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Conserved domains on  [gi|47086709|ref|NP_997831|]
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cytochrome P450 26B1 [Danio rerio]

Protein Classification

cytochrome P450 family protein( domain architecture ID 1750044)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cytochrome_P450 super family cl41757
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
60-489 0e+00

cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs with > 40% sequence identity are members of the same family. There are approximately 2250 CYP families: mammals, insects, plants, fungi, bacteria, and archaea have around 18, 208, 277, 805, 591, and 14 families, respectively. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle. CYPs use a variety of redox partners, such as the eukaryotic diflavin enzyme NADPH-cytochrome P450 oxidoreductase and the bacterial/mitochondrial NAD(P)H-ferredoxin reductase and ferredoxin partners. Some CYPs are naturally linked to their redox partners and others have evolved to bypass requirements for redox partners, and instead react directly with hydrogen peroxide or NAD(P)H to facilitate oxidative or reductive catalysis.


The actual alignment was detected with superfamily member cd20637:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 430  Bit Score: 836.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  60 GETCHWFFQGAGFHASRRQKYGNVFKTHLLGRPLIRVTGAENVRKVLMGEHSLVTVDWPQSTSTLLGPNSLANSIGDIHR 139
Cdd:cd20637   1 GETFHWLLQGSGFQSSRREKYGNVFKTHLLGRPLIRVTGAENVRKILMGEHSLVSTEWPRSTRMLLGPNSLVNSIGDIHR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 140 KRRKIFAKVFSHEALESYLPKIQQVIQETLRVWSSNPDPINVYRESQRLSFNMAVRVLLGFRIPEEEMHCLFSTFQEFVE 219
Cdd:cd20637  81 HKRKVFSKLFSHEALESYLPKIQQVIQDTLRVWSSNPEPINVYQEAQKLTFRMAIRVLLGFRVSEEELSHLFSVFQQFVE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 220 NVFSLPIDLPFSGYRKGIRARDSLQKSIEKAIREKPLHTQGKDYTDALDVLLESAKENNTELTMQELKESTIELIFAAFA 299
Cdd:cd20637 161 NVFSLPLDLPFSGYRRGIRARDSLQKSLEKAIREKLQGTQGKDYADALDILIESAKEHGKELTMQELKDSTIELIFAAFA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 300 TTASASTSLVMQLLRHPAVLEKLREELRSCGLLHDGCLCQGELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFE 379
Cdd:cd20637 241 TTASASTSLIMQLLKHPGVLEKLREELRSNGILHNGCLCEGTLRLDTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFE 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 380 LDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREGRFHYLPFGGGVRSCLGKQLATLFLKLLAVELAG 459
Cdd:cd20637 321 LDGFQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRFGQERSEDKDGRFHYLPFGGGVRTCLGKQLAKLFLKVLAVELAS 400
                       410       420       430
                ....*....|....*....|....*....|
gi 47086709 460 GSRFELSTRTFPRMISVPVVHPTDGLRVKF 489
Cdd:cd20637 401 TSRFELATRTFPRMTTVPVVHPVDGLRVKF 430
 
Name Accession Description Interval E-value
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
60-489 0e+00

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: 836.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  60 GETCHWFFQGAGFHASRRQKYGNVFKTHLLGRPLIRVTGAENVRKVLMGEHSLVTVDWPQSTSTLLGPNSLANSIGDIHR 139
Cdd:cd20637   1 GETFHWLLQGSGFQSSRREKYGNVFKTHLLGRPLIRVTGAENVRKILMGEHSLVSTEWPRSTRMLLGPNSLVNSIGDIHR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 140 KRRKIFAKVFSHEALESYLPKIQQVIQETLRVWSSNPDPINVYRESQRLSFNMAVRVLLGFRIPEEEMHCLFSTFQEFVE 219
Cdd:cd20637  81 HKRKVFSKLFSHEALESYLPKIQQVIQDTLRVWSSNPEPINVYQEAQKLTFRMAIRVLLGFRVSEEELSHLFSVFQQFVE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 220 NVFSLPIDLPFSGYRKGIRARDSLQKSIEKAIREKPLHTQGKDYTDALDVLLESAKENNTELTMQELKESTIELIFAAFA 299
Cdd:cd20637 161 NVFSLPLDLPFSGYRRGIRARDSLQKSLEKAIREKLQGTQGKDYADALDILIESAKEHGKELTMQELKDSTIELIFAAFA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 300 TTASASTSLVMQLLRHPAVLEKLREELRSCGLLHDGCLCQGELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFE 379
Cdd:cd20637 241 TTASASTSLIMQLLKHPGVLEKLREELRSNGILHNGCLCEGTLRLDTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFE 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 380 LDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREGRFHYLPFGGGVRSCLGKQLATLFLKLLAVELAG 459
Cdd:cd20637 321 LDGFQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRFGQERSEDKDGRFHYLPFGGGVRTCLGKQLAKLFLKVLAVELAS 400
                       410       420       430
                ....*....|....*....|....*....|
gi 47086709 460 GSRFELSTRTFPRMISVPVVHPTDGLRVKF 489
Cdd:cd20637 401 TSRFELATRTFPRMTTVPVVHPVDGLRVKF 430
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
1-489 5.14e-59

