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Conserved domains on  [gi|187956757|gb|AAI38968|]
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Cytochrome P450, family 4, subfamily v, polypeptide 3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
76-515 0e+00

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: 929.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  76 QLIYYTEEFRHLPIIKLWIGPVPLVALYKAENVEVILTSSKQIDKSFLYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTFH 155
Cdd:cd20680    1 QIIEYTEEFRHEPLLKLWIGPVPFVILYHAENVEVILSSSKHIDKSYLYKFLHPWLGTGLLTSTGEKWRSRRKMLTPTFH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 156 FTILENFLDVMNEQANILVNKLEKHVNQEAFNCFFYITLCALDIICETAMGKNIGAQSNNDSEYVRTVYRMSDMIYRRMK 235
Cdd:cd20680   81 FTILSDFLEVMNEQSNILVEKLEKHVDGEAFNCFFDITLCALDIICETAMGKKIGAQSNKDSEYVQAVYRMSDIIQRRQK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 236 MPWLWFDLWYLVFKEGRDHKRGLKCLHTFTNNVIAERVKERKAEEDWTGAGRGPIPSKNKRKAFLDLLLSVTDEEGNRLS 315
Cdd:cd20680  161 MPWLWLDLWYLMFKEGKEHNKNLKILHTFTDNVIAERAEEMKAEEDKTGDSDGESPSKKKRKAFLDMLLSVTDEEGNKLS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 316 QEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVTLEDLKKLKYLDCVIKETLRVFPSV 395
Cdd:cd20680  241 HEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKSDRPVTMEDLKKLRYLECVIKESLRLFPSV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 396 PLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVM 475
Cdd:cd20680  321 PLFARSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSGRHPYAYIPFSAGPRNCIGQRFALM 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 187956757 476 EEKTILACILRQFWVESNQKREELGLAGDLILRPNNGIWI 515
Cdd:cd20680  401 EEKVVLSCILRHFWVEANQKREELGLVGELILRPQNGIWI 440
 
Name Accession Description Interval E-value
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
76-515 0e+00

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: 929.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  76 QLIYYTEEFRHLPIIKLWIGPVPLVALYKAENVEVILTSSKQIDKSFLYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTFH 155
Cdd:cd20680    1 QIIEYTEEFRHEPLLKLWIGPVPFVILYHAENVEVILSSSKHIDKSYLYKFLHPWLGTGLLTSTGEKWRSRRKMLTPTFH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 156 FTILENFLDVMNEQANILVNKLEKHVNQEAFNCFFYITLCALDIICETAMGKNIGAQSNNDSEYVRTVYRMSDMIYRRMK 235
Cdd:cd20680   81 FTILSDFLEVMNEQSNILVEKLEKHVDGEAFNCFFDITLCALDIICETAMGKKIGAQSNKDSEYVQAVYRMSDIIQRRQK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 236 MPWLWFDLWYLVFKEGRDHKRGLKCLHTFTNNVIAERVKERKAEEDWTGAGRGPIPSKNKRKAFLDLLLSVTDEEGNRLS 315
Cdd:cd20680  161 MPWLWLDLWYLMFKEGKEHNKNLKILHTFTDNVIAERAEEMKAEEDKTGDSDGESPSKKKRKAFLDMLLSVTDEEGNKLS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 316 QEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVTLEDLKKLKYLDCVIKETLRVFPSV 395
Cdd:cd20680  241 HEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKSDRPVTMEDLKKLRYLECVIKESLRLFPSV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 396 PLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVM 475
Cdd:cd20680  321 PLFARSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSGRHPYAYIPFSAGPRNCIGQRFALM 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 187956757 476 EEKTILACILRQFWVESNQKREELGLAGDLILRPNNGIWI 515
Cdd:cd20680  401 EEKVVLSCILRHFWVEANQKREELGLVGELILRPQNGIWI 440
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
51-517 6.19e-127

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: 378.55  E-value: 6.19e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757   51 PSVARAYPLVGHALyMKPNNAEFFQQLIYYTEEFRhlPIIKLWIGPVPLVALYKAENVEVIL-----TSSKQIDKSFLYK 125
Cdd:pfam00067   1 PPGPPPLPLFGNLL-QLGRKGNLHSVFTKLQKKYG--PIFRLYLGPKPVVVLSGPEAVKEVLikkgeEFSGRPDEPWFAT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  126 FLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQANILVNKLEKHVNQ-EAFNCFFYITLCALDIICETA 204
Cdd:pfam00067  78 SRGPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEpGVIDITDLLFRAALNVICSIL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  205 MGKNIGA-QSNNDSEYVRTVYRMSDMIYRRMKMPWLWF-DLWYLVFKEGRDHKRGLKCLHTFTNNVIaervKERKAEEDw 282
Cdd:pfam00067 158 FGERFGSlEDPKFLELVKAVQELSSLLSSPSPQLLDLFpILKYFPGPHGRKLKRARKKIKDLLDKLI----EERRETLD- 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  283 tgagrgpiPSKNKRKAFLD-LLLSVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDE 361
Cdd:pfam00067 233 --------SAKKSPRDFLDaLLLAKEEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDE 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  362 VFGRsHRPVTLEDLKKLKYLDCVIKETLRVFPSVPLF-ARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFR 440
Cdd:pfam00067 305 VIGD-KRSPTYDDLQNMPYLDAVIKETLRLHPVVPLLlPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFD 383
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187956757  441 PERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQFWVESNQKRE-ELGLAGDLILRPNNGIWIKL 517
Cdd:pfam00067 384 PERFLDENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDpPDIDETPGLLLPPKPYKLKF 461
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
79-515 1.27e-62

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: 210.13  E-value: 1.27e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  79 YYTEEFRHLPIIKLWIGPVPLVALYKAENVEVILTSSKQIDKS-FLYKFLQP--WLGLGLLTSTGSKWRTRRKMLTPTFH 155
Cdd:COG2124   24 FYARLREYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDgGLPEVLRPlpLLGDSLLTLDGPEHTRLRRLVQPAFT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 156 FTILENFLDVMNEQANILVNKLEKHVNQEAFNCFFYITLcalDIICETAMGknigaqsnNDSEYVRTVYRMSDMIYRRMk 235
Cdd:COG2124  104 PRRVAALRPRIREIADELLDRLAARGPVDLVEEFARPLP---VIVICELLG--------VPEEDRDRLRRWSDALLDAL- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 236 MPWLWfdlwylvfKEGRDHKRGLKCLHTFTNNVIAERvkERKAEEDwtgagrgpipsknkrkaFLDLLLSVTDEeGNRLS 315
Cdd:COG2124  172 GPLPP--------ERRRRARRARAELDAYLRELIAER--RAEPGDD-----------------LLSALLAARDD-GERLS 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 316 QEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDevfgrshrpvtledlkklkYLDCVIKETLRVFPSV 395
Cdd:COG2124  224 DEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAEPE-------------------LLPAAVEETLRLYPPV 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 396 PLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPErffpensqgRHPYAYVPFSAGPRNCIGQKFAVM 475
Cdd:COG2124  285 PLLPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPD---------RPPNAHLPFGGGPHRCLGAALARL 355
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 187956757 476 EEKTILACILRQFwvesnqkrEELGLAGDLILRPNNGIWI 515
Cdd:COG2124  356 EARIALATLLRRF--------PDLRLAPPEELRWRPSLTL 387
PLN02936 PLN02936
epsilon-ring hydroxylase
132-525 1.28e-48

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 174.98  E-value: 1.28e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 132 GLGLLTSTGSKWRTRRKMLTPTFHFTILENFLD-VMNEQANILVNKLEKHV-NQEAFNCFFYITLCALDIICETAMGKNI 209
Cdd:PLN02936  96 GSGFAIAEGELWTARRRAVVPSLHRRYLSVMVDrVFCKCAERLVEKLEPVAlSGEAVNMEAKFSQLTLDVIGLSVFNYNF 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 210 GAQSNnDSEYVRTVY--------RMSDMiyrrmkMPWLWFDLWYLVFKEGRDHKRGLKCLHTFTNNVIA------ERVKE 275
Cdd:PLN02936 176 DSLTT-DSPVIQAVYtalkeaetRSTDL------LPYWKVDFLCKISPRQIKAEKAVTVIRETVEDLVDkckeivEAEGE 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 276 RKAEEDWTGAGRgpiPSknkrkaFLDLLLSVTDEegnrLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKV 355
Cdd:PLN02936 249 VIEGEEYVNDSD---PS------VLRFLLASREE----VSSVQLRDDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKA 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 356 DQELDEVFGrsHRPVTLEDLKKLKYLDCVIKETLRVFPSVP-LFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFP 434
Cdd:PLN02936 316 QEELDRVLQ--GRPPTYEDIKELKYLTRCINESMRLYPHPPvLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWE 393
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 435 DPEEFRPERFFPENSQGRHP---YAYVPFSAGPRNCIGQKFAVMEEKTILACILRQFWVE--SNQKreeLGLAGDLILRP 509
Cdd:PLN02936 394 RAEEFVPERFDLDGPVPNETntdFRYIPFSGGPRKCVGDQFALLEAIVALAVLLQRLDLElvPDQD---IVMTTGATIHT 470
                        410
                 ....*....|....*.
gi 187956757 510 NNGIWIKLKRRHEDDP 525
Cdd:PLN02936 471 TNGLYMTVSRRRVPDG 486
 
Name Accession Description Interval E-value
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
76-515 0e+00

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: 929.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  76 QLIYYTEEFRHLPIIKLWIGPVPLVALYKAENVEVILTSSKQIDKSFLYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTFH 155
Cdd:cd20680    1 QIIEYTEEFRHEPLLKLWIGPVPFVILYHAENVEVILSSSKHIDKSYLYKFLHPWLGTGLLTSTGEKWRSRRKMLTPTFH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 156 FTILENFLDVMNEQANILVNKLEKHVNQEAFNCFFYITLCALDIICETAMGKNIGAQSNNDSEYVRTVYRMSDMIYRRMK 235
Cdd:cd20680   81 FTILSDFLEVMNEQSNILVEKLEKHVDGEAFNCFFDITLCALDIICETAMGKKIGAQSNKDSEYVQAVYRMSDIIQRRQK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 236 MPWLWFDLWYLVFKEGRDHKRGLKCLHTFTNNVIAERVKERKAEEDWTGAGRGPIPSKNKRKAFLDLLLSVTDEEGNRLS 315
Cdd:cd20680  161 MPWLWLDLWYLMFKEGKEHNKNLKILHTFTDNVIAERAEEMKAEEDKTGDSDGESPSKKKRKAFLDMLLSVTDEEGNKLS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 316 QEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVTLEDLKKLKYLDCVIKETLRVFPSV 395
Cdd:cd20680  241 HEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKSDRPVTMEDLKKLRYLECVIKESLRLFPSV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 396 PLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVM 475
Cdd:cd20680  321 PLFARSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSGRHPYAYIPFSAGPRNCIGQRFALM 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 187956757 476 EEKTILACILRQFWVESNQKREELGLAGDLILRPNNGIWI 515
Cdd:cd20680  401 EEKVVLSCILRHFWVEANQKREELGLVGELILRPQNGIWI 440
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
88-515 0e+00

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: 783.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVILTSSKQIDKSFLYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMN 167
Cdd:cd20660    2 PIFRIWLGPKPIVVLYSAETVEVILSSSKHIDKSFEYDFLHPWLGTGLLTSTGEKWHSRRKMLTPTFHFKILEDFLDVFN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 168 EQANILVNKLEKHVNQEAFNCFFYITLCALDIICETAMGKNIGAQSNNDSEYVRTVYRMSDMIYRRMKMPWLWFDLWYLV 247
Cdd:cd20660   82 EQSEILVKKLKKEVGKEEFDIFPYITLCALDIICETAMGKSVNAQQNSDSEYVKAVYRMSELVQKRQKNPWLWPDFIYSL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 248 FKEGRDHKRGLKCLHTFTNNVIAERVKERKAEED-WTGAGRGPIPSKNKRKAFLDLLLSVTdEEGNRLSQEDIREEVDTF 326
Cdd:cd20660  162 TPDGREHKKCLKILHGFTNKVIQERKAELQKSLEeEEEDDEDADIGKRKRLAFLDLLLEAS-EEGTKLSDEDIREEVDTF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 327 MFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDC 406
Cdd:cd20660  241 MFEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGDSDRPATMDDLKEMKYLECVIKEALRLFPSVPMFGRTLSEDI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 407 EVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILR 486
Cdd:cd20660  321 EIGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAGRHPYAYIPFSAGPRNCIGQKFALMEEKVVLSSILR 400
                        410       420
                 ....*....|....*....|....*....
gi 187956757 487 QFWVESNQKREELGLAGDLILRPNNGIWI 515
Cdd:cd20660  401 NFRIESVQKREDLKPAGELILRPVDGIRV 429
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
88-515 0e+00

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: 691.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVILTSSKQIDKSFLYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMN 167
Cdd:cd20628    2 GVFRLWIGPKPYVVVTNPEDIEVILSSSKLITKSFLYDFLKPWLGDGLLTSTGEKWRKRRKLLTPAFHFKILESFVEVFN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 168 EQANILVNKLEKHVNQEAFNCFFYITLCALDIICETAMGKNIGAQSNNDSEYVRTVYRMSDMIYRRMKMPWLWFDLWYLV 247
Cdd:cd20628   82 ENSKILVEKLKKKAGGGEFDIFPYISLCTLDIICETAMGVKLNAQSNEDSEYVKAVKRILEIILKRIFSPWLRFDFIFRL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 248 FKEGRDHKRGLKCLHTFTNNVIAERVKERKAEEDWTGAGRGPipSKNKRKAFLDLLLSVTdEEGNRLSQEDIREEVDTFM 327
Cdd:cd20628  162 TSLGKEQRKALKVLHDFTNKVIKERREELKAEKRNSEEDDEF--GKKKRKAFLDLLLEAH-EDGGPLTDEDIREEVDTFM 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 328 FEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCE 407
Cdd:cd20628  239 FAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDDRRPTLEDLNKMKYLERVIKETLRLYPSVPFIGRRLTEDIK 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 408 VGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQ 487
Cdd:cd20628  319 LDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSAKRHPYAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRN 398
                        410       420
                 ....*....|....*....|....*...
gi 187956757 488 FWVESNQKREELGLAGDLILRPNNGIWI 515
Cdd:cd20628  399 FRVLPVPPGEDLKLIAEIVLRSKNGIRV 426
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
92-516 2.31e-162

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: 467.42  E-value: 2.31e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  92 LWIGPV-PLVALYKAENVEVILTSSKQIDKSFlYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQA 170
Cdd:cd20659    6 FWLGPFrPILVLNHPDTIKAVLKTSEPKDRDS-YRFLKPWLGDGLLLSNGKKWKRNRRLLTPAFHFDILKPYVPVYNECT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 171 NILVNKLEKHVNQ-EAFNCFFYITLCALDIICETAMGKNI-GAQSNNDSEYVRTVYRMSDMIYRRMKMPWLWFDLWYLVF 248
Cdd:cd20659   85 DILLEKWSKLAETgESVEVFEDISLLTLDIILRCAFSYKSnCQQTGKNHPYVAAVHELSRLVMERFLNPLLHFDWIYYLT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 249 KEGRDHKRGLKCLHTFTNNVIAERVKERKAEEDwtgagrgPIPSKNKRKAFLDLLLSVTDEEGNRLSQEDIREEVDTFMF 328
Cdd:cd20659  165 PEGRRFKKACDYVHKFAEEIIKKRRKELEDNKD-------EALSKRKYLDFLDILLTARDEDGKGLTDEEIRDEVDTFLF 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 329 EGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGrsHR-PVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCE 407
Cdd:cd20659  238 AGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLG--DRdDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPIT 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 408 VGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQ 487
Cdd:cd20659  316 IDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIKKRDPFAFIPFSAGPRNCIGQNFAMNEMKVVLARILRR 395
                        410       420
                 ....*....|....*....|....*....
gi 187956757 488 FWVESNQKREELGLAGdLILRPNNGIWIK 516
Cdd:cd20659  396 FELSVDPNHPVEPKPG-LVLRSKNGIKLK 423
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
88-512 8.48e-139

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: 407.76  E-value: 8.48e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVILTSSKQIDKSFLYKFLqpWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMN 167
Cdd:cd11057    2 SPFRAWLGPRPFVITSDPEIVQVVLNSPHCLNKSFFYDFF--RLGRGLFSAPYPIWKLQRKALNPSFNPKILLSFLPIFN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 168 EQANILVNKLEKHVNQEAFNCFFYITLCALDIICETAMGKNIGAQSNNDSEYVRTVYRMSDMIYRRMKMPWLWFDLWYLV 247
Cdd:cd11057   80 EEAQKLVQRLDTYVGGGEFDILPDLSRCTLEMICQTTLGSDVNDESDGNEEYLESYERLFELIAKRVLNPWLHPEFIYRL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 248 FKEGRDHKRGLKCLHTFTNNVIAERVKERKAEEdwTGAGRGPIPSKNKRKAFLDLLLSVTdEEGNRLSQEDIREEVDTFM 327
Cdd:cd11057  160 TGDYKEEQKARKILRAFSEKIIEKKLQEVELES--NLDSEEDEENGRKPQIFIDQLLELA-RNGEEFTDEEIMDEIDTMI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 328 FEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCE 407
Cdd:cd11057  237 FAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDDGQFITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQ 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 408 VG-GYKVTKGTEAIIIPYALHRDPRYF-PDPEEFRPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACIL 485
Cdd:cd11057  317 LSnGVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLPERSAQRHPYAFIPFSAGPRNCIGWRYAMISMKIMLAKIL 396
                        410       420
                 ....*....|....*....|....*..
gi 187956757 486 RQFWVESNQKREELGLAGDLILRPNNG 512
Cdd:cd11057  397 RNYRLKTSLRLEDLRFKFNITLKLANG 423
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
51-517 6.19e-127

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: 378.55  E-value: 6.19e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757   51 PSVARAYPLVGHALyMKPNNAEFFQQLIYYTEEFRhlPIIKLWIGPVPLVALYKAENVEVIL-----TSSKQIDKSFLYK 125
Cdd:pfam00067   1 PPGPPPLPLFGNLL-QLGRKGNLHSVFTKLQKKYG--PIFRLYLGPKPVVVLSGPEAVKEVLikkgeEFSGRPDEPWFAT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  126 FLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQANILVNKLEKHVNQ-EAFNCFFYITLCALDIICETA 204
Cdd:pfam00067  78 SRGPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEpGVIDITDLLFRAALNVICSIL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  205 MGKNIGA-QSNNDSEYVRTVYRMSDMIYRRMKMPWLWF-DLWYLVFKEGRDHKRGLKCLHTFTNNVIaervKERKAEEDw 282
Cdd:pfam00067 158 FGERFGSlEDPKFLELVKAVQELSSLLSSPSPQLLDLFpILKYFPGPHGRKLKRARKKIKDLLDKLI----EERRETLD- 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  283 tgagrgpiPSKNKRKAFLD-LLLSVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDE 361
Cdd:pfam00067 233 --------SAKKSPRDFLDaLLLAKEEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDE 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  362 VFGRsHRPVTLEDLKKLKYLDCVIKETLRVFPSVPLF-ARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFR 440
Cdd:pfam00067 305 VIGD-KRSPTYDDLQNMPYLDAVIKETLRLHPVVPLLlPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFD 383
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187956757  441 PERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQFWVESNQKRE-ELGLAGDLILRPNNGIWIKL 517
Cdd:pfam00067 384 PERFLDENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDpPDIDETPGLLLPPKPYKLKF 461
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
74-516 1.39e-119

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: 358.90  E-value: 1.39e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  74 FQQLIYYTEEFRHlpIIKLWIGP-VPLVALYKAENVEVILTSSKQIDkSFLYKFLQPWLGLGLLTSTGSKWRTRRKMLTP 152
Cdd:cd20678    1 LQKILKWVEKYPY--AFPLWFGGfKAFLNIYDPDYAKVVLSRSDPKA-QGVYKFLIPWIGKGLLVLNGQKWFQHRRLLTP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 153 TFHFTILENFLDVMNEQANILVNKLEKHVNQEA-FNCFFYITLCALDIICETAMGKNIGAQSN-NDSEYVRTVYRMSDMI 230
Cdd:cd20678   78 AFHYDILKPYVKLMADSVRVMLDKWEKLATQDSsLEIFQHVSLMTLDTIMKCAFSHQGSCQLDgRSNSYIQAVSDLSNLI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 231 YRRMKMPWLWFDLWYLVFKEGRDHKRGLKCLHTFTNNVIAERVKERKAEEDWTGAgrgpipSKNKRKAFLDLLLSVTDEE 310
Cdd:cd20678  158 FQRLRNFFYHNDFIYKLSPHGRRFRRACQLAHQHTDKVIQQRKEQLQDEGELEKI------KKKRHLDFLDILLFAKDEN 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 311 GNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFG-RSHrpVTLEDLKKLKYLDCVIKETL 389
Cdd:cd20678  232 GKSLSDEDLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGdGDS--ITWEHLDQMPYTTMCIKEAL 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 390 RVFPSVPLFARSLSEDCE-VGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGPRNCI 468
Cdd:cd20678  310 RLYPPVPGISRELSKPVTfPDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSSKRHSHAFLPFSAGPRNCI 389
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 187956757 469 GQKFAVMEEKTILACILRQFWVESNQKREELGLAGdLILRPNNGIWIK 516
Cdd:cd20678  390 GQQFAMNEMKVAVALTLLRFELLPDPTRIPIPIPQ-LVLKSKNGIHLY 436
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
88-515 6.48e-111

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: 335.32  E-value: 6.48e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENV-EVILTSSKQIDKSFLYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVM 166
Cdd:cd20620    2 DVVRLRLGPRRVYLVTHPDHIqHVLVTNARNYVKGGVYERLKLLLGNGLLTSEGDLWRRQRRLAQPAFHRRRIAAYADAM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 167 NEQANILVNKLEKH-------VNQEAfncffyiTLCALDIICETAMGKNIGAQSNNDSEYVRTVyrmSDMIYRRMKMPWL 239
Cdd:cd20620   82 VEATAALLDRWEAGarrgpvdVHAEM-------MRLTLRIVAKTLFGTDVEGEADEIGDALDVA---LEYAARRMLSPFL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 240 WFDLWYLvfKEGRDHKRGLKCLHTFTNNVIAERVKERKAEEDwtgagrgpipsknkrkaFLDLLLSVTDEE-GNRLSQED 318
Cdd:cd20620  152 LPLWLPT--PANRRFRRARRRLDEVIYRLIAERRAAPADGGD-----------------LLSMLLAARDEEtGEPMSDQQ 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 319 IREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRshRPVTLEDLKKLKYLDCVIKETLRVFPSVPLF 398
Cdd:cd20620  213 LRDEVMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLGG--RPPTAEDLPQLPYTEMVLQESLRLYPPAWII 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 399 ARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEK 478
Cdd:cd20620  291 GREAVEDDEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREAARPRYAYFPFGGGPRICIGNHFAMMEAV 370
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 187956757 479 TILACILRQFwvesnqkreELGLAGD--------LILRPNNGIWI 515
Cdd:cd20620  371 LLLATIAQRF---------RLRLVPGqpvepeplITLRPKNGVRM 406
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
84-516 7.28e-110

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: 333.97  E-value: 7.28e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  84 FRHlpIIKLWIGPV-PLVALYKAENVEVILTSSKQI---DKSFlYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTIL 159
Cdd:cd20679   11 YPQ--GCLWWLGPFyPIIRLFHPDYIRPVLLASAAVapkDELF-YGFLKPWLGDGLLLSSGDKWSRHRRLLTPAFHFNIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 160 ENFLDVMNEQANILVNKLEKHVNQEA--FNCFFYITLCALDIICETAMGKNIGAQSNNdSEYVRTVYRMSDMIYRRMKMP 237
Cdd:cd20679   88 KPYVKIFNQSTNIMHAKWRRLASEGSarLDMFEHISLMTLDSLQKCVFSFDSNCQEKP-SEYIAAILELSALVVKRQQQL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 238 WLWFDLWYLVFKEGRDHKRGLKCLHTFTNNVIAERVKE--RKAEEDWTGAGRgpipsKNKRKAFLDLLLSVTDEEGNRLS 315
Cdd:cd20679  167 LLHLDFLYYLTADGRRFRRACRLVHDFTDAVIQERRRTlpSQGVDDFLKAKA-----KSKTLDFIDVLLLSKDEDGKELS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 316 QEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVF-GRSHRPVTLEDLKKLKYLDCVIKETLRVFPS 394
Cdd:cd20679  242 DEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLkDREPEEIEWDDLAQLPFLTMCIKESLRLHPP 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 395 VPLFARSLSEDCEV-GGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFA 473
Cdd:cd20679  322 VTAISRCCTQDIVLpDGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGRSPLAFIPFSAGPRNCIGQTFA 401
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 187956757 474 VMEEKTILACILRQFWVESNQKreELGLAGDLILRPNNGIWIK 516
Cdd:cd20679  402 MAEMKVVLALTLLRFRVLPDDK--EPRRKPELILRAEGGLWLR 442
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
88-514 2.50e-100

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: 309.06  E-value: 2.50e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVILTSSKQIDKSFLYKFL-----QPWLGLGLLTSTG-SKWRTRRKMLTPTFHFTILEN 161
Cdd:cd20613   13 PVFVFWILHRPIVVVSDPEAVKEVLITLNLPKPPRVYSRLaflfgERFLGNGLVTEVDhEKWKKRRAILNPAFHRKYLKN 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 162 FLDVMNEQANILVNKLEK------HVN-QEAFNCFfyitlcALDIICETAMGKNIGAQSNNDSEYVRTVYRMSDMIYRRM 234
Cdd:cd20613   93 LMDEFNESADLLVEKLSKkadgktEVNmLDEFNRV------TLDVIAKVAFGMDLNSIEDPDSPFPKAISLVLEGIQESF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 235 KMPWLWFDLWYLVFKegRDHKRGLKCLHTFTNNVIAERVKERKAEEDwtgagrgpIPSknkrkaflDLL---LSVTDEEG 311
Cdd:cd20613  167 RNPLLKYNPSKRKYR--REVREAIKFLRETGRECIEERLEALKRGEE--------VPN--------DILthiLKASEEEP 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 312 NrLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGrSHRPVTLEDLKKLKYLDCVIKETLRV 391
Cdd:cd20613  229 D-FDMEELLDDFVTFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLG-SKQYVEYEDLGKLEYLSQVLKETLRL 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 392 FPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGPRNCIGQK 471
Cdd:cd20613  307 YPPVPGTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEAPEKIPSYAYFPFSLGPRSCIGQQ 386
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 187956757 472 FAVMEEKTILACILRQFWVE--SNQKREELGLagdLILRPNNGIW 514
Cdd:cd20613  387 FAQIEAKVILAKLLQNFKFElvPGQSFGILEE---VTLRPKDGVK 428
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
131-514 1.52e-99

