEVLGQRIPAGAV 430
Cdd:PLN02687  319 WAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQ-LTYLQAVIKETFRLHPSTpLSLPRMAAEECEINGYHIPKGAT 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 431 LEMAVGALHHDPEHWPSPETFNPERFT-----AEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQaC 505
Cdd:PLN02687  398 LLVNVWAIARDPEQWPDPLEFRPDRFLpggehAGVDVKGSDFELIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWE-L 476
                         490
                  ....*....|....*.
gi 1488188862 506 PETQVPLQLESKSALG 521
Cdd:PLN02687  477 ADGQTPDKLNMEEAYG 492
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
96-501 4.27e-24

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: 103.83  E-value: 4.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  96 IKQVLV--ENFS-NFTNRMASGLEFKSvADSVLFLRDKRWEEVRGALMSAFSPEKLNEMVPLISQACDLLLAHLkryaES 172
Cdd:cd11032    23 VKRVLSdpATFSsDLGRLLPGEDDALT-EGSLLTMDPPRHRKLRKLVSQAFTPRLIADLEPRIAEITDELLDAV----DG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 173 GDAFDIqrcycnyttdvVASVAFgtpvdswqapedpfvkhckrffefciPRPILVL--LLSFPSimvplarilpnKNRDe 250
Cdd:cd11032    98 RGEFDL-----------VEDLAY--------------------------PLPVIVIaeLLGVPA-----------EDRE- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 251 lngFFNKLIRNVIALRDQQAAEErrrDFLQMVLDARHsasPMGVQDFDIVRDvfsstgCKPNP-----SRQHQPSPMARP 325
Cdd:cd11032   129 ---LFKKWSDALVSGLGDDSFEE---EEVEEMAEALR---ELNAYLLEHLEE------RRRNPrddliSRLVEAEVDGER 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 326 LTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLrevdvfKEKHMAPEFcsleeglpyldmvIAETLRMYP 405
Cdd:cd11032   194 LTDEEIVGFAILLLIAGHETTTNLLGNAVLCLDEDPEVAARLR------ADPSLIPGA-------------IEEVLRYRP 254
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 406 PAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERftaearqqhRPFTYLPFGAGPRSCLGVRLG 485
Cdd:cd11032   255 PVQRTARVTTEDVELGGVTIPAGQLVIAWLASANRDERQFEDPDTFDIDR---------NPNPHLSFGHGIHFCLGAPLA 325
                         410
                  ....*....|....*.
gi 1488188862 486 LLEVKLTLLHVLHKFR 501
Cdd:cd11032   326 RLEARIALEALLDRFP 341
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
326-507 5.78e-24

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: 104.45  E-value: 5.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 326 LTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCSLEEgLPYLDMVIAETLRMYP 405
Cdd:cd20648   230 LPMKSIYGNVTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVAR-MPLLKAVVKEVLRLYP 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 406 PAFRFTREAA-QDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEaRQQHRPFTYLPFGAGPRSCLGVRL 484
Cdd:cd20648   309 VIPGNARVIPdRDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLGK-GDTHHPYASLPFGFGKRSCIGRRI 387
                         170       180
                  ....*....|....*....|...
gi 1488188862 485 GLLEVKLTLLHVLHKFRFQACPE 507
Cdd:cd20648   388 AELEVYLALARILTHFEVRPEPG 410
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
326-521 6.85e-24

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: 104.43  E-value: 6.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 326 LTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDV-------FKEKHMApefcsleeGLPYLDMVIA 398
Cdd:cd20657   224 LTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQvigrdrrLLESDIP--------NLPYLQAICK 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 399 ETLRMYPPA-FRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRP----FTYLPFG 473
Cdd:cd20657   296 ETFRLHPSTpLNLPRIASEACEVDGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPGRNAKVDVrgndFELIPFG 375
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1488188862 474 AGPRSCLGVRLGLLEVKLTLLHVLHKFRFQaCPETQVPLQLESKSALG 521
Cdd:cd20657   376 AGRRICAGTRMGIRMVEYILATLVHSFDWK-LPAGQTPEELNMEEAFG 422
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
349-510 1.27e-23

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: 103.26  E-value: 1.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 349 TLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCSLEeGLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAG 428
Cdd:cd20643   253 TLQWTLYELARNPNVQEMLRAEVLAARQEAQGDMVKMLK-SVPLLKAAIKETLRLHPVAVSLQRYITEDLVLQNYHIPAG 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 429 AVLEMAVGALHHDPEHWPSPETFNPERFTaEARQQHrpFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPET 508
Cdd:cd20643   332 TLVQVGLYAMGRDPTVFPKPEKYDPERWL-SKDITH--FRNLGFGFGPRQCLGRRIAETEMQLFLIHMLENFKIETQRLV 408

                  ..
gi 1488188862 509 QV 510
Cdd:cd20643   409 EV 410
PLN02302 PLN02302
ent-kaurenoic acid oxidase
324-511 1.32e-23

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 104.02  E-value: 1.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 324 RPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD-VFKEKHMAPEFCSLEE--GLPYLDMVIAET 400
Cdd:PLN02302  281 RKLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEVLQKAKAEQEeIAKKRPPGQKGLTLKDvrKMEYLSQVIDET 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 401 LRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFtaeARQQHRPFTYLPFGAGPRSCL 480
Cdd:PLN02302  361 LRLINISLTVFREAKTDVEVNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRW---DNYTPKAGTFLPFGLGSRLCP 437
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1488188862 481 GVRLGLLEVKLTLLHVLHKFRFQA----CPETQVP 511
Cdd:PLN02302  438 GNDLAKLEISIFLHHFLLGYRLERlnpgCKVMYLP 472
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
75-512 1.78e-23

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: 102.87  E-value: 1.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  75 GPLCGYYLGRRMFIVISEPDMIKQVLveNFSNFTNRMASGLEFKSVADSVLFL------RDKRwEEVRGAL----MSAFS 144
Cdd:cd20652     1 GSIFSLKMGSVYTVVLSDPKLIRDTF--RRDEFTGRAPLYLTHGIMGGNGIICaegdlwRDQR-RFVHDWLrqfgMTKFG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 145 PEKlNEMVPLISQACDLLLAHLKryAESGDAFDIQRCYCNYTTDVVASVAFGTPVDswqaPEDPfvkhCKRFFEFCIPRP 224
Cdd:cd20652    78 NGR-AKMEKRIATGVHELIKHLK--AESGQPVDPSPVLMHSLGNVINDLVFGFRYK----EDDP----TWRWLRFLQEEG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 225 ILVLLLSFPSIMVPLARILPNKNRDelngfFNKLIRNvialrdqqaaEERRRDFLQMVLDARHsaspmgvQDFDIVRDVF 304
Cdd:cd20652   147 TKLIGVAGPVNFLPFLRHLPSYKKA-----IEFLVQG----------QAKTHAIYQKIIDEHK-------RRLKPENPRD 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 305 SSTGCKPNPSRQHQPSPMARPlTVDEIVGQAFIFLI-----AGYEIITNTLSFATYLLATNPDCQEKLLREVDvfkEKHM 379
Cdd:cd20652   205 AEDFELCELEKAKKEGEDRDL-FDGFYTDEQLHHLLadlfgAGVDTTITTLRWFLLYMALFPKEQRRIQRELD---EVVG 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 380 APEFCSLEEG--LPYLDMVIAETLRM---YPPAFrfTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPE 454
Cdd:cd20652   281 RPDLVTLEDLssLPYLQACISESQRIrsvVPLGI--PHGCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPE 358
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1488188862 455 RFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPL 512
Cdd:cd20652   359 RFLDTDGKYLKPEAFIPFQTGKRMCLGDELARMILFLFTARILRKFRIALPDGQPVDS 416
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
74-512 2.76e-23

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: 102.16  E-value: 2.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRmasglefKSVADSVLFLRDKR---------WEEVRGALMSA-- 142
Cdd:cd20666     1 YGNIFSLFIGSQLVVVLNDFESVREALVQKAEVFSDR-------PSVPLVTILTKGKGivfapygpvWRQQRKFSHSTlr 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 143 -FSPEKLNeMVPLISQACDLLLAHLKRYaeSGDAFDIQRCYCNYTTDVVASVAFGTPVDsWQAPE-DPFVKHCKRFFEFC 220
Cdd:cd20666    74 hFGLGKLS-LEPKIIEEFRYVKAEMLKH--GGDPFNPFPIVNNAVSNVICSMSFGRRFD-YQDVEfKTMLGLMSRGLEIS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 221 IPRPilvLLLSFPSIMVPLARILPNKNRDELNGFFNKLIRNVIALRDQQAAEERRRDFLQMVL----DARHSASPMGVQD 296
Cdd:cd20666   150 VNSA---AILVNICPWLYYLPFGPFRELRQIEKDITAFLKKIIADHRETLDPANPRDFIDMYLlhieEEQKNNAESSFNE 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 297 ---FDIVRDVFsstgckpnpsrqhqpspmarpltvdeivgqafiflIAGYEIITNTLSFATYLLATNPDCQEKLLREVDV 373
Cdd:cd20666   227 dylFYIIGDLF-----------------------------------IAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDT 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 374 FKEKHMAPEFCSlEEGLPYLDMVIAETLRMYP-PAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFN 452
Cdd:cd20666   272 VIGPDRAPSLTD-KAQMPFTEATIMEVQRMTVvVPLSIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFM 350
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 453 PERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPL 512
Cdd:cd20666   351 PSRFLDENGQLIKKEAFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTFLLPPNAPKPS 410
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
47-500 1.41e-22