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 202.09  E-value: 5.14e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709    1 MLFESFDLVSALATLAACLVSMALLLAvsqqlwqlrwtatRDKSCKLPMPKGSMGFPIIGETCHWFFQGAG-FHASRRQK 79
Cdd:PLN02196   1 MDFSALFLTLFAGALFLCLLRFLAGFR-------------RSSSTKLPLPPGTMGWPYVGETFQLYSQDPNvFFASKQKR 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   80 YGNVFKTHLLGRPLIRVTGAENVRKVLMGEHSLVTVDWPQSTSTLLGPNSLANSIGDIHRKRRKIFAKVFSHEALESYLP 159
Cdd:PLN02196  68 YGSVFKTHVLGCPCVMISSPEAAKFVLVTKSHLFKPTFPASKERMLGKQAIFFHQGDYHAKLRKLVLRAFMPDAIRNMVP 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  160 KIQQVIQETLRVWSSNpdPINVYRESQRLSFNMAVRVLLG---FRIPEEEMHCLFstfqeFVENVF-SLPIDLPFSGYRK 235
Cdd:PLN02196 148 DIESIAQESLNSWEGT--QINTYQEMKTYTFNVALLSIFGkdeVLYREDLKRCYY-----ILEKGYnSMPINLPGTLFHK 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  236 GIRARDSLQKSIEKAIREKplHTQGKDYTDaldvLLESAKENNTELTMQELKESTIELIFAAFATTASASTSLVMQLLRH 315
Cdd:PLN02196 221 SMKARKELAQILAKILSKR--RQNGSSHND----LLGSFMGDKEGLTDEQIADNIIGVIFAARDTTASVLTWILKYLAEN 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  316 PAVLEKLREElrscgllhdgclcQGELRLDSI--ISLKYLDC--------VIKEVLRLFAPVSGGYRIATQTFELDGVQV 385
Cdd:PLN02196 295 PSVLEAVTEE-------------QMAIRKDKEegESLTWEDTkkmpltsrVIQETLRVASILSFTFREAVEDVEYEGYLI 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  386 PKGWSVMYSIRDTHDTSAVFKDVEAFDPDRF--SPERSEdregrfhYLPFGGGVRSCLGKQLATLFLKLLAVELAGGSRF 463
Cdd:PLN02196 362 PKGWKVLPLFRNIHHSADIFSDPGKFDPSRFevAPKPNT-------FMPFGNGTHSCPGNELAKLEISVLIHHLTTKYRW 434
                        490       500
                 ....*....|....*....|....*.
gi 47086709  464 ELSTRTFPRMISvPVVHPTDGLRVKF 489
Cdd:PLN02196 435 SIVGTSNGIQYG-PFALPQNGLPIAL 459
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
76-489 5.98e-58

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: 197.42  E-value: 5.98e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  76 RRQKYGNVFKTHLLGRPLIRVTGAENVRKVLMgEHSLVTVDWPQSTS---TLLGPNSLANSIGDIHRKRRKIFAKVFSHE 152
Cdd:COG2124  27 RLREYGPVFRVRLPGGGAWLVTRYEDVREVLR-DPRTFSSDGGLPEVlrpLPLLGDSLLTLDGPEHTRLRRLVQPAFTPR 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 153 ALESYLPKIQQVIQETLRVWSSnPDPINVYRESQRLSFNMAVRVLLGfrIPEEEMHclfsTFQEFVENVFSLPIDLPFSG 232
Cdd:COG2124 106 RVAALRPRIREIADELLDRLAA-RGPVDLVEEFARPLPVIVICELLG--VPEEDRD----RLRRWSDALLDALGPLPPER 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 233 YRKGIRARDSLQKSIEKAIREKPLHTQGkdytDALDVLLEsAKENNTELTMQELK-----------ESTIELIFAafatt 301
Cdd:COG2124 179 RRRARRARAELDAYLRELIAERRAEPGD----DLLSALLA-ARDDGERLSDEELRdellllllaghETTANALAW----- 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 302 asastsLVMQLLRHPAVLEKLREELRscgllhdgclcqgelrldsiislkYLDCVIKEVLRLFAPVSGGYRIATQTFELD 381
Cdd:COG2124 249 ------ALYALLRHPEQLARLRAEPE------------------------LLPAAVEETLRLYPPVPLLPRTATEDVELG 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 382 GVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRfspersedreGRFHYLPFGGGVRSCLGKQLATLFLKLLAVELAggS 461
Cdd:COG2124 299 GVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR----------PPNAHLPFGGGPHRCLGAALARLEARIALATLL--R 366
                       410       420       430
                ....*....|....*....|....*....|.
gi 47086709 462 RF---ELSTRTFPRMISVPVVHPTDGLRVKF 489
Cdd:COG2124 367 RFpdlRLAPPEELRWRPSLTLRGPKSLPVRL 397
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
50-489 4.24e-49