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: 306.82  E-value: 1.52e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 131 LGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQANILVNKLEKHVNQ-EAFNCFFYITLCALDIICETAMGKNI 209
Cdd:cd11055   48 FDSSLLFLKGERWKRLRTTLSPTFSSGKLKLMVPIINDCCDELVEKLEKAAETgKPVDMKDLFQGFTLDVILSTAFGIDV 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 210 GAQSNNDSEYVRTVYR-MSDMIYRRMK----MPWLWFDLWYLVFKEGRDhkrglkcLHTFTNNVIAERVKERKAEEdwtg 284
Cdd:cd11055  128 DSQNNPDDPFLKAAKKiFRNSIIRLFLllllFPLRLFLFLLFPFVFGFK-------SFSFLEDVVKKIIEQRRKNK---- 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 285 agrgpipsKNKRKAFLDLLL----SVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELD 360
Cdd:cd11055  197 --------SSRRKDLLQLMLdaqdSDEDVSKKKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEID 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 361 EVFGRSHRPvTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFR 440
Cdd:cd11055  269 EVLPDDGSP-TYDTVSKLKYLDMVINETLRLYPPAFFISRECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFD 347
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187956757 441 PERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF-WVESNQKREELGLAGDLILRPNNGIW 514
Cdd:cd11055  348 PERFSPENKAKRHPYAYLPFGAGPRNCIGMRFALLEVKLALVKILQKFrFVPCKETEIPLKLVGGATLSPKNGIY 422
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
88-513 5.26e-89

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: 278.63  E-value: 5.26e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVILTSSKQIDKSFLYKFLQ--PWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDV 165
Cdd:cd00302    2 PVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPAlgDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRPV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 166 MNEQANILVNKLEKHVnQEAFNCFFYITLCALDIICETAMGKNIGAQsnndseyVRTVYRMSDMIYRRMKMPWLWFdLWY 245
Cdd:cd00302   82 IREIARELLDRLAAGG-EVGDDVADLAQPLALDVIARLLGGPDLGED-------LEELAELLEALLKLLGPRLLRP-LPS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 246 LVFKEGRDHKRGLkclhtftNNVIAERVKERKAEEDwtgagrgpipsknkrkAFLDLLLSVTDEEGNRLSQEDIREEVDT 325
Cdd:cd00302  153 PRLRRLRRARARL-------RDYLEELIARRRAEPA----------------DDLDLLLLADADDGGGLSDEEIVAELLT 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 326 FMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRShrpvTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSED 405
Cdd:cd00302  210 LLLAGHETTASLLAWALYLLARHPEVQERLRAEIDAVLGDG----TPEDLSKLPYLEAVVEETLRLYPPVPLLPRVATED 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 406 CEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSqgRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACIL 485
Cdd:cd00302  286 VELGGYTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPERE--EPRYAHLPFGAGPHRCLGARLARLELKLALATLL 363
                        410       420
                 ....*....|....*....|....*...
gi 187956757 486 RQFwvesnqkREELGLAGDLILRPNNGI 513
Cdd:cd00302  364 RRF-------DFELVPDEELEWRPSLGT 384
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
135-514 1.36e-86

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: 273.65  E-value: 1.36e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 135 LLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQANILVNKLEKHVNQ----EAFN-CFFYITlcalDIICETAMGKNI 209
Cdd:cd11056   53 LFSLDGEKWKELRQKLTPAFTSGKLKNMFPLMVEVGDELVDYLKKQAEKgkelEIKDlMARYTT----DVIASCAFGLDA 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 210 GAQSNNDSEYVRTVYRMSDMIYRRMKMPWLWFDLWYLVFKEGRdhKRGLKCLHTFTNNVIAERVKERKaeedwtgagrgp 289
Cdd:cd11056  129 NSLNDPENEFREMGRRLFEPSRLRGLKFMLLFFFPKLARLLRL--KFFPKEVEDFFRKLVRDTIEYRE------------ 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 290 iPSKNKRKAFLDLLL-------SVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEV 362
Cdd:cd11056  195 -KNNIVRNDFIDLLLelkkkgkIEDDKSEKELTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEV 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 363 FGRSHRPVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVT--KGTeAIIIP-YALHRDPRYFPDPEEF 439
Cdd:cd11056  274 LEKHGGELTYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGTDVVieKGT-PVIIPvYALHHDPKYYPEPEKF 352
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187956757 440 RPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQFWVE-SNQKREELGLAGD-LILRPNNGIW 514
Cdd:cd11056  353 DPERFSPENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEpSSKTKIPLKLSPKsFVLSPKGGIW 429
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
109-520 1.56e-86

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: 273.76  E-value: 1.56e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 109 EVILTSSKQIDKSFLYK-FLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQANILVNKLEKHVNQEA-- 185
Cdd:cd11069   26 HILVTNSYDFEKPPAFRrLLRRILGDGLLAAEGEEHKRQRKILNPAFSYRHVKELYPIFWSKAEELVDKLEEEIEESGde 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 186 ---FNCFFYITLCALDIICETAMGKNIGAQSNNDSEYvRTVYRM------SDMIYRRMKMPWLWFDLWYLVFKEGRDHKR 256
Cdd:cd11069  106 sisIDVLEWLSRATLDIIGLAGFGYDFDSLENPDNEL-AEAYRRlfeptlLGSLLFILLLFLPRWLVRILPWKANREIRR 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 257 GLKCLHTFTNNVIAERVKERKAEEDWTGagrgpipsknkrKAFLDLLLSVTDEEGN-RLSQEDIREEVDTFMFEGHDTTA 335
Cdd:cd11069  185 AKDVLRRLAREIIREKKAALLEGKDDSG------------KDILSILLRANDFADDeRLSDEELIDQILTFLAAGHETTS 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 336 AAINWSLYLLGTNPEVQRKVDQELDEVF-GRSHRPVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVT 414
Cdd:cd11069  253 TALTWALYLLAKHPDVQERLREEIRAALpDPPDGDLSYDDLDRLPYLNAVCRETLRLYPPVPLTSREATKDTVIKGVPIP 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 415 KGTEAIIIPYALHRDPR-YFPDPEEFRPERFF-----PENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd11069  333 KGTVVLIPPAAINRSPEiWGPDAEEFNPERWLepdgaASPGGAGSNYALLTFLHGPRSCIGKKFALAEMKVLLAALVSRF 412
                        410       420       430
                 ....*....|....*....|....*....|..
gi 187956757 489 WVESNQKREelglagdlILRPNNGIWIKLKRR 520
Cdd:cd11069  413 EFELDPDAE--------VERPIGIITRPPVDG 436
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
84-514 3.25e-84

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: 267.69  E-value: 3.25e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  84 FRHLPIIKLWIGPVPLVALYKAENVEVILTSS--KQIDKSFLYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILEN 161
Cdd:cd11046    8 LEYGPIYKLAFGPKSFLVISDPAIAKHVLRSNafSYDKKGLLAEILEPIMGKGLIPADGEIWKKRRRALVPALHKDYLEM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 162 FLDVMNEQANILVNKLEK------HVNQEAFNCFFyitlcALDIICETAMGKNIGAQSNnDSEYVRTVYR-MSDMIYRRM 234
Cdd:cd11046   88 MVRVFGRCSERLMEKLDAaaetgeSVDMEEEFSSL-----TLDIIGLAVFNYDFGSVTE-ESPVIKAVYLpLVEAEHRSV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 235 KMPWLW-FDLWYLVFKEGRDHKRGLKCLHTFTNNVIAERvKERKAEEDWTGAGRgpiPSKNKRKAflDLLLSVTDEEGNR 313
Cdd:cd11046  162 WEPPYWdIPAALFIVPRQRKFLRDLKLLNDTLDDLIRKR-KEMRQEEDIELQQE---DYLNEDDP--SLLRFLVDMRDED 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 314 LSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPvTLEDLKKLKYLDCVIKETLRVFP 393
Cdd:cd11046  236 VDSKQLRDDLMTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPP-TYEDLKKLKYTRRVLNESLRLYP 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 394 SVPLFAR-SLSED-CEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRH----PYAYVPFSAGPRNC 467
Cdd:cd11046  315 QPPVLIRrAVEDDkLPGGGVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPNevidDFAFLPFGGGPRKC 394
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 187956757 468 IGQKFAVMEEKTILACILRQFWVESNQKREELGLAGDLILRPNNGIW 514
Cdd:cd11046  395 LGDQFALLEATVALAMLLRRFDFELDVGPRHVGMTTGATIHTKNGLK 441
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
88-511 6.78e-79

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: 253.60  E-value: 6.78e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVILTSSKQIDKSFLykfLQPW--------LGLGLLTSTGSKWRTRRK-----MLTPTf 154
Cdd:cd11054    6 PIVREKLGGRDIVHLFDPDDIEKVFRNEGKYPIRPS---LEPLekyrkkrgKPLGLLNSNGEEWHRLRSavqkpLLRPK- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 155 hftILENFLDVMNEQANILVNKLEKHVNQEAF---NCFFYITLCALDIICETAMGKNIGAQSNNDS----EYVRTVYRMS 227
Cdd:cd11054   82 ---SVASYLPAINEVADDFVERIRRLRDEDGEevpDLEDELYKWSLESIGTVLFGKRLGCLDDNPDsdaqKLIEAVKDIF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 228 DMIYRRMKMPWLWfdlWYLVFKEGRDHKRGLKCLHTFTNNVIAERVKERKAEEDwtgagrgpipSKNKRKAFLDLLLSVt 307
Cdd:cd11054  159 ESSAKLMFGPPLW---KYFPTPAWKKFVKAWDTIFDIASKYVDEALEELKKKDE----------EDEEEDSLLEYLLSK- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 308 deegNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHrPVTLEDLKKLKYLDCVIKE 387
Cdd:cd11054  225 ----PGLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGE-PITAEDLKKMPYLKACIKE 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 388 TLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGR--HPYAYVPFSAGPR 465
Cdd:cd11054  300 SLRLYPVAPGNGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDDSENKniHPFASLPFGFGPR 379
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 187956757 466 NCIGQKFAVMEEKTILACILRQFWVESNQkrEELGLAGDLILRPNN 511
Cdd:cd11054  380 MCIGRRFAELEMYLLLAKLLQNFKVEYHH--EELKVKTRLILVPDK 423
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
86-488 1.29e-74

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: 242.16  E-value: 1.29e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  86 HLPIIKLWIGPVPLVALYKAENVEVILTSSKQIDKS-FLYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLD 164
Cdd:cd11049   12 HGDLVRIRLGPRPAYVVTSPELVRQVLVNDRVFDKGgPLFDRARPLLGNGLATCPGEDHRRQRRLMQPAFHRSRIPAYAE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 165 VMNEQANILVNKLEKHVNQEAFNCFFYITLcalDIICETAMGKNIGAQSNndSEYVRTVYRMSDMIYRRMKMPwLWFDLw 244
Cdd:cd11049   92 VMREEAEALAGSWRPGRVVDVDAEMHRLTL---RVVARTLFSTDLGPEAA--AELRQALPVVLAGMLRRAVPP-KFLER- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 245 yLVFKEGRDHKRGLKCLHTFTNNVIAERvkeRKAEEDwtgagrgpipsknkRKAFLDLLLSVTDEEGNRLSQEDIREEVD 324
Cdd:cd11049  165 -LPTPGNRRFDRALARLRELVDEIIAEY---RASGTD--------------RDDLLSLLLAARDEEGRPLSDEELRDQVI 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 325 TFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGrsHRPVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSE 404
Cdd:cd11049  227 TLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLG--GRPATFEDLPRLTYTRRVVTEALRLYPPVWLLTRRTTA 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 405 DCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACI 484
Cdd:cd11049  305 DVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVPRGAFIPFGAGARKCIGDTFALTELTLALATI 384

                 ....
gi 187956757 485 LRQF 488
Cdd:cd11049  385 ASRW 388
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
85-517 5.13e-74

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: 240.56  E-value: 5.13e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  85 RHLPIIKLWIGPV-PLVALYKAENVEVILTSSKQI-DKSFLYKFLQPWLG-LGLLTSTGSKWRTRRKMLTPTFHFTILEN 161
Cdd:cd11053   10 RYGDVFTLRVPGLgPVVVLSDPEAIKQIFTADPDVlHPGEGNSLLEPLLGpNSLLLLDGDRHRRRRKLLMPAFHGERLRA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 162 FLDVMNEQANILVNKLEK----HVNQEAFNcffyITLcalDIICETAMGKNIGAQSNndsEYVRTVYRMSDMIYRRMKM- 236
Cdd:cd11053   90 YGELIAEITEREIDRWPPgqpfDLRELMQE----ITL---EVILRVVFGVDDGERLQ---ELRRLLPRLLDLLSSPLASf 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 237 PWLWFDL-----WylvfkegRDHKRGLKCLhtftNNVIAERVKERKAEEDwtgAGRGPIpsknkrkafLDLLLSVTDEEG 311
Cdd:cd11053  160 PALQRDLgpwspW-------GRFLRARRRI----DALIYAEIAERRAEPD---AERDDI---------LSLLLSARDEDG 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 312 NRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRshrpVTLEDLKKLKYLDCVIKETLRV 391
Cdd:cd11053  217 QPLSDEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGD----PDPEDIAKLPYLDAVIKETLRL 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 392 FPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPensQGRHPYAYVPFSAGPRNCIGQK 471
Cdd:cd11053  293 YPVAPLVPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLG---RKPSPYEYLPFGGGVRRCIGAA 369
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 187956757 472 FAVMEEKTILACILRQFWVE-SNQKREELGLAGdLILRPNNGIWIKL 517
Cdd:cd11053  370 FALLEMKVVLATLLRRFRLElTDPRPERPVRRG-VTLAPSRGVRMVV 415
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
88-511 2.30e-72

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: 236.34  E-value: 2.30e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENV-EVILTSSKQ-IDKSFLYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTF----HFTILEn 161
Cdd:cd20617    2 GIFTLWLGDVPTVVLSDPEIIkEAFVKNGDNfSDRPLLPSFEIISGGKGILFSNGDYWKELRRFALSSLtktkLKKKME- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 162 flDVMNEQANILVNKLEKHVNQ-EAFNCFFYITLCALDIICETAMGKNIgaqSNNDSEYVRTVYRMSDMIYRRMKMPWLW 240
Cdd:cd20617   81 --ELIEEEVNKLIESLKKHSKSgEPFDPRPYFKKFVLNIINQFLFGKRF---PDEDDGEFLKLVKPIEEIFKELGSGNPS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 241 FDLWYLVFKegrdHKRGLKCLHTFTNNV---IAERVKERKAEEDwtgagrgpiPSKNKRKAFLDLLLSVTDEEGNRLSQE 317
Cdd:cd20617  156 DFIPILLPF----YFLYLKKLKKSYDKIkdfIEKIIEEHLKTID---------PNNPRDLIDDELLLLLKEGDSGLFDDD 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 318 DIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRShRPVTLEDLKKLKYLDCVIKETLRVFPSVPL 397
Cdd:cd20617  223 SIISTCLDLFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGND-RRVTLSDRSKLPYLNAVIKEVLRLRPILPL 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 398 -FARSLSEDCEVGGYKVTKGTeaIIIP--YALHRDPRYFPDPEEFRPERFFpENSQGRHPYAYVPFSAGPRNCIGQKFAV 474
Cdd:cd20617  302 gLPRVTTEDTEIGGYFIPKGT--QIIIniYSLHRDEKYFEDPEEFNPERFL-ENDGNKLSEQFIPFGIGKRNCVGENLAR 378
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 187956757 475 MEEKTILACILRQFWVES-NQKREELGLAGDLILRPNN 511
Cdd:cd20617  379 DELFLFFANLLLNFKFKSsDGLPIDEKEVFGLTLKPKP 416
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
94-517 1.53e-70

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: 231.76  E-value: 1.53e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  94 IGPVPLVALYKAENVEVILTSSKQIDKSFLYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQANIL 173
Cdd:cd20621   10 LGSKPLISLVDPEYIKEFLQNHHYYKKKFGPLGIDRLFGKGLLFSEGEEWKKQRKLLSNSFHFEKLKSRLPMINEITKEK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 174 VNKLEKhVNQEAFNCFFYITLcalDIICETAMGKNIGAQSNND-SEYVRTVYRMSDMIYRRMKMP-----WLWFDLWYLV 247
Cdd:cd20621   90 IKKLDN-QNVNIIQFLQKITG---EVVIRSFFGEEAKDLKINGkEIQVELVEILIESFLYRFSSPyfqlkRLIFGRKSWK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 248 F---KEGRDHKRGLKCLHTFTNNVIAERVKERKAEEDwtgagrgpipSKNKRKAFLDLLLSVTDEEGNRLSQEDIREEVD 324
Cdd:cd20621  166 LfptKKEKKLQKRVKELRQFIEKIIQNRIKQIKKNKD----------EIKDIIIDLDLYLLQKKKLEQEITKEEIIQQFI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 325 TFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGrSHRPVTLEDLKKLKYLDCVIKETLRVFPSVP-LFARSLS 403
Cdd:cd20621  236 TFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVG-NDDDITFEDLQKLNYLNAFIKEVLRLYNPAPfLFPRVAT 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 404 EDCEVGGYKVTKGTeaIIIPYAL--HRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTIL 481
Cdd:cd20621  315 QDHQIGDLKIKKGW--IVNVGYIynHFNPKYFENPDEFNPERWLNQNNIEDNPFVFIPFSAGPRNCIGQHLALMEAKIIL 392
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 187956757 482 ACILRQFWVEsNQKREELGLAGDLILRPNNGIWIKL 517
Cdd:cd20621  393 IYILKNFEIE-IIPNPKLKLIFKLLYEPVNDLLLKL 427
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
93-491 2.67e-65

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: 218.23  E-value: 2.67e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  93 WIGPVP----LVALYKAENVEVILtsSKQID-----KSFLYKFlQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFL 163
Cdd:cd11064    3 FRGPWPggpdGIVTADPANVEHIL--KTNFDnypkgPEFRDLF-FDLLGDGIFNVDGELWKFQRKTASHEFSSRALREFM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 164 -DVMNEQANILVNKLEKHVNQE--AFNCFFYITLCALDIICETAMGKNIG--AQSNNDSEYVRTVYRMSDMIYRRMKMP- 237
Cdd:cd11064   80 eSVVREKVEKLLVPLLDHAAESgkVVDLQDVLQRFTFDVICKIAFGVDPGslSPSLPEVPFAKAFDDASEAVAKRFIVPp 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 238 WLW-FDLWYLVFKEgRDHKRGLKCLHTFTNNVIAERVKERKAEEdwtgagrgpiPSKNKRKAFLDLLLSVTDEEGNRLSQ 316
Cdd:cd11064  160 WLWkLKRWLNIGSE-KKLREAIRVIDDFVYEVISRRREELNSRE----------EENNVREDLLSRFLASEEEEGEPVSD 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 317 EDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEV----FGRSHRPVTLEDLKKLKYLDCVIKETLRVF 392
Cdd:cd11064  229 KFLRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKlpklTTDESRVPTYEELKKLVYLHAALSESLRLY 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 393 PSVPLFARS-LSEDCEVGGYKVTKGTEAIIIPYALHRDPRYF-PDPEEFRPERFFPENSQGRH--PYAYVPFSAGPRNCI 468
Cdd:cd11064  309 PPVPFDSKEaVNDDVLPDGTFVKKGTRIVYSIYAMGRMESIWgEDALEFKPERWLDEDGGLRPesPYKFPAFNAGPRICL 388
                        410       420
                 ....*....|....*....|...
gi 187956757 469 GQKFAVMEEKTILACILRQFWVE 491
Cdd:cd11064  389 GKDLAYLQMKIVAAAILRRFDFK 411
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
93-488 6.45e-65

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: 216.82  E-value: 6.45e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  93 WIGPVPLVALYKAENVEVILT-SSKQIDKSFLYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQAN 171
Cdd:cd11052   18 WYGTDPRLYVTEPELIKELLSkKEGYFGKSPLQPGLKKLLGRGLVMSNGEKWAKHRRIANPAFHGEKLKGMVPAMVESVS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 172 ILVNKLEKHVNQEA--FNCFFYITLCALDIICETAMGKNIgaqsNNDSEYVRTVYRMSDMIYRRMKMpwLWFDLWYlvFK 249
Cdd:cd11052   98 DMLERWKKQMGEEGeeVDVFEEFKALTADIISRTAFGSSY----EEGKEVFKLLRELQKICAQANRD--VGIPGSR--FL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 250 EGRDHKRGLKCLHTFT---NNVIAERVKERKAEEdwtgagrgpipSKNKRKAFLDLLLSV--TDEEGNRLSQEDIREEVD 324
Cdd:cd11052  170 PTKGNKKIKKLDKEIEdslLEIIKKREDSLKMGR-----------GDDYGDDLLGLLLEAnqSDDQNKNMTVQEIVDECK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 325 TFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVtlEDLKKLKYLDCVIKETLRVFPSVPLFARSLSE 404
Cdd:cd11052  239 TFFFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDKPPS--DSLSKLKTVSMVINESLRLYPPAVFLTRKAKE 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 405 DCEVGGYKVTKGTEAIIIPYALHRDPRYF-PDPEEFRPERFFPENSQGR-HPYAYVPFSAGPRNCIGQKFAVMEEKTILA 482
Cdd:cd11052  317 DIKLGGLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFADGVAKAAkHPMAFLPFGLGPRNCIGQNFATMEAKIVLA 396

                 ....*.
gi 187956757 483 CILRQF 488
Cdd:cd11052  397 MILQRF 402
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
106-515 2.13e-64

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: 215.50  E-value: 2.13e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 106 ENVEVIL-TSSKQIDKSFLYKF-LQPWLGLGLLTSTGSKWRTRRKMLTPTF---HFTILENFldvmneqanilvnklEKH 180
Cdd:cd11063   21 ENIKAVLaTQFKDFGLGERRRDaFKPLLGDGIFTSDGEEWKHSRALLRPQFsrdQISDLELF---------------ERH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 181 VnQEAFNC-------------FFYITLcalDIICETAMGKNIGAQSNNDS-----EYVRTVYRMSDMIYRRMKMPWLWFD 242
Cdd:cd11063   86 V-QNLIKLlprdgstvdlqdlFFRLTL---DSATEFLFGESVDSLKPGGDsppaaRFAEAFDYAQKYLAKRLRLGKLLWL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 243 LWylvfkeGRDHKRGLKCLHTFTNNVIAERVKERKAEEDwtgagrgpiPSKNKRKAFLDLLLSVTDEEgnrlsqEDIREE 322
Cdd:cd11063  162 LR------DKKFREACKVVHRFVDPYVDKALARKEESKD---------EESSDRYVFLDELAKETRDP------KELRDQ 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 323 VDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPvTLEDLKKLKYLDCVIKETLRVFPSVPLFARSL 402
Cdd:cd11063  221 LLNILLAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTP-TYEDLKNMKYLRAVINETLRLYPPVPLNSRVA 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 403 SEDC--EVGGYK-------VTKGTEAIIIPYALHRDPR-YFPDPEEFRPERFFPEnsqGRHPYAYVPFSAGPRNCIGQKF 472
Cdd:cd11063  300 VRDTtlPRGGGPdgkspifVPKGTRVLYSVYAMHRRKDiWGPDAEEFRPERWEDL---KRPGWEYLPFNGGPRICLGQQF 376
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 187956757 473 AVMEEKTILACILRQF-WVESNQKR---EELGLAgdliLRPNNGIWI 515
Cdd:cd11063  377 ALTEASYVLVRLLQTFdRIESRDVRppeERLTLT----LSNANGVKV 419
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
98-494 3.61e-64

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: 214.84  E-value: 3.61e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  98 PLVALYKAENVEVILTSSKQIDKSFLYKFLQPWLG-LGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQANILVNK 176
Cdd:cd11044   33 PTVFVIGAEAVRFILSGEGKLVRYGWPRSVRRLLGeNSLSLQDGEEHRRRRKLLAPAFSREALESYVPTIQAIVQSYLRK 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 177 LEKHvnqEAFNCFFYITLCALDIICETAMGKNIGAQSNNDSEYvrtvyrMSDMIYRRMKMPWlwfDL-WYLVFKEGRDHK 255
Cdd:cd11044  113 WLKA---GEVALYPELRRLTFDVAARLLLGLDPEVEAEALSQD------FETWTDGLFSLPV---PLpFTPFGRAIRARN 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 256 RglkcLHTFTNNVIAERVKERKAEEdwTGAgrgpipsknkrkafLDLLLSVTDEEGNRLSQEDIREEVDTFMFEGHDTTA 335
Cdd:cd11044  181 K----LLARLEQAIRERQEEENAEA--KDA--------------LGLLLEAKDEDGEPLSMDELKDQALLLLFAGHETTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 336 AAINWSLYLLGTNPEVQRKVDQELDEVfgRSHRPVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTK 415
Cdd:cd11044  241 SALTSLCFELAQHPDVLEKLRQEQDAL--GLEEPLTLESLKKMPYLDQVIKEVLRLVPPVGGGFRKVLEDFELGGYQIPK 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 416 GTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQG-RHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF-W-VES 492
Cdd:cd11044  319 GWLVYYSIRDTHRDPELYPDPERFDPERFSPARSEDkKKPFSLIPFGGGPRECLGKEFAQLEMKILASELLRNYdWeLLP 398

                 ..
gi 187956757 493 NQ 494
Cdd:cd11044  399 NQ 400
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
92-513 1.06e-63

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: 212.88  E-value: 1.06e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  92 LWigPV--PLVALYKAENVEVILTSSKQIDKSFLYKFLQPWLG-LGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNE 168
Cdd:cd11051    5 LW--PFapPLLVVTDPELAEQITQVTNLPKPPPLRKFLTPLTGgSSLISMEGEEWKRLRKRFNPGFSPQHLMTLVPTILD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 169 QANILVNKLEKHV-NQEAFNCFFYITLCALDIICETAMGKNIGAQS--NNDSEYVRT---VYRMSDMIYRRMkMPWLWFD 242
Cdd:cd11051   83 EVEIFAAILRELAeSGEVFSLEELTTNLTFDVIGRVTLDIDLHAQTgdNSLLTALRLllaLYRSLLNPFKRL-NPLRPLR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 243 LWYLVfkegrdhkRGLkclhtftNNVIAERVKERkaeedwtgagrgpipsknkrkafldlllsvtdeegnrLSQEDIREE 322
Cdd:cd11051  162 RWRNG--------RRL-------DRYLKPEVRKR-------------------------------------FELERAIDQ 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 323 VDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVTL------EDLKKLKYLDCVIKETLRVFPsVP 396
Cdd:cd11051  190 IKTFLFAGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGPDPSAAAEllregpELLNQLPYTTAVIKETLRLFP-PA 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 397 LFARSLSEDCEV----GGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHP--YAYVPFSAGPRNCIGQ 470
Cdd:cd11051  269 GTARRGPPGVGLtdrdGKEYPTDGCIVYVCHHAIHRDPEYWPRPDEFIPERWLVDEGHELYPpkSAWRPFERGPRNCIGQ 348
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 187956757 471 KFAVMEEKTILACILRQF--------WVESNQ--KREELGLAGDLILRPNNGI 513
Cdd:cd11051  349 ELAMLELKIILAMTVRRFdfekaydeWDAKGGykGLKELFVTGQGTAHPVDGM 401
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
127-520 2.26e-63

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: 212.82  E-value: 2.26e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 127 LQPWLGLGLLTSTGS--KWRTRRKMLTPTFHFTILENFLDVMNEQANILVNKLEKHVNQEAFNCFFYITLCALDIICETA 204
Cdd:cd11068   54 LRDFAGDGLFTAYTHepNWGKAHRILMPAFGPLAMRGYFPMMLDIAEQLVLKWERLGPDEPIDVPDDMTRLTLDTIALCG 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 205 MGKNIGAQSNNDS-----EYVRTvyrMSDMIYRRMKMPWLWFdlwyLVFKEGRDHKRGLKCLHTFTNNVIAERVKerkae 279
Cdd:cd11068  134 FGYRFNSFYRDEPhpfveAMVRA---LTEAGRRANRPPILNK----LRRRAKRQFREDIALMRDLVDEIIAERRA----- 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 280 edwtgagrGPIPSKNKrkaFLDLLLSVTDEE-GNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQE 358
Cdd:cd11068  202 --------NPDGSPDD---LLNLMLNGKDPEtGEKLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAE 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 359 LDEVFGRshRPVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGG-YKVTKGTEAIIIPYALHRDPR-YFPDP 436
Cdd:cd11068  271 VDEVLGD--DPPPYEQVAKLRYIRRVLDETLRLWPTAPAFARKPKEDTVLGGkYPLKKGDPVLVLLPALHRDPSvWGEDA 348
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 437 EEFRPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQFWVESNQkREELGLAGDLILRPnNGIWIK 516
Cdd:cd11068  349 EEFRPERFLPEEFRKLPPNAWKPFGNGQRACIGRQFALQEATLVLAMLLQRFDFEDDP-DYELDIKETLTLKP-DGFRLK 426