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 100.92  E-value: 1.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  47 PKPSPFIGNL----TFFRQGFWesqMELRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNR-MASGLEFKSVA 121
Cdd:PLN03234   33 PKGLPIIGNLhqmeKFNPQHFL---FRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTARpLLKGQQTMSYQ 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 122 DSVL-------FLRDKRweevRGALMSAFSPEKLNEMVPLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVA 194
Cdd:PLN03234  110 GRELgfgqytaYYREMR----KMCMVNLFSPNRVASFRPVREEECQRMMDKIYKAADQSGTVDLSELLLSFTNCVVCRQA 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 195 FGTPVDSWQApedpfvkHCKRFFEFCIPRPILVLLLSFpSIMVPLARILpnknrDELNGFFNKLirnvialrdqQAAEER 274
Cdd:PLN03234  186 FGKRYNEYGT-------EMKRFIDILYETQALLGTLFF-SDLFPYFGFL-----DNLTGLSARL----------KKAFKE 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 275 RRDFLQMVLDarhsaspmgvQDFDIVRDVFSSTGCKPNPSRQHQPSPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFAT 354
Cdd:PLN03234  243 LDTYLQELLD----------ETLDPNRPKQETESFIDLLMQIYKDQPFSIKFTHENVKAMILDIVVPGTDTAAAVVVWAM 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 355 YLLATNPDCQEKLLREV-DVFKEKHmapeFCSLEE--GLPYLDMVIAETLRMYPP-AFRFTREAAQDCEVLGQRIPAGAV 430
Cdd:PLN03234  313 TYLIKYPEAMKKAQDEVrNVIGDKG----YVSEEDipNLPYLKAVIKESLRLEPViPILLHRETIADAKIGGYDIPAKTI 388
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1488188862 431 LEMAVGALHHDPEHW-PSPETFNPERFTAEARQ---QHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKF 500
Cdd:PLN03234  389 IQVNAWAVSRDTAAWgDNPNEFIPERFMKEHKGvdfKGQDFELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKF 462
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
326-509 1.69e-22

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: 99.87  E-value: 1.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 326 LTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD--VFKEKHMAPEFCSLeegLPYLDMVIAETLRM 403
Cdd:cd20656   226 LSEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDrvVGSDRVMTEADFPQ---LPYLQCVVKEALRL 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 404 YPPA-FRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQ-QHRPFTYLPFGAGPRSCLG 481
Cdd:cd20656   303 HPPTpLMLPHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVDiKGHDFRLLPFGAGRRVCPG 382
                         170       180
                  ....*....|....*....|....*...
gi 1488188862 482 VRLGLLEVKLTLLHVLHKFRFQACPETQ 509
Cdd:cd20656   383 AQLGINLVTLMLGHLLHHFSWTPPEGTP 410
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
326-500 2.66e-22

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


Pssm-ID: 410718 [Multi-domain]  Cd Length: 369  Bit Score: 98.39  E-value: 2.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 326 LTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDcQEKLLREvdvfkekhmAPEFcsleeglpyLDMVIAETLRMYP 405
Cdd:cd20625   197 LSEDELVANCILLLVAGHETTVNLIGNGLLALLRHPE-QLALLRA---------DPEL---------IPAAVEELLRYDS 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 406 PAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERftaeARQQHrpftyLPFGAGPRSCLGVRLG 485
Cdd:cd20625   258 PVQLTARVALEDVEIGGQTIPAGDRVLLLLGAANRDPAVFPDPDRFDITR----APNRH-----LAFGAGIHFCLGAPLA 328
                         170
                  ....*....|....*
gi 1488188862 486 LLEVKLTLLHVLHKF 500
Cdd:cd20625   329 RLEAEIALRALLRRF 343
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
357-512 6.05e-22

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: 98.17  E-value: 6.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 357 LATNPDCQEKLLREVDVFKEKHMAPEFCSLEEgLPYLDMVIAETLRMYPPA--FRFTREAAQDCEVLGQRIPAG--AVLE 432
Cdd:cd11076   251 MVLHPDIQSKAQAEIDAAVGGSRRVADSDVAK-LPYLQAVVKETLRLHPPGplLSWARLAIHDVTVGGHVVPAGttAMVN 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 433 MavGALHHDPEHWPSPETFNPERFTAEARQQHrpFTYL-------PFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQAC 505
Cdd:cd11076   330 M--WAITHDPHVWEDPLEFKPERFVAAEGGAD--VSVLgsdlrlaPFGAGRRVCPGKALGLATVHLWVAQLLHEFEWLPD 405

                  ....*..
gi 1488188862 506 PETQVPL 512
Cdd:cd11076   406 DAKPVDL 412
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
134-513 2.29e-21

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: 95.75  E-value: 2.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 134 EVRGALMSAFSPEKLNEMVPLISQACDLLLAhlkRYAESGDAfdiqrcycnyttDVVASVAFGTPVDswqapedpfvkhc 213
Cdd:cd11078    74 RLRRLVSRAFTPRRIAALEPRIRELAAELLD---RLAEDGRA------------DFVADFAAPLPAL------------- 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 214 krffefciprpILVLLLSFPSIMVPLARilpnknrdelnGFFNKLIRNVIALRDQQAAEERRRDFLQM------VLDARH 287
Cdd:cd11078   126 -----------VIAELLGVPEEDMERFR-----------RWADAFALVTWGRPSEEEQVEAAAAVGELwayfadLVAERR 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 288 sASPmgvQDFDIVRDVFSSTGckpnpsrqhqpspMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKL 367
Cdd:cd11078   184 -REP---RDDLISDLLAAADG-------------DGERLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRL 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 368 LREVdvfkekhmapefcSLeeglpyLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPS 447
Cdd:cd11078   247 RADP-------------SL------IPNAVEETLRYDSPVQGLRRTATRDVEIGGVTIPAGARVLLLFGSANRDERVFPD 307
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1488188862 448 PETFNPERftaEARQQHrpftyLPFGAGPRSCLGVRLGLLEVKLTLLHVLhkfrfQACPETQVPLQ 513
Cdd:cd11078   308 PDRFDIDR---PNARKH-----LTFGHGIHFCLGAALARMEARIALEELL-----RRLPGMRVPGQ 360
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
229-511 3.12e-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: 96.21  E-value: 3.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 229 LLSFPSIMVPL-ARILPNKNRdeLNGFFN---KLIRNVIALRDQQAA---EERRRDFLQMVLDArhsaspmgvqdfdivr 301
Cdd:cd11041   155 LRLFPPFLRPLvAPFLPEPRR--LRRLLRrarPLIIPEIERRRKLKKgpkEDKPNDLLQWLIEA---------------- 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 302 dvfsstgCKPNPSRqhqpspmarplTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREV-DVFKEkHMA 380
Cdd:cd11041   217 -------AKGEGER-----------TPYDLADRQLALSFAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIrSVLAE-HGG 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 381 PEFCSLEEgLPYLDMVIAETLRMYPPAFR-FTREAAQDcEVL--GQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFt 457
Cdd:cd11041   278 WTKAALNK-LKKLDSFMKESQRLNPLSLVsLRRKVLKD-VTLsdGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRF- 354
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1488188862 458 AEARQQH-----RPFT-----YLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVP 511
Cdd:cd11041   355 YRLREQPgqekkHQFVstspdFLGFGHGRHACPGRFFASNEIKLILAHLLLNYDFKLPEGGERP 418
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
322-501 3.27e-21

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: 96.06  E-value: 3.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 322 MARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVdVFKEKHMAPEFCSLEEGLPYLDMVIAETL 401
Cdd:cd20644   224 LQAELSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQES-LAAAAQISEHPQKALTELPLLKAALKETL 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 402 RMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEaRQQHRPFTYLPFGAGPRSCLG 481
Cdd:cd20644   303 RLYPVGITVQRVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDI-RGSGRNFKHLAFGFGMRQCLG 381
                         170       180
                  ....*....|....*....|
gi 1488188862 482 VRLGLLEVKLTLLHVLHKFR 501
Cdd:cd20644   382 RRLAEAEMLLLLMHVLKNFL 401
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
326-488 4.93e-21

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: 94.67  E-value: 4.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 326 LTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDvfkekhmapefcsleeglpYLDMVIAETLRMYP 405
Cdd:cd20629   188 LDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLERVRRDRS-------------------LIPAAIEEGLRWEP 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 406 PAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPErftaeaRQQHRPFTylpFGAGPRSCLGVRLG 485
Cdd:cd20629   249 PVASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDID------RKPKPHLV---FGGGAHRCLGEHLA 319

                  ...
gi 1488188862 486 LLE 488
Cdd:cd20629   320 RVE 322
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
251-500 6.65e-21

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


Pssm-ID: 410666 [Multi-domain]  Cd Length: 432  Bit Score: 95.12  E-value: 6.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 251 LNGFFNKLIRNVIALRDQ-QAAEERrrdFLQMVLDARHSASPMgVQDFDivrDVFSSTGckpnpsrqhqpspmarpLTVD 329
Cdd:cd11040   167 LLGLPRLLARKAYAARDRlLKALEK---YYQAAREERDDGSEL-IRARA---KVLREAG-----------------LSEE 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 330 EIVGQAFIFLIAgyeIITNTLSFATYLLA---TNPDCQEKLLREVD-VFKEKHMAPEFC---SLEEGLPYLDMVIAETLR 402
Cdd:cd11040   223 DIARAELALLWA---INANTIPAAFWLLAhilSDPELLERIREEIEpAVTPDSGTNAILdltDLLTSCPLLDSTYLETLR 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 403 MYPPAFRfTREAAQDCEVLGQ-RIPAGAVLEMAVGALHHDPEHW-PSPETFNPERF---TAEARQQHRPFTYLPFGAGPR 477
Cdd:cd11040   300 LHSSSTS-VRLVTEDTVLGGGyLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFlkkDGDKKGRGLPGAFRPFGGGAS 378
                         250       260
                  ....*....|....*....|...
gi 1488188862 478 SCLGVRLGLLEVKLTLLHVLHKF 500
Cdd:cd11040   379 LCPGRHFAKNEILAFVALLLSRF 401
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
340-510 1.03e-20

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: 94.49  E-value: 1.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 340 IAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCSLEEgLPYLDMVIAETLRMyPPAFRFTREAAQDCE 419
Cdd:cd20645   236 IGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKN-MPYLKACLKESMRL-TPSVPFTSRTLDKDT 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 420 VLGQR-IPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHrPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLH 498
Cdd:cd20645   314 VLGDYlLPKGTVLMINSQALGSSEEYFEDGRQFKPERWLQEKHSIN-PFAHVPFGIGKRMCIGRRLAELQLQLALCWIIQ 392
                         170
                  ....*....|..
gi 1488188862 499 KFRFQACPETQV 510
Cdd:cd20645   393 KYQIVATDNEPV 404
PLN00168 PLN00168
Cytochrome P450; Provisional
47-510 1.68e-20