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: 175.16  E-value: 4.24e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709    50 PKGSMGFPIIGetcHWFFQGAG-----FHASRRQKYGNVFKTHLLGRPLIRVTGAENVRKVLMGEHSLVTVDWPQS-TST 123
Cdd:pfam00067   1 PPGPPPLPLFG---NLLQLGRKgnlhsVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPwFAT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   124 LLGPN---SLANSIGDIHRKRRKIFAKVFSHEALESYLPKIQQVIQ---ETLRVWSSNPDPINVYRESQRLSFNMAVRVL 197
Cdd:pfam00067  78 SRGPFlgkGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARdlvEKLRKTAGEPGVIDITDLLFRAALNVICSIL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   198 LGFRIPEEEMHcLFSTFQEFVENVFSL------------PIDLPFSG--YRKGIRARDSLQKSIEKAI--REKPLHTQGK 261
Cdd:pfam00067 158 FGERFGSLEDP-KFLELVKAVQELSSLlsspspqlldlfPILKYFPGphGRKLKRARKKIKDLLDKLIeeRRETLDSAKK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   262 DYTDALDVLLE-SAKENNTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRScgLLHDgclcQG 340
Cdd:pfam00067 237 SPRDFLDALLLaKEEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDE--VIGD----KR 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   341 ELRLDSIISLKYLDCVIKEVLRLFAPVSGG-YRIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPE 419
Cdd:pfam00067 311 SPTYDDLQNMPYLDAVIKETLRLHPVVPLLlPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDE 390
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47086709   420 RSEDREgRFHYLPFGGGVRSCLGKQLATLFLKL-LAVELaggSRFELSTRTF----PRMISVPVVHPTDGLRVKF 489
Cdd:pfam00067 391 NGKFRK-SFAFLPFGAGPRNCLGERLARMEMKLfLATLL---QNFEVELPPGtdppDIDETPGLLLPPKPYKLKF 461
 
Name Accession Description Interval E-value
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
60-489 0e+00

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: 836.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  60 GETCHWFFQGAGFHASRRQKYGNVFKTHLLGRPLIRVTGAENVRKVLMGEHSLVTVDWPQSTSTLLGPNSLANSIGDIHR 139
Cdd:cd20637   1 GETFHWLLQGSGFQSSRREKYGNVFKTHLLGRPLIRVTGAENVRKILMGEHSLVSTEWPRSTRMLLGPNSLVNSIGDIHR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 140 KRRKIFAKVFSHEALESYLPKIQQVIQETLRVWSSNPDPINVYRESQRLSFNMAVRVLLGFRIPEEEMHCLFSTFQEFVE 219
Cdd:cd20637  81 HKRKVFSKLFSHEALESYLPKIQQVIQDTLRVWSSNPEPINVYQEAQKLTFRMAIRVLLGFRVSEEELSHLFSVFQQFVE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 220 NVFSLPIDLPFSGYRKGIRARDSLQKSIEKAIREKPLHTQGKDYTDALDVLLESAKENNTELTMQELKESTIELIFAAFA 299
Cdd:cd20637 161 NVFSLPLDLPFSGYRRGIRARDSLQKSLEKAIREKLQGTQGKDYADALDILIESAKEHGKELTMQELKDSTIELIFAAFA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 300 TTASASTSLVMQLLRHPAVLEKLREELRSCGLLHDGCLCQGELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFE 379
Cdd:cd20637 241 TTASASTSLIMQLLKHPGVLEKLREELRSNGILHNGCLCEGTLRLDTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFE 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 380 LDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREGRFHYLPFGGGVRSCLGKQLATLFLKLLAVELAG 459
Cdd:cd20637 321 LDGFQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRFGQERSEDKDGRFHYLPFGGGVRTCLGKQLAKLFLKVLAVELAS 400
                       410       420       430
                ....*....|....*....|....*....|
gi 47086709 460 GSRFELSTRTFPRMISVPVVHPTDGLRVKF 489
Cdd:cd20637 401 TSRFELATRTFPRMTTVPVVHPVDGLRVKF 430
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
59-489 0e+00

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: 621.47  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  59 IGETCHWFFQGAGFHASRRQKYGNVFKTHLLGRPLIRVTGAENVRKVLMGEHSLVTVDWPQSTSTLLGPNSLANSIGDIH 138
Cdd:cd20636   1 FGETLHWLVQGSSFHSSRREKYGNVFKTHLLGRPVIRVTGAENIRKILLGEHTLVSTQWPQSTRILLGSNTLLNSVGELH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 139 RKRRKIFAKVFSHEALESYLPKIQQVIQETLRVWSSNPDPINVYRESQRLSFNMAVRVLLGFRIPEEEMHCLFSTFQEFV 218
Cdd:cd20636  81 RQRRKVLARVFSRAALESYLPRIQDVVRSEVRGWCRGPGPVAVYTAAKSLTFRIAVRILLGLRLEEQQFTYLAKTFEQLV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 219 ENVFSLPIDLPFSGYRKGIRARDSLQKSIEKAIREKPLHTQGKDYTDALDVLLESAKENNTELTMQELKESTIELIFAAF 298
Cdd:cd20636 161 ENLFSLPLDVPFSGLRKGIKARDILHEYMEKAIEEKLQRQQAAEYCDALDYMIHSARENGKELTMQELKESAVELIFAAF 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 299 ATTASASTSLVMQLLRHPAVLEKLREELRSCGLLHDGCLCQGELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTF 378
Cdd:cd20636 241 STTASASTSLVLLLLQHPSAIEKIRQELVSHGLIDQCQCCPGALSLEKLSRLRYLDCVVKEVLRLLPPVSGGYRTALQTF 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 379 ELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREGRFHYLPFGGGVRSCLGKQLATLFLKLLAVELA 458
Cdd:cd20636 321 ELDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEREESKSGRFNYIPFGGGVRSCIGKELAQVILKTLAVELV 400
                       410       420       430
                ....*....|....*....|....*....|.
gi 47086709 459 GGSRFELSTRTFPRMISVPVVHPTDGLRVKF 489
Cdd:cd20636 401 TTARWELATPTFPKMQTVPIVHPVDGLQLFF 431
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
60-489 0e+00