                 ....
gi 187956757 517 LKRR 520
Cdd:cd11068  427 ARPR 430
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
79-515 1.27e-62

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: 210.13  E-value: 1.27e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  79 YYTEEFRHLPIIKLWIGPVPLVALYKAENVEVILTSSKQIDKS-FLYKFLQP--WLGLGLLTSTGSKWRTRRKMLTPTFH 155
Cdd:COG2124   24 FYARLREYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDgGLPEVLRPlpLLGDSLLTLDGPEHTRLRRLVQPAFT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 156 FTILENFLDVMNEQANILVNKLEKHVNQEAFNCFFYITLcalDIICETAMGknigaqsnNDSEYVRTVYRMSDMIYRRMk 235
Cdd:COG2124  104 PRRVAALRPRIREIADELLDRLAARGPVDLVEEFARPLP---VIVICELLG--------VPEEDRDRLRRWSDALLDAL- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 236 MPWLWfdlwylvfKEGRDHKRGLKCLHTFTNNVIAERvkERKAEEDwtgagrgpipsknkrkaFLDLLLSVTDEeGNRLS 315
Cdd:COG2124  172 GPLPP--------ERRRRARRARAELDAYLRELIAER--RAEPGDD-----------------LLSALLAARDD-GERLS 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 316 QEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDevfgrshrpvtledlkklkYLDCVIKETLRVFPSV 395
Cdd:COG2124  224 DEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAEPE-------------------LLPAAVEETLRLYPPV 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 396 PLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPErffpensqgRHPYAYVPFSAGPRNCIGQKFAVM 475
Cdd:COG2124  285 PLLPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPD---------RPPNAHLPFGGGPHRCLGAALARL 355
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 187956757 476 EEKTILACILRQFwvesnqkrEELGLAGDLILRPNNGIWI 515
Cdd:COG2124  356 EARIALATLLRRF--------PDLRLAPPEELRWRPSLTL 387
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
87-509 1.57e-61

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: 208.34  E-value: 1.57e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  87 LPIIKLWIGPVPLVALYKAENVEVILTSSKQIDKS-FLYKFLQPwLGLGLLTSTGSKWRTRRKMLTPTF-HFTILENFLD 164
Cdd:cd11070    2 LGAVKILFVSRWNILVTKPEYLTQIFRRRDDFPKPgNQYKIPAF-YGPNVISSEGEDWKRYRKIVAPAFnERNNALVWEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 165 VMnEQANILVnKLEKHVNQEAFNCFF----YITLCALDIICETAMGKNIGAQSNNDSEYVRTVYRMSDMI--YRRMKMPW 238
Cdd:cd11070   81 SI-RQAQRLI-RYLLEEQPSAKGGGVdvrdLLQRLALNVIGEVGFGFDLPALDEEESSLHDTLNAIKLAIfpPLFLNFPF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 239 LWFdLWYLVFKegrDHKRGLKCLHTFTNNVIAERVKERKAEedwtgagrgpipSKNKRKAFLDLLLSVTDEEGN-RLSQE 317
Cdd:cd11070  159 LDR-LPWVLFP---SRKRAFKDVDEFLSELLDEVEAELSAD------------SKGKQGTESVVASRLKRARRSgGLTEK 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 318 DIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPV-TLEDLKKLKYLDCVIKETLRVFPSVP 396
Cdd:cd11070  223 ELLGNLFIFFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDWdYEEDFPKLPYLLAVIYETLRLYPPVQ 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 397 LFARSLSEDCEV-----GGYKVTKGTEAIIIPYALHRDP-RYFPDPEEFRPERFFPENSQGRHPY-------AYVPFSAG 463
Cdd:cd11070  303 LLNRKTTEPVVVitglgQEIVIPKGTYVGYNAYATHRDPtIWGPDADEFDPERWGSTSGEIGAATrftpargAFIPFSAG 382
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 187956757 464 PRNCIGQKFAVMEEKTILACILRQF-WVESNQKREELGLAGDLILRP 509
Cdd:cd11070  383 PRACLGRKFALVEFVAALAELFRQYeWRVDPEWEEGETPAGATRDSP 429
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
135-514 4.47e-59

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: 202.38  E-value: 4.47e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 135 LLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQANILVNKLEKHVN-------QEAFNCFfyitlcALDIICETAMGK 207
Cdd:cd20649   52 LLCLRDERWKRVRSILTPAFSAAKMKEMVPLINQACDVLLRNLKSYAEsgnafniQRCYGCF------TMDVVASVAFGT 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 208 NIGAQSNNDSEYVRTVYRMSDMIYRR------MKMPWLWFDLWYLVFKEGRDHkrglkcLHTFTNNVIAERVKERKAEed 281
Cdd:cd20649  126 QVDSQKNPDDPFVKNCKRFFEFSFFRpililfLAFPFIMIPLARILPNKSRDE------LNSFFTQCIRNMIAFRDQQ-- 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 282 wtgagrgpiPSKNKRKAFLDLLLSVTDEEG------------------------------------NRLSQEDIREEVDT 325
Cdd:cd20649  198 ---------SPEERRRDFLQLMLDARTSAKflsvehfdivndadesaydghpnspaneqtkpskqkRMLTEDEIVGQAFI 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 326 FMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEvFGRSHRPVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSED 405
Cdd:cd20649  269 FLIAGYETTTNTLSFATYLLATHPECQKKLLREVDE-FFSKHEMVDYANVQELPYLDMVIAETLRMYPPAFRFAREAAED 347
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 406 CEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACIL 485
Cdd:cd20649  348 CVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQRRHPFVYLPFGAGPRSCIGMRLALLEIKVTLLHIL 427
                        410       420       430
                 ....*....|....*....|....*....|
gi 187956757 486 RQFWVESNQKRE-ELGLAGDLILRPNNGIW 514
Cdd:cd20649  428 RRFRFQACPETEiPLQLKSKSTLGPKNGVY 457
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
108-488 1.18e-58

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: 200.14  E-value: 1.18e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 108 VEVILTSSKQIDKSFLYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQANILVNKLEKHVNQE--- 184
Cdd:cd11061   19 LKDIYGHGSNCLKGPFYDALSPSASLTFTTRDKAEHARRRRVWSHAFSDKALRGYEPRILSHVEQLCEQLDDRAGKPvsw 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 185 AFNCFFYITLCALDIICETAMGKNIGAQSNNDSEYV-----RTVYRMSDMIYrrmkMPWLWFDLWYLVFkeGRDHKRGLK 259
Cdd:cd11061   99 PVDMSDWFNYLSFDVMGDLAFGKSFGMLESGKDRYIldlleKSMVRLGVLGH----APWLRPLLLDLPL--FPGATKARK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 260 CLHTFtnnvIAERVKERKAEEdwtgagrgpipsKNKRKAFLDLLLSVTDEE-GNRLSQEDIREEVDTFMFEGHDTTAAAI 338
Cdd:cd11061  173 RFLDF----VRAQLKERLKAE------------EEKRPDIFSYLLEAKDPEtGEGLDLEELVGEARLLIVAGSDTTATAL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 339 NWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVTLEDLKKLKYLDCVIKETLRVFPSVP--LFARSLSEDCEVGGYKVTKG 416
Cdd:cd11061  237 SAIFYYLARNPEAYEKLRAELDSTFPSDDEIRLGPKLKSLPYLRACIDEALRLSPPVPsgLPRETPPGGLTIDGEYIPGG 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187956757 417 TEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQ-GRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd11061  317 TTVSVPIYSIHRDERYFPDPFEFIPERWLSRPEElVRARSAFIPFSIGPRGCIGKNLAYMELRLVLARLLHRY 389
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
88-469 1.59e-57

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: 197.39  E-value: 1.59e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVILTSSKQID---------KSFLYKFLQpwlglGLLTSTGSKWRTRRKMLTpTFHFTI 158
Cdd:cd20618    2 PLMYLRLGSVPTVVVSSPEMAKEVLKTQDAVFasrprtaagKIFSYNGQD-----IVFAPYGPHWRHLRKICT-LELFSA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 159 --LENFLDVMNEQANILVNKL-EKHVNQEAFNCFFYITLCALDIICETAMGKNIGAQSNNDSEYVRTVYRMSDMIYRRMK 235
Cdd:cd20618   76 krLESFQGVRKEELSHLVKSLlEESESGKPVNLREHLSDLTLNNITRMLFGKRYFGESEKESEEAREFKELIDEAFELAG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 236 -------MPWL-WFDLWYLVFKEGRDHKRglkcLHTFTNNVIAERVKERKaeedwtgagrgpiPSKNKRKAFLDLLLSVT 307
Cdd:cd20618  156 afnigdyIPWLrWLDLQGYEKRMKKLHAK----LDRFLQKIIEEHREKRG-------------ESKKGGDDDDDLLLLLD 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 308 DEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRShRPVTLEDLKKLKYLDCVIKE 387
Cdd:cd20618  219 LDGEGKLSDDNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRE-RLVEESDLPKLPYLQAVVKE 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 388 TLRVFPSVPL-FARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENS---QGRHpYAYVPFSAG 463
Cdd:cd20618  298 TLRLHPPGPLlLPHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIddvKGQD-FELLPFGSG 376

                 ....*.
gi 187956757 464 PRNCIG 469
Cdd:cd20618  377 RRMCPG 382
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
119-492 3.75e-57

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: 196.37  E-value: 3.75e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 119 DKSFLYKFLQPWLGLGLLTSTGSK-WRTRRKMLTPTFH--FTILENFLDVMNEQANILVNKLEKH-VNQEAFNCFFYITL 194
Cdd:cd11059   30 TKSYWYFTLRGGGGPNLFSTLDPKeHSARRRLLSGVYSksSLLRAAMEPIIRERVLPLIDRIAKEaGKSGSVDVYPLFTA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 195 CALDIICETAMGKNIGAQSNNDSEYvrtvyRMSDMIYRRMKMPWLWfdLWYLVFKEGRDHKRGLKCLHTFTNNVIAERVK 274
Cdd:cd11059  110 LAMDVVSHLLFGESFGTLLLGDKDS-----RERELLRRLLASLAPW--LRWLPRYLPLATSRLIIGIYFRAFDEIEEWAL 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 275 ER--KAEEDwtgagrgpIPSKNKRKAFLDLLLSVTDEEGNR-LSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEV 351
Cdd:cd11059  183 DLcaRAESS--------LAESSDSESLTVLLLEKLKGLKKQgLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNL 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 352 QRKVDQELDEVFGRSHRPVTLEDLKKLKYLDCVIKETLRVFPSVPL-FARSLSEDCEV-GGYKVTKGTEAIIIPYALHRD 429
Cdd:cd11059  255 QEKLREELAGLPGPFRGPPDLEDLDKLPYLNAVIRETLRLYPPIPGsLPRVVPEGGATiGGYYIPGGTIVSTQAYSLHRD 334
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187956757 430 PRYFPDPEEFRPERFFPENSQGRHPY--AYVPFSAGPRNCIGQKFAVMEEKTILACILRQFWVES 492
Cdd:cd11059  335 PEVFPDPEEFDPERWLDPSGETAREMkrAFWPFGSGSRMCIGMNLALMEMKLALAAIYRNYRTST 399
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
142-488 1.15e-55

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: 192.63  E-value: 1.15e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 142 KWRTRRKMLTPTFHFTILENFLDVMNEQANILVNKLEKHVN-------QEAFNCFfyitlcALDIICETAMGKNIGAQSN 214
Cdd:cd20650   59 EWKRIRSLLSPTFTSGKLKEMFPIIAQYGDVLVKNLRKEAEkgkpvtlKDVFGAY------SMDVITSTSFGVNIDSLNN 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 215 NDSEYVRTVYRMsdmiyrrmkmpwLWFD------LWYLVFKEGRDHKRGLKcLHTFTNNVIA------ERVKERKAEEDW 282
Cdd:cd20650  133 PQDPFVENTKKL------------LKFDfldplfLSITVFPFLTPILEKLN-ISVFPKDVTNffyksvKKIKESRLDSTQ 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 283 TGagrgpipsknkRKAFLDLLL-SVTDEEGNR---LSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQE 358
Cdd:cd20650  200 KH-----------RVDFLQLMIdSQNSKETEShkaLSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEE 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 359 LDEVFgRSHRPVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEE 438
Cdd:cd20650  269 IDAVL-PNKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKDVEINGVFIPKGTVVMIPTYALHRDPQYWPEPEE 347
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 187956757 439 FRPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd20650  348 FRPERFSKKNKDNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNF 397
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
140-488 3.31e-55

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: 191.27  E-value: 3.31e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 140 GSKWRTRRKMLTPTFH--FTILENFLDVMNEQANILVNKLEKHVNQeAFNCFFYITLCALDIICETAMGKNIgaqSNNDS 217
Cdd:cd11027   59 SPTWKLHRKLAHSALRlyASGGPRLEEKIAEEAEKLLKRLASQEGQ-PFDPKDELFLAVLNVICSITFGKRY---KLDDP 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 218 EYVRTVYrMSDMIYRRMKM-------PWLWfdlwYLVFKEGRDHKRGLKCLhtftNNVIAERVKERKAEEDwtgagrgpi 290
Cdd:cd11027  135 EFLRLLD-LNDKFFELLGAgslldifPFLK----YFPNKALRELKELMKER----DEILRKKLEEHKETFD--------- 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 291 pSKNKRKaFLDLLLSVTDEEGNR-------LSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVF 363
Cdd:cd11027  197 -PGNIRD-LTDALIKAKKEAEDEgdedsglLTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVI 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 364 GRSHRPvTLEDLKKLKYLDCVIKETLRVFPSVPL-FARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPE 442
Cdd:cd11027  275 GRDRLP-TLSDRKRLPYLEATIAEVLRLSSVVPLaLPHKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPE 353
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 187956757 443 RFFPENSQGR-HPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd11027  354 RFLDENGKLVpKPESFLPFSAGRRVCLGESLAKAELFLFLARLLQKF 400
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
72-491 1.24e-54

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: 189.07  E-value: 1.24e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  72 EFFQQLIYyteefRHLPIIKLWIGPVPLVALYKAENVEVILTSSKQIDKSFL--YKFLQPWLGLGLLTSTGSKWRTRRKM 149
Cdd:cd11045    1 EFARQRYR-----RYGPVSWTGMLGLRVVALLGPDANQLVLRNRDKAFSSKQgwDPVIGPFFHRGLMLLDFDEHRAHRRI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 150 LTPTFHFTILENFLDVMNEQanilVNKLEKH-VNQEAFNCFFYITLCALDIICETAMGKNIGAQSNNDSEYVRTVYRMSD 228
Cdd:cd11045   76 MQQAFTRSALAGYLDRMTPG----IERALARwPTGAGFQFYPAIKELTLDLATRVFLGVDLGPEADKVNKAFIDTVRAST 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 229 MIYRRMKMPWLWfdlwylvfkegrdhKRGLKClHTFTNNVIAERVKERKAeedwtGAGrgpipsknkrKAFLDLLLSVTD 308
Cdd:cd11045  152 AIIRTPIPGTRW--------------WRGLRG-RRYLEEYFRRRIPERRA-----GGG----------DDLFSALCRAED 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 309 EEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVdqeLDEVFGRSHRPVTLEDLKKLKYLDCVIKET 388
Cdd:cd11045  202 EDGDRFSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERL---REESLALGKGTLDYEDLGQLEVTDWVFKEA 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 389 LRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPE-NSQGRHPYAYVPFSAGPRNC 467
Cdd:cd11045  279 LRLVPPVPTLPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPErAEDKVHRYAWAPFGGGAHKC 358
                        410       420
                 ....*....|....*....|....*.
gi 187956757 468 IGQKFAVMEEKTILACILRQF--WVE 491
Cdd:cd11045  359 IGLHFAGMEVKAILHQMLRRFrwWSV 384
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
134-512 2.87e-54

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: 188.68  E-value: 2.87e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 134 GLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQANILVNKLEKHVNQ-EAFNCFFYITLCALDIICETAMGKNIGAQ 212
Cdd:cd11083   50 GVFSAEGDAWRRQRRLVMPAFSPKHLRYFFPTLRQITERLRERWERAAAEgEAVDVHKDLMRYTVDVTTSLAFGYDLNTL 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 213 SNND---SEYVRTVYRMsdmIYRRMKMPwlwFDLW-YLVFKEGRDHKRGLKCLHTFTNNVIAeRVKERKAEEdwtgagrg 288
Cdd:cd11083  130 ERGGdplQEHLERVFPM---LNRRVNAP---FPYWrYLRLPADRALDRALVEVRALVLDIIA-AARARLAAN-------- 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 289 piPSKNKRKAFLDLLLSVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHR 368
Cdd:cd11083  195 --PALAEAPETLLAMMLAEDDPDARLTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARV 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 369 PVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFF--P 446
Cdd:cd11083  273 PPLLEALDRLPYLEAVARETLRLKPVAPLLFLEPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLdgA 352
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187956757 447 ENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQFWVESNQKREELGLAGDLILRPNNG 512
Cdd:cd11083  353 RAAEPHDPSSLLPFGAGPRLCPGRSLALMEMKLVFAMLCRNFDIELPEPAPAVGEEFAFTMSPEGL 418
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
93-488 1.34e-51

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: 181.49  E-value: 1.34e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  93 WIGPVPLVALYKAENV-EVILTSSKQIDKSFLYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQAN 171
Cdd:cd20639   18 WFGPTPRLTVADPELIrEILLTRADHFDRYEAHPLVRQLEGDGLVSLRGEKWAHHRRVITPAFHMENLKRLVPHVVKSVA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 172 ILVNKLEKHVNQ-EAFNCFFYITLCAL--DIICETAMGKNIgaqsnndsEYVRTVYRMSDmiyRRMKMPWLWFDLWYLvf 248
Cdd:cd20639   98 DMLDKWEAMAEAgGEGEVDVAEWFQNLteDVISRTAFGSSY--------EDGKAVFRLQA---QQMLLAAEAFRKVYI-- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 249 kegrdhkRGLKCLHTFTNNVIAERVKE-RKAEEDWTGAGRGPIPSKNKRKAFLDLL----LSVTDEEGNRLSQEDIREEV 323
Cdd:cd20639  165 -------PGYRFLPTKKNRKSWRLDKEiRKSLLKLIERRQTAADDEKDDEDSKDLLglmiSAKNARNGEKMTVEEIIEEC 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 324 DTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPvTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLS 403
Cdd:cd20639  238 KTFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVP-TKDHLPKLKTLGMILNETLRLYPPAVATIRRAK 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 404 EDCEVGGYKVTKGTEAIIIPYALHRDPRYF-PDPEEFRPERFF-PENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTIL 481
Cdd:cd20639  317 KDVKLGGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFAdGVARAAKHPLAFIPFGLGPRTCVGQNLAILEAKLTL 396

                 ....*..
gi 187956757 482 ACILRQF 488
Cdd:cd20639  397 AVILQRF 403
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
88-473 3.41e-50

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: 177.77  E-value: 3.41e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVIL--TSSKQIDKSFLYkFLQPWLGLGLLTST---GSKWRTRRKMLTPTFHFTILENF 162
Cdd:cd11065    3 PIISLKVGGQTIIVLNSPKAAKDLLekRSAIYSSRPRMP-MAGELMGWGMRLLLmpyGPRWRLHRRLFHQLLNPSAVRKY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 163 LDVMNEQANILVNKLEKHvnqeafNCFFY--ITLCALDIICETAMGKNIgaqSNNDSEYVRTVYRMSDMIYRRMK----- 235
Cdd:cd11065   82 RPLQELESKQLLRDLLES------PDDFLdhIRRYAASIILRLAYGYRV---PSYDDPLLRDAEEAMEGFSEAGSpgayl 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 236 ---MPWL-----WFDLWYLvfKEGRDHKRGLKCLHtftnNVIAERVKERKAEEDwtgagrgPIPSknkrkaFLDLLLSVT 307
Cdd:cd11065  153 vdfFPFLrylpsWLGAPWK--RKARELRELTRRLY----EGPFEAAKERMASGT-------ATPS------FVKDLLEEL 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 308 DEEGNrLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGrSHRPVTLEDLKKLKYLDCVIKE 387
Cdd:cd11065  214 DKEGG-LSEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVG-PDRLPTFEDRPNLPYVNAIVKE 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 388 TLRVFPSVPL-FARSLSEDCEVGGYKVTKGTeaIIIP--YALHRDPRYFPDPEEFRPERFFPENSQGRHPYA--YVPFSA 462
Cdd:cd11065  292 VLRWRPVAPLgIPHALTEDDEYEGYFIPKGT--TVIPnaWAIHHDPEVYPDPEEFDPERYLDDPKGTPDPPDppHFAFGF 369
                        410
                 ....*....|.
gi 187956757 463 GPRNCIGQKFA 473
Cdd:cd11065  370 GRRICPGRHLA 380
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
267-519 8.08e-50

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: 176.22  E-value: 8.08e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 267 NVIAERVKERKAEedwtgagrgpIPSKNKRKAFLDLLLSVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLG 346
Cdd:cd11043  169 KELKKIIEERRAE----------LEKASPKGDLLDVLLEEKDEDGDSLTDEEILDNILTLLFAGHETTSTTLTLAVKFLA 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 347 TNPEVQRKVDQELDEVFGR--SHRPVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPY 424
Cdd:cd11043  239 ENPKVLQELLEEHEEIAKRkeEGEGLTWEDYKSMKYTWQVINETLRLAPIVPGVFRKALQDVEYKGYTIPKGWKVLWSAR 318
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 425 ALHRDPRYFPDPEEFRPERFfpENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQFWVESNQKREelgLAGD 504
Cdd:cd11043  319 ATHLDPEYFPDPLKFNPWRW--EGKGKGVPYTFLPFGGGPRLCPGAELAKLEILVFLHHLVTRFRWEVVPDEK---ISRF 393
                        250
                 ....*....|....*
gi 187956757 505 LILRPNNGIWIKLKR 519
Cdd:cd11043  394 PLPRPPKGLPIRLSP 408
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
135-488 9.03e-50

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: 176.62  E-value: 9.03e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 135 LLTSTGSKW-RTRRKMLTPTFHFTILENFLDVMNEQANILVNKL-EKHVNQEAFNCFFYITLCALDIICETAMGKNIG-- 210
Cdd:cd11060   48 LFSERDEKRhAALRRKVASGYSMSSLLSLEPFVDECIDLLVDLLdEKAVSGKEVDLGKWLQYFAFDVIGEITFGKPFGfl 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 211 AQSNNDSEYVRTVYRMsdMIYRRM--KMPWL--WFDLWYLVFKEGRdhKRGLKCLHTFTNNVIAERVKERKAEEDwtgag 286
Cdd:cd11060  128 EAGTDVDGYIASIDKL--LPYFAVvgQIPWLdrLLLKNPLGPKRKD--KTGFGPLMRFALEAVAERLAEDAESAK----- 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 287 rgpipsknKRKAFLDLLLSVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVF--G 364
Cdd:cd11060  199 --------GRKDMLDSFLEAGLKDPEKVTDREVVAEALSNILAGSDTTAIALRAILYYLLKNPRVYAKLRAEIDAAVaeG 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 365 RSHRPVTLEDLKKLKYLDCVIKETLRVFPSVPL-FARSLSED-CEVGGYKVTKGTEAIIIPYALHRDPRYF-PDPEEFRP 441
Cdd:cd11060  271 KLSSPITFAEAQKLPYLQAVIKEALRLHPPVGLpLERVVPPGgATICGRFIPGGTIVGVNPWVIHRDKEVFgEDADVFRP 350
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 187956757 442 ERFFPENSQ--GRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd11060  351 ERWLEADEEqrRMMDRADLTFGAGSRTCLGKNIALLELYKVIPELLRRF 399
PLN02936 PLN02936
epsilon-ring hydroxylase
132-525 1.28e-48

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 174.98  E-value: 1.28e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 132 GLGLLTSTGSKWRTRRKMLTPTFHFTILENFLD-VMNEQANILVNKLEKHV-NQEAFNCFFYITLCALDIICETAMGKNI 209
Cdd:PLN02936  96 GSGFAIAEGELWTARRRAVVPSLHRRYLSVMVDrVFCKCAERLVEKLEPVAlSGEAVNMEAKFSQLTLDVIGLSVFNYNF 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 210 GAQSNnDSEYVRTVY--------RMSDMiyrrmkMPWLWFDLWYLVFKEGRDHKRGLKCLHTFTNNVIA------ERVKE 275
Cdd:PLN02936 176 DSLTT-DSPVIQAVYtalkeaetRSTDL------LPYWKVDFLCKISPRQIKAEKAVTVIRETVEDLVDkckeivEAEGE 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 276 RKAEEDWTGAGRgpiPSknkrkaFLDLLLSVTDEegnrLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKV 355
Cdd:PLN02936 249 VIEGEEYVNDSD---PS------VLRFLLASREE----VSSVQLRDDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKA 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 356 DQELDEVFGrsHRPVTLEDLKKLKYLDCVIKETLRVFPSVP-LFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFP 434
Cdd:PLN02936 316 QEELDRVLQ--GRPPTYEDIKELKYLTRCINESMRLYPHPPvLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWE 393
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 435 DPEEFRPERFFPENSQGRHP---YAYVPFSAGPRNCIGQKFAVMEEKTILACILRQFWVE--SNQKreeLGLAGDLILRP 509
Cdd:PLN02936 394 RAEEFVPERFDLDGPVPNETntdFRYIPFSGGPRKCVGDQFALLEAIVALAVLLQRLDLElvPDQD---IVMTTGATIHT 470
                        410
                 ....*....|....*.
gi 187956757 510 NNGIWIKLKRRHEDDP 525
Cdd:PLN02936 471 TNGLYMTVSRRRVPDG 486
PLN02738 PLN02738
carotene beta-ring hydroxylase
89-488 1.76e-48

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 177.41  E-value: 1.76e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  89 IIKLWIGPVPLVALYKAENVEVILT-SSKQIDKSFLYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMN 167
Cdd:PLN02738 167 IFRLTFGPKSFLIVSDPSIAKHILRdNSKAYSKGILAEILEFVMGKGLIPADGEIWRVRRRAIVPALHQKYVAAMISLFG 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 168 EQANILVNKLEK------HVNQEAFncFFYITLcalDIICETAMGKNIGAQSNNDS--EYVRTVYRMSDMiyrRMKMPWL 239
Cdd:PLN02738 247 QASDRLCQKLDAaasdgeDVEMESL--FSRLTL---DIIGKAVFNYDFDSLSNDTGivEAVYTVLREAED---RSVSPIP 318
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 240 WFDL--WYLVFKEGRDHKRGLKCLHTFTNNVIA--ERVKERKA---EEDWTgagrgpipskNKRK-AFLDLLLSVTDEeg 311
Cdd:PLN02738 319 VWEIpiWKDISPRQRKVAEALKLINDTLDDLIAicKRMVEEEElqfHEEYM----------NERDpSILHFLLASGDD-- 386
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 312 nrLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGrsHRPVTLEDLKKLKYLDCVIKETLRV 391
Cdd:PLN02738 387 --VSSKQLRDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLG--DRFPTIEDMKKLKYTTRVINESLRL 462
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 392 FPSVP-LFARSLSEDCeVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERF---FPENSQGRHPYAYVPFSAGPRNC 467
Cdd:PLN02738 463 YPQPPvLIRRSLENDM-LGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWpldGPNPNETNQNFSYLPFGGGPRKC 541
                        410       420
                 ....*....|....*....|.
gi 187956757 468 IGQKFAVMEEKTILACILRQF 488
Cdd:PLN02738 542 VGDMFASFENVVATAMLVRRF 562
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
88-488 2.99e-48