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 94.63  E-value: 1.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  47 PKPSPFIGNLTFFRQGFWESQMELRKL---YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSVADS 123
Cdd:PLN00168   40 PPAVPLLGSLVWLTNSSADVEPLLRRLiarYGPVVSLRVGSRLSVFVADRRLAHAALVERGAALADRPAVASSRLLGESD 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 124 VLFLRDKR---WEEVRGALMS-AFSPEKLNEMVPLISQACDLLLAHLKRYAESGDAfdiqrcycnyttdvvasvafgtpv 199
Cdd:PLN00168  120 NTITRSSYgpvWRLLRRNLVAeTLHPSRVRLFAPARAWVRRVLVDKLRREAEDAAA------------------------ 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 200 dswqapedPFVKHCKRFFEFCIprpiLVLLLSFPSIMVPLARILPNKNRDEL---------NGFFNKLIRNVIALRDQQA 270
Cdd:PLN00168  176 --------PRVVETFQYAMFCL----LVLMCFGERLDEPAVRAIAAAQRDWLlyvskkmsvFAFFPAVTKHLFRGRLQKA 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 271 AEERRR--DFLQMVLDARHSASPMGVQdfdivrdvfSSTGCKPNPSRQHQ----------PSPMARPLTVDEIVGQAFIF 338
Cdd:PLN00168  244 LALRRRqkELFVPLIDARREYKNHLGQ---------GGEPPKKETTFEHSyvdtlldirlPEDGDRALTDDEIVNLCSEF 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 339 LIAGYEIITNTLSFATYLLATNPDCQEKLLREVdvfKEKHMAPEFCSLEE---GLPYLDMVIAETLRMYPPA-FRFTREA 414
Cdd:PLN00168  315 LNAGTDTTSTALQWIMAELVKNPSIQSKLHDEI---KAKTGDDQEEVSEEdvhKMPYLKAVVLEGLRKHPPAhFVLPHKA 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 415 AQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQ------HRPFTYLPFGAGPRSCLGVRLGLLE 488
Cdd:PLN00168  392 AEDMEVGGYLIPKGATVNFMVAEMGRDEREWERPMEFVPERFLAGGDGEgvdvtgSREIRMMPFGVGRRICAGLGIAMLH 471
                         490       500
                  ....*....|....*....|..
gi 1488188862 489 VKLTLLHVLHKFRFQACPETQV 510
Cdd:PLN00168  472 LEYFVANMVREFEWKEVPGDEV 493
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
326-516 3.49e-20

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: 92.24  E-value: 3.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 326 LTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDcQEKLLREvdvfkekhmAPEFcsleeglpyLDMVIAETLRMYP 405
Cdd:cd11031   202 LSEEELVTLAVGLLVAGHETTASQIGNGVLLLLRHPE-QLARLRA---------DPEL---------VPAAVEELLRYIP 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 406 P--AFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAearqQHrpftyLPFGAGPRSCLGVR 483
Cdd:cd11031   263 LgaGGGFPRYATEDVELGGVTIRAGEAVLVSLNAANRDPEVFPDPDRLDLDREPN----PH-----LAFGHGPHHCLGAP 333
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1488188862 484 LGLLEVKLTLLHVLHKF---RFqACPETQVPLQLES 516
Cdd:cd11031   334 LARLELQVALGALLRRLpglRL-AVPEEELRWREGL 368
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
326-488 4.92e-20

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: 91.82  E-value: 4.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 326 LTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDcQEKLLREvdvfkekhmapefcslEEGLpyLDMVIAETLRMYP 405
Cdd:cd11029   207 LSEEELVSTVFLLLVAGHETTVNLIGNGVLALLTHPD-QLALLRA----------------DPEL--WPAAVEELLRYDG 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 406 PAFRFT-REAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERftaeARQQHrpftyLPFGAGPRSCLGVRL 484
Cdd:cd11029   268 PVALATlRFATEDVEVGGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITR----DANGH-----LAFGHGIHYCLGAPL 338

                  ....
gi 1488188862 485 GLLE 488
Cdd:cd11029   339 ARLE 342
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
341-511 6.06e-20

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: 92.38  E-value: 6.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 341 AGYEIITNTLSFATYLLATNP--DCQEKLLREV-DVFKEKHMAPEFCSLEEGLPYLDMVIAETLRMYPP-AFRFTREAAQ 416
Cdd:cd11066   239 AGLDTVPLNLNHLIGHLSHPPgqEIQEKAYEEIlEAYGNDEDAWEDCAAEEKCPYVVALVKETLRYFTVlPLGLPRKTTK 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 417 DCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHV 496
Cdd:cd11066   319 DIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIPGPPHFSFGAGSRMCAGSHLANRELYTAICRL 398
                         170
                  ....*....|....*
gi 1488188862 497 LHKFRFQACPETQVP 511
Cdd:cd11066   399 ILLFRIGPKDEEEPM 413
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
325-499 1.53e-19

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: 90.96  E-value: 1.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 325 PLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEkhmAPEFCSLEEGLPYLDMVIAETLRMY 404
Cdd:cd20614   203 GLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAAGD---VPRTPAELRRFPLAEALFRETLRLH 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 405 PPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTaEARQQHRPFTYLPFGAGPRSCLGVRL 484
Cdd:cd20614   280 PPVPFVFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWL-GRDRAPNPVELLQFGGGPHFCLGYHV 358
                         170
                  ....*....|....*...
gi 1488188862 485 GLLEVKL---TLLHVLHK 499
Cdd:cd20614   359 ACVELVQfivALARELGA 376
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
74-503 1.84e-19

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: 90.59  E-value: 1.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFK-SVADSVLFLRDKRWEEVRgalmsAFSPEKLNE-- 150
Cdd:cd20669     1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRGDYPVFFNfTKGNGIAFSNGERWKILR-----RFALQTLRNfg 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 151 -----MVPLISQACDLLLAHLKryAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSwqapEDPFVKHCKRFFE--FCI-P 222
Cdd:cd20669    76 mgkrsIEERILEEAQFLLEELR--KTKGAPFDPTFLLSRAVSNIICSVVFGSRFDY----DDKRLLTILNLINdnFQImS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 223 RPILVLLLSFPSIMvplarilpnknrDELNGFFNKLIRNVIALRDQQAaeERRRDFLQmvldarhSASPMGVQDFdivrd 302
Cdd:cd20669   150 SPWGELYNIFPSVM------------DWLPGPHQRIFQNFEKLRDFIA--ESVREHQE-------SLDPNSPRDF----- 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 303 vfssTGCKPNPSRQHQPSPMARpLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPe 382
Cdd:cd20669   204 ----IDCFLTKMAEEKQDPLSH-FNMETLVMTTHNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLP- 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 383 fcSLEE--GLPYLDMVIAETLR---MYPpaFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFT 457
Cdd:cd20669   278 --TLEDraRMPYTDAVIHEIQRfadIIP--MSLPHAVTRDTNFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFL 353
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1488188862 458 AEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQ 503
Cdd:cd20669   354 DDNGSFKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQ 399
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
327-501 2.00e-19

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: 90.42  E-value: 2.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 327 TVDEIvgqafifLIAGYEIITNTLSFATYLLATNPDCQEKLLREVdvfkEKHMAPEFCSLEEGL----PYLDMVIAETLR 402
Cdd:cd20615   219 TLDEM-------LFANLDVTTGVLSWNLVFLAANPAVQEKLREEI----SAAREQSGYPMEDYIlstdTLLAYCVLESLR 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 403 MYP-PAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHW-PSPETFNPERFTAEARQQHRpFTYLPFGAGPRSCL 480
Cdd:cd20615   288 LRPlLAFSVPESSPTDKIIGGYRIPANTPVVVDTYALNINNPFWgPDGEAYRPERFLGISPTDLR-YNFWRFGFGPRKCL 366
                         170       180
                  ....*....|....*....|.
gi 1488188862 481 GVRLGLLEVKLTLLHVLHKFR 501
Cdd:cd20615   367 GQHVADVILKALLAHLLEQYE 387
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
324-493 2.10e-19

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: 89.96  E-value: 2.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 324 RPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREvdvfkekhmaPEFcsleeglpyLDMVIAETLRM 403
Cdd:cd11035   184 RPLTDDELLGLCFLLFLAGLDTVASALGFIFRHLARHPEDRRRLRED----------PEL---------IPAAVEELLRR 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 404 YPPAFRFtREAAQDCEVLGQRIPAG--AVLEMAVGALhhDPEHWPSPETFNPERftaearqqhRPFTYLPFGAGPRSCLG 481
Cdd:cd11035   245 YPLVNVA-RIVTRDVEFHGVQLKAGdmVLLPLALANR--DPREFPDPDTVDFDR---------KPNRHLAFGAGPHRCLG 312
                         170
                  ....*....|..
gi 1488188862 482 VRLGLLEVKLTL 493
Cdd:cd11035   313 SHLARLELRIAL 324
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
317-500 2.32e-19

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 91.07  E-value: 2.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 317 HQPSPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCSLEEgLPYLDMV 396
Cdd:PLN00110  276 NQENSTGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRRLVESDLPK-LPYLQAI 354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 397 IAETLRMYPPA-FRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRP----FTYLP 471
Cdd:PLN00110  355 CKESFRKHPSTpLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEKNAKIDPrgndFELIP 434
                         170       180
                  ....*....|....*....|....*....
gi 1488188862 472 FGAGPRSCLGVRLGLLEVKLTLLHVLHKF 500
Cdd:PLN00110  435 FGAGRRICAGTRMGIVLVEYILGTLVHSF 463
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
339-507 8.37e-19

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: 88.57  E-value: 8.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 339 LIAGYEIITNTLSFATYLLATNPDCQEKLLREVD-VFKEKHMAPEFCSleeGLPYLDMVIAETLRmYPPAFRFT-REAAQ 416
Cdd:cd20616   233 LIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQtVLGERDIQNDDLQ---KLKVLENFINESMR-YQPVVDFVmRKALE 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 417 DCEVLGQRIPAGAVLEMAVGALHHDpEHWPSPETFNPERFtaearQQHRPFTYL-PFGAGPRSCLGVRLGLLEVKLTLLH 495
Cdd:cd20616   309 DDVIDGYPVKKGTNIILNIGRMHRL-EFFPKPNEFTLENF-----EKNVPSRYFqPFGFGPRSCVGKYIAMVMMKAILVT 382
                         170
                  ....*....|..
gi 1488188862 496 VLHkfRFQACPE 507
Cdd:cd20616   383 LLR--RFQVCTL 392
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
329-518 3.31e-18