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: 543.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  60 GETCHWFFQGAGFHASRRQKYGNVFKTHLLGRPLIRVTGAENVRKVLMGEHSLVTVDWPQSTSTLLGPNSLANSIGDIHR 139
Cdd:cd11044   1 GETLEFLRDPEDFIQSRYQKYGPVFKTHLLGRPTVFVIGAEAVRFILSGEGKLVRYGWPRSVRRLLGENSLSLQDGEEHR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 140 KRRKIFAKVFSHEALESYLPKIQQVIQETLRVWSSNpDPINVYRESQRLSFNMAVRVLLGFRIPEEEMHcLFSTFQEFVE 219
Cdd:cd11044  81 RRRKLLAPAFSREALESYVPTIQAIVQSYLRKWLKA-GEVALYPELRRLTFDVAARLLLGLDPEVEAEA-LSQDFETWTD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 220 NVFSLPIDLPFSGYRKGIRARDSLQKSIEKAIREKpLHTQGKDYTDALDVLLESAKENNTELTMQELKESTIELIFAAFA 299
Cdd:cd11044 159 GLFSLPVPLPFTPFGRAIRARNKLLARLEQAIRER-QEEENAEAKDALGLLLEAKDEDGEPLSMDELKDQALLLLFAGHE 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 300 TTASASTSLVMQLLRHPAVLEKLREELRSCGLlhdgclcQGELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFE 379
Cdd:cd11044 238 TTASALTSLCFELAQHPDVLEKLRQEQDALGL-------EEPLTLESLKKMPYLDQVIKEVLRLVPPVGGGFRKVLEDFE 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 380 LDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREGRFHYLPFGGGVRSCLGKQLATLFLKLLAVELAG 459
Cdd:cd11044 311 LGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPARSEDKKKPFSLIPFGGGPRECLGKEFAQLEMKILASELLR 390
                       410       420       430
                ....*....|....*....|....*....|
gi 47086709 460 GSRFELSTRTFPRMISVPVVHPTDGLRVKF 489
Cdd:cd11044 391 NYDWELLPNQDLEPVVVPTPRPKDGLRVRF 420
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
60-489 1.34e-139

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: 409.20  E-value: 1.34e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  60 GETCHWFFQGAGFHASRRQKYGNVFKTHLLGRPLIRVTGAENVRKVLMGEHSLVTVDWPQSTSTLLGPNSLANSIGDIHR 139
Cdd:cd20638   1 GETLQMVLQRRKFLQMKRQKYGYIYKTHLFGRPTVRVMGAENVRQILLGEHKLVSVQWPASVRTILGSGCLSNLHDSQHK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 140 KRRKIFAKVFSHEALESYLPKIQQVIQETLRVWSSNPDPINVYRESQRLSFNMAVRVLLGFR----IPEEEMHcLFSTFQ 215
Cdd:cd20638  81 HRKKVIMRAFSREALENYVPVIQEEVRSSVNQWLQSGPCVLVYPEVKRLMFRIAMRILLGFEpqqtDREQEQQ-LVEAFE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 216 EFVENVFSLPIDLPFSGYRKGIRARDSLQKSIEKAIREKplhTQGKD----YTDALDVLLESAKENNTELTMQELKESTI 291
Cdd:cd20638 160 EMIRNLFSLPIDVPFSGLYRGLRARNLIHAKIEENIRAK---IQREDteqqCKDALQLLIEHSRRNGEPLNLQALKESAT 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 292 ELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRSCGLLHDGCLCQGELRLDSIISLKYLDCVIKEVLRLFAPVSGGY 371
Cdd:cd20638 237 ELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQEKGLLSTKPNENKELSMEVLEQLKYTGCVIKETLRLSPPVPGGF 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 372 RIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDrEGRFHYLPFGGGVRSCLGKQLATLFLK 451
Cdd:cd20638 317 RVALKTFELNGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPED-SSRFSFIPFGGGSRSCVGKEFAKVLLK 395
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 47086709 452 LLAVELAGGSRFELSTRTfPRMISVPVVHPTDGLRVKF 489
Cdd:cd20638 396 IFTVELARHCDWQLLNGP-PTMKTSPTVYPVDNLPAKF 432
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
76-446 4.12e-84

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: 265.97  E-value: 4.12e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  76 RRQKYGNVFKTHLLGRPLIRVTGAENVRKVLMGEHSLVTVDWPQSTSTLLGPNSLANSIGDIHRKRRKIFAKVFSHEALE 155
Cdd:cd11043   1 RIKRYGPVFKTSLFGRPTVVSADPEANRFILQNEGKLFVSWYPKSVRKLLGKSSLLTVSGEEHKRLRGLLLSFLGPEALK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 156 S-YLPKIQQVIQETLRVWSSNPDpINVYRESQRLSFNMAVRVLLGFRiPEEEMHCLFSTFQEFVENVFSLPIDLPFSGYR 234
Cdd:cd11043  81 DrLLGDIDELVRQHLDSWWRGKS-VVVLELAKKMTFELICKLLLGID-PEEVVEELRKEFQAFLEGLLSFPLNLPGTTFH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 235 KGIRARDSLQKSIEKAIREKPLH-TQGKDYTDALDVLLESAKENNTELTMQELKESTIELIFAAFATTASASTSLVMQLL 313
Cdd:cd11043 159 RALKARKRIRKELKKIIEERRAElEKASPKGDLLDVLLEEKDEDGDSLTDEEILDNILTLLFAGHETTSTTLTLAVKFLA 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 314 RHPAVLEKLREElrscgllHDGCLCQ----GELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGW 389
Cdd:cd11043 239 ENPKVLQELLEE-------HEEIAKRkeegEGLTWEDYKSMKYTWQVINETLRLAPIVPGVFRKALQDVEYKGYTIPKGW 311
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 47086709 390 SVMYSIRDTHDTSAVFKDVEAFDPDRFspeRSEDREGRFHYLPFGGGVRSCLGKQLA 446
Cdd:cd11043 312 KVLWSARATHLDPEYFPDPLKFNPWRW---EGKGKGVPYTFLPFGGGPRLCPGAELA 365
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
81-485 1.87e-66