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: 172.60  E-value: 2.99e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENV-EVILTSSKQIDK-SFLYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDV 165
Cdd:cd20640   13 PIFTYSTGNKQFLYVSRPEMVkEINLCVSLDLGKpSYLKKTLKPLFGGGILTSNGPHWAHQRKIIAPEFFLDKVKGMVDL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 166 MNEQANILVNKLEKHVNQEAFNCF-----FYITLCALDIICETAMGknigaqsnndSEYV--RTVYRMSDMIYRRMKMPW 238
Cdd:cd20640   93 MVDSAQPLLSSWEERIDRAGGMAAdivvdEDLRAFSADVISRACFG----------SSYSkgKEIFSKLRELQKAVSKQS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 239 LWF--DLWYLvFKEGRDhkRGLKCLHTFTNNVIAERVKERKAEEDwtgagrgpiPSKNKRKAFLDlllSVTDEEGNRLSQ 316
Cdd:cd20640  163 VLFsiPGLRH-LPTKSN--RKIWELEGEIRSLILEIVKEREEECD---------HEKDLLQAILE---GARSSCDKKAEA 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 317 ED-IREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGrsHRPVTLEDLKKLKYLDCVIKETLRVFPSV 395
Cdd:cd20640  228 EDfIVDNCKNIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCK--GGPPDADSLSRMKTVTMVIQETLRLYPPA 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 396 PLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYF-PDPEEFRPERFfpENSQG---RHPYAYVPFSAGPRNCIGQK 471
Cdd:cd20640  306 AFVSREALRDMKLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERF--SNGVAaacKPPHSYMPFGAGARTCLGQN 383
                        410
                 ....*....|....*..
gi 187956757 472 FAVMEEKTILACILRQF 488
Cdd:cd20640  384 FAMAELKVLVSLILSKF 400
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
146-493 6.66e-48

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: 171.24  E-value: 6.66e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 146 RRKMLTPTFHFTILENFLDVMNEQANILVNKLEKHVNQEAFNCFFYITLCaldIICETAMGKNIgaQSNNDSEYVRtvyr 225
Cdd:cd11042   67 QLKFGLNILRRGKLRGYVPLIVEEVEKYFAKWGESGEVDLFEEMSELTIL---TASRCLLGKEV--RELLDDEFAQ---- 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 226 msdmIYRRMKM---PWLWFDLWYLV--FKEgRDHKRglKCLHTFTNNVIAERVKERKAEEDwtgagrgpipsknkrkAFL 300
Cdd:cd11042  138 ----LYHDLDGgftPIAFFFPPLPLpsFRR-RDRAR--AKLKEIFSEIIQKRRKSPDKDED----------------DML 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 301 DLLLSVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVTLEDLKKLKY 380
Cdd:cd11042  195 QTLMDAKYKDGRPLTDDEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDDPLTYDVLKEMPL 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 381 LDCVIKETLRVFPSVPLFARSLSED--CEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENS--QGRHPYA 456
Cdd:cd11042  275 LHACIKETLRLHPPIHSLMRKARKPfeVEGGGYVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAedSKGGKFA 354
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 187956757 457 YVPFSAGPRNCIGQKFAVMEEKTILACILRQF---WVESN 493
Cdd:cd11042  355 YLPFGAGRHRCIGENFAYLQIKTILSTLLRNFdfeLVDSP 394
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
93-488 1.49e-47

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


Pssm-ID: 410734 [Multi-domain]  Cd Length: 431  Bit Score: 170.71  E-value: 1.49e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  93 WIGPVPLVALYKAENVEVILTSSKQI-DKSFLYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQAN 171
Cdd:cd20641   18 WQGTTPRICISDHELAKQVLSDKFGFfGKSKARPEILKLSGKGLVFVNGDDWVRHRRVLNPAFSMDKLKSMTQVMADCTE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 172 ILVNKLEKH-VNQEAFNCFFYIT--LCAL--DIICETAMGKNIgAQSNNDSEYVRTVYRMSDMIYRRMKMPwlwfDLWYL 246
Cdd:cd20641   98 RMFQEWRKQrNNSETERIEVEVSreFQDLtaDIIATTAFGSSY-AEGIEVFLSQLELQKCAAASLTNLYIP----GTQYL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 247 VFKEGRDHKRglkcLHTFTNNVIAERVKERKAEEdwtGAGRGpipsknkrKAFLDLLLSV--TDEEGNR----LSQEDIR 320
Cdd:cd20641  173 PTPRNLRVWK----LEKKVRNSIKRIIDSRLTSE---GKGYG--------DDLLGLMLEAasSNEGGRRterkMSIDEII 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 321 EEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVTlEDLKKLKYLDCVIKETLRVFPSVPLFAR 400
Cdd:cd20641  238 DECKTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDA-DTLSKLKLMNMVLMETLRLYGPVINIAR 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 401 SLSEDCEVGGYKVTKGTeAIIIPYA-LHRDPRYF-PDPEEFRPERFfpENSQGR---HPYAYVPFSAGPRNCIGQKFAVM 475
Cdd:cd20641  317 RASEDMKLGGLEIPKGT-TIIIPIAkLHRDKEVWgSDADEFNPLRF--ANGVSRaatHPNALLSFSLGPRACIGQNFAMI 393
                        410
                 ....*....|...
gi 187956757 476 EEKTILACILRQF 488
Cdd:cd20641  394 EAKTVLAMILQRF 406
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
85-475 2.03e-47

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: 170.34  E-value: 2.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  85 RHLPIIKLWIGPVPLVALYKAENVEVILT----------SSKQIDKsFLYKFLQ----PWlglglltstGSKWRTRRKML 150
Cdd:cd11072    1 KYGPLMLLRLGSVPTVVVSSPEAAKEVLKthdlvfasrpKLLAARI-LSYGGKDiafaPY---------GEYWRQMRKIC 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 151 TptfhftiLE--------NFLDVMNEQANILVNKLEKHV-NQEAFNcfFYITLCAL--DIICETAMGKNIGAQSNND-SE 218
Cdd:cd11072   71 V-------LEllsakrvqSFRSIREEEVSLLVKKIRESAsSSSPVN--LSELLFSLtnDIVCRAAFGRKYEGKDQDKfKE 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 219 YVRTVYRM------SDMIyrrmkmPWLWFdLWYLVFKEGRdHKRGLKCLHTFTNNVIAERVKERKAEEDwtgagrgpips 292
Cdd:cd11072  142 LVKEALELlggfsvGDYF------PSLGW-IDLLTGLDRK-LEKVFKELDAFLEKIIDEHLDKKRSKDE----------- 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 293 KNKRKAFLDLLLSVTDEEGNRLSQEDIREEV-DtfMFE-GHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGrSHRPV 370
Cdd:cd11072  203 DDDDDDLLDLRLQKEGDLEFPLTRDNIKAIIlD--MFLaGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVG-GKGKV 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 371 TLEDLKKLKYLDCVIKETLRVFPSVPLFA-RSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFfpENS 449
Cdd:cd11072  280 TEEDLEKLKYLKAVIKETLRLHPPAPLLLpRECREDCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERF--LDS 357
                        410       420       430
                 ....*....|....*....|....*....|
gi 187956757 450 ----QGRHpYAYVPFSAGPRNCIGQKFAVM 475
Cdd:cd11072  358 sidfKGQD-FELIPFGAGRRICPGITFGLA 386
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
88-491 4.20e-47

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: 169.32  E-value: 4.20e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVILTSSkQID---KSFLYKFLQPWLGLGLLTSTGSKWRTRRKmltptfhFTI--LENF 162
Cdd:cd20651    2 DVVGLKLGKDKVVVVSGYEAVREVLSRE-EFDgrpDGFFFRLRTFGKRLGITFTDGPFWKEQRR-------FVLrhLRDF 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 163 -------LDVMNEQANILVNKLEKHVnQEAFNC--FFYITLcaLDIICETAMGKNIGAQSNNDSEYVRTVYRMSDMI--Y 231
Cdd:cd20651   74 gfgrrsmEEVIQEEAEELIDLLKKGE-KGPIQMpdLFNVSV--LNVLWAMVAGERYSLEDQKLRKLLELVHLLFRNFdmS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 232 RRM--KMPWLWFdlwylVFKEGRDHKRGLKcLHTFTNNVIAERVKERKAEEDwtgagrgpipsKNKRKAFLDLLLSVTDE 309
Cdd:cd20651  151 GGLlnQFPWLRF-----IAPEFSGYNLLVE-LNQKLIEFLKEEIKEHKKTYD-----------EDNPRDLIDAYLREMKK 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 310 EGNRLS--QED--IREEVDtFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPvTLEDLKKLKYLDCVI 385
Cdd:cd20651  214 KEPPSSsfTDDqlVMICLD-LFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLP-TLDDRSKLPYTEAVI 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 386 KETLRVFPSVPL-FARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGP 464
Cdd:cd20651  292 LEVLRIFTLVPIgIPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKLLKDEWFLPFGAGK 371
                        410       420
                 ....*....|....*....|....*..
gi 187956757 465 RNCIGQKFAVMEEKTILACILRQFWVE 491
Cdd:cd20651  372 RRCLGESLARNELFLFFTGLLQNFTFS 398
PLN02290 PLN02290
cytokinin trans-hydroxylase
93-518 5.05e-47

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 171.15  E-value: 5.05e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  93 WIGPVPLVALYKAENVEVILTSSKQID-KSFLYK-FLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQA 170
Cdd:PLN02290 100 WNGTEPRLCLTETELIKELLTKYNTVTgKSWLQQqGTKHFIGRGLLMANGADWYHQRHIAAPAFMGDRLKGYAGHMVECT 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 171 NILVNKLEKHVN--QEAFNCFFYITLCALDIICETAMGKNIgaqsnndsEYVRTVYRMSDMIYRRMKMP--WLWF-DLWY 245
Cdd:PLN02290 180 KQMLQSLQKAVEsgQTEVEIGEYMTRLTADIISRTEFDSSY--------EKGKQIFHLLTVLQRLCAQAtrHLCFpGSRF 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 246 LVFKegrdHKRGLKCLHTFTNNVIAERVKERKaeeDWTGAGRgpipSKNKRKAFLDLLLSVTD---EEGNRLSQEDIREE 322
Cdd:PLN02290 252 FPSK----YNREIKSLKGEVERLLMEIIQSRR---DCVEIGR----SSSYGDDLLGMLLNEMEkkrSNGFNLNLQLIMDE 320
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 323 VDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRShrPVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSL 402
Cdd:PLN02290 321 CKTFFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGE--TPSVDHLSKLTLLNMVINESLRLYPPATLLPRMA 398
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 403 SEDCEVGGYKVTKGTEAIIIPYALHRDPRYF-PDPEEFRPERFFPEN-SQGRHpyaYVPFSAGPRNCIGQKFAVMEEKTI 480
Cdd:PLN02290 399 FEDIKLGDLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPfAPGRH---FIPFAAGPRNCIGQAFAMMEAKII 475
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 187956757 481 LACILRQF--WVESNQKREELGLagdLILRPNNGIWIKLK 518
Cdd:PLN02290 476 LAMLISKFsfTISDNYRHAPVVV---LTIKPKYGVQVCLK 512
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
147-488 7.08e-47

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: 168.53  E-value: 7.08e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 147 RKMLTPTFHftilENFL----DVMNEQANILVNKLEKHVNQEA-------FNCffyitlCALDIICETAMGKNIGA-QSN 214
Cdd:cd11058   62 RRLLAHAFS----EKALreqePIIQRYVDLLVSRLRERAGSGTpvdmvkwFNF------TTFDIIGDLAFGESFGClENG 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 215 NDSEYVRTVY---RMSDMIYRRMKMPWLWFDLWYLVFKEGRDHKRglKCLHTftnnvIAERVKERKAeedwtgagrgpip 291
Cdd:cd11058  132 EYHPWVALIFdsiKALTIIQALRRYPWLLRLLRLLIPKSLRKKRK--EHFQY-----TREKVDRRLA------------- 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 292 SKNKRKAFLDLLLSVtDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFgRSHRPVT 371
Cdd:cd11058  192 KGTDRPDFMSYILRN-KDEKKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIRSAF-SSEDDIT 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 372 LEDLKKLKYLDCVIKETLRVFPSVPLFA--RSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENS 449
Cdd:cd11058  270 LDSLAQLPYLNAVIQEALRLYPPVPAGLprVVPAGGATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLGDPR 349
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 187956757 450 QGRHP---YAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd11058  350 FEFDNdkkEAFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNF 391
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
92-491 7.77e-47

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: 169.00  E-value: 7.77e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  92 LWIGPVPLVALYKAENVEVILTSSKQIDKSFLYKFLQpWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQAN 171
Cdd:cd20642   17 TWFGPIPRVIIMDPELIKEVLNKVYDFQKPKTNPLTK-LLATGLASYEGDKWAKHRKIINPAFHLEKLKNMLPAFYLSCS 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 172 ILVNKLEKHVNQEA---FNCFFYITLCALDIICETAMGKNIgaqsnndSEYVRTVYRMSDMIYRRMK------MPWLWFd 242
Cdd:cd20642   96 EMISKWEKLVSSKGsceLDVWPELQNLTSDVISRTAFGSSY-------EEGKKIFELQKEQGELIIQalrkvyIPGWRF- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 243 lwyLVFKEGRDHKRGLKCLHTFTNNVIAERVKERKAEEDwtgagrgpipsknKRKAFLDLLLSVTDEE-------GNRLS 315
Cdd:cd20642  168 ---LPTKRNRRMKEIEKEIRSSLRGIINKREKAMKAGEA-------------TNDDLLGILLESNHKEikeqgnkNGGMS 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 316 QEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRShRPvTLEDLKKLKYLDCVIKETLRVFPSV 395
Cdd:cd20642  232 TEDVIEECKLFYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFGNN-KP-DFEGLNHLKVVTMILYEVLRLYPPV 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 396 PLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYF-PDPEEFRPERF---FPENSQGRhpYAYVPFSAGPRNCIGQK 471
Cdd:cd20642  310 IQLTRAIHKDTKLGDLTLPAGVQVSLPILLVHRDPELWgDDAKEFNPERFaegISKATKGQ--VSYFPFGWGPRICIGQN 387
                        410       420
                 ....*....|....*....|
gi 187956757 472 FAVMEEKTILACILRQFWVE 491
Cdd:cd20642  388 FALLEAKMALALILQRFSFE 407
PLN02687 PLN02687
flavonoid 3'-monooxygenase
140-469 9.02e-46

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 167.68  E-value: 9.02e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 140 GSKWRTRRKMLT-PTFHFTILENFLDVMNEQANILVNKLEKHVNQEAFNCFFYITLCALDIICETAMGKNI-GAQSNNDS 217
Cdd:PLN02687 124 GPRWRALRKICAvHLFSAKALDDFRHVREEEVALLVRELARQHGTAPVNLGQLVNVCTTNALGRAMVGRRVfAGDGDEKA 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 218 EYVRtvyrmsDMIYRRMKM----------PWL-WFDLWYLVFKEGRDHKRglkcLHTFTNNVIAERVKerkaeedwtgag 286
Cdd:PLN02687 204 REFK------EMVVELMQLagvfnvgdfvPALrWLDLQGVVGKMKRLHRR----FDAMMNGIIEEHKA------------ 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 287 rGPIPSKNKRKAFLDLLLSVTDE-----EGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDE 361
Cdd:PLN02687 262 -AGQTGSEEHKDLLSTLLALKREqqadgEGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDA 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 362 VFGRShRPVTLEDLKKLKYLDCVIKETLRVFPSVPL-FARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFR 440
Cdd:PLN02687 341 VVGRD-RLVSESDLPQLTYLQAVIKETFRLHPSTPLsLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFR 419
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 187956757 441 PERFFPensQGRHP--------YAYVPFSAGPRNCIG 469
Cdd:PLN02687 420 PDRFLP---GGEHAgvdvkgsdFELIPFGAGRRICAG 453
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
144-488 1.90e-44

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: 162.04  E-value: 1.90e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 144 RTRRKMLTPTF---HFTILENfldVMNEQANILVNKLEKH------VN-QEAFNCFfyitlcALDIICETAMGKNIGA-Q 212
Cdd:cd11062   56 RLRRKALSPFFskrSILRLEP---LIQEKVDKLVSRLREAkgtgepVNlDDAFRAL------TADVITEYAFGRSYGYlD 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 213 SNNDSEYVRTVYRMSDMIYRRMK-MPWLwfdLWYLVFKEGRDHKRGLKCLHTFTN--NVIAERVKERKAEEDwtgagrgp 289
Cdd:cd11062  127 EPDFGPEFLDALRALAEMIHLLRhFPWL---LKLLRSLPESLLKRLNPGLAVFLDfqESIAKQVDEVLRQVS-------- 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 290 IPSKNKRKAFLDLLLSVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRP 369
Cdd:cd11062  196 AGDPPSIVTSLFHALLNSDLPPSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKTAMPDPDSP 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 370 VTLEDLKKLKYLDCVIKETLRVFPSVPL-FAR-SLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFF-P 446
Cdd:cd11062  276 PSLAELEKLPYLTAVIKEGLRLSYGVPTrLPRvVPDEGLYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWLgA 355
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 187956757 447 ENSQGRHPYaYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd11062  356 AEKGKLDRY-LVPFSKGSRSCLGINLAYAELYLALAALFRRF 396
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
88-488 2.99e-44

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: 162.00  E-value: 2.99e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVILtssKQIDKSFLYKFLQPWLGLGLLTST-------GSKWRTRRK-MLTPTFHFTIL 159
Cdd:cd20655    2 PLLHLRIGSVPCVVVSSASVAKEIL---KTHDLNFSSRPVPAAAESLLYGSSgfafapyGDYWKFMKKlCMTELLGPRAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 160 ENFLDV-MNEQANILVNKLEKHVNQEAFNcffyITLCAL----DIICETAMGKNIgAQSNNDSEYVRTVYRMSDMIYRRM 234
Cdd:cd20655   79 ERFRPIrAQELERFLRRLLDKAEKGESVD----IGKELMkltnNIICRMIMGRSC-SEENGEAEEVRKLVKESAELAGKF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 235 K-MPWLWF----DLWylVFKegrdhKRGLKCLHTFtnNVIAERV-KERkaEEDwtgagrgpiPSKNKR---KAFLDLLLS 305
Cdd:cd20655  154 NaSDFIWPlkklDLQ--GFG-----KRIMDVSNRF--DELLERIiKEH--EEK---------RKKRKEggsKDLLDILLD 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 306 VTDEEG--NRLSQEDIRE-EVDTFMfEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRShRPVTLEDLKKLKYLD 382
Cdd:cd20655  214 AYEDENaeYKITRNHIKAfILDLFI-AGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKT-RLVQESDLPNLPYLQ 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 383 CVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQG------RHPYA 456
Cdd:cd20655  292 AVVKETLRLHPPGPLLVRESTEGCKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLASSRSGqeldvrGQHFK 371
                        410       420       430
                 ....*....|....*....|....*....|..
gi 187956757 457 YVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd20655  372 LLPFGSGRRGCPGASLAYQVVGTAIAAMVQCF 403
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
140-488 5.26e-44

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


Pssm-ID: 410747 [Multi-domain]  Cd Length: 447  Bit Score: 161.63  E-value: 5.26e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 140 GSKWRTRRKMLTptFHFTI---LENFLDVMNEQANILVNKL----EKHVNQEAF------NCFFYITLcalDIICETAMG 206
Cdd:cd20654   58 GPYWRELRKIAT--LELLSnrrLEKLKHVRVSEVDTSIKELyslwSNNKKGGGGvlvemkQWFADLTF---NVILRMVVG 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 207 KNIGAQSNNDSE-----YVRTVYRM---------SDMIyrrmkmPWL-WFDLwylvFKEGRDHKRGLKCLHTFTNNVIAE 271
Cdd:cd20654  133 KRYFGGTAVEDDeeaerYKKAIREFmrlagtfvvSDAI------PFLgWLDF----GGHEKAMKRTAKELDSILEEWLEE 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 272 RVKERKAEEDwtgagrgpipSKNKRKAFLDLLLSVtdEEGNRLSQED----IREEVDTFMFEGHDTTAAAINWSLYLLGT 347
Cdd:cd20654  203 HRQKRSSSGK----------SKNDEDDDDVMMLSI--LEDSQISGYDadtvIKATCLELILGGSDTTAVTLTWALSLLLN 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 348 NPEVQRKVDQELDEVFGRShRPVTLEDLKKLKYLDCVIKETLRVFPSVPLFA-RSLSEDCEVGGYKVTKGTEAIIIPYAL 426
Cdd:cd20654  271 NPHVLKKAQEELDTHVGKD-RWVEESDIKNLVYLQAIVKETLRLYPPGPLLGpREATEDCTVGGYHVPKGTRLLVNVWKI 349
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187956757 427 HRDPRYFPDPEEFRPERFFPENSQ----GRHpYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd20654  350 QRDPNVWSDPLEFKPERFLTTHKDidvrGQN-FELIPFGSGRRSCPGVSFGLQVMHLTLARLLHGF 414
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
88-503 3.09e-43

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: 158.88  E-value: 3.09e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVILtsskqIDKS----------FLYKFLQpwlGLGLLTSTGSKWRTRRKmltptFHFT 157
Cdd:cd11026    3 PVFTVYLGSKPVVVLCGYEAVKEAL-----VDQAeefsgrppvpLFDRVTK---GYGVVFSNGERWKQLRR-----FSLT 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 158 ILENF-------LDVMNEQANILVNKLEKHvNQEAFNCFFYITLCALDIICETAMGKnigaQSNNDSEYVRTVYRMSDMI 230
Cdd:cd11026   70 TLRNFgmgkrsiEERIQEEAKFLVEAFRKT-KGKPFDPTFLLSNAVSNVICSIVFGS----RFDYEDKEFLKLLDLINEN 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 231 YRRMKMPWL-------WFdLWYLvfkEGRDHK--RGLKCLHTFtnnvIAERVKERKAEEDwtgagrgpiPSkNKRKaFLD 301
Cdd:cd11026  145 LRLLSSPWGqlynmfpPL-LKHL---PGPHQKlfRNVEEIKSF----IRELVEEHRETLD---------PS-SPRD-FID 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 302 -LLLSVTDEEGNRLSQEDIREEVDTFM---FEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRsHRPVTLEDLKK 377
Cdd:cd11026  206 cFLLKMEKEKDNPNSEFHEENLVMTVLdlfFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGR-NRTPSLEDRAK 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 378 LKYLDCVIKETLRVFPSVPL-FARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYA 456
Cdd:cd11026  285 MPYTDAVIHEVQRFGDIVPLgVPHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGKFKKNEA 364
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 187956757 457 YVPFSAGPRNCIGQKFAVMEEKTILACILRQFWVESNQKREELGLAG 503
Cdd:cd11026  365 FMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSLSSPVGPKDPDLTP 411
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
85-489 7.16e-43

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: 158.08  E-value: 7.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  85 RHLPIIKLWIGPVPLVALYKAENVEVILTSSkqiDKSFLYKFL-QPWLGLG------LLTSTGSKWRTRRKMLTpTFHFT 157
Cdd:cd11073    3 KYGPIMSLKLGSKTTVVVSSPEAAREVLKTH---DRVLSGRDVpDAVRALGhhkssiVWPPYGPRWRMLRKICT-TELFS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 158 --ILENFLDVMNEQANILVNKLEKHV-NQEAFNCFFYITLCALDIICETAMGKNIGaqsNNDSEyvrTVYRMSDMIYRRM 234
Cdd:cd11073   79 pkRLDATQPLRRRKVRELVRYVREKAgSGEAVDIGRAAFLTSLNLISNTLFSVDLV---DPDSE---SGSEFKELVREIM 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 235 KM----------PWL-WFDLWYLVfKEGRDHkrgLKCLHTFTNNVIAERVKERKAEEDwtgagrgpipskNKRKAFLDLL 303
Cdd:cd11073  153 ELagkpnvadffPFLkFLDLQGLR-RRMAEH---FGKLFDIFDGFIDERLAEREAGGD------------KKKDDDLLLL 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 304 LSVTDEEGNRLSQEDIReevdTFMFE----GHDTTAAAINWSL-YLLGtNPEVQRKVDQELDEVFGRShRPVTLEDLKKL 378
Cdd:cd11073  217 LDLELDSESELTRNHIK----ALLLDlfvaGTDTTSSTIEWAMaELLR-NPEKMAKARAELDEVIGKD-KIVEESDISKL 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 379 KYLDCVIKETLRVFPSVP-LFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFF--PENSQGRHpY 455
Cdd:cd11073  291 PYLQAVVKETLRLHPPAPlLLPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLgsEIDFKGRD-F 369
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 187956757 456 AYVPFSAGPRNCIGQKFAVMEEKTILACILRQF-W 489
Cdd:cd11073  370 ELIPFGSGRRICPGLPLAERMVHLVLASLLHSFdW 404
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
88-492 5.78e-42

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: 155.47  E-value: 5.78e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVILTSSKQ----------IDKSFLykflqpwlGLGLLTSTGSKWRTRRKmltptFHFT 157
Cdd:cd20670    3 PVFTVYMGPRPVVVLCGHEAVKEALVDQADefsgrgelatIERNFQ--------GHGVALANGERWRILRR-----FSLT 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 158 ILENF-------LDVMNEQANILVNKLEKhVNQEAFNCFFYITLCALDIICETAMGKNIgaqsNNDSEYVRTVYRMSDMI 230
Cdd:cd20670   70 ILRNFgmgkrsiEERIQEEAGYLLEEFRK-TKGAPIDPTFFLSRTVSNVISSVVFGSRF----DYEDKQFLSLLRMINES 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 231 YRRMKMPWL-WFDLWYLVFK--EGRdHKRgLKCLHTFTNNVIAERVKERKAEEDwtgagrgpipSKNKRKaFLD-LLLSV 306
Cdd:cd20670  145 FIEMSTPWAqLYDMYSGIMQylPGR-HNR-IYYLIEELKDFIASRVKINEASLD----------PQNPRD-FIDcFLIKM 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 307 TDEEGNRLSQEDIREEVDT---FMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGrSHRPVTLEDLKKLKYLDC 383
Cdd:cd20670  212 HQDKNNPHTEFNLKNLVLTtlnLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIG-PHRLPSVDDRVKMPYTDA 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 384 VIKETLRVFPSVPL-FARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSA 462
Cdd:cd20670  291 VIHEIQRLTDIVPLgVPHNVIRDTQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQGRFKKNEAFVPFSS 370
                        410       420       430
                 ....*....|....*....|....*....|
gi 187956757 463 GPRNCIGQKFAVMEEKTILACILRQFWVES 492
Cdd:cd20670  371 GKRVCLGEAMARMELFLYFTSILQNFSLRS 400
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
137-511 8.18e-42