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 87.30  E-value: 3.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 329 DEIVGQAFifliAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCSLEEG--LPYLDMVIAETLRMyPP 406
Cdd:PLN02196  267 DNIIGVIF----AARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRKDKEEGESLTWEDTkkMPLTSRVIQETLRV-AS 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 407 AFRFT-REAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARqqhrPFTYLPFGAGPRSCLGVRLG 485
Cdd:PLN02196  342 ILSFTfREAVEDVEYEGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRFEVAPK----PNTFMPFGNGTHSCPGNELA 417
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1488188862 486 LLEVKLTLLHVLHKFRFQ-------------ACPETQVPLQLESKS 518
Cdd:PLN02196  418 KLEISVLIHHLTTKYRWSivgtsngiqygpfALPQNGLPIALSRKP 463
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
74-521 4.31e-18

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: 86.40  E-value: 4.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASG-LEFKSVADSVLFLRDKRWEEVRGALMSAFSPEKLNE-- 150
Cdd:cd20664     1 YGSIFTVQMGTKKVVVLAGYKTVKEALVNHAEAFGGRPIIPiFEDFNKGYGILFSNGENWKEMRRFTLTTLRDFGMGKkt 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 151 MVPLISQACDLLLAHLKRYaeSGDAFDIQRCYCNYTTDVVASVAFGTPVDSwqapEDP-FVKHCKRFFEFciprpilVLL 229
Cdd:cd20664    81 SEDKILEEIPYLIEVFEKH--KGKPFETTLSMNVAVSNIIASIVLGHRFEY----TDPtLLRMVDRINEN-------MKL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 230 LSFPSI----MVPLARILPNKNrdelngffNKLIRNVIALRDQqaaeerRRDFLQMVLDARHSASPMGVQDFDIVRdvfS 305
Cdd:cd20664   148 TGSPSVqlynMFPWLGPFPGDI--------NKLLRNTKELNDF------LMETFMKHLDVLEPNDQRGFIDAFLVK---Q 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 306 STGCKPNPSRQHQPSpmarpLTvdEIVGQAFIfliAGYEIITNTLSFATYLLATNPDCQEKLLREVD-VFKEKHMAPEFc 384
Cdd:cd20664   211 QEEEESSDSFFHDDN-----LT--CSVGNLFG---AGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDrVIGSRQPQVEH- 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 385 slEEGLPYLDMVIAETLRMYPPA-FRFTREAAQDCEVLGQRIPAGA-VLEMAVGALHhDPEHWPSPETFNPERFTAEARQ 462
Cdd:cd20664   280 --RKNMPYTDAVIHEIQRFANIVpMNLPHATTRDVTFRGYFIPKGTyVIPLLTSVLQ-DKTEWEKPEEFNPEHFLDSQGK 356
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1488188862 463 QHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPlQLESKSALG 521
Cdd:cd20664   357 FVKRDAFMPFSAGRRVCIGETLAKMELFLFFTSLLQRFRFQPPPGVSED-DLDLTPGLG 414
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
339-511 7.90e-18

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: 86.02  E-value: 7.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 339 LIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFcSLEEGLPYLDMVIAETLRMYPPA----FRFTrea 414
Cdd:cd20661   247 IIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSF-EDKCKMPYTEAVLHEVLRFCNIVplgiFHAT--- 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 415 AQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLL 494
Cdd:cd20661   323 SKDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLFFT 402
                         170
                  ....*....|....*..
gi 1488188862 495 HVLHKFRFQAcPETQVP 511
Cdd:cd20661   403 ALLQRFHLHF-PHGLIP 418
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
233-506 1.13e-17

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: 85.45  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 233 PSIMVPLARILPNKNRD---ELNGFFNKLIRNVIalrdqqaaEERRRDFlqmvldarhsaspmgvqDFDIVRDVfssTGC 309
Cdd:cd20676   164 PADFIPILRYLPNPAMKrfkDINKRFNSFLQKIV--------KEHYQTF-----------------DKDNIRDI---TDS 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 310 KPNPSRQHQPSPMARPLTVDE-IVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFcSLEE 388
Cdd:cd20676   216 LIEHCQDKKLDENANIQLSDEkIVNIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRL-SDRP 294
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 389 GLPYLDMVIAETLR--MYPPaFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERF-TAEARQQHR 465
Cdd:cd20676   295 QLPYLEAFILETFRhsSFVP-FTIPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFlTADGTEINK 373
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1488188862 466 PFT--YLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACP 506
Cdd:cd20676   374 TESekVMLFGLGKRRCIGESIARWEVFLFLAILLQQLEFSVPP 416
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
326-494 1.34e-17

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: 84.72  E-value: 1.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 326 LTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDcQEKLLREvdvfkekhmapefcslEEGLPylDMVIAETLRMYP 405
Cdd:cd11038   210 LSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPD-QWRALRE----------------DPELA--PAAVEEVLRWCP 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 406 PAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDpehwpsPETFNPERFTAEARQQhRPFTylpFGAGPRSCLGVRLG 485
Cdd:cd11038   271 TTTWATREAVEDVEYNGVTIPAGTVVHLCSHAANRD------PRVFDADRFDITAKRA-PHLG---FGGGVHHCLGAFLA 340
                         170
                  ....*....|.
gi 1488188862 486 LLE--VKLTLL 494
Cdd:cd11038   341 RAElaEALTVL 351
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
338-533 1.35e-17

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 85.60  E-value: 1.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 338 FLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKE---KHMAPE-FCSLEE---------------GLPYLDMVIA 398
Cdd:PLN03195  300 FVIAGRDTTATTLSWFVYMIMMNPHVAEKLYSELKALEKeraKEEDPEdSQSFNQrvtqfaglltydslgKLQYLHAVIT 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 399 ETLRMYPPAFRFTREAAQDcEVL--GQRIPAGAVLEMAVGALHHDPEHW-PSPETFNPERFTAE-ARQQHRPFTYLPFGA 474
Cdd:PLN03195  380 ETLRLYPAVPQDPKGILED-DVLpdGTKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERWIKDgVFQNASPFKFTAFQA 458
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1488188862 475 GPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVplQLESKSALGPKNGVYIKIVSR 533
Cdd:PLN03195  459 GPRICLGKDSAYLQMKMALALLCRFFKFQLVPGHPV--KYRMMTILSMANGLKVTVSRR 515
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
47-500 1.40e-17

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 85.64  E-value: 1.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  47 PKPSPFIGNLTFFRQGFWESQMELRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNR---MASGLEFKSVADS 123
Cdd:PLN03112   37 PPRWPIVGNLLQLGPLPHRDLASLCKKYGPLVYLRLGSVDAITTDDPELIREILLRQDDVFASRprtLAAVHLAYGCGDV 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 124 VLFLRDKRWEEVRGALMSAF-SPEKLNEMVPLISQACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTpvdSW 202
Cdd:PLN03112  117 ALAPLGPHWKRMRRICMEHLlTTKRLESFAKHRAEEARHLIQDVWEAAQTGKPVNLREVLGAFSMNNVTRMLLGK---QY 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 203 QAPEDPFVKHCKRFFEFCIPrpiLVLLLSFpsimVPLARILPNKNRDELNGFfnklirnviaLRDQQAAEERRRDFLQMV 282
Cdd:PLN03112  194 FGAESAGPKEAMEFMHITHE---LFRLLGV----IYLGDYLPAWRWLDPYGC----------EKKMREVEKRVDEFHDKI 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 283 LD----ARHSASPMGVqDFDIVRDVFSSTGckpNPSRQHQPSPMARPLTVDEIVGQAfifliaGYEIITNTLSFATYLla 358
Cdd:PLN03112  257 IDehrrARSGKLPGGK-DMDFVDVLLSLPG---ENGKEHMDDVEIKALMQDMIAAAT------DTSAVTNEWAMAEVI-- 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 359 TNPDCQEKLLREVD-VFKEKHMAPEfcSLEEGLPYLDMVIAETLRMYPPA-FRFTREAAQDCEVLGQRIPAGAVLEMAVG 436
Cdd:PLN03112  325 KNPRVLRKIQEELDsVVGRNRMVQE--SDLVHLNYLRCVVRETFRMHPAGpFLIPHESLRATTINGYYIPAKTRVFINTH 402
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1488188862 437 ALHHDPEHWPSPETFNPERF----TAEARQQHRP-FTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKF 500
Cdd:PLN03112  403 GLGRNTKIWDDVEEFRPERHwpaeGSRVEISHGPdFKILPFSAGKRKCPGAPLGVTMVLMALARLFHCF 471
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
324-501 9.76e-17

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: 81.81  E-value: 9.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 324 RPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDcQEKLLREvdvfkekhmapefcslEEGLpyLDMVIAETLRM 403
Cdd:cd11033   203 EPLTDEEFASFFILLAVAGNETTRNSISGGVLALAEHPD-QWERLRA----------------DPSL--LPTAVEEILRW 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 404 YPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERftaeARQQHrpftyLPFGAGPRSCLGVR 483
Cdd:cd11033   264 ASPVIHFRRTATRDTELGGQRIRAGDKVVLWYASANRDEEVFDDPDRFDITR----SPNPH-----LAFGGGPHFCLGAH 334
                         170
                  ....*....|....*...
gi 1488188862 484 LGLLEVKLTLLHVLHKFR 501
Cdd:cd11033   335 LARLELRVLFEELLDRVP 352
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
74-500 2.92e-16

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


Pssm-ID: 410763 [Multi-domain]  Cd Length: 425  Bit Score: 81.12  E-value: 2.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNR--MASgLEFKSVADSVLFLRDKRWEEVRG---ALMSAFSPEKl 148
Cdd:cd20670     1 YGPVFTVYMGPRPVVVLCGHEAVKEALVDQADEFSGRgeLAT-IERNFQGHGVALANGERWRILRRfslTILRNFGMGK- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 149 NEMVPLISQACDLLLAHLKRyaESGDAFDIQRCYCNYTTDVVASVAFGTPVDSwqapEDpfvkhcKRFFEFciprpILVL 228
Cdd:cd20670    79 RSIEERIQEEAGYLLEEFRK--TKGAPIDPTFFLSRTVSNVISSVVFGSRFDY----ED------KQFLSL-----LRMI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 229 LLSFPSIMVPLARI----------LPNK-NR-----DELNGFFNKLIRNVIALRDQQAAeerrRDFLQMVLDARHsaspm 292
Cdd:cd20670   142 NESFIEMSTPWAQLydmysgimqyLPGRhNRiyyliEELKDFIASRVKINEASLDPQNP----RDFIDCFLIKMH----- 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 293 gvQDfdivrdvfsstgcKPNPSRQhqpspmarpLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD 372
Cdd:cd20670   213 --QD-------------KNNPHTE---------FNLKNLVLTTLNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEIN 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 373 VFKEKHMAPefcSLEE--GLPYLDMVIAETLRMYPPA-FRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPE 449
Cdd:cd20670   269 QVIGPHRLP---SVDDrvKMPYTDAVIHEIQRLTDIVpLGVPHNVIRDTQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPE 345
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1488188862 450 TFNPERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKF 500
Cdd:cd20670   346 AFYPQHFLDEQGRFKKNEAFVPFSSGKRVCLGEAMARMELFLYFTSILQNF 396
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
330-501 2.99e-16