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: 219.69  E-value: 1.87e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  81 GNVFKTHLLGRPLIRVTGAENVRKVLMGEHSL-VTVDWPQSTSTLLGPNSLANSIGDIHRKRRKIFAKVFSHEALESYLP 159
Cdd:cd00302   1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFsSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 160 KIQQVIQETLRVWSSNPD-PINVYRESQRLSFNMAVRVLLGFRIPEEEMHcLFSTFQEFVENVFSLPI-DLPFSGYRKGI 237
Cdd:cd00302  81 VIREIARELLDRLAAGGEvGDDVADLAQPLALDVIARLLGGPDLGEDLEE-LAELLEALLKLLGPRLLrPLPSPRLRRLR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 238 RARDSLQKSIEKAIREKPlhtqgKDYTDALDVLLESAKENNTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPA 317
Cdd:cd00302 160 RARARLRDYLEELIARRR-----AEPADDLDLLLLADADDGGGLSDEEIVAELLTLLLAGHETTASLLAWALYLLARHPE 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 318 VLEKLREELRSCGLLHDgclcqgelrLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRD 397
Cdd:cd00302 235 VQERLRAEIDAVLGDGT---------PEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVELGGYTIPAGTLVLLSLYA 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 398 THDTSAVFKDVEAFDPDRFSPERSEDregRFHYLPFGGGVRSCLGKQLATLFLKLLAVELAggSRFELSTRTFP---RMI 474
Cdd:cd00302 306 AHRDPEVFPDPDEFDPERFLPEREEP---RYAHLPFGAGPHRCLGARLARLELKLALATLL--RRFDFELVPDEeleWRP 380
                       410
                ....*....|.
gi 47086709 475 SVPVVHPTDGL 485
Cdd:cd00302 381 SLGTLGPASLP 391
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
71-489 1.01e-61

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: 207.82  E-value: 1.01e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  71 GFHASRRQKYGNVFKTHLLG-RPLIRVTGAENVRKVLMGE-HSLVTVDWPQSTSTLLGPNSLANSIGDIHRKRRKIFAKV 148
Cdd:cd11053   2 GFLERLRARYGDVFTLRVPGlGPVVVLSDPEAIKQIFTADpDVLHPGEGNSLLEPLLGPNSLLLLDGDRHRRRRKLLMPA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 149 FSHEALESYLPKIQQVIQETLRVWSSNpDPINVYRESQRLSFNMAVRVLLGFRIPEE--EMHCLFSTFQEFVENVFSL-- 224
Cdd:cd11053  82 FHGERLRAYGELIAEITEREIDRWPPG-QPFDLRELMQEITLEVILRVVFGVDDGERlqELRRLLPRLLDLLSSPLASfp 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 225 ---PIDLPFSGYRKGIRARDSLQKSIEKAIREKPLHTQGKDyTDALDVLLESAKENNTELTMQELKEstiELIFaafatt 301
Cdd:cd11053 161 alqRDLGPWSPWGRFLRARRRIDALIYAEIAERRAEPDAER-DDILSLLLSARDEDGQPLSDEELRD---ELMT------ 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 302 asastsLVM---------------QLLRHPAVLEKLREELRSCGllhdgclcqGELRLDSIISLKYLDCVIKEVLRLFAP 366
Cdd:cd11053 231 ------LLFaghettatalawafyWLHRHPEVLARLLAELDALG---------GDPDPEDIAKLPYLDAVIKETLRLYPV 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 367 VSGGYRIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSedreGRFHYLPFGGGVRSCLGKQLA 446
Cdd:cd11053 296 APLVPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGRKP----SPYEYLPFGGGVRRCIGAAFA 371
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 47086709 447 TLFLKL-LAVELaggSRFELSTRT----FPRMISVPVVhPTDGLRVKF 489
Cdd:cd11053 372 LLEMKVvLATLL---RRFRLELTDprpeRPVRRGVTLA-PSRGVRMVV 415
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
1-489 5.14e-59