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: 155.15  E-value: 8.18e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 137 TSTGSKWRTRRKMLTPTFH-FTILE--NFL-DVMNEQANILVNKLEKHVNQEA-FNCFFYITLCALDIICETAMGKNiga 211
Cdd:cd11028   55 SDYGPRWKLHRKLAQNALRtFSNARthNPLeEHVTEEAEELVTELTENNGKPGpFDPRNEIYLSVGNVICAICFGKR--- 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 212 QSNNDSEYVRTVYRMSDMiyrrMK----------MPWL-WFDLWYL-VFKEgrdhkrglkCLHTFtNNVIAERVKERKAE 279
Cdd:cd11028  132 YSRDDPEFLELVKSNDDF----GAfvgagnpvdvMPWLrYLTRRKLqKFKE---------LLNRL-NSFILKKVKEHLDT 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 280 EDwtgagrgpipsKNKRKAFLDLLLSVTDE------EGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQR 353
Cdd:cd11028  198 YD-----------KGHIRDITDALIKASEEkpeeekPEVGLTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQE 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 354 KVDQELDEVFGRSHRPvTLEDLKKLKYLDCVIKETLRVFPSVPL-FARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRY 432
Cdd:cd11028  267 KVQAELDRVIGRERLP-RLSDRPNLPYTEAFILETMRHSSFVPFtIPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKL 345
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 433 FPDPEEFRPERFFPENSQGRHPYA--YVPFSAGPRNCIGQKFAVMEEKTILACILRQFWVESNqKREELGLAG--DLILR 508
Cdd:cd11028  346 WPDPSVFRPERFLDDNGLLDKTKVdkFLPFGAGRRRCLGEELARMELFLFFATLLQQCEFSVK-PGEKLDLTPiyGLTMK 424

                 ...
gi 187956757 509 PNN 511
Cdd:cd11028  425 PKP 427
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
88-501 1.44e-40

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: 151.45  E-value: 1.44e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVILTS-----SKQIDKSFLYKFLQpwlGLGLLTSTGSKWRTRRKmltptFHFTILENF 162
Cdd:cd20669    3 SVYTVYLGPRPVVVLCGYQAVKEALVDqaeefSGRGDYPVFFNFTK---GNGIAFSNGERWKILRR-----FALQTLRNF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 163 -------LDVMNEQANILVNKLeKHVNQEAFNCFFYITLCALDIICETAMGKNIgaqSNNDSEYVRTVYRMSDMiYRRMK 235
Cdd:cd20669   75 gmgkrsiEERILEEAQFLLEEL-RKTKGAPFDPTFLLSRAVSNIICSVVFGSRF---DYDDKRLLTILNLINDN-FQIMS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 236 MPWLWFdlwYLVFKEGRD-----HKRglkclhTFTN-----NVIAERVKERKAEEDwtgagrgpipsKNKRKAFLDLLLS 305
Cdd:cd20669  150 SPWGEL---YNIFPSVMDwlpgpHQR------IFQNfeklrDFIAESVREHQESLD-----------PNSPRDFIDCFLT 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 306 VTDEE-GNRLSQEDIREEVDT---FMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPvTLEDLKKLKYL 381
Cdd:cd20669  210 KMAEEkQDPLSHFNMETLVMTthnLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLP-TLEDRARMPYT 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 382 DCVIKETLRVFPSVPL-FARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPF 460
Cdd:cd20669  289 DAVIHEIQRFADIIPMsLPHAVTRDTNFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPF 368
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 187956757 461 SAGPRNCIGQKFAVMEEKTILACILRQFWVESNQKREELGL 501
Cdd:cd20669  369 SAGKRICLGESLARMELFLYLTAILQNFSLQPLGAPEDIDL 409
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
140-489 1.93e-40

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: 151.42  E-value: 1.93e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 140 GSKWRTRRK-----MLTPTfhftILENFLDV-MNEQANILVNKLEKHVNQEAFNCFFYITLCALDIICETAMGKNI---- 209
Cdd:cd20657   58 GPRWRLLRKlcnlhLFGGK----ALEDWAHVrENEVGHMLKSMAEASRKGEPVVLGEMLNVCMANMLGRVMLSKRVfaak 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 210 -GAQSNNDSEYVRTVYRMS------DMIyrrmkmPWL-WFDLWYLVFKEGRDHKRglkcLHTFTNNVIAERvkERKAEEd 281
Cdd:cd20657  134 aGAKANEFKEMVVELMTVAgvfnigDFI------PSLaWMDLQGVEKKMKRLHKR----FDALLTKILEEH--KATAQE- 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 282 wtgagrgpipsKNKRKAFLDLLLSVTDE--EGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQEL 359
Cdd:cd20657  201 -----------RKGKPDFLDFVLLENDDngEGERLTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEM 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 360 DEVFGRShRPVTLEDLKKLKYLDCVIKETLRVFPSVPL-FARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEE 438
Cdd:cd20657  270 DQVIGRD-RRLLESDIPNLPYLQAICKETFRLHPSTPLnLPRIASEACEVDGYYIPKGTRLLVNIWAIGRDPDVWENPLE 348
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 439 FRPERFFPensqGRHP--------YAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF-W 489
Cdd:cd20657  349 FKPERFLP----GRNAkvdvrgndFELIPFGAGRRICAGTRMGIRMVEYILATLVHSFdW 404
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
88-495 9.58e-39

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: 146.82  E-value: 9.58e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVILtssKQIDKSFLYKFLQPW--------LGLGLLTSTGSKWRTRRKMLTP-TFHFTI 158
Cdd:cd20648    7 PVWKASFGPILTVHVADPALIEQVL---RQEGKHPVRSDLSSWkdyrqlrgHAYGLLTAEGEEWQRLRSLLAKhMLKPKA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 159 LENFLDVMNEQANILVNKLEKHVNQEA----------FNCFfyitlcALDIICETAMGKNIGAQSNNDSE----YVRTVY 224
Cdd:cd20648   84 VEAYAGVLNAVVTDLIRRLRRQRSRSSpgvvkdiageFYKF------GLEGISSVLFESRIGCLEANVPEetetFIQSIN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 225 RMSDMIYRRMKMP-WLWfdlwYLVFKEGRDHKRGLKCLHTFTNNVIAERVKERKAEEdwtgAGRGPIPSKnkrkaFLDLL 303
Cdd:cd20648  158 TMFVMTLLTMAMPkWLH----RLFPKPWQRFCRSWDQMFAFAKGHIDRRMAEVAAKL----PRGEAIEGK-----YLTYF 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 304 LSVtdeegNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPvTLEDLKKLKYLDC 383
Cdd:cd20648  225 LAR-----EKLPMKSIYGNVTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVP-SAADVARMPLLKA 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 384 VIKETLRVFPSVPLFARSLSE-DCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPEnSQGRHPYAYVPFSA 462
Cdd:cd20648  299 VVKEVLRLYPVIPGNARVIPDrDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLGK-GDTHHPYASLPFGF 377
                        410       420       430
                 ....*....|....*....|....*....|...
gi 187956757 463 GPRNCIGQKFAVMEEKTILACILRQFWVESNQK 495
Cdd:cd20648  378 GKRSCIGRRIAELEVYLALARILTHFEVRPEPG 410
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
20-488 1.25e-38

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 148.00  E-value: 1.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  20 SAVSLAGATILISIFPMLVSYA--RKWQQM-RSIPsvaRAYPLVGHALYMKPNNAEFFQQLIYYTEEFRHLPIiklwigP 96
Cdd:PLN03195   1 MKFPVSGMSGVLFIALAVLSWIfiHRWSQRnRKGP---KSWPIIGAALEQLKNYDRMHDWLVEYLSKDRTVVV------K 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  97 VPLVAL-YKAE--NVEVIL-TSSKQIDKSFLY-KFLQPWLGLGLLTSTGSKWRTRRKmlTPTFHFT--ILENFLDVMNEQ 169
Cdd:PLN03195  72 MPFTTYtYIADpvNVEHVLkTNFANYPKGEVYhSYMEVLLGDGIFNVDGELWRKQRK--TASFEFAskNLRDFSTVVFRE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 170 -----ANILVNKLEKHVNQEAFNCFFYITLcalDIICETAMGKNIGAQS----------NNDSEYVRTVYRMSDMIYRRM 234
Cdd:PLN03195 150 yslklSSILSQASFANQVVDMQDLFMRMTL---DSICKVGFGVEIGTLSpslpenpfaqAFDTANIIVTLRFIDPLWKLK 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 235 KMpwlwfdlwylvFKEGRDH--KRGLKCLHTFTNNVIaervKERKAEEDWTGAgrgpipSKNKRKAflDLL---LSVTDE 309
Cdd:PLN03195 227 KF-----------LNIGSEAllSKSIKVVDDFTYSVI----RRRKAEMDEARK------SGKKVKH--DILsrfIELGED 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 310 EGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQEL---DEVFGRSHRP----------------V 370
Cdd:PLN03195 284 PDSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMIMMNPHVAEKLYSELkalEKERAKEEDPedsqsfnqrvtqfaglL 363
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 371 TLEDLKKLKYLDCVIKETLRVFPSVPLFARS-LSEDCEVGGYKVTKGTEAIIIPYALHRDP-RYFPDPEEFRPERFFPEN 448
Cdd:PLN03195 364 TYDSLGKLQYLHAVITETLRLYPAVPQDPKGiLEDDVLPDGTKVKAGGMVTYVPYSMGRMEyNWGPDAASFKPERWIKDG 443
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 187956757 449 S-QGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:PLN03195 444 VfQNASPFKFTAFQAGPRICLGKDSAYLQMKMALALLCRFF 484
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
85-489 1.60e-38

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: 146.23  E-value: 1.60e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  85 RHLPIIKLWIGPVPLVALYKAEnveviLTSSKQIDKSFLYKFLQPWLGLGLLTST----------GSKWRT-RRKMLTPT 153
Cdd:cd11075    1 KYGPIFTLRMGSRPLIVVASRE-----LAHEALVQKGSSFASRPPANPLRVLFSSnkhmvnsspyGPLWRTlRRNLVSEV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 154 FHFTILENFLDVMNEQANILVNKLEKHV--NQEAFNC--FFYITLCALDIIceTAMGKNIgaqsnnDSEYVRTVYR-MSD 228
Cdd:cd11075   76 LSPSRLKQFRPARRRALDNLVERLREEAkeNPGPVNVrdHFRHALFSLLLY--MCFGERL------DEETVRELERvQRE 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 229 MIYRRMKMPWLWF--DLWYLVFKEgrdHKRGLKCLHTFTNNVIAERVKERKAEedwTGAGRGPIPSKNKrkAFLDLLLSV 306
Cdd:cd11075  148 LLLSFTDFDVRDFfpALTWLLNRR---RWKKVLELRRRQEEVLLPLIRARRKR---RASGEADKDYTDF--LLLDLLDLK 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 307 TDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGrSHRPVTLEDLKKLKYLDCVIK 386
Cdd:cd11075  220 EEGGERKLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVG-DEAVVTEEDLPKMPYLKAVVL 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 387 ETLRVFPSVPLF-ARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPEN-----SQGRHPYAYVPF 460
Cdd:cd11075  299 ETLRRHPPGHFLlPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGGeaadiDTGSKEIKMMPF 378
                        410       420       430
                 ....*....|....*....|....*....|
gi 187956757 461 SAGPRNCIGQKFAVMEEKTILACILRQF-W 489
Cdd:cd11075  379 GAGRRICPGLGLATLHLELFVARLVQEFeW 408
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
88-513 4.43e-38

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: 144.80  E-value: 4.43e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVILtssKQIDKSFLYKFLQPW--------LGLGLLTSTGSKWRTRRKMLTP-TFHFTI 158
Cdd:cd20646    6 PIWKSKFGPYDIVNVASAELIEQVL---RQEGKYPMRSDMPHWkehrdlrgHAYGPFTEEGEKWYRLRSVLNQrMLKPKE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 159 LENFLDVMNEQANILVNKLEK---------HVNQEAfNCFFYITLCAL-DIICETAMG---KNIGAQSNNDSEYVRTVYR 225
Cdd:cd20646   83 VSLYADAINEVVSDLMKRIEYlrersgsgvMVSDLA-NELYKFAFEGIsSILFETRIGcleKEIPEETQKFIDSIGEMFK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 226 MSDMIYRRMKMPWLWFDLWYLvFKEGRDHkrglkcLHTFTNNVIAERVKERkaeEDWTGAGrGPIPSKnkrkaFLDLLLS 305
Cdd:cd20646  162 LSEIVTLLPKWTRPYLPFWKR-YVDAWDT------IFSFGKKLIDKKMEEI---EERVDRG-EPVEGE-----YLTYLLS 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 306 vtdeeGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVTlEDLKKLKYLDCVI 385
Cdd:cd20646  226 -----SGKLSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTA-EDIAKMPLLKAVI 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 386 KETLRVFPSVPLFARSLSE-DCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGP 464
Cdd:cd20646  300 KETLRLYPVVPGNARVIVEkEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRDGGLKHHPFGSIPFGYGV 379
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 187956757 465 RNCIGQKFAVMEEKTILACILRQFWVESNQKREELGLAGDLILRPNNGI 513
Cdd:cd20646  380 RACVGRRIAELEMYLALSRLIKRFEVRPDPSGGEVKAITRTLLVPNKPI 428
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
132-488 9.03e-38

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: 144.09  E-value: 9.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 132 GLGLLTSTGSKWRTRRKMLTP---TFHFTILENFLDVMNEQANILVNKLEKHVNQE---AFNCFFYITLCALDIICETAM 205
Cdd:cd20652   46 GNGIICAEGDLWRDQRRFVHDwlrQFGMTKFGNGRAKMEKRIATGVHELIKHLKAEsgqPVDPSPVLMHSLGNVINDLVF 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 206 GknigaqsnndseyvrTVYRMSDMIYRRMK------------------MPWLWFDLWYLVFKEGRdhKRGLKCLHTFTNN 267
Cdd:cd20652  126 G---------------FRYKEDDPTWRWLRflqeegtkligvagpvnfLPFLRHLPSYKKAIEFL--VQGQAKTHAIYQK 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 268 VIAERvKERKAEEDWTGAGRGPIPSKNKRKAFLdlllSVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGT 347
Cdd:cd20652  189 IIDEH-KRRLKPENPRDAEDFELCELEKAKKEG----EDRDLFDGFYTDEQLHHLLADLFGAGVDTTITTLRWFLLYMAL 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 348 NPEVQRKVDQELDEVFGRsHRPVTLEDLKKLKYLDCVIKETLRVFPSVPL-FARSLSEDCEVGGYKVTKGTEAIIIPYAL 426
Cdd:cd20652  264 FPKEQRRIQRELDEVVGR-PDLVTLEDLSSLPYLQACISESQRIRSVVPLgIPHGCTEDAVLAGYRIPKGSMIIPLLWAV 342
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187956757 427 HRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd20652  343 HMDPNLWEEPEEFRPERFLDTDGKYLKPEAFIPFQTGKRMCLGDELARMILFLFTARILRKF 404
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
293-469 2.16e-36

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: 139.66  E-value: 2.16e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 293 KNKRKAF---LDLLLSVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRShRP 369
Cdd:cd20653  199 KNKESGKntmIDHLLSLQESQPEYYTDEIIKGLILVMLLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQD-RL 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 370 VTLEDLKKLKYLDCVIKETLRVFPSVP-LFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFfpeN 448
Cdd:cd20653  278 IEESDLPKLPYLQNIISETLRLYPAAPlLVPHESSEDCKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERF---E 354
                        170       180
                 ....*....|....*....|.
gi 187956757 449 SQGRHPYAYVPFSAGPRNCIG 469
Cdd:cd20653  355 GEEREGYKLIPFGLGRRACPG 375
PTZ00404 PTZ00404
cytochrome P450; Provisional
56-510 1.81e-35

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 138.32  E-value: 1.81e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  56 AYPLVG--HALYMKPNnaeffQQLIYYTEEFRHlpIIKLWIGPVPLVALykaenVEVILTSSKQIDK--SFLYKFLQPWL 131
Cdd:PTZ00404  36 PIPILGnlHQLGNLPH-----RDLTKMSKKYGG--IFRIWFADLYTVVL-----SDPILIREMFVDNfdNFSDRPKIPSI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 132 GLG-----LLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQANILVNKLEK-HVNQEAFNCFFYITLCALdiiceTAM 205
Cdd:PTZ00404 104 KHGtfyhgIVTSSGEYWKRNREIVGKAMRKTNLKHIYDLLDDQVDVLIESMKKiESSGETFEPRYYLTKFTM-----SAM 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 206 GKNIGAQS---NNDSEYVRTVYRMSDM--IYRRMKMPWLwFDL------WYLVFKEGRDhkRGLKCLHTFTNNVIAERVK 274
Cdd:PTZ00404 179 FKYIFNEDisfDEDIHNGKLAELMGPMeqVFKDLGSGSL-FDVieitqpLYYQYLEHTD--KNFKKIKKFIKEKYHEHLK 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 275 ERKAEedwtgagrgpipsknKRKAFLDLLLS--VTDEEGNRLSqedIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQ 352
Cdd:PTZ00404 256 TIDPE---------------VPRDLLDLLIKeyGTNTDDDILS---ILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQ 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 353 RKVDQELDEVFGrSHRPVTLEDLKKLKYLDCVIKETLRVFPSVPL-FARSLSEDCEVG-GYKVTKGTEAIIIPYALHRDP 430
Cdd:PTZ00404 318 EKAYNEIKSTVN-GRNKVLLSDRQSTPYTVAIIKETLRYKPVSPFgLPRSTSNDIIIGgGHFIPKDAQILINYYSLGRNE 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 431 RYFPDPEEFRPERFFPENSqgrhPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQFWVES--NQKREELGLAGdLILR 508
Cdd:PTZ00404 397 KYFENPEQFDPSRFLNPDS----NDAFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLKSidGKKIDETEEYG-LTLK 471

                 ..
gi 187956757 509 PN 510
Cdd:PTZ00404 472 PN 473
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
314-513 3.32e-35

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: 136.97  E-value: 3.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 314 LSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPvTLEDLKKLKYLDCVIKETLRVFP 393
Cdd:cd20647  233 LTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVP-TAEDVPKLPLIRALLKETLRLFP 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 394 SVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGR-HPYAYVPFSAGPRNCIGQKF 472
Cdd:cd20647  312 VLPGNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKDALDRvDNFGSIPFGYGIRSCIGRRI 391
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 187956757 473 AVMEEKTILACILRQFWVESNQKREELGLAGDLILRPNNGI 513
Cdd:cd20647  392 AELEIHLALIQLLQNFEIKVSPQTTEVHAKTHGLLCPGGSI 432
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
140-488 3.87e-35

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


Pssm-ID: 410759 [Multi-domain]  Cd Length: 426  Bit Score: 136.44  E-value: 3.87e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 140 GSKWRTRRKMLTPTF-HFTI-LENFLDVMNEQANILVNKLEKHvNQEAFNCFFYITLCALDIICETAMGKNIGAQsnnDS 217
Cdd:cd20666   58 GPVWRQQRKFSHSTLrHFGLgKLSLEPKIIEEFRYVKAEMLKH-GGDPFNPFPIVNNAVSNVICSMSFGRRFDYQ---DV 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 218 EYvrtvYRMSDMIYRRMKM------------PWLWfdlwYLVFKEGRDHKRGLKCLHTFTNNVIAERvkerkaeedwtga 285
Cdd:cd20666  134 EF----KTMLGLMSRGLEIsvnsaailvnicPWLY----YLPFGPFRELRQIEKDITAFLKKIIADH------------- 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 286 gRGPIPSKNKRKaFLDLLLSVTDEEGNRLSQEDIREE-----VDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELD 360
Cdd:cd20666  193 -RETLDPANPRD-FIDMYLLHIEEEQKNNAESSFNEDylfyiIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEID 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 361 EVFGRShRPVTLEDLKKLKYLDCVIKETLRVFPSVPL-FARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEF 439
Cdd:cd20666  271 TVIGPD-RAPSLTDKAQMPFTEATIMEVQRMTVVVPLsIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDF 349
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 187956757 440 RPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd20666  350 MPSRFLDENGQLIKKEAFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSF 398
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
300-491 6.61e-35

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: 135.91  E-value: 6.61e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 300 LDLLL----------SVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRShRP 369
Cdd:cd20673  204 LDALLqakmnaennnAGPDQDSVGLSDDHILMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFS-RT 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 370 VTLEDLKKLKYLDCVIKETLRVFPSVPLFA--RSLSeDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFpe 447
Cdd:cd20673  283 PTLSDRNHLPLLEATIREVLRIRPVAPLLIphVALQ-DSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFL-- 359
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 187956757 448 NSQGRHPY----AYVPFSAGPRNCIGQKFAVMEEKTILACILRQFWVE 491
Cdd:cd20673  360 DPTGSQLIspslSYLPFGAGPRVCLGEALARQELFLFMAWLLQRFDLE 407
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
88-488 1.71e-34

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: 134.92  E-value: 1.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVILtssKQIDKSF--------LYKFLQPwlGLGLLTST-GSKWRTRRKMLT-PTFHFT 157
Cdd:cd20656    3 PIISVWIGSTLNVVVSSSELAKEVL---KEKDQQLadrhrtrsAARFSRN--GQDLIWADyGPHYVKVRKLCTlELFTPK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 158 ILENFLDVMNEQANILVNKLEKHVN-----QEAFNCFFYITLCALDIICETAMGKNIGAQSNNDSEYVRtvyRMSDMIYR 232
Cdd:cd20656   78 RLESLRPIREDEVTAMVESIFNDCMspeneGKPVVLRKYLSAVAFNNITRLAFGKRFVNAEGVMDEQGV---EFKAIVSN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 233 RMKMP-------WLWFDLWYLVFKEGRDHKRGLKcLHTFTNNVIAERVKERKAeedwTGAGrgpipsknkrKAFLDLLLS 305
Cdd:cd20656  155 GLKLGasltmaeHIPWLRWMFPLSEKAFAKHGAR-RDRLTKAIMEEHTLARQK----SGGG----------QQHFVALLT 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 306 VTDEEGnrLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRShRPVTLEDLKKLKYLDCVI 385
Cdd:cd20656  220 LKEQYD--LSEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSD-RVMTEADFPQLPYLQCVV 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 386 KETLRVFPSVPL-FARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGR-HPYAYVPFSAG 463
Cdd:cd20656  297 KEALRLHPPTPLmLPHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVDIKgHDFRLLPFGAG 376
                        410       420
                 ....*....|....*....|....*
gi 187956757 464 PRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd20656  377 RRVCPGAQLGINLVTLMLGHLLHHF 401
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
86-488 3.24e-34

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: 133.78  E-value: 3.24e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  86 HLPIIKLWIGPVPLVAL--YKAENVEVILTSSKQIDKSF---LYKFLQpwlGLGLLTSTGSKWRTRRKmltptFHFTILE 160
Cdd:cd20664    1 YGSIFTVQMGTKKVVVLagYKTVKEALVNHAEAFGGRPIipiFEDFNK---GYGILFSNGENWKEMRR-----FTLTTLR 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 161 NF-------LDVMNEQANILVNKLEKHvNQEAFNCFFYITLCALDIICETAMGKNIgaqsnndsEYVRTVY-RMSDMIYR 232
Cdd:cd20664   73 DFgmgkktsEDKILEEIPYLIEVFEKH-KGKPFETTLSMNVAVSNIIASIVLGHRF--------EYTDPTLlRMVDRINE 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 233 RMKM------------PWLWFDLwylvfkegRDHK---RGLKCLHTFTNNVIaerVKERKAEEdwtgagrgpipsKNKRK 297
Cdd:cd20664  144 NMKLtgspsvqlynmfPWLGPFP--------GDINkllRNTKELNDFLMETF---MKHLDVLE------------PNDQR 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 298 AFLD--LLLSVTDEEGNR--LSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGrSHRPVTlE 373
Cdd:cd20664  201 GFIDafLVKQQEEEESSDsfFHDDNLTCSVGNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIG-SRQPQV-E 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 374 DLKKLKYLDCVIKETLRVFPSVPLFA-RSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFpeNSQGR 452
Cdd:cd20664  279 HRKNMPYTDAVIHEIQRFANIVPMNLpHATTRDVTFRGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFL--DSQGK 356
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 187956757 453 HPY--AYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd20664  357 FVKrdAFMPFSAGRRVCIGETLAKMELFLFFTSLLQRF 394
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
292-495 1.00e-33

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: 132.24  E-value: 1.00e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 292 SKNKRKAFLDLLLSvtdeeGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPvT 371
Cdd:cd20645  205 SQGPANDFLCDIYH-----DNELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTP-R 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 372 LEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFpENSQG 451
Cdd:cd20645  279 AEDLKNMPYLKACLKESMRLTPSVPFTSRTLDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWL-QEKHS 357
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 187956757 452 RHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQFWVESNQK 495
Cdd:cd20645  358 INPFAHVPFGIGKRMCIGRRLAELQLQLALCWIIQKYQIVATDN 401
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
256-502 2.30e-33

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 132.67  E-value: 2.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 256 RGLKCLHTFTNNVIAERVKERKAeedwtgagrgpipSKNKRKA---FLDLLLS-VTDEEGNRLSQEDIREEVDTFMFEGH 331
Cdd:PLN00110 236 RGMKHLHKKFDKLLTRMIEEHTA-------------SAHERKGnpdFLDVVMAnQENSTGEKLTLTNIKALLLNLFTAGT 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 332 DTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVTlEDLKKLKYLDCVIKETLRVFPSVPL-FARSLSEDCEVGG 410
Cdd:PLN00110 303 DTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRRLVE-SDLPKLPYLQAICKESFRKHPSTPLnLPRVSTQACEVNG 381
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 411 YKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHP----YAYVPFSAGPRNCIGQKFAVMEEKTILACILR 486
Cdd:PLN00110 382 YYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEKNAKIDPrgndFELIPFGAGRRICAGTRMGIVLVEYILGTLVH 461
                        250       260
                 ....*....|....*....|..
gi 187956757 487 QF-W-----VESNQKrEELGLA 502
Cdd:PLN00110 462 SFdWklpdgVELNMD-EAFGLA 482
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
86-501 5.79e-33

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: 130.34  E-value: 5.79e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  86 HLPIIKLWIGPVPLVALYKAENV-EVILTSSKQIDKSFLYKFLQPWLG-LGLLTSTGSKWRTRRKmltptFHFTILENF- 162
Cdd:cd20667    1 YGNIYTLWLGSTPIVVLSGFKAVkEGLVSHSEEFSGRPLTPFFRDLFGeKGIICTNGLTWKQQRR-----FCMTTLRELg 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 163 -----LDV-MNEQANILVNKLEKHvNQEAFNCFFYITLCALDIICETAMGKNIGAQSNNDSEYVRTVY---RMSDMIYRR 233
Cdd:cd20667   76 lgkqaLESqIQHEAAELVKVFAQE-NGRPFDPQDPIVHATANVIGAVVFGHRFSSEDPIFLELIRAINlglAFASTIWGR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 234 M--KMPWLwfdLWYLvfkEGRDHKrgLKCLHTFTNNVIAERVKERKAEedwtgagrgpipSKNKRKAFLDLLLS----VT 307
Cdd:cd20667  155 LydAFPWL---MRYL---PGPHQK--IFAYHDAVRSFIKKEVIRHELR------------TNEAPQDFIDCYLAqitkTK 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 308 DEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHrPVTLEDLKKLKYLDCVIKE 387
Cdd:cd20667  215 DDPVSTFSEENMIQVVIDLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQ-LICYEDRKRLPYTNAVIHE 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 388 TLRVFPSVPLFA-RSLSEDCEVGGYKVTKGTeaIIIP--YALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGP 464
Cdd:cd20667  294 VQRLSNVVSVGAvRQCVTSTTMHGYYVEKGT--IILPnlASVLYDPECWETPHKFNPGHFLDKDGNFVMNEAFLPFSAGH 371
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 187956757 465 RNCIGQKFAVMEEKTILACILRQFWVESNQKREELGL 501
Cdd:cd20667  372 RVCLGEQLARMELFIFFTTLLRTFNFQLPEGVQELNL 408
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
88-488 6.96e-33