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: 80.59  E-value: 2.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 330 EIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEkllrevDVFKEKHMAPEfcsleeglpyldmVIAETLRMYPPAFR 409
Cdd:cd11080   193 DIKALILNVLLAATEPADKTLALMIYHLLNNPEQLA------AVRADRSLVPR-------------AIAETLRYHPPVQL 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 410 FTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPER--------FTAEARqqhrpftYLPFGAGPRSCLG 481
Cdd:cd11080   254 IPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHRedlgirsaFSGAAD-------HLAFGSGRHFCVG 326
                         170       180
                  ....*....|....*....|
gi 1488188862 482 VRLGLLEVKLTLLHVLHKFR 501
Cdd:cd11080   327 AALAKREIEIVANQVLDALP 346
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
339-503 5.27e-16

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: 80.23  E-value: 5.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 339 LIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFcSLEEGLPYLDMVIAETLR---MYPpaFRFTREAA 415
Cdd:cd20668   235 FFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKF-EDRAKMPYTEAVIHEIQRfgdVIP--MGLARRVT 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 416 QDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLH 495
Cdd:cd20668   312 KDTKFRDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDDKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTT 391

                  ....*...
gi 1488188862 496 VLHKFRFQ 503
Cdd:cd20668   392 IMQNFRFK 399
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
326-491 7.47e-16

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: 79.88  E-value: 7.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 326 LTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD---VFKEKHMAPEFCSLEE--GLPYLDMVIAET 400
Cdd:cd20636   223 LTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPSAIEKIRQELVshgLIDQCQCCPGALSLEKlsRLRYLDCVVKEV 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 401 LRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAE-ARQQHRPFTYLPFGAGPRSC 479
Cdd:cd20636   303 LRLLPPVSGGYRTALQTFELDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVErEESKSGRFNYIPFGGGVRSC 382
                         170
                  ....*....|..
gi 1488188862 480 LGVRLGLLEVKL 491
Cdd:cd20636   383 IGKELAQVILKT 394
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
338-497 7.77e-16

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


Pssm-ID: 410663 [Multi-domain]  Cd Length: 371  Bit Score: 79.16  E-value: 7.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 338 FLIAGYEIITNTLSFATYLLATNPDcQEKLLREvdvfkEKHMAPEfcsleeglpyldmVIAETLRMYPPAFRFTREAAQD 417
Cdd:cd11037   210 YLSAGLDTTISAIGNALWLLARHPD-QWERLRA-----DPSLAPN-------------AFEEAVRLESPVQTFSRTTTRD 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 418 CEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERftaearqqhRPFTYLPFGAGPRSCLGVRLGLLEVKlTLLHVL 497
Cdd:cd11037   271 TELAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITR---------NPSGHVGFGHGVHACVGQHLARLEGE-ALLTAL 340
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
329-500 1.11e-15

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 79.64  E-value: 1.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 329 DEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEfcSLE----EGLPYLDMVIAETLRMY 404
Cdd:PLN02987  266 EEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEHEKIRAMKSDSY--SLEwsdyKSMPFTQCVVNETLRVA 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 405 PPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCLGVRL 484
Cdd:PLN02987  344 NIIGGIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGTTVPSNVFTPFGGGPRLCPGYEL 423
                         170
                  ....*....|....*.
gi 1488188862 485 GLLEVKLTLLHVLHKF 500
Cdd:PLN02987  424 ARVALSVFLHRLVTRF 439
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
357-506 1.52e-15

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: 78.67  E-value: 1.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 357 LATNPDCQEKLLREVD-VFKEKHMAPEfcSLEEGLPYLDMVIAETLR--MYPPAFrFTREAAQDCEVLGQRIPAGAVLEM 433
Cdd:cd11074   260 LVNHPEIQKKLRDELDtVLGPGVQITE--PDLHKLPYLQAVVKETLRlrMAIPLL-VPHMNLHDAKLGGYDIPAESKILV 336
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1488188862 434 AVGALHHDPEHWPSPETFNPERFTAEARQQHR---PFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACP 506
Cdd:cd11074   337 NAWWLANNPAHWKKPEEFRPERFLEEESKVEAngnDFRYLPFGVGRRSCPGIILALPILGITIGRLVQNFELLPPP 412
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
349-502 2.77e-15

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: 77.74  E-value: 2.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 349 TLSFatylLATNPDCQEKLLREVD-VFKEKHMAPEFCSLE--EGLPYLDMVIAETLRMYPPAFrFTREAAQDCEVLGQRI 425
Cdd:cd20635   233 TLAF----ILSHPSVYKKVMEEISsVLGKAGKDKIKISEDdlKKMPYIKRCVLEAIRLRSPGA-ITRKVVKPIKIKNYTI 307
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1488188862 426 PAGAVLEMAVGALHHDPEHWPSPETFNPERF-TAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRF 502
Cdd:cd20635   308 PAGDMLMLSPYWAHRNPKYFPDPELFKPERWkKADLEKNVFLEGFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKYDF 385
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
136-516 4.10e-15

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: 77.18  E-value: 4.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 136 RGALMSAFSPEKLNEMVPLISQACDLLLahlkryaesgDAFdiqrcycnyttdvvasVAFGTPVDswqapedpFVKHckr 215
Cdd:cd11030    81 RRMLAPEFTVRRVRALRPRIQEIVDELL----------DAM----------------EAAGPPAD--------LVEA--- 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 216 ffeFCIPRPILVL--LLSfpsimVPLARilpnknRDELNGFFNKLIRNVIALRDQQAAEERRRDFL-QMVldARHSASPm 292
Cdd:cd11030   124 ---FALPVPSLVIceLLG-----VPYED------REFFQRRSARLLDLSSTAEEAAAAGAELRAYLdELV--ARKRREP- 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 293 gvQDfDIVRDVfsstgckpnpSRQHQPSPmarPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDcQEKLLREvd 372
Cdd:cd11030   187 --GD-DLLSRL----------VAEHGAPG---ELTDEELVGIAVLLLVAGHETTANMIALGTLALLEHPE-QLAALRA-- 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 373 vfkEKHMAPEFcsLEEGLPYLDMVIAETLRMyppafrftreAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFN 452
Cdd:cd11030   248 ---DPSLVPGA--VEELLRYLSIVQDGLPRV----------ATEDVEIGGVTIRAGEGVIVSLPAANRDPAVFPDPDRLD 312
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1488188862 453 PERftaEARQQhrpftyLPFGAGPRSCLGVRLGLLEVKLTLLHVLHkfRFQ----ACPETQVPLQLES 516
Cdd:cd11030   313 ITR---PARRH------LAFGHGVHQCLGQNLARLELEIALPTLFR--RFPglrlAVPAEELPFRPDS 369
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
318-483 5.68e-15

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: 76.90  E-value: 5.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 318 QPSPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVF---KEKHMAPEfcSLEEgLPYLD 394
Cdd:cd11082   208 EGEPPPPHSSDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLrpnDEPPLTLD--LLEE-MKYTR 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 395 MVIAETLRMYPPA----------FRFTREAAqdcevlgqrIPAGAVLEMAVGALHHDPehWPSPETFNPERFTAEaRQQH 464
Cdd:cd11082   285 QVVKEVLRYRPPApmvphiakkdFPLTEDYT---------VPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPE-RQED 352
                         170       180
                  ....*....|....*....|.
gi 1488188862 465 RPFT--YLPFGAGPRSCLGVR 483
Cdd:cd11082   353 RKYKknFLVFGAGPHQCVGQE 373
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
222-529 5.88e-15

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: 76.81  E-value: 5.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 222 PRPILVLL----LSFP-SIMVPLARILPNKNRDELNGFFNKLIRNVIALR-DQQAAEERR----RDFLQMVLDARHSASP 291
Cdd:cd20637   117 PEPINVYQeaqkLTFRmAIRVLLGFRVSEEELSHLFSVFQQFVENVFSLPlDLPFSGYRRgiraRDSLQKSLEKAIREKL 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 292 MGVQDfdivRDVFSSTGCKPNPSRQHqpspmARPLTVDEIVGQAFIFLIAGYeiiTNTLSFATYL---LATNPDCQEKL- 367
Cdd:cd20637   197 QGTQG----KDYADALDILIESAKEH-----GKELTMQELKDSTIELIFAAF---ATTASASTSLimqLLKHPGVLEKLr 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 368 --LREVDVFKEKHMAPEFCSLEE--GLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPE 443
Cdd:cd20637   265 eeLRSNGILHNGCLCEGTLRLDTisSLKYLDCVIKEVLRLFTPVSGGYRTALQTFELDGFQIPKGWSVLYSIRDTHDTAP 344
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 444 HWPSPETFNPERFtAEARQQHRP--FTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACpeTQVPLQLESKSALG 521
Cdd:cd20637   345 VFKDVDAFDPDRF-GQERSEDKDgrFHYLPFGGGVRTCLGKQLAKLFLKVLAVELASTSRFELA--TRTFPRMTTVPVVH 421

                  ....*...
gi 1488188862 522 PKNGVYIK 529
Cdd:cd20637   422 PVDGLRVK 429
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
329-521 1.22e-14

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: 75.99  E-value: 1.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 329 DEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFcSLEEGLPYLDMVIAETLRMYPPAF 408
Cdd:cd20671   222 ANVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNY-EDRKALPYTSAVIHEVQRFITLLP 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 409 RFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERF-TAEARQQHRPfTYLPFGAGPRSCLGVRLGLL 487
Cdd:cd20671   301 HVPRCTAADTQFKGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFlDAEGKFVKKE-AFLPFSAGRRVCVGESLART 379
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1488188862 488 EVKLTLLHVLHKFRFQAcPETQVPLQLESKSALG 521
Cdd:cd20671   380 ELFIFFTGLLQKFTFLP-PPGVSPADLDATPAAA 412
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
325-481 1.29e-14