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 202.09  E-value: 5.14e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709    1 MLFESFDLVSALATLAACLVSMALLLAvsqqlwqlrwtatRDKSCKLPMPKGSMGFPIIGETCHWFFQGAG-FHASRRQK 79
Cdd:PLN02196   1 MDFSALFLTLFAGALFLCLLRFLAGFR-------------RSSSTKLPLPPGTMGWPYVGETFQLYSQDPNvFFASKQKR 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   80 YGNVFKTHLLGRPLIRVTGAENVRKVLMGEHSLVTVDWPQSTSTLLGPNSLANSIGDIHRKRRKIFAKVFSHEALESYLP 159
Cdd:PLN02196  68 YGSVFKTHVLGCPCVMISSPEAAKFVLVTKSHLFKPTFPASKERMLGKQAIFFHQGDYHAKLRKLVLRAFMPDAIRNMVP 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  160 KIQQVIQETLRVWSSNpdPINVYRESQRLSFNMAVRVLLG---FRIPEEEMHCLFstfqeFVENVF-SLPIDLPFSGYRK 235
Cdd:PLN02196 148 DIESIAQESLNSWEGT--QINTYQEMKTYTFNVALLSIFGkdeVLYREDLKRCYY-----ILEKGYnSMPINLPGTLFHK 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  236 GIRARDSLQKSIEKAIREKplHTQGKDYTDaldvLLESAKENNTELTMQELKESTIELIFAAFATTASASTSLVMQLLRH 315
Cdd:PLN02196 221 SMKARKELAQILAKILSKR--RQNGSSHND----LLGSFMGDKEGLTDEQIADNIIGVIFAARDTTASVLTWILKYLAEN 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  316 PAVLEKLREElrscgllhdgclcQGELRLDSI--ISLKYLDC--------VIKEVLRLFAPVSGGYRIATQTFELDGVQV 385
Cdd:PLN02196 295 PSVLEAVTEE-------------QMAIRKDKEegESLTWEDTkkmpltsrVIQETLRVASILSFTFREAVEDVEYEGYLI 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  386 PKGWSVMYSIRDTHDTSAVFKDVEAFDPDRF--SPERSEdregrfhYLPFGGGVRSCLGKQLATLFLKLLAVELAGGSRF 463
Cdd:PLN02196 362 PKGWKVLPLFRNIHHSADIFSDPGKFDPSRFevAPKPNT-------FMPFGNGTHSCPGNELAKLEISVLIHHLTTKYRW 434
                        490       500
                 ....*....|....*....|....*.
gi 47086709  464 ELSTRTFPRMISvPVVHPTDGLRVKF 489
Cdd:PLN02196 435 SIVGTSNGIQYG-PFALPQNGLPIAL 459
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
76-489 5.98e-58

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: 197.42  E-value: 5.98e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  76 RRQKYGNVFKTHLLGRPLIRVTGAENVRKVLMgEHSLVTVDWPQSTS---TLLGPNSLANSIGDIHRKRRKIFAKVFSHE 152
Cdd:COG2124  27 RLREYGPVFRVRLPGGGAWLVTRYEDVREVLR-DPRTFSSDGGLPEVlrpLPLLGDSLLTLDGPEHTRLRRLVQPAFTPR 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 153 ALESYLPKIQQVIQETLRVWSSnPDPINVYRESQRLSFNMAVRVLLGfrIPEEEMHclfsTFQEFVENVFSLPIDLPFSG 232
Cdd:COG2124 106 RVAALRPRIREIADELLDRLAA-RGPVDLVEEFARPLPVIVICELLG--VPEEDRD----RLRRWSDALLDALGPLPPER 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 233 YRKGIRARDSLQKSIEKAIREKPLHTQGkdytDALDVLLEsAKENNTELTMQELK-----------ESTIELIFAafatt 301
Cdd:COG2124 179 RRRARRARAELDAYLRELIAERRAEPGD----DLLSALLA-ARDDGERLSDEELRdellllllaghETTANALAW----- 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 302 asastsLVMQLLRHPAVLEKLREELRscgllhdgclcqgelrldsiislkYLDCVIKEVLRLFAPVSGGYRIATQTFELD 381
Cdd:COG2124 249 ------ALYALLRHPEQLARLRAEPE------------------------LLPAAVEETLRLYPPVPLLPRTATEDVELG 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 382 GVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRfspersedreGRFHYLPFGGGVRSCLGKQLATLFLKLLAVELAggS 461
Cdd:COG2124 299 GVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR----------PPNAHLPFGGGPHRCLGAALARLEARIALATLL--R 366
                       410       420       430
                ....*....|....*....|....*....|.
gi 47086709 462 RF---ELSTRTFPRMISVPVVHPTDGLRVKF 489
Cdd:COG2124 367 RFpdlRLAPPEELRWRPSLTLRGPKSLPVRL 397
PLN02302 PLN02302
ent-kaurenoic acid oxidase
23-448 5.55e-57

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 197.24  E-value: 5.55e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   23 ALLLAVSQQLWQLR-----WTATRDKSCKLPMPKGSMGFPIIGETchWFFQGA-------GFHASRRQKYGN--VFKTHL 88
Cdd:PLN02302  12 AIVAGVFVLKWVLRrvnswLYEPKLGEGQPPLPPGDLGWPVIGNM--WSFLRAfkssnpdSFIASFISRYGRtgIYKAFM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   89 LGRPLIRVTGAENVRKVLMgEHSLVTVDWPQSTSTLLGPNSLANSIGDIHRKRRKIF-AKVFSHEALESYLPKIQQVIQE 167
Cdd:PLN02302  90 FGQPTVLVTTPEACKRVLT-DDDAFEPGWPESTVELIGRKSFVGITGEEHKRLRRLTaAPVNGPEALSTYIPYIEENVKS 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  168 TLRVWSSnPDPINVYRESQRLSFNMAVRVLLGfRIPEEEMHCLFSTFQEFVENVFSLPIDLPFSGYRKGIRARDSLQKSI 247
Cdd:PLN02302 169 CLEKWSK-MGEIEFLTELRKLTFKIIMYIFLS-SESELVMEALEREYTTLNYGVRAMAINLPGFAYHRALKARKKLVALF 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  248 E------KAIREKPLHTQGKDytdALDVLLESAKENNTELTMQELkestIELIFAAFATTASASTSLVMQ----LLRHPA 317
Cdd:PLN02302 247 QsivderRNSRKQNISPRKKD---MLDLLLDAEDENGRKLDDEEI----IDLLLMYLNAGHESSGHLTMWatifLQEHPE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  318 VLEKLREELRscGLLHDGCLCQGELRLDSIISLKYLDCVIKEVLRL--FAPVSggYRIATQTFELDGVQVPKGWSVMYSI 395
Cdd:PLN02302 320 VLQKAKAEQE--EIAKKRPPGQKGLTLKDVRKMEYLSQVIDETLRLinISLTV--FREAKTDVEVNGYTIPKGWKVLAWF 395
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 47086709  396 RDTHDTSAVFKDVEAFDPDRFspERSEDREGRFhyLPFGGGVRSCLGKQLATL 448
Cdd:PLN02302 396 RQVHMDPEVYPNPKEFDPSRW--DNYTPKAGTF--LPFGLGSRLCPGNDLAKL 444
PLN02774 PLN02774
brassinosteroid-6-oxidase
19-447 1.48e-53