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: 131.27  E-value: 6.96e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIG----PVPLVALYKaENVEVILTSSKQIDKSflyKFLQPWLGL-----GLLTSTGSKWRTRRKML----TPTF 154
Cdd:cd20622    2 PIIQLFIRpfgkPWVIVADFR-EAQDILMRRTKEFDRS---DFTIDVFGGigphhHLVKSTGPAFRKHRSLVqdlmTPSF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 155 -HFT----ILENFLDVMNeqaniLVNKLEKHVNQEAFNCFFYITLCALDIICETAMGKNI-------------------- 209
Cdd:cd20622   78 lHNVaapaIHSKFLDLID-----LWEAKARLAKGRPFSAKEDIHHAALDAIWAFAFGINFdasqtrpqlelleaedstil 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 210 GAQSNNDSEY--------VRTVYRMSDMIYRRMKMP---WLWFdlWYLVFKEGRdhkRGLKCLHTFTNNVI--AERVKER 276
Cdd:cd20622  153 PAGLDEPVEFpeaplpdeLEAVLDLADSVEKSIKSPfpkLSHW--FYRNQPSYR---RAAKIKDDFLQREIqaIARSLER 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 277 KAEEDWTGAGrgpipsknkrkafLDLLLS---VTDEEGNR---LSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPE 350
Cdd:cd20622  228 KGDEGEVRSA-------------VDHMVRrelAAAEKEGRkpdYYSQVIHDELFGYLIAGHDTTSTALSWGLKYLTANQD 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 351 VQRKVDQELDEVFGRSH---RPVTLEDLK--KLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYA 425
Cdd:cd20622  295 VQSKLRKALYSAHPEAVaegRLPTAQEIAqaRIPYLDAVIEEILRCANTAPILSREATVDTQVLGYSIPKGTNVFLLNNG 374
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 426 lhrdPRYF---------------------------PDPEEFRPERFFPENSQGRH----PYAY--VPFSAGPRNCIGQKF 472
Cdd:cd20622  375 ----PSYLsppieidesrrssssaakgkkagvwdsKDIADFDPERWLVTDEETGEtvfdPSAGptLAFGLGPRGCFGRRL 450
                        490
                 ....*....|....*.
gi 187956757 473 AVMEEKTILACILRQF 488
Cdd:cd20622  451 AYLEMRLIITLLVWNF 466
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
88-499 1.71e-32

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: 129.15  E-value: 1.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVILTSS--------KQIDKSFLYKflqpwlGLGLLTSTGSKWRTRRKmltptFHFTIL 159
Cdd:cd20668    3 PVFTIHLGPRRVVVLCGYDAVKEALVDQaeefsgrgEQATFDWLFK------GYGVAFSNGERAKQLRR-----FSIATL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 160 ENF-------LDVMNEQANILVNKLEKhVNQEAFNCFFYITLCALDIICETAMGKNIGAQsnnDSEYVrTVYRMSDMIYR 232
Cdd:cd20668   72 RDFgvgkrgiEERIQEEAGFLIDALRG-TGGAPIDPTFYLSRTVSNVISSIVFGDRFDYE---DKEFL-SLLRMMLGSFQ 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 233 RMKMPW-LWFDLWYLVFKE--GRDHK--RGLKCLHTFtnnvIAERVKERKAEEDwtgagrgpipsKNKRKAFLD-LLLSV 306
Cdd:cd20668  147 FTATSTgQLYEMFSSVMKHlpGPQQQafKELQGLEDF----IAKKVEHNQRTLD-----------PNSPRDFIDsFLIRM 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 307 TDEEGNRLSQEDIREEVDT---FMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPvTLEDLKKLKYLDC 383
Cdd:cd20668  212 QEEKKNPNTEFYMKNLVMTtlnLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQP-KFEDRAKMPYTEA 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 384 VIKETLRVFPSVPL-FARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSA 462
Cdd:cd20668  291 VIHEIQRFGDVIPMgLARRVTKDTKFRDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDDKGQFKKSDAFVPFSI 370
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 187956757 463 GPRNCIGQKFAVMEEKTILACILRQFWVESNQKREEL 499
Cdd:cd20668  371 GKRYCFGEGLARMELFLFFTTIMQNFRFKSPQSPEDI 407
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
98-473 1.77e-32

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: 129.16  E-value: 1.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  98 PLVALYKAENVEVILTSSKQIDKSFLYKFLQPWLGLGLLTST-GSKWRTRRKMLTPTFHFTILENFLDVMNEQANILVNK 176
Cdd:cd20638   33 PTVRVMGAENVRQILLGEHKLVSVQWPASVRTILGSGCLSNLhDSQHKHRKKVIMRAFSREALENYVPVIQEEVRSSVNQ 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 177 -LEKH----VNQEAFNCFFYITLCALdIICETAmgknigaQSNNDSEYvRTVYRMSDMIYRRMKMPW-LWFDLWYlvfke 250
Cdd:cd20638  113 wLQSGpcvlVYPEVKRLMFRIAMRIL-LGFEPQ-------QTDREQEQ-QLVEAFEEMIRNLFSLPIdVPFSGLY----- 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 251 grdhkRGLKClHTFTNNVIAERVKERKAEEDwtgagrgpipSKNKRKAFLDLLLSVTDEEGNRLSQEDIREEVDTFMFEG 330
Cdd:cd20638  179 -----RGLRA-RNLIHAKIEENIRAKIQRED----------TEQQCKDALQLLIEHSRRNGEPLNLQALKESATELLFGG 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 331 HDTTAAAINWSLYLLGTNPEVQRKVDQELDE--VFGRSHRP---VTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSED 405
Cdd:cd20638  243 HETTASAATSLIMFLGLHPEVLQKVRKELQEkgLLSTKPNEnkeLSMEVLEQLKYTGCVIKETLRLSPPVPGGFRVALKT 322
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187956757 406 CEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFA 473
Cdd:cd20638  323 FELNGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSRFSFIPFGGGSRSCVGKEFA 390
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
22-474 2.07e-32

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 130.33  E-value: 2.07e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  22 VSLAGATILISIFPMLVSYARKWQQMRsIPSVARAYPLVGHALYMKPNNAEFFQQLIYyteefRHLPIIKLWIGPVPLVA 101
Cdd:PLN03112   6 LSLLFSVLIFNVLIWRWLNASMRKSLR-LPPGPPRWPIVGNLLQLGPLPHRDLASLCK-----KYGPLVYLRLGSVDAIT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 102 LYKAENVEVILTSSKQIDKSFLYKFLQPWLGLGL----LTSTGSKWRTRRK-----MLTPTFhftiLENFLDVMNEQANI 172
Cdd:PLN03112  80 TDDPELIREILLRQDDVFASRPRTLAAVHLAYGCgdvaLAPLGPHWKRMRRicmehLLTTKR----LESFAKHRAEEARH 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 173 LVNK-LEKHVNQEAFNCFFYITLCALDIICETAMGKN-IGAQSNNDSE------YVRTVYRMSDMIYRRMKMP-WLWFDL 243
Cdd:PLN03112 156 LIQDvWEAAQTGKPVNLREVLGAFSMNNVTRMLLGKQyFGAESAGPKEamefmhITHELFRLLGVIYLGDYLPaWRWLDP 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 244 wYLVFKEGRDHKRGLKCLHTftnNVIAERVKERKAEEDwtgagrgpipsKNKRKAFLDLLLSVTDEEGNR-LSQEDIREE 322
Cdd:PLN03112 236 -YGCEKKMREVEKRVDEFHD---KIIDEHRRARSGKLP-----------GGKDMDFVDVLLSLPGENGKEhMDDVEIKAL 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 323 VDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRsHRPVTLEDLKKLKYLDCVIKETLRVFPSVP-LFARS 401
Cdd:PLN03112 301 MQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVGR-NRMVQESDLVHLNYLRCVVRETFRMHPAGPfLIPHE 379
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187956757 402 LSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFP------ENSQGRHpYAYVPFSAGPRNCIGQKFAV 474
Cdd:PLN03112 380 SLRATTINGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERHWPaegsrvEISHGPD-FKILPFSAGKRKCPGAPLGV 457
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
94-501 2.49e-32

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: 128.36  E-value: 2.49e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  94 IGPVPLVALYKAENV-EVILTSSKQIDKSFLYKFLQPWL-GLGLLTSTGSKWRTRRKmltptFHFTILENF-------LD 164
Cdd:cd20672    9 LGPRPVVMLCGTDAIrEALVDQAEAFSGRGTIAVVDPIFqGYGVIFANGERWKTLRR-----FSLATMRDFgmgkrsvEE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 165 VMNEQANILVNKLEKHVNQEAFNCFFYITLCAlDIICETAMGKNIGAQsnnDSEYVRtvyrMSDMIYRRMKMPWLW---- 240
Cdd:cd20672   84 RIQEEAQCLVEELRKSKGALLDPTFLFQSITA-NIICSIVFGERFDYK---DPQFLR----LLDLFYQTFSLISSFssqv 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 241 FDLW--YLVFKEGRdHKRGLKCLHTFtNNVIAERVKERKAEEDwtgagrgpiPSKNKRkaFLDL-LLSVTDEEGNRLSQ- 316
Cdd:cd20672  156 FELFsgFLKYFPGA-HRQIYKNLQEI-LDYIGHSVEKHRATLD---------PSAPRD--FIDTyLLRMEKEKSNHHTEf 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 317 --EDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGrSHRPVTLEDLKKLKYLDCVIKETLRVFPS 394
Cdd:cd20672  223 hhQNLMISVLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIG-SHRLPTLDDRAKMPYTDAVIHEIQRFSDL 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 395 VPL-FARSLSEDCEVGGYKVTKGTEAI-IIPYALHrDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGPRNCIGQKF 472
Cdd:cd20672  302 IPIgVPHRVTKDTLFRGYLLPKNTEVYpILSSALH-DPQYFEQPDTFNPDHFLDANGALKKSEAFMPFSTGKRICLGEGI 380
                        410       420
                 ....*....|....*....|....*....
gi 187956757 473 AVMEEKTILACILRQFWVESNQKREELGL 501
Cdd:cd20672  381 ARNELFLFFTTILQNFSVASPVAPEDIDL 409
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
237-500 3.32e-32

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: 128.22  E-value: 3.32e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 237 PWL-WFDLwylvfkegRDHKRGLKCL----HTFTNNVIAERVKERkaeedwtgaGRGPIPSKNkrkaFLDLLLSVTDEEg 311
Cdd:cd11076  161 PWLrWLDL--------QGIRRRCSALvprvNTFVGKIIEEHRAKR---------SNRARDDED----DVDVLLSLQGEE- 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 312 nRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRShRPVTLEDLKKLKYLDCVIKETLRV 391
Cdd:cd11076  219 -KLSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGS-RRVADSDVAKLPYLQAVVKETLRL 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 392 FPSVPL--FARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPEnsqgrHPYAYV----------P 459
Cdd:cd11076  297 HPPGPLlsWARLAIHDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVAA-----EGGADVsvlgsdlrlaP 371
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 187956757 460 FSAGPRNCIGQKFAVMEEKTILACILRQF-WVESNQKREELG 500
Cdd:cd11076  372 FGAGRRVCPGKALGLATVHLWVAQLLHEFeWLPDDAKPVDLS 413
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
309-510 7.13e-32

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: 127.09  E-value: 7.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 309 EEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGrsHRPVTLEDLKKLKYLDCVIKET 388
Cdd:cd20616  215 QKRGELTAENVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLG--ERDIQNDDLQKLKVLENFINES 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 389 LRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPrYFPDPEEFRPERFfpensQGRHPYAYV-PFSAGPRNC 467
Cdd:cd20616  293 MRYQPVVDFVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENF-----EKNVPSRYFqPFGFGPRSC 366
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 187956757 468 IGQKFAVMEEKTILACILRQFWVESNQKR--EELGLAGDLILRPN 510
Cdd:cd20616  367 VGKYIAMVMMKAILVTLLRRFQVCTLQGRcvENIQKTNDLSLHPD 411
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
88-488 9.62e-32

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: 126.99  E-value: 9.62e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVILTS-----SKQIDKSFLYKFLQpwlGLGLLTSTGSKWR-TRRkmltptFHFTILEN 161
Cdd:cd20665    3 PVFTLYLGMKPTVVLHGYEAVKEALIDlgeefSGRGRFPIFEKVNK---GLGIVFSNGERWKeTRR------FSLMTLRN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 162 F-------LDVMNEQANILVNKLEKhVNQEAFNCFFYITLCALDIICETAMGKNIgaqSNNDSEYVRTVYRMSDMIyRRM 234
Cdd:cd20665   74 FgmgkrsiEDRVQEEARCLVEELRK-TNGSPCDPTFILGCAPCNVICSIIFQNRF---DYKDQDFLNLMEKLNENF-KIL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 235 KMPWLWFdlwYLVFKEGRD-----HKRGLKClHTFTNNVIAERVKERKAEEDWTgagrgpipskNKRKaFLD-LLLSVTD 308
Cdd:cd20665  149 SSPWLQV---CNNFPALLDylpgsHNKLLKN-VAYIKSYILEKVKEHQESLDVN----------NPRD-FIDcFLIKMEQ 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 309 EEGNRLSQ---EDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRsHRPVTLEDLKKLKYLDCVI 385
Cdd:cd20665  214 EKHNQQSEftlENLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGR-HRSPCMQDRSHMPYTDAVI 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 386 KETLRVFPSVPL-FARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGP 464
Cdd:cd20665  293 HEIQRYIDLVPNnLPHAVTCDTKFRNYLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDENGNFKKSDYFMPFSAGK 372
                        410       420
                 ....*....|....*....|....
gi 187956757 465 RNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd20665  373 RICAGEGLARMELFLFLTTILQNF 396
PLN02183 PLN02183
ferulate 5-hydroxylase
259-469 2.05e-31

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 127.27  E-value: 2.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 259 KCLHTFTNNVIAERVKERKAEEDWTGAGRGPIPSKNKRKAFL--DLLLSVTDEEGN--RLSQEDIREEVDTFMFEGHDTT 334
Cdd:PLN02183 241 KSLDGFIDDIIDDHIQKRKNQNADNDSEEAETDMVDDLLAFYseEAKVNESDDLQNsiKLTRDNIKAIIMDVMFGGTETV 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 335 AAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRpVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVT 414
Cdd:PLN02183 321 ASAIEWAMAELMKSPEDLKRVQQELADVVGLNRR-VEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAEDAEVAGYFIP 399
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 187956757 415 KGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENS---QGRHpYAYVPFSAGPRNCIG 469
Cdd:PLN02183 400 KRSRVMINAWAIGRDKNSWEDPDTFKPSRFLKPGVpdfKGSH-FEFIPFGSGRRSCPG 456
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
117-488 4.00e-31

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: 124.91  E-value: 4.00e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 117 QIDKSFLYKFLQP-----WLGLGLLTSTGSKWRTRRKmltptFHFTILENF------LDV-MNEQANILVNKLeKHVNQE 184
Cdd:cd20662   29 TQEQNFMNRPETPlreriFNKNGLIFSSGQTWKEQRR-----FALMTLRNFglgkksLEErIQEECRHLVEAI-REEKGN 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 185 AFNCFFYITLCALDIICETAMGKNIGAQSNNDSEYVR----TVYRMSDMIYRRMK-MPWLwfdLWYL------VFKEGRD 253
Cdd:cd20662  103 PFNPHFKINNAVSNIICSVTFGERFEYHDEWFQELLRlldeTVYLEGSPMSQLYNaFPWI---MKYLpgshqtVFSNWKK 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 254 HKRglkclhtFTNNVIaervkeRKAEEDWTgagrgPIPSKNKRKAFLDLLLSVTDEEGNRLSQEDIREEVDTFmFEGHDT 333
Cdd:cd20662  180 LKL-------FVSDMI------DKHREDWN-----PDEPRDFIDAYLKEMAKYPDPTTSFNEENLICSTLDLF-FAGTET 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 334 TAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPvTLEDLKKLKYLDCVIKETLRVFPSVPL-FARSLSEDCEVGGYK 412
Cdd:cd20662  241 TSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQP-SLADRESMPYTNAVIHEVQRMGNIIPLnVPREVAVDTKLAGFH 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187956757 413 VTKGTeaIIIP--YALHRDPRYFPDPEEFRPERFFpENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd20662  320 LPKGT--MILTnlTALHRDPKEWATPDTFNPGHFL-ENGQFKKREAFLPFSMGKRACLGEQLARSELFIFFTSLLQKF 394
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
255-489 4.99e-31

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: 125.17  E-value: 4.99e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 255 KRGLKCLHTFTNNVIAERVK-----ERKAEEDWtgagrgpipsknkrkafLDLLLSVTDEEGNRL-SQEDIREEVDTFMF 328
Cdd:cd20658  185 REAMRIIRKYHDPIIDERIKqwregKKKEEEDW-----------------LDVFITLKDENGNPLlTPDEIKAQIKELMI 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 329 EGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRShRPVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLS-EDCE 407
Cdd:cd20658  248 AAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKE-RLVQESDIPNLNYVKACAREAFRLHPVAPFNVPHVAmSDTT 326
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 408 VGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQ---GRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACI 484
Cdd:cd20658  327 VGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSEvtlTEPDLRFISFSTGRRGCPGVKLGTAMTVMLLARL 406

                 ....*.
gi 187956757 485 LRQF-W 489
Cdd:cd20658  407 LQGFtW 412
PLN02302 PLN02302
ent-kaurenoic acid oxidase
292-481 5.13e-30

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 122.90  E-value: 5.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 292 SKNKRKAFLDLLLSVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGR---SHR 368
Cdd:PLN02302 261 ISPRKKDMLDLLLDAEDENGRKLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEVLQKAKAEQEEIAKKrppGQK 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 369 PVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFfpEN 448
Cdd:PLN02302 341 GLTLKDVRKMEYLSQVIDETLRLINISLTVFREAKTDVEVNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRW--DN 418
                        170       180       190
                 ....*....|....*....|....*....|...
gi 187956757 449 SQGRhPYAYVPFSAGPRNCIGQKFAVMEEKTIL 481
Cdd:PLN02302 419 YTPK-AGTFLPFGLGSRLCPGNDLAKLEISIFL 450
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
319-491 6.05e-30

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 122.88  E-value: 6.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 319 IREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVTLEDLKKLKYLDCVIKETLRVFPSVPLF 398
Cdd:PLN02426 294 LRDIVVSFLLAGRDTVASALTSFFWLLSKHPEVASAIREEADRVMGPNQEAASFEEMKEMHYLHAALYESMRLFPPVQFD 373
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 399 AR-SLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYF-PDPEEFRPER------FFPENsqgrhPYAYVPFSAGPRNCIGQ 470
Cdd:PLN02426 374 SKfAAEDDVLPDGTFVAKGTRVTYHPYAMGRMERIWgPDCLEFKPERwlkngvFVPEN-----PFKYPVFQAGLRVCLGK 448
                        170       180
                 ....*....|....*....|.
gi 187956757 471 KFAVMEEKTILACILRQFWVE 491
Cdd:PLN02426 449 EMALMEMKSVAVAVVRRFDIE 469
PLN02655 PLN02655
ent-kaurene oxidase
290-489 1.05e-29

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 121.77  E-value: 1.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 290 IPSKNKRKAFLDLLLSvtdeEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGrsHRP 369
Cdd:PLN02655 238 IARGEERDCYLDFLLS----EATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYREIREVCG--DER 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 370 VTLEDLKKLKYLDCVIKETLRVFPSVPLF-ARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPEN 448
Cdd:PLN02655 312 VTEEDLPNLPYLNAVFHETLRKYSPVPLLpPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLGEK 391
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 187956757 449 SQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF-W 489
Cdd:PLN02655 392 YESADMYKTMAFGAGKRVCAGSLQAMLIACMAIARLVQEFeW 433
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
286-488 7.75e-29

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


Pssm-ID: 410754 [Multi-domain]  Cd Length: 436  Bit Score: 118.76  E-value: 7.75e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 286 GRGPIPSKNKRKAFLDLLLSVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGR 365
Cdd:cd20661  206 NRKPQSPRHFIDAYLDEMDQNKNDPESTFSMENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGP 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 366 SHRPvTLEDLKKLKYLDCVIKETLRVFPSVPL-FARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERF 444
Cdd:cd20661  286 NGMP-SFEDKCKMPYTEAVLHEVLRFCNIVPLgIFHATSKDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERF 364
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 187956757 445 FPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd20661  365 LDSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLFFTALLQRF 408
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
98-480 7.90e-29

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: 118.78  E-value: 7.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  98 PLVALYKAENVEVILTSSKQIDKSFLYKFLQPWLGLG-LLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQANILVNK 176
Cdd:cd20636   34 PVIRVTGAENIRKILLGEHTLVSTQWPQSTRILLGSNtLLNSVGELHRQRRKVLARVFSRAALESYLPRIQDVVRSEVRG 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 177 LEKHVNQ-EAFNCFFYITLCaldIICETAMGknIGAQSNNDSEYVRTVYRMSDMIYR-RMKMPwlwfdlwylvFKEGRDH 254
Cdd:cd20636  114 WCRGPGPvAVYTAAKSLTFR---IAVRILLG--LRLEEQQFTYLAKTFEQLVENLFSlPLDVP----------FSGLRKG 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 255 KRGLKCLHTFTNNVIAERVKERKAEEDWTGagrgpipsknkrkafLDLLLSVTDEEGNRLSQEDIREEVDTFMFEGHDTT 334
Cdd:cd20636  179 IKARDILHEYMEKAIEEKLQRQQAAEYCDA---------------LDYMIHSARENGKELTMQELKESAVELIFAAFSTT 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 335 AAAINWSLYLLGTNPEVQRKVDQELD-EVFGRSHR----PVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVG 409
Cdd:cd20636  244 ASASTSLVLLLLQHPSAIEKIRQELVsHGLIDQCQccpgALSLEKLSRLRYLDCVVKEVLRLLPPVSGGYRTALQTFELD 323
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187956757 410 GYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHP-YAYVPFSAGPRNCIGQKFAVMEEKTI 480
Cdd:cd20636  324 GYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEREESKSGrFNYIPFGGGVRSCIGKELAQVILKTL 395
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
323-488 4.05e-28

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: 116.36  E-value: 4.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 323 VDTFMfEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGrSHRPVTLEDLKKLKYLDCVIKETLRVFPSVPL-FARS 401
Cdd:cd20674  232 VDLFI-GGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLG-PGASPSYKDRARLPLLNATIAEVLRLRPVVPLaLPHR 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 402 LSEDCEVGGYKVTKGTeaIIIP--YALHRDPRYFPDPEEFRPERFFpenSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKT 479
Cdd:cd20674  310 TTRDSSIAGYDIPKGT--VVIPnlQGAHLDETVWEQPHEFRPERFL---EPGAANRALLPFGCGARVCLGEPLARLELFV 384

                 ....*....
gi 187956757 480 ILACILRQF 488
Cdd:cd20674  385 FLARLLQAF 393
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
88-513 1.51e-27

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: 114.81  E-value: 1.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVILTSSKQIDKSFLykfLQPWLG--------LGLLTSTGSKWRTRRKML-TPTFHFTI 158
Cdd:cd20643    6 PIYREKIGYYESVNIINPEDAAILFKSEGMFPERLS---VPPWVAyrdyrkrkYGVLLKNGEAWRKDRLILnKEVLAPKV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 159 LENFLDVMNEQANILVNKLEKHVNQ--------EAFNCFFYItlcALDIICETAMGKNIGA-QSNNDSEYVRTVYRMSDM 229
Cdd:cd20643   83 IDNFVPLLNEVSQDFVSRLHKRIKKsgsgkwtaDLSNDLFRF---ALESICNVLYGERLGLlQDYVNPEAQRFIDAITLM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 230 IYRRMKMPWLWFDLWYLV-FKEGRDHKRGLKCLHT----FTNNVIAERVKERKAEEDWTGAgrgpipsknkrkaFLDLLL 304
Cdd:cd20643  160 FHTTSPMLYIPPDLLRLInTKIWRDHVEAWDVIFNhadkCIQNIYRDLRQKGKNEHEYPGI-------------LANLLL 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 305 SvtdeegNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSH-RPVTLedLKKLKYLDC 383
Cdd:cd20643  227 Q------DKLPIEDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLAARQEAQgDMVKM--LKSVPLLKA 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 384 VIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFP-ENSQGRHpyayVPFSA 462
Cdd:cd20643  299 AIKETLRLHPVAVSLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSkDITHFRN----LGFGF 374
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 187956757 463 GPRNCIGQKFAVMEEKTILACILRQFWVESnQKREELGLAGDLILRPNNGI 513
Cdd:cd20643  375 GPRQCLGRRIAETEMQLFLIHMLENFKIET-QRLVEVKTTFDLILVPEKPI 424
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
294-476 2.67e-27

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


Pssm-ID: 410707 [Multi-domain]  Cd Length: 406  Bit Score: 113.69  E-value: 2.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 294 NKRKAFLDLLLSVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVdqeLDEVFGRSHRPVTLE 373
Cdd:cd20614  184 GARTGLVAALIRARDDNGAGLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDAL---CDEAAAAGDVPRTPA 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 374 DLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFpENSQGRH 453
Cdd:cd20614  261 ELRRFPLAEALFRETLRLHPPVPFVFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWL-GRDRAPN 339
                        170       180
                 ....*....|....*....|...
gi 187956757 454 PYAYVPFSAGPRNCIGQKFAVME 476
Cdd:cd20614  340 PVELLQFGGGPHFCLGYHVACVE 362
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
256-488 3.29e-27

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: 113.64  E-value: 3.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 256 RGLKCLHTFTNNVIAERvkerkaEEDWTGAGrgpiPSKNKRKAFLDLLLSVTDEEGNRLSQEDIREEVDTFMFEGHDTTA 335
Cdd:cd20663  178 PGQKAFLALLDELLTEH------RTTWDPAQ----PPRDLTDAFLAEMEKAKGNPESSFNDENLRLVVADLFSAGMVTTS 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 336 AAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPvTLEDLKKLKYLDCVIKETLRVFPSVPL-FARSLSEDCEVGGYKVT 414
Cdd:cd20663  248 TTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRP-EMADQARMPYTNAVIHEVQRFGDIVPLgVPHMTSRDIEVQGFLIP 326
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187956757 415 KGTEAIIIPYALHRDPRYFPDPEEFRPERFFpeNSQGR--HPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd20663  327 KGTTLITNLSSVLKDETVWEKPLRFHPEHFL--DAQGHfvKPEAFMPFSAGRRACLGEPLARMELFLFFTCLLQRF 400
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
315-475 5.86e-27

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: 112.73  E-value: 5.86e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 315 SQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVTLEDLKKLKYLDCVIKETLRVFPS 394
Cdd:cd11082  217 SDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDEPPLTLDLLEEMKYTRQVVKEVLRYRPP 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 395 VPLFARSLSEDCEVG-GYKVTKGTeaIIIP--YALHRDPryFPDPEEFRPERFFPENSQGR-HPYAYVPFSAGPRNCIGQ 470
Cdd:cd11082  297 APMVPHIAKKDFPLTeDYTVPKGT--IVIPsiYDSCFQG--FPEPDKFDPDRFSPERQEDRkYKKNFLVFGAGPHQCVGQ 372