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: 76.01  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 325 PLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREV--------DVFKEKHMAPEFCsleEGLPYLDMV 396
Cdd:cd20638   225 PLNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELqekgllstKPNENKELSMEVL---EQLKYTGCV 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 397 IAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGP 476
Cdd:cd20638   302 IKETLRLSPPVPGGFRVALKTFELNGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSRFSFIPFGGGS 381

                  ....*
gi 1488188862 477 RSCLG 481
Cdd:cd20638   382 RSCVG 386
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
339-515 1.38e-14

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: 75.65  E-value: 1.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 339 LIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEkhmAPEFCSLE--EGLPYLDMVIAETLRMYP-PAFRFTREAA 415
Cdd:cd20667   234 FLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLG---ASQLICYEdrKRLPYTNAVIHEVQRLSNvVSVGAVRQCV 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 416 QDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLH 495
Cdd:cd20667   311 TSTTMHGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDGNFVMNEAFLPFSAGHRVCLGEQLARMELFIFFTT 390
                         170       180
                  ....*....|....*....|
gi 1488188862 496 VLHKFRFQaCPETQVPLQLE 515
Cdd:cd20667   391 LLRTFNFQ-LPEGVQELNLE 409
PLN02774 PLN02774
brassinosteroid-6-oxidase
325-503 1.56e-14

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 75.97  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 325 PLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCSLEE--GLPYLDMVIAETLR 402
Cdd:PLN02774  259 KLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKALQELRKEHLAIRERKRPEDPIDWNDykSMRFTRAVIFETSR 338
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 403 MYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFtyLPFGAGPRSCLGV 482
Cdd:PLN02774  339 LATIVNGVLRKTTQDMELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWLDKSLESHNYF--FLFGGGTRLCPGK 416
                         170       180
                  ....*....|....*....|.
gi 1488188862 483 RLGLLEVKLTLLHVLHKFRFQ 503
Cdd:PLN02774  417 ELGIVEISTFLHYFVTRYRWE 437
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
327-512 2.51e-14

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: 75.13  E-value: 2.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 327 TVDEIVGqafifliAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCSLEEgLPYLDMVIAETLR--MY 404
Cdd:cd20677   240 TVNDIFG-------AGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKS-LHYTEAFINEVFRhsSF 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 405 PPaFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFT--YLPFGAGPRSCLGV 482
Cdd:cd20677   312 VP-FTIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQLNKSLVekVLIFGMGVRKCLGE 390
                         170       180       190
                  ....*....|....*....|....*....|
gi 1488188862 483 RLGLLEVKLTLLHVLHKFRFQACPETQVPL 512
Cdd:cd20677   391 DVARNEIFVFLTTILQQLKLEKPPGQKLDL 420
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
357-506 2.56e-14

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 75.54  E-value: 2.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 357 LATNPDCQEKLLREVD-VFKEKHMAPEfcSLEEGLPYLDMVIAETLRMYPP-AFRFTREAAQDCEVLGQRIPAGAVLEMA 434
Cdd:PLN02394  320 LVNHPEIQKKLRDELDtVLGPGNQVTE--PDTHKLPYLQAVVKETLRLHMAiPLLVPHMNLEDAKLGGYDIPAESKILVN 397
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1488188862 435 VGALHHDPEHWPSPETFNPERFTAEARQ---QHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACP 506
Cdd:PLN02394  398 AWWLANNPELWKNPEEFRPERFLEEEAKveaNGNDFRFLPFGVGRRSCPGIILALPILGIVLGRLVQNFELLPPP 472
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
74-523 7.30e-14

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: 73.50  E-value: 7.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNR--MASgleFKSVAD--SVLFLR-DKRWEEVRG---ALMSAFS- 144
Cdd:cd20675     1 YGDVFQIRLGSRPVVVLNGERAIRQALVQQGTDFAGRpdFAS---FRVVSGgrSLAFGGySERWKAHRRvahSTVRAFSt 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 145 ----PEKLNEMvPLISQACDLLLAHLKRYAEsGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEfc 220
Cdd:cd20675    78 rnprTRKAFER-HVLGEARELVALFLRKSAG-GAYFDPAPPLVVAVANVMSAVCFGKRYSHDDAEFRSLLGRNDQFGR-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 221 iprpiLVLLLSFPSIMvPLARILPNKNRDELNGFfnklirnvialrdqqaaEERRRDFLQMVLD--ARHSASPMGvqdfD 298
Cdd:cd20675   154 -----TVGAGSLVDVM-PWLQYFPNPVRTVFRNF-----------------KQLNREFYNFVLDkvLQHRETLRG----G 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 299 IVRDVF----------SSTGCKPNPSRQHQPSpmarplTVDEIVGqafifliAGYEIITNTLSFATYLLATNPDCQEKLL 368
Cdd:cd20675   207 APRDMMdafilalekgKSGDSGVGLDKEYVPS------TVTDIFG-------ASQDTLSTALQWILLLLVRYPDVQARLQ 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 369 REVDVFKEKHMAPefcSLEE--GLPYLDMVIAETLRmyppafrFT--------REAAQDCEVLGQRIPAGAVLEMAVGAL 438
Cdd:cd20675   274 EELDRVVGRDRLP---CIEDqpNLPYVMAFLYEAMR-------FSsfvpvtipHATTADTSILGYHIPKDTVVFVNQWSV 343
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 439 HHDPEHWPSPETFNPERFTAEARQQHRPFT--YLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLES 516
Cdd:cd20675   344 NHDPQKWPNPEVFDPTRFLDENGFLNKDLAssVMIFSVGKRRCIGEELSKMQLFLFTSILAHQCNFTANPNEPLTMDFSY 423

                  ....*..
gi 1488188862 517 KSALGPK 523
Cdd:cd20675   424 GLTLKPK 430
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
326-497 1.85e-13

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: 72.16  E-value: 1.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 326 LTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD-VFKEKHMAPEfcSLEEgLPYLDMVIAETLRmy 404
Cdd:cd20627   198 LSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQKKLYKEVDqVLGKGPITLE--KIEQ-LRYCQQVLCETVR-- 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 405 ppAFRFTREAAQDCEVLGQ----RIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHrpFTYLPFgAGPRSCL 480
Cdd:cd20627   273 --TAKLTPVSARLQELEGKvdqhIIPKETLVLYALGVVLQDNTTWPLPYRFDPDRFDDESVMKS--FSLLGF-SGSQECP 347
                         170
                  ....*....|....*..
gi 1488188862 481 GVRLGLLeVKLTLLHVL 497
Cdd:cd20627   348 ELRFAYM-VATVLLSVL 363
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
324-501 2.48e-13

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: 71.60  E-value: 2.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 324 RPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVfkekhmapefcsleeglpyLDMVIAETLRM 403
Cdd:cd11034   184 KPLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHPEDRRRLIADPSL-------------------IPNAVEEFLRF 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 404 YPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFtaearqqhrPFTYLPFGAGPRSCLGVR 483
Cdd:cd11034   245 YSPVAGLARTVTQEVEVGGCRLKPGDRVLLAFASANRDEEKFEDPDRIDIDRT---------PNRHLAFGSGVHRCLGSH 315
                         170
                  ....*....|....*...
gi 1488188862 484 LGLLEVKLTLLHVLHKFR 501
Cdd:cd11034   316 LARVEARVALTEVLKRIP 333
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
393-500 6.26e-13

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: 69.83  E-value: 6.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 393 LDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARqqhrpftylPF 472
Cdd:cd11036   221 AAAAVAETLRYDPPVRLERRFAAEDLELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGRPTARSA---------HF 291
                          90       100
                  ....*....|....*....|....*...
gi 1488188862 473 GAGPRSCLGVRLGLLEVKLTLLHVLHKF 500
Cdd:cd11036   292 GLGRHACLGAALARAAAAAALRALAARF 319
PLN03018 PLN03018
homomethionine N-hydroxylase
326-519 8.16e-13

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 70.81  E-value: 8.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 326 LTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD-VFKEKHMAPEfcSLEEGLPYLDMVIAETLRMY 404
Cdd:PLN03018  310 VTPDEIKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDeVVGKDRLVQE--SDIPNLNYLKACCRETFRIH 387
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 405 PPAFRFTREAA-QDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPER------FTAEARQQHRPFTYLPFGAGPR 477
Cdd:PLN03018  388 PSAHYVPPHVArQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERhlqgdgITKEVTLVETEMRFVSFSTGRR 467
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1488188862 478 SCLGVRLGLLEVKLTLLHVLHKFRFQACPETQvPLQLESKSA 519
Cdd:PLN03018  468 GCVGVKVGTIMMVMMLARFLQGFNWKLHQDFG-PLSLEEDDA 508
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
336-503 1.50e-12

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 69.65  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 336 FIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDV-FKEKHMapefcsleEGLPYLDMVIAETLRMYPP-AFRFTRE 413
Cdd:PLN02169  307 FSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEINTkFDNEDL--------EKLVYLHAALSESMRLYPPlPFNHKAP 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 414 AAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPET-FNPERFTAE-ARQQHRP-FTYLPFGAGPRSCLGVRLGLLEVK 490
Cdd:PLN02169  379 AKPDVLPSGHKVDAESKIVICIYALGRMRSVWGEDALdFKPERWISDnGGLRHEPsYKFMAFNSGPRTCLGKHLALLQMK 458
                         170
                  ....*....|...
gi 1488188862 491 LTLLHVLHKFRFQ 503
Cdd:PLN02169  459 IVALEIIKNYDFK 471
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
339-509 2.59e-12

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: 68.57  E-value: 2.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 339 LIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEKHMAPEFCSlEEGLPYLDMVIAETLRMYPPA-FRFTREAAQD 417
Cdd:cd20663   239 FSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMAD-QARMPYTNAVIHEVQRFGDIVpLGVPHMTSRD 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 418 CEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVL 497
Cdd:cd20663   318 IEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQGHFVKPEAFMPFSAGRRACLGEPLARMELFLFFTCLL 397
                         170
                  ....*....|..
gi 1488188862 498 HKFRFQAcPETQ 509
Cdd:cd20663   398 QRFSFSV-PAGQ 408
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
74-500 2.95e-12