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 187.29  E-value: 1.48e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   19 LVSMALLLAVSQQLWQLRWTATRDKscKLPMPKGSMGFPIIGETCHWFFQGAGFHASRRQKYGNVFKTHLLGRPLIRVTG 98
Cdd:PLN02774   4 VVLGVLVIIVCLCSALLRWNEVRYS--KKGLPPGTMGWPLFGETTEFLKQGPDFMKNQRLRYGSFFKSHILGCPTIVSMD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   99 AENVRKVLMGEHSLVTVDWPQSTSTLLGPNSLANSIGDIHRKRR-KIFAKVFSHEALESYLPKIQQVIQETLRVWSSnPD 177
Cdd:PLN02774  82 PELNRYILMNEGKGLVPGYPQSMLDILGTCNIAAVHGSTHRYMRgSLLSLISPTMIRDHLLPKIDEFMRSHLSGWDG-LK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  178 PINVYRESQRLSFNMAVRVLLGFR---IPEEEMhclfSTFQEFVENVFSLPIDLPFSGYRKGIRARDSLQKSIEKAIREK 254
Cdd:PLN02774 161 TIDIQEKTKEMALLSALKQIAGTLskpISEEFK----TEFFKLVLGTLSLPIDLPGTNYRSGVQARKNIVRMLRQLIQER 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  255 plHTQGKDYTDALDVLLeSAKENNTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREE---LRSCGL 331
Cdd:PLN02774 237 --RASGETHTDMLGYLM-RKEGNRYKLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKALQELRKEhlaIRERKR 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  332 LHDgclcqgELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAF 411
Cdd:PLN02774 314 PED------PIDWNDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDMELNGYVIPKGWRIYVYTREINYDPFLYPDPMTF 387
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 47086709  412 DPDRFSPERSEDREgrfHYLPFGGGVRSCLGKQLAT 447
Cdd:PLN02774 388 NPWRWLDKSLESHN---YFFLFGGGTRLCPGKELGI 420
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
42-448 4.18e-53

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 186.10  E-value: 4.18e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   42 DKSCKLPMPKGSMGFPIIGET-----CHWFFQGAGFHASRRQKYGNVFKTHLLGRPLIRVTGAEnVRKVLMGEHSLVTVD 116
Cdd:PLN03141   1 SSKKKSRLPKGSLGWPVIGETldfisCAYSSRPESFMDKRRSLYGKVFKSHIFGTPTIVSTDAE-VNKVVLQSDGNAFVP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  117 W-PQSTSTLLGPNSLANSIGDIHRKRRKIFAKVFSHEALESYLPK-IQQVIQETLRVWSSNPdPINVYRESQRLSFNMAV 194
Cdd:PLN03141  80 AyPKSLTELMGKSSILLINGSLQRRVHGLIGAFLKSPHLKAQITRdMERYVSESLDSWRDDP-PVLVQDETKKIAFEVLV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  195 RVLLGFRiPEEEMHCLFSTFQEFVENVFSLPIDLPFSGYRKGIRARDSLQKSIEKAIREKPLHTQGKDYT------DALD 268
Cdd:PLN03141 159 KALISLE-PGEEMEFLKKEFQEFIKGLMSLPIKLPGTRLYRSLQAKKRMVKLVKKIIEEKRRAMKNKEEDetgipkDVVD 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  269 VLLesaKENNTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREE---LRSCGLLHdgclcqGE-LRL 344
Cdd:PLN03141 238 VLL---RDGSDELTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSDCPVALQQLTEEnmkLKRLKADT------GEpLYW 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  345 DSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTHdtsavfKDVEAFD-PDRFSPERSED 423
Cdd:PLN03141 309 TDYMSLPFTQNVITETLRMGNIINGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVH------LDEENYDnPYQFNPWRWQE 382
                        410       420
                 ....*....|....*....|....*.
gi 47086709  424 RE-GRFHYLPFGGGVRSCLGKQLATL 448
Cdd:PLN03141 383 KDmNNSSFTPFGGGQRLCPGLDLARL 408
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
73-489 2.72e-51