                 ....*
gi 187956757 471 KFAVM 475
Cdd:cd11082  373 EYAIN 377
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
88-498 1.12e-26

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: 111.99  E-value: 1.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  88 PIIKLWIGPVPLVALYKAENVEVILTSS----KQIDKSFLYKFLQpWLG--LGLLTstGSKWRTRRKMLTPTFHFTILEN 161
Cdd:cd20615    2 PIYRIWSGPTPEIVLTTPEHVKEFYRDSnkhhKAPNNNSGWLFGQ-LLGqcVGLLS--GTDWKRVRKVFDPAFSHSAAVY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 162 FLDVMNEQANILVNKLEKHVNQE-------AFNCFFYitlcALDIICETAMGKnigAQSNNDSEYVRTVYRMSDMiyrrm 234
Cdd:cd20615   79 YIPQFSREARKWVQNLPTNSGDGrrfvidpAQALKFL----PFRVIAEILYGE---LSPEEKEELWDLAPLREEL----- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 235 kMPWLWFDLWYLvFKEGR----DHKRGLKCLHTFTNNV---IAERVKERKAEEdwtgagrgPIPSknkrkafldllLSVT 307
Cdd:cd20615  147 -FKYVIKGGLYR-FKISRylptAANRRLREFQTRWRAFnlkIYNRARQRGQST--------PIVK-----------LYEA 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 308 DEEGNrLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVfgRSHRPVTLED--LKKLKYLDCVI 385
Cdd:cd20615  206 VEKGD-ITFEELLQTLDEMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEISAA--REQSGYPMEDyiLSTDTLLAYCV 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 386 KETLRVFP----SVPlfaRSLSEDCEVGGYKVTKGTEAIIIPYAL-HRDPRYFPDPEEFRPERFF-PENSQGRhpYAYVP 459
Cdd:cd20615  283 LESLRLRPllafSVP---ESSPTDKIIGGYRIPANTPVVVDTYALnINNPFWGPDGEAYRPERFLgISPTDLR--YNFWR 357
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 187956757 460 FSAGPRNCIGQKFAVMEEKTILACILRQFWVE--SNQKREE 498
Cdd:cd20615  358 FGFGPRKCLGQHVADVILKALLAHLLEQYELKlpDQGENEE 398
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
127-509 1.17e-26

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: 112.24  E-value: 1.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 127 LQPWLG--------LGLLTSTGSKWRTRRKMLTP-TFHFTILENFLDVMNEQANILVNKLEKHVNQEAFNCF-------- 189
Cdd:cd20644   42 LEPWVAhrqhrghkCGVFLLNGPEWRFDRLRLNPeVLSPAAVQRFLPMLDAVARDFSQALKKRVLQNARGSLtldvqpdl 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 190 FYITLCAldiICETAMGKNIGAQS---NNDSE-YVRTVYRMSDMIYRRMKMP-----WLWFDLWylvfkegRDHKRGLKC 260
Cdd:cd20644  122 FRFTLEA---SNLALYGERLGLVGhspSSASLrFISAVEVMLKTTVPLLFMPrslsrWISPKLW-------KEHFEAWDC 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 261 LHTFTNNVIAERVKERKAEEDWTGAGrgpipsknkrkAFLDLLLSVtdeegnRLSQEDIREEVDTFMFEGHDTTAAAINW 340
Cdd:cd20644  192 IFQYADNCIQKIYQELAFGRPQHYTG-----------IVAELLLQA------ELSLEAIKANITELTAGGVDTTAFPLLF 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 341 SLYLLGTNPEVQRKVDQELDEVFGRSHRPVtLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAI 420
Cdd:cd20644  255 TLFELARNPDVQQILRQESLAAAAQISEHP-QKALTELPLLKAALKETLRLYPVGITVQRVPSSDLVLQNYHIPAGTLVQ 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 421 IIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYAyVPFSAGPRNCIGQKFAVMEEKTILACILRQFWVESNQKrEELG 500
Cdd:cd20644  334 VFLYSLGRSAALFPRPERYDPQRWLDIRGSGRNFKH-LAFGFGMRQCLGRRLAEAEMLLLLMHVLKNFLVETLSQ-EDIK 411

                 ....*....
gi 187956757 501 LAGDLILRP 509
Cdd:cd20644  412 TVYSFILRP 420
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
261-485 2.08e-25

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 109.44  E-value: 2.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 261 LHTFTNNVIAERVKERKAeedwtgagrgPIPSKNKRKAFLDLLLSVtdEEGNRLSQEDIREEVDTFMFEGHDTTAAAINW 340
Cdd:PLN02394 248 LALFKDYFVDERKKLMSA----------KGMDKEGLKCAIDHILEA--QKKGEINEDNVLYIVENINVAAIETTLWSIEW 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 341 SLYLLGTNPEVQRKVDQELDEVFGRSHrPVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLS-EDCEVGGYKVTKGTEA 419
Cdd:PLN02394 316 GIAELVNHPEIQKKLRDELDTVLGPGN-QVTEPDTHKLPYLQAVVKETLRLHMAIPLLVPHMNlEDAKLGGYDIPAESKI 394
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187956757 420 IIIPYALHRDPRYFPDPEEFRPERFFPENSQGR---HPYAYVPFSAGPRNCIGQKFAVmeekTILACIL 485
Cdd:PLN02394 395 LVNAWWLANNPELWKNPEEFRPERFLEEEAKVEangNDFRFLPFGVGRRSCPGIILAL----PILGIVL 459
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
285-488 2.68e-25

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


Pssm-ID: 410764 [Multi-domain]  Cd Length: 422  Bit Score: 107.96  E-value: 2.68e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 285 AGRGPIPSkNKRKAFLDLLLSVTDEE--GNRLSQED--IREEVDTFMfEGHDTTAAAINWSLYLLGTNPEVQRKVDQELD 360
Cdd:cd20671  188 ARRPTIDG-NPLHSYIEALIQKQEEDdpKETLFHDAnvLACTLDLVM-AGTETTSTTLQWAVLLMMKYPHIQKRVQEEID 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 361 EVFGrSHRPVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFR 440
Cdd:cd20671  266 RVLG-PGCLPNYEDRKALPYTSAVIHEVQRFITLLPHVPRCTAADTQFKGYLIPKGTPVIPLLSSVLLDKTQWETPYQFN 344
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 187956757 441 PERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd20671  345 PNHFLDAEGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKF 392
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
332-469 1.49e-24

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: 106.02  E-value: 1.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 332 DTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHrPVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLS-EDCEVGG 410
Cdd:cd11074  247 ETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGV-QITEPDLHKLPYLQAVVKETLRLRMAIPLLVPHMNlHDAKLGG 325
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187956757 411 YKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGR---HPYAYVPFSAGPRNCIG 469
Cdd:cd11074  326 YDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEESKVEangNDFRYLPFGVGRRSCPG 387
PLN02971 PLN02971
tryptophan N-hydroxylase
264-499 1.75e-24

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 107.05  E-value: 1.75e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 264 FTNNVIAERVKErkaeedWTGAGRGPIpsknkrKAFLDLLLSVTDEEGNRL-SQEDIREEVDTFMFEGHDTTAAAINWSL 342
Cdd:PLN02971 284 YHDPIIDERIKM------WREGKRTQI------EDFLDIFISIKDEAGQPLlTADEIKPTIKELVMAAPDNPSNAVEWAM 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 343 YLLGTNPEVQRKVDQELDEVFGRsHRPVTLEDLKKLKYLDCVIKETLRVFP----SVPLFARSlseDCEVGGYKVTKGTE 418
Cdd:PLN02971 352 AEMINKPEILHKAMEEIDRVVGK-ERFVQESDIPKLNYVKAIIREAFRLHPvaafNLPHVALS---DTTVAGYHIPKGSQ 427
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 419 AIIIPYALHRDPRYFPDPEEFRPERFFPENSQ---GRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF-W-VESN 493
Cdd:PLN02971 428 VLLSRYGLGRNPKVWSDPLSFKPERHLNECSEvtlTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFkWkLAGS 507

                 ....*.
gi 187956757 494 QKREEL 499
Cdd:PLN02971 508 ETRVEL 513
PLN02966 PLN02966
cytochrome P450 83A1
143-488 3.16e-24

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 105.98  E-value: 3.16e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 143 WRTRRKM-LTPTFHFTILENFLDVMNEQANILVNKLEKHVNQ-EAFNCFFYITLCALDIICETAMGKNIGAQSNNDSEYV 220
Cdd:PLN02966 123 YREIRKMgMNHLFSPTRVATFKHVREEEARRMMDKINKAADKsEVVDISELMLTFTNSVVCRQAFGKKYNEDGEEMKRFI 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 221 RTVYRMSDM---IYRRMKMPWLWF--DLWYLVFKEGRDHKRGlkclHTFTNNVIAERVKERKAeedwtgagrgpipsKNK 295
Cdd:PLN02966 203 KILYGTQSVlgkIFFSDFFPYCGFldDLSGLTAYMKECFERQ----DTYIQEVVNETLDPKRV--------------KPE 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 296 RKAFLDLLLSVTDEE--GNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRP-VTL 372
Cdd:PLN02966 265 TESMIDLLMEIYKEQpfASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEKGSTfVTE 344
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 373 EDLKKLKYLDCVIKETLRVFPSVPLF-ARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPR-YFPDPEEFRPERFFPENSQ 450
Cdd:PLN02966 345 DDVKNLPYFRALVKETLRIEPVIPLLiPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKeWGPNPDEFRPERFLEKEVD 424
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 187956757 451 GRHP-YAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:PLN02966 425 FKGTdYEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNF 463
PLN00168 PLN00168
Cytochrome P450; Provisional
24-497 4.52e-24

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 105.42  E-value: 4.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  24 LAGATILISIFPMLV---SYARKWQQMRSIPSVARAYPLVGHALYMKPNNAEFFQQLIYYTEefRHLPIIKLWIGPVPLV 100
Cdd:PLN00168   7 LLLAALLLLPLLLLLlgkHGGRGGKKGRRLPPGPPAVPLLGSLVWLTNSSADVEPLLRRLIA--RYGPVVSLRVGSRLSV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 101 ALYKAENVEVILTSSKQIDKSFLYKFLQPWLGLGLLT----STGSKWRT-RRKMLTPTFHFTILENFLDVMNEQANILVN 175
Cdd:PLN00168  85 FVADRRLAHAALVERGAALADRPAVASSRLLGESDNTitrsSYGPVWRLlRRNLVAETLHPSRVRLFAPARAWVRRVLVD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 176 KL----EKHVNQEAFNCFFYITLCALDIICetamgknIGAQSNNDSEYVRTVYRMSDMIYRRMKMPWLWF------DLWY 245
Cdd:PLN00168 165 KLrreaEDAAAPRVVETFQYAMFCLLVLMC-------FGERLDEPAVRAIAAAQRDWLLYVSKKMSVFAFfpavtkHLFR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 246 LVFKEGRDHKRGLKCLhtFTNNVIAERVKERKAEEdwtgAGRGPIPSKNKRKAFLDLLLSVT-DEEGNR-LSQEDIREEV 323
Cdd:PLN00168 238 GRLQKALALRRRQKEL--FVPLIDARREYKNHLGQ----GGEPPKKETTFEHSYVDTLLDIRlPEDGDRaLTDDEIVNLC 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 324 DTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVTLEDLKKLKYLDCVIKETLRVFPsvP---LFAR 400
Cdd:PLN00168 312 SEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDDQEEVSEEDVHKMPYLKAVVLEGLRKHP--PahfVLPH 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 401 SLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPE------NSQGRHPYAYVPFSAGPRNCIGQKFAV 474
Cdd:PLN00168 390 KAAEDMEVGGYLIPKGATVNFMVAEMGRDEREWERPMEFVPERFLAGgdgegvDVTGSREIRMMPFGVGRRICAGLGIAM 469
                        490       500       510
                 ....*....|....*....|....*....|.
gi 187956757 475 MEEKTILACILRQF-W-------VESNQKRE 497
Cdd:PLN00168 470 LHLEYFVANMVREFeWkevpgdeVDFAEKRE 500
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
307-519 8.00e-24

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


Pssm-ID: 410769 [Multi-domain]  Cd Length: 437  Bit Score: 103.94  E-value: 8.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 307 TDEEGN-RLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVtLEDLKKLKYLDCVI 385
Cdd:cd20676  225 LDENANiQLSDEKIVNIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPR-LSDRPQLPYLEAFI 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 386 KETLRVFPSVPL-FARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQG---RHPYAYVPFS 461
Cdd:cd20676  304 LETFRHSSFVPFtIPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLTADGTEinkTESEKVMLFG 383
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 462 AGPRNCIGQKFAVMEEKTILACILRQ--FWVESNQKreelglagdLILRPNNGIWIKLKR 519
Cdd:cd20676  384 LGKRRCIGESIARWEVFLFLAILLQQleFSVPPGVK---------VDMTPEYGLTMKHKR 434
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
314-491 1.03e-23

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: 103.60  E-value: 1.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 314 LSQEDI-REEVdTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVTLEDLKKLK----YLDCVIKET 388
Cdd:cd11040  219 LSEEDIaRAEL-ALLWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTNAILDLTDLLtscpLLDSTYLET 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 389 LRvFPSVPLFARSLSEDC-EVGGYKVTKGTEAIIIPYALHRDPRYF-PDPEEFRPERFFPENSQG---RHPYAYVPFSAG 463
Cdd:cd11040  298 LR-LHSSSTSVRLVTEDTvLGGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFLKKDGDKkgrGLPGAFRPFGGG 376
                        170       180
                 ....*....|....*....|....*...
gi 187956757 464 PRNCIGQKFAVMEEKTILACILRQFWVE 491
Cdd:cd11040  377 ASLCPGRHFAKNEILAFVALLLSRFDVE 404
PLN03018 PLN03018
homomethionine N-hydroxylase
240-488 1.93e-23

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 103.55  E-value: 1.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 240 WFDLWYLVFKEGRdHKRGLKCLHTFTNNVIAERVK------ERKAEEDWtgagrgpipsknkrkafLDLLLSVTDEEGNR 313
Cdd:PLN03018 247 WLRGWNIDGQEER-AKVNVNLVRSYNNPIIDERVElwrekgGKAAVEDW-----------------LDTFITLKDQNGKY 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 314 L-SQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRShRPVTLEDLKKLKYLDCVIKETLRVF 392
Cdd:PLN03018 309 LvTPDEIKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGKD-RLVQESDIPNLNYLKACCRETFRIH 387
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 393 PSV----PLFARslsEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFF------PENSQGRHPYAYVPFSA 462
Cdd:PLN03018 388 PSAhyvpPHVAR---QDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHLqgdgitKEVTLVETEMRFVSFST 464
                        250       260
                 ....*....|....*....|....*.
gi 187956757 463 GPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:PLN03018 465 GRRGCVGVKVGTIMMVMMLARFLQGF 490
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
50-488 2.13e-23

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 103.23  E-value: 2.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  50 IPSVARAYPLVGHALYMKPNNAEFFqqLIYYTEEFRhlPIIKLWIGPVPLVALYKAENV-EVILTSSKQIDKSFLYKFLQ 128
Cdd:PLN03234  29 LPPGPKGLPIIGNLHQMEKFNPQHF--LFRLSKLYG--PIFTMKIGGRRLAVISSAELAkELLKTQDLNFTARPLLKGQQ 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 129 PW------LGLGLLTSTgskWRTRRKM-LTPTFHFTILENFLDVMNEQANILVNKLEKHVNQEAF----NCFFYITLCal 197
Cdd:PLN03234 105 TMsyqgreLGFGQYTAY---YREMRKMcMVNLFSPNRVASFRPVREEECQRMMDKIYKAADQSGTvdlsELLLSFTNC-- 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 198 dIICETAMGKNIgaqsnndSEYVRTVYRMSDMIYRRMKMPWLWF--DLW-YLVFKEGRDH-----KRGLKCLHTFTNNVI 269
Cdd:PLN03234 180 -VVCRQAFGKRY-------NEYGTEMKRFIDILYETQALLGTLFfsDLFpYFGFLDNLTGlsarlKKAFKELDTYLQELL 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 270 AERVKerkaeedwtgagrgPIPSKNKRKAFLDLLLSVTDEE--GNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGT 347
Cdd:PLN03234 252 DETLD--------------PNRPKQETESFIDLLMQIYKDQpfSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIK 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 348 NPEVQRKVDQELDEVFGRSHRpVTLEDLKKLKYLDCVIKETLRVFPSVP-LFARSLSEDCEVGGYKVTKGTEAIIIPYAL 426
Cdd:PLN03234 318 YPEAMKKAQDEVRNVIGDKGY-VSEEDIPNLPYLKAVIKESLRLEPVIPiLLHRETIADAKIGGYDIPAKTIIQVNAWAV 396
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187956757 427 HRDPRYFPD-PEEFRPERFFPENS----QGRHpYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:PLN03234 397 SRDTAAWGDnPNEFIPERFMKEHKgvdfKGQD-FELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKF 462
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
301-476 4.28e-22

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 99.24  E-value: 4.28e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 301 DLLLS-VTDEEGnrLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVF--GRSHRPVTLEDLKK 377
Cdd:PLN02196 248 DLLGSfMGDKEG--LTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRkdKEEGESLTWEDTKK 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 378 LKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFfpenSQGRHPYAY 457
Cdd:PLN02196 326 MPLTSRVIQETLRVASILSFTFREAVEDVEYEGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRF----EVAPKPNTF 401
                        170
                 ....*....|....*....
gi 187956757 458 VPFSAGPRNCIGQKFAVME 476
Cdd:PLN02196 402 MPFGNGTHSCPGNELAKLE 420
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
258-518 4.46e-22

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: 98.63  E-value: 4.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 258 LKCLHTFT---NNVIAERVKERKAEEDwtgagrgpipsKNKRKAFLDLLLSVTDE-----EGNRLSQEDIREEVDTFMFE 329
Cdd:cd20677  179 LKALRKFIsrlNNFIAKSVQDHYATYD-----------KNHIRDITDALIALCQErkaedKSAVLSDEQIISTVNDIFGA 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 330 GHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRShRPVTLEDLKKLKYLDCVIKETLRVFPSVPL-FARSLSEDCEV 408
Cdd:cd20677  248 GFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLS-RLPRFEDRKSLHYTEAFINEVFRHSSFVPFtIPHCTTADTTL 326
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 409 GGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYA--YVPFSAGPRNCIGQKFAVMEEKTILACILR 486
Cdd:cd20677  327 NGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQLNKSLVekVLIFGMGVRKCLGEDVARNEIFVFLTTILQ 406
                        250       260       270
                 ....*....|....*....|....*....|..
gi 187956757 487 QFWVESNQKREelglagdLILRPNNGIWIKLK 518
Cdd:cd20677  407 QLKLEKPPGQK-------LDLTPVYGLTMKPK 431
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
228-488 1.26e-21

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 97.77  E-value: 1.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 228 DMIYRRMKMPWLwfdLWYLVFKEGRDHKRGLKCLHTFTNNVIAERVKERKAEEdwTGAGRGPIPSKNKRKAFLDLllsvt 307
Cdd:PLN02169 217 EAIYYRHFKPVI---LWRLQNWIGIGLERKMRTALATVNRMFAKIISSRRKEE--ISRAETEPYSKDALTYYMNV----- 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 308 DEEGNRLSQED----IREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRshrpvtlEDLKKLKYLDC 383
Cdd:PLN02169 287 DTSKYKLLKPKkdkfIRDVIFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEINTKFDN-------EDLEKLVYLHA 359
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 384 VIKETLRVFPSVPLFARSLSE-DCEVGGYKVTKGTEAIIIPYALHR-DPRYFPDPEEFRPERFFPENSQGRH--PYAYVP 459
Cdd:PLN02169 360 ALSESMRLYPPLPFNHKAPAKpDVLPSGHKVDAESKIVICIYALGRmRSVWGEDALDFKPERWISDNGGLRHepSYKFMA 439
                        250       260
                 ....*....|....*....|....*....
gi 187956757 460 FSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:PLN02169 440 FNSGPRTCLGKHLALLQMKIVALEIIKNY 468
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
340-488 4.48e-21

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: 95.46  E-value: 4.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 340 WSLYLLGTNPEVQRKVDQELDEVFGR---SHRPVTLEDLKKLKYLDCVIKETLRVfPSVPLFARSLSEDCEVGGYKVTKG 416
Cdd:cd20635  232 WTLAFILSHPSVYKKVMEEISSVLGKagkDKIKISEDDLKKMPYIKRCVLEAIRL-RSPGAITRKVVKPIKIKNYTIPAG 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 417 TEAIIIPYALHRDPRYFPDPEEFRPERF---------FPEnsqgrhpyAYVPFSAGPRNCIGQKFAVMEEKTILACILRQ 487
Cdd:cd20635  311 DMLMLSPYWAHRNPKYFPDPELFKPERWkkadleknvFLE--------GFVAFGGGRYQCPGRWFALMEIQMFVAMFLYK 382

                 .
gi 187956757 488 F 488
Cdd:cd20635  383 Y 383
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
311-476 1.71e-20

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: 93.92  E-value: 1.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 311 GNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPvTLEDLKKLKYLDCVIKETLR 390
Cdd:cd20675  228 GVGLDKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLP-CIEDQPNLPYVMAFLYEAMR 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 391 vFPS-VPL-FARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYA--YVPFSAGPRN 466
Cdd:cd20675  307 -FSSfVPVtIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDENGFLNKDLAssVMIFSVGKRR 385
                        170
                 ....*....|
gi 187956757 467 CIGQKFAVME 476
Cdd:cd20675  386 CIGEELSKMQ 395
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
294-481 1.79e-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: 93.92  E-value: 1.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 294 NKRKAFLDLLLSVTDEEGNR------------------LSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNP--EVQR 353
Cdd:cd11066  186 NRRDKYLKKLLAKLKEEIEDgtdkpcivgnilkdkeskLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPgqEIQE 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 354 KVDQELDEVFGRSH----RPVTLEdlkKLKYLDCVIKETLRVFPSVPL-FARSLSEDCEVGGYKVTKGTEAIIIPYALHR 428
Cdd:cd11066  266 KAYEEILEAYGNDEdaweDCAAEE---KCPYVVALVKETLRYFTVLPLgLPRKTTKDIVYNGAVIPAGTILFMNAWAANH 342
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 187956757 429 DPRYFPDPEEFRPERFFPENSQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTIL 481
Cdd:cd11066  343 DPEHFGDPDEFIPERWLDASGDLIPGPPHFSFGAGSRMCAGSHLANRELYTAI 395
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
267-519 2.17e-20

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: 93.51  E-value: 2.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 267 NVIAERVKERKAEEDwtgagrgpIPSKNKRKAFLDLLLSVTDEEGNRlsqeDIREEVDTFM---FEGHDTTAAAINWSLY 343
Cdd:cd11041  185 PLIIPEIERRRKLKK--------GPKEDKPNDLLQWLIEAAKGEGER----TPYDLADRQLalsFAAIHTTSMTLTHVLL 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 344 LLGTNPEVQRKVDQELDEVFGrSHRPVTLEDLKKLKYLDCVIKETLRVFPSVPL-FARSLSEDceVG---GYKVTKGTEA 419
Cdd:cd11041  253 DLAAHPEYIEPLREEIRSVLA-EHGGWTKAALNKLKKLDSFMKESQRLNPLSLVsLRRKVLKD--VTlsdGLTLPKGTRI 329
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 420 IIIPYALHRDPRYFPDPEEFRPERFFPENSQG----RHPYA-----YVPFSAGPRNCIGQKFAVMEEKTILACILRQF-- 488
Cdd:cd11041  330 AVPAHAIHRDPDIYPDPETFDGFRFYRLREQPgqekKHQFVstspdFLGFGHGRHACPGRFFASNEIKLILAHLLLNYdf 409
                        250       260       270
                 ....*....|....*....|....*....|..
gi 187956757 489 -WVESNQKREELGLAGDLILRPNNGIWIKLKR 519
Cdd:cd11041  410 kLPEGGERPKNIWFGEFIMPDPNAKVLVRRRE 441
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
334-513 3.19e-20

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: 93.13  E-value: 3.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 334 TAAAINWSLYLLGTNPEVQRKVDQELDEVFG------RSHRPVTL--EDLKKLKYLDCVIKETLRvFPSVPLFARSLSED 405
Cdd:cd20632  231 TIPATFWAMYYLLRHPEALAAVRDEIDHVLQstgqelGPDFDIHLtrEQLDSLVYLESAINESLR-LSSASMNIRVVQED 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 406 C-----EVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERF---------FPENSQgRHPYAYVPFSAGPRNCIGQK 471
Cdd:cd20632  310 FtlkleSDGSVNLRKGDIVALYPQSLHMDPEIYEDPEVFKFDRFvedgkkkttFYKRGQ-KLKYYLMPFGSGSSKCPGRF 388
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 187956757 472 FAVMEEKTILACILRQFWVESNQKREELGL----AGDLILRPNNGI 513
Cdd:cd20632  389 FAVNEIKQFLSLLLLYFDLELLEEQKPPGLdnsrAGLGILPPNSDV 434
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
300-480 5.38e-20

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: 92.22  E-value: 5.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 300 LDLLLSVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELdevfgRSH----------RP 369
Cdd:cd20637  208 LDILIESAKEHGKELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREEL-----RSNgilhngclceGT 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 370 VTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENS 449
Cdd:cd20637  283 LRLDTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFELDGFQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRFGQERS 362
                        170       180       190
                 ....*....|....*....|....*....|..
gi 187956757 450 QGRH-PYAYVPFSAGPRNCIGQKFAVMEEKTI 480
Cdd:cd20637  363 EDKDgRFHYLPFGGGVRTCLGKQLAKLFLKVL 394
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
273-496 8.02e-20

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 92.35  E-value: 8.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 273 VKERKAEEDwtgagrgpiPSKNKRKAFLDLLLSVTDEegnrLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQ 352
Cdd:PLN02987 235 VMKRRKEEE---------EGAEKKKDMLAALLASDDG----FSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLAL 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 353 RKVDQELDEVFGRSHRPVTLE--DLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDP 430
Cdd:PLN02987 302 AQLKEEHEKIRAMKSDSYSLEwsDYKSMPFTQCVVNETLRVANIIGGIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDH 381
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187956757 431 RYFPDPEEFRPERfFPENSQGRHP-YAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF-WVESNQKR 496
Cdd:PLN02987 382 EYFKDARTFNPWR-WQSNSGTTVPsNVFTPFGGGPRLCPGYELARVALSVFLHRLVTRFsWVPAEQDK 448
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
268-515 1.71e-19

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: 90.65  E-value: 1.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 268 VIAERVKERKaeedwtgaGRGPipsknKRKAFLDLLLsvtdeEGNrLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGT 347
Cdd:cd20627  171 VLKKVIKERK--------GKNF-----SQHVFIDSLL-----QGN-LSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTT 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 348 NPEVQRKVDQELDEVFGRShrPVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTeaiIIPYALH 427
Cdd:cd20627  232 SEEVQKKLYKEVDQVLGKG--PITLEKIEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQHIIPKET---LVLYALG 306
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 428 ---RDPRYFPDPEEFRPERFFPENSQgrHPYAYVPFSaGPRNCIGQKFAVMEEKTILACILRQFWVESNQkREELGLAGD 504
Cdd:cd20627  307 vvlQDNTTWPLPYRFDPDRFDDESVM--KSFSLLGFS-GSQECPELRFAYMVATVLLSVLVRKLRLLPVD-GQVMETKYE 382
                        250
                 ....*....|.
gi 187956757 505 LILRPNNGIWI 515
Cdd:cd20627  383 LVTSPREEAWI 393
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
295-488 6.83e-19