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: 68.44  E-value: 2.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNR--------MASGLefksvadSVLFLRDKRWEEVRG-ALMSAFS 144
Cdd:cd20665     1 YGPVFTLYLGMKPTVVLHGYEAVKEALIDLGEEFSGRgrfpifekVNKGL-------GIVFSNGERWKETRRfSLMTLRN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 145 --------PEKLNEmvplisQACDLLLAHLKRYAESGDAFDIQRCY-CNyttdVVASVAFGTPVDSwqapEDP-FVKHCK 214
Cdd:cd20665    74 fgmgkrsiEDRVQE------EARCLVEELRKTNGSPCDPTFILGCApCN----VICSIIFQNRFDY----KDQdFLNLME 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 215 RFFE-FCI-PRPILVLLLSFPSIMvplarilpnknrDELNGFFNKLIRNVIALRDqqaaeerrrDFLQMVLDARHSASPM 292
Cdd:cd20665   140 KLNEnFKIlSSPWLQVCNNFPALL------------DYLPGSHNKLLKNVAYIKS---------YILEKVKEHQESLDVN 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 293 GVQDFdIvrDVFSSTGCKPNPSRQHQpspmarpLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD 372
Cdd:cd20665   199 NPRDF-I--DCFLIKMEQEKHNQQSE-------FTLENLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEID 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 373 VFKEKHMAPefCSLEEG-LPYLDMVIAETLR---MYP---PafrftREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHW 445
Cdd:cd20665   269 RVIGRHRSP--CMQDRShMPYTDAVIHEIQRyidLVPnnlP-----HAVTCDTKFRNYLIPKGTTVITSLTSVLHDDKEF 341
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1488188862 446 PSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKF 500
Cdd:cd20665   342 PNPEKFDPGHFLDENGNFKKSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNF 396
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
326-500 3.53e-12

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: 67.84  E-value: 3.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 326 LTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEkhmapefcsleeglpyldmVIAETLRmYP 405
Cdd:cd20630   199 LSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAEPELLRN-------------------ALEEVLR-WD 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 406 PAFR--FTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERftaearqqhRPFTYLPFGAGPRSCLGVR 483
Cdd:cd20630   259 NFGKmgTARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRR---------DPNANIAFGYGPHFCIGAA 329
                         170
                  ....*....|....*..
gi 1488188862 484 LGLLEVKLTLLHVLHKF 500
Cdd:cd20630   330 LARLELELAVSTLLRRF 346
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
326-504 6.05e-12

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 67.84  E-value: 6.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 326 LTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLRE---VDVFKEKHMAPEFCSLEEGLPYLDMVIAETLR 402
Cdd:PLN03141  247 LTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSDCPVALQQLTEEnmkLKRLKADTGEPLYWTDYMSLPFTQNVITETLR 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 403 MYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTaEARQQHRPFTylPFGAGPRSCLGV 482
Cdd:PLN03141  327 MGNIINGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRWQ-EKDMNNSSFT--PFGGGQRLCPGL 403
                         170       180
                  ....*....|....*....|..
gi 1488188862 483 RLGLLEVKLTLLHVLHKFRFQA 504
Cdd:PLN03141  404 DLARLEASIFLHHLVTRFRWVA 425
PLN02500 PLN02500
cytochrome P450 90B1
326-503 3.66e-11

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 65.27  E-value: 3.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 326 LTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLlrevdvfKEKHMAPEFCSLEEG-----------LPYLD 394
Cdd:PLN02500  275 LSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQEL-------REEHLEIARAKKQSGeselnwedykkMEFTQ 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 395 MVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERF-------TAEARQQHRPF 467
Cdd:PLN02500  348 CVINETLRLGNVVRFLHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWqqnnnrgGSSGSSSATTN 427
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1488188862 468 TYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQ 503
Cdd:PLN02500  428 NFMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFNWE 463
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
338-511 3.88e-11

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 65.48  E-value: 3.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 338 FLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDvfkeKHMAP--EFCSLEE--GLPYLDMVIAETLRMYPPAfRFTRE 413
Cdd:PLN02426  301 FLLAGRDTVASALTSFFWLLSKHPEVASAIREEAD----RVMGPnqEAASFEEmkEMHYLHAALYESMRLFPPV-QFDSK 375
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 414 AAQDCEVL--GQRIPAGAVLEMAVGALHHDPEHW-PSPETFNPERFTAEAR-QQHRPFTYLPFGAGPRSCLGVRLGLLEV 489
Cdd:PLN02426  376 FAAEDDVLpdGTFVAKGTRVTYHPYAMGRMERIWgPDCLEFKPERWLKNGVfVPENPFKYPVFQAGLRVCLGKEMALMEM 455
                         170       180
                  ....*....|....*....|...
gi 1488188862 490 KLTLLHVLHKFRFQACPE-TQVP 511
Cdd:PLN02426  456 KSVAVAVVRRFDIEVVGRsNRAP 478
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
77-520 4.02e-11

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: 65.08  E-value: 4.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  77 LCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNR--------MASGleFKSVadsVLFLRDKRWEEVRGALMSA-FSPEK 147
Cdd:cd20658     3 IACIRLGNTHVIPVTCPKIAREILRKQDAVFASRpltyateiISGG--YKTT---VISPYGEQWKKMRKVLTTElMSPKR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 148 LNEMVPLISQACDLLLAHLKRYAESGDAF---DIQRCYCNYTTDVVASVAFGT------PVDSWQAPEDpfVKHCKRFFE 218
Cdd:cd20658    78 HQWLHGKRTEEADNLVAYVYNMCKKSNGGglvNVRDAARHYCGNVIRKLMFGTryfgkgMEDGGPGLEE--VEHMDAIFT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 219 fciprpILVLLLSFP-SIMVPLARILpnknrdELNGFFNKLIRNVIALRDQQaaeerrrdflQMVLDAR----HSASPMG 293
Cdd:cd20658   156 ------ALKCLYAFSiSDYLPFLRGL------DLDGHEKIVREAMRIIRKYH----------DPIIDERikqwREGKKKE 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 294 VQDFdivRDVFSSTgckpnpsRQHQPSPMarpLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD- 372
Cdd:cd20658   214 EEDW---LDVFITL-------KDENGNPL---LTPDEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDr 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 373 -VFKEKHMApefcslEEGLPYLDMVIA---ETLRMYPPA-FRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPS 447
Cdd:cd20658   281 vVGKERLVQ------ESDIPNLNYVKAcarEAFRLHPVApFNVPHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDD 354
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1488188862 448 PETFNPERFTAEARQ---QHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQAcPETQVPLQL-ESKSAL 520
Cdd:cd20658   355 PLKFKPERHLNEDSEvtlTEPDLRFISFSTGRRGCPGVKLGTAMTVMLLARLLQGFTWTL-PPNVSSVDLsESKDDL 430
PLN02971 PLN02971
tryptophan N-hydroxylase
82-516 6.16e-11

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 64.67  E-value: 6.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  82 LGRRMFIVISEPDMIKQVLVENFSNFTNR---MASGLEFKSVADSVLFLRDKRWEEVRGALMSAF-SPEKLNEMVPLISQ 157
Cdd:PLN02971  100 LGNTHVIPVTCPKIAREIFKQQDALFASRpltYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIvCPARHRWLHDNRAE 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 158 ACDLLLAHLKRYAESGDAFDIQRCYCNYTTDVVASVAFGTPVDSWQAPED-----PFVKHCKRFFE-------FCIprpi 225
Cdd:PLN02971  180 ETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEPDggptlEDIEHMDAMFEglgftfaFCI---- 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 226 lvlllsfpsimvplARILPNKNRDELNGFfNKLIRNVIALRDQ---QAAEERrrdfLQMVLDARHSAspmgVQDFdivRD 302
Cdd:PLN02971  256 --------------SDYLPMLTGLDLNGH-EKIMRESSAIMDKyhdPIIDER----IKMWREGKRTQ----IEDF---LD 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 303 VFSSTgckpnpsRQHQPSPMarpLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVD--VFKEKHMA 380
Cdd:PLN02971  310 IFISI-------KDEAGQPL---LTADEIKPTIKELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDrvVGKERFVQ 379
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 381 pefcslEEGLP---YLDMVIAETLRMYP-PAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERF 456
Cdd:PLN02971  380 ------ESDIPklnYVKAIIREAFRLHPvAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERH 453
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1488188862 457 TAEARQ---QHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQ-ACPETQVPLQLES 516
Cdd:PLN02971  454 LNECSEvtlTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKlAGSETRVELMESS 517
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
265-493 8.31e-11

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: 63.53  E-value: 8.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 265 LRDQQAAEeRRRDFLQMVLDArhsaspmgvQDFD-IVRDVFSSTGCKPNPSRQHQ-PSPMA-----RPLTVDEIVGQAFI 337
Cdd:cd11079   121 VNKNHAAT-RSGDRAATAEVA---------EEFDgIIRDLLADRRAAPRDADDDVtARLLRervdgRPLTDEEIVSILRN 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 338 FLIAGYEIITNTLSFATYLLATNPDCQEKLlrevdvfkekhmapefcslEEGLPYLDMVIAETLRMYPPAFRFTREAAQD 417
Cdd:cd11079   191 WTVGELGTIAACVGVLVHYLARHPELQARL-------------------RANPALLPAAIDEILRLDDPFVANRRITTRD 251
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1488188862 418 CEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERftaEARQQhrpftyLPFGAGPRSCLGVRLGLLEVKLTL 493
Cdd:cd11079   252 VELGGRTIPAGSRVTLNWASANRDERVFGDPDEFDPDR---HAADN------LVYGRGIHVCPGAPLARLELRILL 318
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
74-500 1.41e-10

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: 63.26  E-value: 1.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862  74 YGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSVAD-SVLFLRDKRWEEVRG---ALMSAFSPEKlN 149
Cdd:cd20672     1 YGDVFTVHLGPRPVVMLCGTDAIREALVDQAEAFSGRGTIAVVDPIFQGyGVIFANGERWKTLRRfslATMRDFGMGK-R 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 150 EMVPLISQACDLLLAHLKRYaeSGDAFDIQRCYCNYTTDVVASVAFGTPVDsWQAPEdpFVKHCKRFFEfciprpILVLL 229
Cdd:cd20672    80 SVEERIQEEAQCLVEELRKS--KGALLDPTFLFQSITANIICSIVFGERFD-YKDPQ--FLRLLDLFYQ------TFSLI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 230 LSFPSIMVPL----ARILPN------KNRDELNGFFNKLIRNVIALRDQQAAeerrRDFLQMVLDARHSAspmgvqdfdi 299
Cdd:cd20672   149 SSFSSQVFELfsgfLKYFPGahrqiyKNLQEILDYIGHSVEKHRATLDPSAP----RDFIDTYLLRMEKE---------- 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 300 vrdvfsstgcKPNPSRQ--HQpspmarpltvdEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDVFKEK 377
Cdd:cd20672   215 ----------KSNHHTEfhHQ-----------NLMISVLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGS 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 378 HMAPefcSLEE--GLPYLDMVIAETLRMYPPA-FRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPE 454
Cdd:cd20672   274 HRLP---TLDDraKMPYTDAVIHEIQRFSDLIpIGVPHRVTKDTLFRGYLLPKNTEVYPILSSALHDPQYFEQPDTFNPD 350
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1488188862 455 RFTAEARQQHRPFTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKF 500
Cdd:cd20672   351 HFLDANGALKKSEAFMPFSTGKRICLGEGIARNELFLFFTTILQNF 396
CYP_unk cd20623
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
326-497 7.99e-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: 410716 [Multi-domain]  Cd Length: 367  Bit Score: 60.74  E-value: 7.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 326 LTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPdcqekllrevdvfkekhmapEF-CSLEEGLPYLDMVIAETLRMY 404
Cdd:cd20623   192 LTDEEVVHDLVLLLGAGHEPTTNLIGNTLRLMLTDP--------------------RFaASLSGGRLSVREALNEVLWRD 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 405 PP----AFRFtreAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETfnperfTAEARQQHrpftyLPFGAGPRSCL 480
Cdd:cd20623   252 PPlanlAGRF---AARDTELGGQWIRAGDLVVLGLAAANADPRVRPDPGA------SMSGNRAH-----LAFGAGPHRCP 317
                         170       180
                  ....*....|....*....|
gi 1488188862 481 GVRLGLLEVKL---TLLHVL 497
Cdd:cd20623   318 AQELAETIARTaveVLLDRL 337
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
356-508 1.35e-09

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: 60.17  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 356 LLATNPDCQEKLLREVDVFKEkhmapefcslEEGLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAV 435
Cdd:cd20624   217 LLAAHPEQAARAREEAAVPPG----------PLARPYLRACVLDAVRLWPTTPAVLRESTEDTVWGGRTVPAGTGFLIFA 286
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1488188862 436 GALHHDPEHWPSPETFNPERFtAEARQQHRPfTYLPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPET 508
Cdd:cd20624   287 PFFHRDDEALPFADRFVPEIW-LDGRAQPDE-GLVPFSAGPARCPGENLVLLVASTALAALLRRAEIDPLESP 357
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
393-484 1.72e-09

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: 59.66  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 393 LDMVIAETLRMYPPAFRFTREAAQDCEVL-----GQRIPAGAVLEMAVGALHHDPEHWPSPETFNPerftaearqqHRPF 467
Cdd:cd20612   240 LRGYVLEALRLNPIAPGLYRRATTDTTVAdgggrTVSIKAGDRVFVSLASAMRDPRAFPDPERFRL----------DRPL 309
                          90
                  ....*....|....*...
gi 1488188862 468 T-YLPFGAGPRSCLGVRL 484
Cdd:cd20612   310 EsYIHFGHGPHQCLGEEI 327
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
350-475 1.86e-09

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: 59.85  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 350 LSFATYLLATNPDCQEKLLREVDvfkekhmapefcsleeglPYLDMVIAETLRMYP--PAF--RftreAAQDCEVLGQRI 425
Cdd:cd11067   240 VTFAALALHEHPEWRERLRSGDE------------------DYAEAFVQEVRRFYPffPFVgaR----ARRDFEWQGYRF 297
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1488188862 426 PAGAVLEMAVGALHHDPEHWPSPETFNPERFtaeARQQHRPFTYLPFGAG 475
Cdd:cd11067   298 PKGQRVLLDLYGTNHDPRLWEDPDRFRPERF---LGWEGDPFDFIPQGGG 344
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
360-460 5.32e-08

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


Pssm-ID: 410694 [Multi-domain]  Cd Length: 424  Bit Score: 55.34  E-value: 5.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 360 NPDCQEKLLREVDVFKEKHMAPEFCSLEEgLPYLDMVIAETLRMYPPAFRFTREAAQDCEVLGQ----RIPAGavlEMAV 435
Cdd:cd11071   256 GEELHARLAEEIRSALGSEGGLTLAALEK-MPLLKSVVYETLRLHPPVPLQYGRARKDFVIESHdasyKIKKG---ELLV 331
                          90       100
                  ....*....|....*....|....*...
gi 1488188862 436 GAL---HHDPEHWPSPETFNPERFTAEA 460
Cdd:cd11071   332 GYQplaTRDPKVFDNPDEFVPDRFMGEE 359
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
354-479 2.41e-07

cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a putative cytochrome P450 of unknown function. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle.


Pssm-ID: 410719  Cd Length: 381  Bit Score: 52.79  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 354 TYLLATNPDCQEkllrEVDVFKEKHMAPEfCSLEeglpyldMVIAETLRMYPPAFRFTReAAQDCEVLGQRIPAGAVLEM 433
Cdd:cd20626   231 TLRDPTHPEWRE----ANADFAKSATKDG-ISAK-------NLVKEALRLYPPTRRIYR-AFQRPGSSKPEIIAADIEAC 297
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1488188862 434 avgalHHDPEHW-PSPETFNPERFTAEARQQHRPFtyLPFGAGPRSC 479
Cdd:cd20626   298 -----HRSESIWgPDALEFNPSRWSKLTPTQKEAF--LPFGSGPFRC 337
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
354-511 8.20e-06

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: 48.13  E-value: 8.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 354 TYLLaTNPDCQEKLLREVD-VFKE--KHMAPEFC------SLEEGLPYLDMVIAETLRMYPPAFrFTREAAQDcevlgqr 424
Cdd:cd20633   249 LYLL-KHPEAMKAVREEVEqVLKEtgQEVKPGGPlinltrDMLLKTPVLDSAVEETLRLTAAPV-LIRAVVQD------- 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 425 ipagAVLEMAVG-----------------ALHHDPEHWPSPETFNPERFTAEARQQHRPF--------TY-LPFGAGPRS 478
Cdd:cd20633   320 ----MTLKMANGreyalrkgdrlalfpylAVQMDPEIHPEPHTFKYDRFLNPDGGKKKDFykngkklkYYnMPWGAGVSI 395
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1488188862 479 CLGVRLGLLEVKLTLLHVLHKFRFQAC-PETQVP 511
Cdd:cd20633   396 CPGRFFAVNEMKQFVFLMLTYFDLELVnPDEEIP 429
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
310-481 9.13e-06

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: 47.88  E-value: 9.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 310 KPNPS-RQHQ-PSPMARPLtvDEIVGQAFIFLIAGYEIITNTLSFATYLLATNPDCQEKLLREVDvfkekhmaPEFCSLE 387
Cdd:cd11039   182 NPNPSlLSVMlNAGMPMSL--EQIRANIKVAIGGGLNEPRDAIAGTCWGLLSNPEQLAEVMAGDV--------HWLRAFE 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 388 EGLPYLdmviaETLRMYPpafrftREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERftaeARQQHrpf 467
Cdd:cd11039   252 EGLRWI-----SPIGMSP------RRVAEDFEIRGVTLPAGDRVFLMFGSANRDEARFENPDRFDVFR----PKSPH--- 313
                         170
                  ....*....|....
gi 1488188862 468 tyLPFGAGPRSCLG 481
Cdd:cd11039   314 --VSFGAGPHFCAG 325
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
355-512 1.33e-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: 47.83  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 355 YLLaTNPDCQEKLLREVDVFKEKH---MAPEFCSLEEGL---PYLDMVIAETLRMYPPAFrFTREAAQDcevlgqripag 428
Cdd:cd20634   247 FLL-KHPEAMAAVRGEIQRIKHQRgqpVSQTLTINQELLdntPVFDSVLSETLRLTAAPF-ITREVLQD----------- 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 429 AVLEMAVGALHH-----------------DPEHWPSPETFNPERFTAEARQQHRPF-------TY--LPFGAGPRSCLGV 482
Cdd:cd20634   314 MKLRLADGQEYNlrrgdrlclfpflspqmDPEIHQEPEVFKYDRFLNADGTEKKDFykngkrlKYynMPWGAGDNVCIGR 393
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1488188862 483 RLGLLEVKLTLLHVLHKFRFQAC-PETQVPL 512
Cdd:cd20634   394 HFAVNSIKQFVFLILTHFDVELKdPEAEIPE 424
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
394-481 1.57e-05

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


Pssm-ID: 410712 [Multi-domain]  Cd Length: 358  Bit Score: 47.04  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 394 DMVIAETLRMYPPAFRFTREAAQDCEVLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQqhrpftyLPFG 473
Cdd:cd20619   235 AAIINEMVRMDPPQLSFLRFPTEDVEIGGVLIEAGSPIRFMIGAANRDPEVFDDPDVFDHTRPPAASRN-------LSFG 307

                  ....*...
gi 1488188862 474 AGPRSCLG 481
Cdd:cd20619   308 LGPHSCAG 315
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
336-521 4.96e-05

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: 45.75  E-value: 4.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 336 FIFLIAGyeiITNTL--SF-ATYLLATNPDCQEKLLREVD-VFKEKHM--APEF---CSLEE--GLPYLDMVIAETLRM- 403
Cdd:cd20632   221 FAFLWAS---VGNTIpaTFwAMYYLLRHPEALAAVRDEIDhVLQSTGQelGPDFdihLTREQldSLVYLESAINESLRLs 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 404 -YPPAFR-----FTREAAQDCEVlgqRIPAGAVLEMAVGALHHDPEHWPSPETFNPERF--------TAEARQQHRPFTY 469
Cdd:cd20632   298 sASMNIRvvqedFTLKLESDGSV---NLRKGDIVALYPQSLHMDPEIYEDPEVFKFDRFvedgkkktTFYKRGQKLKYYL 374
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1488188862 470 LPFGAGPRSCLGVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLESKSALG 521
Cdd:cd20632   375 MPFGSGSSKCPGRFFAVNEIKQFLSLLLLYFDLELLEEQKPPGLDNSRAGLG 426
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
388-494 2.97e-04

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: 43.52  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488188862 388 EGLPYLDMVIAETLRMYPPAFRFtREAAQDCEVL---GQR--IPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQ 462
Cdd:cd20631   294 DDMPVLGSIIKEALRLSSASLNI-RVAKEDFTLHldsGESyaIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGK 372
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1488188862 463 QHRPFT---------YLPFGAGPRSCLGVRLGLLEVK--LTLL 494
Cdd:cd20631   373 EKTTFYkngrklkyyYMPFGSGTSKCPGRFFAINEIKqfLSLM 415
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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