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: 88.39  E-value: 6.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 295 KRKA----FLDLLLSVTDEEGnRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEvQRKV---DQELdevfgrsh 367
Cdd:cd11031  180 RRAEpgddLLSALVAARDDDD-RLSEEELVTLAVGLLVAGHETTASQIGNGVLLLLRHPE-QLARlraDPEL-------- 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 368 RPVTLEdlkklkyldcvikETLRVFP--SVPLFARSLSEDCEVGGYKVTKGtEAIIIPY-ALHRDPRYFPDPEEFRPERf 444
Cdd:cd11031  250 VPAAVE-------------ELLRYIPlgAGGGFPRYATEDVELGGVTIRAG-EAVLVSLnAANRDPEVFPDPDRLDLDR- 314
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 187956757 445 fPENSqgrHpyayVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd11031  315 -EPNP---H----LAFGHGPHHCLGAPLARLELQVALGALLRRL 350
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
301-488 1.47e-18

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: 87.22  E-value: 1.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 301 DLL--LSVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEvqrkvdqELDEVfgRSHrPVTLEDlkkl 378
Cdd:cd20625  182 DLIsaLVAAEEDGDRLSEDELVANCILLLVAGHETTVNLIGNGLLALLRHPE-------QLALL--RAD-PELIPA---- 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 379 kyldcVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERffpenSQGRHpyayV 458
Cdd:cd20625  248 -----AVEELLRYDSPVQLTARVALEDVEIGGQTIPAGDRVLLLLGAANRDPAVFPDPDRFDITR-----APNRH----L 313
                        170       180       190
                 ....*....|....*....|....*....|
gi 187956757 459 PFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd20625  314 AFGAGIHFCLGAPLARLEAEIALRALLRRF 343
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
302-488 4.30e-18

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: 86.12  E-value: 4.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 302 LLLSVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKV--DQELDEVFgrshrpvtledlkklk 379
Cdd:cd11078  193 DLLAAADGDGERLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLraDPSLIPNA---------------- 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 380 yldcvIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERffpENsQGRHpyayVP 459
Cdd:cd11078  257 -----VEETLRYDSPVQGLRRTATRDVEIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR---PN-ARKH----LT 323
                        170       180
                 ....*....|....*....|....*....
gi 187956757 460 FSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd11078  324 FGHGIHFCLGAALARMEARIALEELLRRL 352
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
97-488 5.83e-18

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: 85.43  E-value: 5.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757  97 VPLVALYKAENVEVILTSSKQIDKSFLYK-FLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQ-ANILV 174
Cdd:cd20629    9 RGVYVLLRHDDVMAVLRDPRTFSSETYDAtLGGPFLGHSILAMDGEEHRRRRRLLQPAFAPRAVARWEEPIVRPiAEELV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 175 NKLekhVNQEAFNCF--FYITLCALdIICETamgknIGAQSNNDSEYVRTVYRMSDmiyrrmkmpWLWFDlWYLVFKEGR 252
Cdd:cd20629   89 DDL---ADLGRADLVedFALELPAR-VIYAL-----LGLPEEDLPEFTRLALAMLR---------GLSDP-PDPDVPAAE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 253 DHKRGLKclhTFTNNVIAERvkeRKAEEDwtgagrgpipsknkrkaflDLL--LSVTDEEGNRLSQEDIREEVDTFMFEG 330
Cdd:cd20629  150 AAAAELY---DYVLPLIAER---RRAPGD-------------------DLIsrLLRAEVEGEKLDDEEIISFLRLLLPAG 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 331 HDTTAAAINWSLYLLGTNPEVQRKVDQEldevfgRSHRPVTLEdlkklkyldcvikETLRVFPSVPLFARSLSEDCEVGG 410
Cdd:cd20629  205 SDTTYRALANLLTLLLQHPEQLERVRRD------RSLIPAAIE-------------EGLRWEPPVASVPRMALRDVELDG 265
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187956757 411 YKVTKGTEAIIIPYALHRDPRYFPDPEEFRperffpensQGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd20629  266 VTIPAGSLLDLSVGSANRDEDVYPDPDVFD---------IDRKPKPHLVFGGGAHRCLGEHLARVELREALNALLDRL 334
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
295-513 9.00e-18

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: 85.89  E-value: 9.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 295 KRKAFLDLLLSVTDEEGNRLSQEDIREEVDT---FMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPV- 370
Cdd:cd20631  201 QKRENISELISLRMLLNDTLSTLDEMEKARThvaMLWASQANTLPATFWSLFYLLRCPEAMKAATKEVKRTLEKTGQKVs 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 371 --------TLEDLKKLKYLDCVIKETLRVfPSVPLFARSLSED----CEVGG-YKVTKGTEAIIIPYALHRDPRYFPDPE 437
Cdd:cd20631  281 dggnpivlTREQLDDMPVLGSIIKEALRL-SSASLNIRVAKEDftlhLDSGEsYAIRKDDIIALYPQLLHLDPEIYEDPL 359
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 438 EFRPERFFPENSQ--------GRH-PYAYVPFSAGPRNCIGQKFAVMEEKTILACILRQFWVES----------NQKREE 498
Cdd:cd20631  360 TFKYDRYLDENGKekttfyknGRKlKYYYMPFGSGTSKCPGRFFAINEIKQFLSLMLCYFDMELldgnakcpplDQSRAG 439
                        250
                 ....*....|....*
gi 187956757 499 LGlagdlILRPNNGI 513
Cdd:cd20631  440 LG-----ILPPTHDV 449
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
299-488 5.83e-17

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


Pssm-ID: 410723 [Multi-domain]  Cd Length: 373  Bit Score: 82.47  E-value: 5.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 299 FLDLLLSvTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQEldevfgrshrPVTLEDlkkl 378
Cdd:cd20630  185 LLTTLLR-AEEDGERLSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAE----------PELLRN---- 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 379 kyldcVIKETLR--VFPSVPlFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPErffpensqgRHPYA 456
Cdd:cd20630  250 -----ALEEVLRwdNFGKMG-TARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVR---------RDPNA 314
                        170       180       190
                 ....*....|....*....|....*....|..
gi 187956757 457 YVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd20630  315 NIAFGYGPHFCIGAALARLELELAVSTLLRRF 346
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
301-488 7.19e-17

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: 82.00  E-value: 7.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 301 DLLLSVTDEE--GNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVdqeLDEvfgrshrpvtlEDLkkl 378
Cdd:cd11034  171 DLISRLIEGEidGKPLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHPEDRRRL---IAD-----------PSL--- 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 379 kyLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERffPENsqgRHpyayV 458
Cdd:cd11034  234 --IPNAVEEFLRFYSPVAGLARTVTQEVEVGGCRLKPGDRVLLAFASANRDEEKFEDPDRIDIDR--TPN---RH----L 302
                        170       180       190
                 ....*....|....*....|....*....|
gi 187956757 459 PFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd11034  303 AFGSGVHRCLGSHLARVEARVALTEVLKRI 332
PLN02500 PLN02500
cytochrome P450 90B1
314-476 7.93e-17

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 82.99  E-value: 7.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 314 LSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHR----PVTLEDLKKLKYLDCVIKETL 389
Cdd:PLN02500 275 LSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEHLEIARAKKQsgesELNWEDYKKMEFTQCVINETL 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 390 RVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQG-------RHPYAYVPFSA 462
Cdd:PLN02500 355 RLGNVVRFLHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQNNNRGgssgsssATTNNFMPFGG 434
                        170
                 ....*....|....
gi 187956757 463 GPRNCIGQKFAVME 476
Cdd:PLN02500 435 GPRLCAGSELAKLE 448
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
348-488 1.23e-16

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: 81.92  E-value: 1.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 348 NPEVQRKVDQELDEVFGrSHRPVTLEDLKKLKYLDCVIKETLRVFPSVPL-FARSlSEDCEV----GGYKVTKGtEAII- 421
Cdd:cd11071  256 GEELHARLAEEIRSALG-SEGGLTLAALEKMPLLKSVVYETLRLHPPVPLqYGRA-RKDFVIeshdASYKIKKG-ELLVg 332
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187956757 422 -IPYAlHRDPRYFPDPEEFRPERFFPENSQGRHpyaYVPFSAGP---------RNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd11071  333 yQPLA-TRDPKVFDNPDEFVPDRFMGEEGKLLK---HLIWSNGPeteeptpdnKQCPGKDLVVLLARLFVAELFLRY 405
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
332-488 1.41e-16

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: 81.35  E-value: 1.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 332 DTTAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPvtledlkklkYLDCVIKETLRVFPSVPLFARSLSEDCEVGGY 411
Cdd:cd20624  205 DAAGMALLRALALLAAHPEQAARAREEAAVPPGPLARP----------YLRACVLDAVRLWPTTPAVLRESTEDTVWGGR 274
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187956757 412 KVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGrHPyAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd20624  275 TVPAGTGFLIFAPFFHRDDEALPFADRFVPEIWLDGRAQP-DE-GLVPFSAGPARCPGENLVLLVASTALAALLRRA 349
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
299-487 2.69e-16

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: 80.33  E-value: 2.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 299 FLDLLLSVtDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRkvdqELDEvfgrshRPVTLEDlkkl 378
Cdd:cd11035  172 LISAILNA-EIDGRPLTDDELLGLCFLLFLAGLDTVASALGFIFRHLARHPEDRR----RLRE------DPELIPA---- 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 379 kyldcVIKETLRVFPSVPLfARSLSEDCEVGGYKVTKGtEAIIIPYALH-RDPRYFPDPEEFRPERffpenSQGRHpyay 457
Cdd:cd11035  237 -----AVEELLRRYPLVNV-ARIVTRDVEFHGVQLKAG-DMVLLPLALAnRDPREFPDPDTVDFDR-----KPNRH---- 300
                        170       180       190
                 ....*....|....*....|....*....|
gi 187956757 458 VPFSAGPRNCIGQKFAVMEEKTILACILRQ 487
Cdd:cd11035  301 LAFGAGPHRCLGSHLARLELRIALEEWLKR 330
PLN02774 PLN02774
brassinosteroid-6-oxidase
298-492 4.05e-16

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 80.59  E-value: 4.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 298 AFLDLLLSVTDEEGNR--LSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPevqrKVDQEL-DEVFG-----RSHRP 369
Cdd:PLN02774 242 THTDMLGYLMRKEGNRykLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHP----KALQELrKEHLAirerkRPEDP 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 370 VTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFpENS 449
Cdd:PLN02774 318 IDWNDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDMELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWL-DKS 396
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 187956757 450 QGRHPYAYVpFSAGPRNCIGQKFAVMEEKTILACILRQF-WVES 492
Cdd:PLN02774 397 LESHNYFFL-FGGGTRLCPGKELGIVEISTFLHYFVTRYrWEEV 439
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
295-493 5.60e-16

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: 79.49  E-value: 5.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 295 KRKAFLDLLLSV---TDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKV--DQELdevfgrshrp 369
Cdd:cd11033  183 RRANPGDDLISVlanAEVDGEPLTDEEFASFFILLAVAGNETTRNSISGGVLALAEHPDQWERLraDPSL---------- 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 370 vtledlkklkyLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGtEAIIIPY-ALHRDPRYFPDPEEFRPERffpen 448
Cdd:cd11033  253 -----------LPTAVEEILRWASPVIHFRRTATRDTELGGQRIRAG-DKVVLWYaSANRDEEVFDDPDRFDITR----- 315
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 187956757 449 SQGRHpyayVPFSAGPRNCIGQKFAVMEEKTILACILRQF----------WVESN 493
Cdd:cd11033  316 SPNPH----LAFGGGPHFCLGAHLARLELRVLFEELLDRVpdielagepeRLRSN 366
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
310-488 8.19e-16

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: 79.18  E-value: 8.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 310 EGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVdqeldevfgRSHRpvtlEDLKKlkyldcVIKETL 389
Cdd:cd11032  190 DGERLTDEEIVGFAILLLIAGHETTTNLLGNAVLCLDEDPEVAARL---------RADP----SLIPG------AIEEVL 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 390 RVFPSVPLFARSLSEDCEVGGYKVTKGteAIIIPY--ALHRDPRYFPDPEEFRPerffpensqGRHPYAYVPFSAGPRNC 467
Cdd:cd11032  251 RYRPPVQRTARVTTEDVELGGVTIPAG--QLVIAWlaSANRDERQFEDPDTFDI---------DRNPNPHLSFGHGIHFC 319
                        170       180
                 ....*....|....*....|.
gi 187956757 468 IGQKFAVMEEKTILACILRQF 488
Cdd:cd11032  320 LGAPLARLEARIALEALLDRF 340
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
300-488 1.71e-15

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


Pssm-ID: 410655 [Multi-domain]  Cd Length: 384  Bit Score: 78.34  E-value: 1.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 300 LDLLLSVTDEEGnRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQEldevfgrshrPVTLEDlkklk 379
Cdd:cd11029  194 LSALVAARDEGD-RLSEEELVSTVFLLLVAGHETTVNLIGNGVLALLTHPDQLALLRAD----------PELWPA----- 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 380 yldcVIKETLRVFPSVPL----FARslsEDCEVGGYKVTKGtEAIIIPY-ALHRDPRYFPDPEEFRPERffpenSQGRHp 454
Cdd:cd11029  258 ----AVEELLRYDGPVALatlrFAT---EDVEVGGVTIPAG-EPVLVSLaAANRDPARFPDPDRLDITR-----DANGH- 323
                        170       180       190
                 ....*....|....*....|....*....|....
gi 187956757 455 yayVPFSAGPRNCIGQKFAVMEEKTILACILRQF 488
Cdd:cd11029  324 ---LAFGHGIHYCLGAPLARLEAEIALGALLTRF 354
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
330-513 8.87e-15

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: 76.08  E-value: 8.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 330 GHDTTAAAINWSLYLLGTNPEVQRKVDQEldevfgRSHRPVTLEdlkklkyldcvikETLRVFPSVPLFARSLSEDCEVG 409
Cdd:cd11037  214 GLDTTISAIGNALWLLARHPDQWERLRAD------PSLAPNAFE-------------EAVRLESPVQTFSRTTTRDTELA 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 410 GYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERffpenSQGRHpyayVPFSAGPRNCIGQKFAVMEEKTILACILRQfw 489
Cdd:cd11037  275 GVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITR-----NPSGH----VGFGHGVHACVGQHLARLEGEALLTALARR-- 343
                        170       180
                 ....*....|....*....|....
gi 187956757 490 VESnqkreeLGLAGDLILRPNNGI 513
Cdd:cd11037  344 VDR------IELAGPPVRALNNTL 361
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
301-485 3.97e-13

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: 70.96  E-value: 3.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 301 DLL--LSVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEvqrkvdqELDEVfgRSHRpvtledlkkl 378
Cdd:cd11080  174 DLIsiLCTAEYEGEALSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPE-------QLAAV--RADR---------- 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 379 KYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFFPENSQGRHPYA-Y 457
Cdd:cd11080  235 SLVPRAIAETLRYHPPVQLIPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHREDLGIRSAFSGAAdH 314
                        170       180
                 ....*....|....*....|....*...
gi 187956757 458 VPFSAGPRNCIGQKFAVMEEKTILACIL 485
Cdd:cd11080  315 LAFGSGRHFCVGAALAKREIEIVANQVL 342
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
309-469 1.39e-12

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: 69.32  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 309 EEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEvQRKVDQELDEVFGRShrpvtledlkklkyldcvIKET 388
Cdd:cd11038  205 QDGDRLSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPD-QWRALREDPELAPAA------------------VEEV 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 389 LRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPeefrpeRFFPENSQGRHpyayVPFSAGPRNCI 468
Cdd:cd11038  266 LRWCPTTTWATREAVEDVEYNGVTIPAGTVVHLCSHAANRDPRVFDAD------RFDITAKRAPH----LGFGGGVHHCL 335

                 .
gi 187956757 469 G 469
Cdd:cd11038  336 G 336
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
334-499 1.95e-12

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: 69.32  E-value: 1.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 334 TAAAINWSLYLLGTNPEVQRKVDQELDEVFGRSHRPVTLED---------LKKLKYLDCVIKETLRVFPSvPLFARSLSE 404
Cdd:cd20633  240 TGPASFWLLLYLLKHPEAMKAVREEVEQVLKETGQEVKPGGplinltrdmLLKTPVLDSAVEETLRLTAA-PVLIRAVVQ 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 405 DCEV---GG--YKVTKGTEAIIIPY-ALHRDPRYFPDPEEFRPERFFPENS--------QGRH-PYAYVPFSAGPRNCIG 469
Cdd:cd20633  319 DMTLkmaNGreYALRKGDRLALFPYlAVQMDPEIHPEPHTFKYDRFLNPDGgkkkdfykNGKKlKYYNMPWGAGVSICPG 398
                        170       180       190
                 ....*....|....*....|....*....|
gi 187956757 470 QKFAVMEEKTILACILRQFWVESNQKREEL 499
Cdd:cd20633  399 RFFAVNEMKQFVFLMLTYFDLELVNPDEEI 428
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
326-488 1.84e-11

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: 65.59  E-value: 1.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 326 FMFEGHDTTAAAINWSLYLLGTNPEvQRKVDQELDEVfgrshrpvtledlkklkyLDCVIKETLRVFPSVPLFARSLSED 405
Cdd:cd11036  185 LAVQGAEAAAGLVGNAVLALLRRPA-QWARLRPDPEL------------------AAAAVAETLRYDPPVRLERRFAAED 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 406 CEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPerffpensqGRHPYAYVPFSAGPRNCIGQKFAVMEEKTILACIL 485
Cdd:cd11036  246 LELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDL---------GRPTARSAHFGLGRHACLGAALARAAAAAALRALA 316

                 ...
gi 187956757 486 RQF 488
Cdd:cd11036  317 ARF 319
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
333-477 2.56e-11

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: 65.63  E-value: 2.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 333 TTAAA--INWSLYLLGTNPEVQRKVDQELDEvfgrshrpvtledlkklkYLDCVIKETLRVFPSVPLFARSLSEDCEVGG 410
Cdd:cd11067  233 TVAVArfVTFAALALHEHPEWRERLRSGDED------------------YAEAFVQEVRRFYPFFPFVGARARRDFEWQG 294
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187956757 411 YKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERFfpeNSQGRHPYAYVP-----FSAGPRnCIGQKFAV--MEE 477
Cdd:cd11067  295 YRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERF---LGWEGDPFDFIPqgggdHATGHR-CPGEWITIalMKE 364
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
337-499 3.70e-11

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: 65.17  E-value: 3.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 337 AINWSLYLLGTNPEVQRKVDQELDEVF---GRSHRPVTL---EDLKKLKYLDCVIKETLRVfPSVPLFARSLSED---CE 407
Cdd:cd20634  240 AAFWLLLFLLKHPEAMAAVRGEIQRIKhqrGQPVSQTLTinqELLDNTPVFDSVLSETLRL-TAAPFITREVLQDmklRL 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 408 VGG--YKVTKGTEAIIIPY-ALHRDPRYFPDPEEFRPERFFpeNSQG-----------RHPYAYVPFSAGPRNCIGQKFA 473
Cdd:cd20634  319 ADGqeYNLRRGDRLCLFPFlSPQMDPEIHQEPEVFKYDRFL--NADGtekkdfykngkRLKYYNMPWGAGDNVCIGRHFA 396
                        170       180
                 ....*....|....*....|....*.
gi 187956757 474 VMEEKTILACILRQFWVESNQKREEL 499
Cdd:cd20634  397 VNSIKQFVFLILTHFDVELKDPEAEI 422
PLN02648 PLN02648
allene oxide synthase
342-491 3.24e-10

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 62.26  E-value: 3.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 342 LYLLGT-NPEVQRKVDQELDEVFGRSHRPVTLEDLKKLKYLDCVIKETLRVFPSVPL-FARSlSEDCEV----GGYKVTK 415
Cdd:PLN02648 296 LKWVGRaGEELQARLAEEVRSAVKAGGGGVTFAALEKMPLVKSVVYEALRIEPPVPFqYGRA-REDFVIeshdAAFEIKK 374
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 416 GtEAI--IIPYALhRDPRYFPDPEEFRPERFFPEnsQGRHPYAYVPFSAGP---------RNCIGQKFAVMeektilacI 484
Cdd:PLN02648 375 G-EMLfgYQPLVT-RDPKVFDRPEEFVPDRFMGE--EGEKLLKYVFWSNGRetesptvgnKQCAGKDFVVL--------V 442

                 ....*..
gi 187956757 485 LRQFWVE 491
Cdd:PLN02648 443 ARLFVAE 449
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
303-487 7.12e-10

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: 60.83  E-value: 7.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 303 LLSVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDEvfgrshrpvtledlkklkyLD 382
Cdd:cd11079  168 RLLRERVDGRPLTDEEIVSILRNWTVGELGTIAACVGVLVHYLARHPELQARLRANPAL-------------------LP 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 383 CVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPErffpensqgRHPYAYVPFSA 462
Cdd:cd11079  229 AAIDEILRLDDPFVANRRITTRDVELGGRTIPAGSRVTLNWASANRDERVFGDPDEFDPD---------RHAADNLVYGR 299
                        170       180
                 ....*....|....*....|....*
gi 187956757 463 GPRNCIGQKFAVMEEKTILACILRQ 487
Cdd:cd11079  300 GIHVCPGAPLARLELRILLEELLAQ 324
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
330-488 1.72e-09

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: 59.46  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 330 GHDTTAAAINWSLYLLGTNPEvqrkvdqELDEVFGRSHRpvtledlkklkyLDCVIKETLRVFPSVPL-FARSLSEDCEV 408
Cdd:cd11030  220 GHETTANMIALGTLALLEHPE-------QLAALRADPSL------------VPGAVEELLRYLSIVQDgLPRVATEDVEI 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 409 GGYKVTKGtEAIII-PYALHRDPRYFPDPEEFRPERffpenSQGRHpyayVPFSAGPRNCIGQKFAVMEEKTILACILRQ 487
Cdd:cd11030  281 GGVTIRAG-EGVIVsLPAANRDPAVFPDPDRLDITR-----PARRH----LAFGHGVHQCLGQNLARLELEIALPTLFRR 350

                 .
gi 187956757 488 F 488
Cdd:cd11030  351 F 351
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
357-487 6.24e-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: 57.74  E-value: 6.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 357 QELDEVFGR---SHRPV----TLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEV-----GGYKVTKGTEAIIIPY 424
Cdd:cd20612  209 QILDFYLRRpgaAHLAEiqalARENDEADATLRGYVLEALRLNPIAPGLYRRATTDTTVadgggRTVSIKAGDRVFVSLA 288
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187956757 425 ALHRDPRYFPDPEEFRPERffPENSqgrhpyaYVPFSAGPRNCIGQKFAvmeeKTILACILRQ 487
Cdd:cd20612  289 SAMRDPRAFPDPERFRLDR--PLES-------YIHFGHGPHQCLGEEIA----RAALTEMLRV 338
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
382-470 3.34e-08

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


Pssm-ID: 410712 [Multi-domain]  Cd Length: 358  Bit Score: 55.51  E-value: 3.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 382 DCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEFRPERfFPENSQGrhpyayVPFS 461
Cdd:cd20619  235 AAIINEMVRMDPPQLSFLRFPTEDVEIGGVLIEAGSPIRFMIGAANRDPEVFDDPDVFDHTR-PPAASRN------LSFG 307

                 ....*....
gi 187956757 462 AGPRNCIGQ 470
Cdd:cd20619  308 LGPHSCAGQ 316
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
273-523 1.28e-07

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 53.98  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 273 VKERKAEEDWTGAGRGPIPsknkrKAFLDLLLSVTDEEgnrLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQ 352
Cdd:PLN03141 214 IEEKRRAMKNKEEDETGIP-----KDVVDVLLRDGSDE---LTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSDCPVAL 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 353 RKVDQE---LDEVFGRSHRPVTLEDLKKLKYLDCVIKETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRD 429
Cdd:PLN03141 286 QQLTEEnmkLKRLKADTGEPLYWTDYMSLPFTQNVITETLRMGNIINGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVHLD 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 430 PRYFPDPEEFRPERFFPENSQGRhpyAYVPFSAGPRNCIGQKFAVMEEKTILACILRQF-WVEsnqkrEELGLAGDLILR 508
Cdd:PLN03141 366 EENYDNPYQFNPWRWQEKDMNNS---SFTPFGGGQRLCPGLDLARLEASIFLHHLVTRFrWVA-----EEDTIVNFPTVR 437
                        250
                 ....*....|....*
gi 187956757 509 PNNGIWIKLKRRHED 523
Cdd:PLN03141 438 MKRKLPIWVTRIDDS 452
CYP_unk cd20623
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
312-473 2.03e-05

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: 46.88  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 312 NRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEV-------QRKVDQELDEVFGRShrPvtledlkklkyldcv 384
Cdd:cd20623  190 AGLTDEEVVHDLVLLLGAGHEPTTNLIGNTLRLMLTDPRFaaslsggRLSVREALNEVLWRD--P--------------- 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 385 iketlrvfPSVPLFARSLSEDCEVGGYKVTKGtEAIIIPY-ALHRDPRYFPDPeefrperffPENSQGRHpyAYVPFSAG 463
Cdd:cd20623  253 --------PLANLAGRFAARDTELGGQWIRAG-DLVVLGLaAANADPRVRPDP---------GASMSGNR--AHLAFGAG 312
                        170
                 ....*....|
gi 187956757 464 PRNCIGQKFA 473
Cdd:cd20623  313 PHRCPAQELA 322
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
303-473 1.24e-04

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


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 44.42  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 303 LLSVTDEEGNRLSQEDIREEVDTFMFEGHDTTAAAINWSLYLLGTNPEVQRKVDQELDevfgrsHRPVTLEdlkklkyld 382
Cdd:cd11039  187 LLSVMLNAGMPMSLEQIRANIKVAIGGGLNEPRDAIAGTCWGLLSNPEQLAEVMAGDV------HWLRAFE--------- 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 383 cvikETLRVFPSVPLFARSLSEDCEVGGYKVTKGTEAIIIPYALHRDPRYFPDPEEF---RPERffpensqgrhpyAYVP 459
Cdd:cd11039  252 ----EGLRWISPIGMSPRRVAEDFEIRGVTLPAGDRVFLMFGSANRDEARFENPDRFdvfRPKS------------PHVS 315
                        170
                 ....*....|....
gi 187956757 460 FSAGPRNCIGQKFA 473
Cdd:cd11039  316 FGAGPHFCAGAWAS 329
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
384-490 4.95e-04

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: 42.39  E-value: 4.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956757 384 VIKETLRVFPSVPLFARSLSEDcevGGYKVTKGTEAIIipyALHRDPRYF-PDPEEFRPERFFP-ENSQGRhpyAYVPFS 461
Cdd:cd20626  261 LVKEALRLYPPTRRIYRAFQRP---GSSKPEIIAADIE---ACHRSESIWgPDALEFNPSRWSKlTPTQKE---AFLPFG 331
                         90       100       110
                 ....*....|....*....|....*....|...
gi 187956757 462 AGPRNCIGQK-FAVMEEKTILACILRQF---WV 490
Cdd:cd20626  332 SGPFRCPAKPvFGPRMIALLVGALLDALgdeWE 364
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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