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: 179.82  E-value: 2.72e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  73 HASRRQK-YGNVFKTHLLGRPLIRVTGAENVRKVLMGEHSLVTVDwpQSTSTLLGP---NSLANSIGDIHRKRRKIFAKV 148
Cdd:cd11045   2 FARQRYRrYGPVSWTGMLGLRVVALLGPDANQLVLRNRDKAFSSK--QGWDPVIGPffhRGLMLLDFDEHRAHRRIMQQA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 149 FSHEALESYLPKIQQVIQETLRVWSSNPdPINVYRESQRLSFNMAVRVLLGFRiPEEEMHCLFSTFQEFVENVFSL-PID 227
Cdd:cd11045  80 FTRSALAGYLDRMTPGIERALARWPTGA-GFQFYPAIKELTLDLATRVFLGVD-LGPEADKVNKAFIDTVRASTAIiRTP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 228 LPFSGYRKGIRARDSLQKSIEKAIREKplhtQGKDYTDALDVLLESAKENNTELTMQELKESTIELIFAAFATTASASTS 307
Cdd:cd11045 158 IPGTRWWRGLRGRRYLEEYFRRRIPER----RAGGGDDLFSALCRAEDEDGDRFSDDDIVNHMIFLMMAAHDTTTSTLTS 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 308 LVMQLLRHPAVLEKLREELRSCGllhdgclcQGELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPK 387
Cdd:cd11045 234 MAYFLARHPEWQERLREESLALG--------KGTLDYEDLGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTEVLGYRIPA 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 388 GWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREGRFHYLPFGGGVRSCLGKQLATLFLKLLAVELAGGSRFELST 467
Cdd:cd11045 306 GTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEDKVHRYAWAPFGGGAHKCIGLHFAGMEVKAILHQMLRRFRWWSVP 385
                       410       420
                ....*....|....*....|..
gi 47086709 468 RTFPRMISVPVVHPTDGLRVKF 489
Cdd:cd11045 386 GYYPPWWQSPLPAPKDGLPVVL 407
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
88-487 1.11e-50

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: 178.16  E-value: 1.11e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  88 LLGRPLIRVTGAENVRKVLMGEH-SLVTVDWPQSTSTLLGpNSLANSIGDIHRKRRKIFAKVFSHEALESYLPKIQQVIQ 166
Cdd:cd20620   8 LGPRRVYLVTHPDHIQHVLVTNArNYVKGGVYERLKLLLG-NGLLTSEGDLWRRQRRLAQPAFHRRRIAAYADAMVEATA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 167 ETLRVWSSNPD--PINVYRESQRLSFNMAVRVLLGFRIPEE--EMHCLFSTFQEFVENVFSLPIDLPFS----GYRKGIR 238
Cdd:cd20620  87 ALLDRWEAGARrgPVDVHAEMMRLTLRIVAKTLFGTDVEGEadEIGDALDVALEYAARRMLSPFLLPLWlptpANRRFRR 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 239 ARDSLQKSIEKAIREKplHTQGKDYTDALDVLLESAKENNTE-LTMQELKESTIELIFAAFATTASASTSLVMQLLRHPA 317
Cdd:cd20620 167 ARRRLDEVIYRLIAER--RAAPADGGDLLSMLLAARDEETGEpMSDQQLRDEVMTLFLAGHETTANALSWTWYLLAQHPE 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 318 VLEKLREELrscgllhDGCLCQGELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRD 397
Cdd:cd20620 245 VAARLRAEV-------DRVLGGRPPTAEDLPQLPYTEMVLQESLRLYPPAWIIGREAVEDDEIGGYRIPAGSTVLISPYV 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 398 THDTSAVFKDVEAFDPDRFSPERSEDReGRFHYLPFGGGVRSCLGKQLATLFLKLLAVELAggSRFELStrtfpRMISVP 477
Cdd:cd20620 318 THRDPRFWPDPEAFDPERFTPEREAAR-PRYAYFPFGGGPRICIGNHFAMMEAVLLLATIA--QRFRLR-----LVPGQP 389
                       410
                ....*....|....*..
gi 47086709 478 VV-------HPTDGLRV 487
Cdd:cd20620 390 VEpeplitlRPKNGVRM 406
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
50-489 4.24e-49

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: 175.16  E-value: 4.24e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709    50 PKGSMGFPIIGetcHWFFQGAG-----FHASRRQKYGNVFKTHLLGRPLIRVTGAENVRKVLMGEHSLVTVDWPQS-TST 123
Cdd:pfam00067   1 PPGPPPLPLFG---NLLQLGRKgnlhsVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPwFAT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   124 LLGPN---SLANSIGDIHRKRRKIFAKVFSHEALESYLPKIQQVIQ---ETLRVWSSNPDPINVYRESQRLSFNMAVRVL 197
Cdd:pfam00067  78 SRGPFlgkGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARdlvEKLRKTAGEPGVIDITDLLFRAALNVICSIL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   198 LGFRIPEEEMHcLFSTFQEFVENVFSL------------PIDLPFSG--YRKGIRARDSLQKSIEKAI--REKPLHTQGK 261
Cdd:pfam00067 158 FGERFGSLEDP-KFLELVKAVQELSSLlsspspqlldlfPILKYFPGphGRKLKRARKKIKDLLDKLIeeRRETLDSAKK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   262 DYTDALDVLLE-SAKENNTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRScgLLHDgclcQG 340
Cdd:pfam00067 237 SPRDFLDALLLaKEEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDE--VIGD----KR 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   341 ELRLDSIISLKYLDCVIKEVLRLFAPVSGG-YRIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPE 419
Cdd:pfam00067 311 SPTYDDLQNMPYLDAVIKETLRLHPVVPLLlPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDE 390
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47086709   420 RSEDREgRFHYLPFGGGVRSCLGKQLATLFLKL-LAVELaggSRFELSTRTF----PRMISVPVVHPTDGLRVKF 489
Cdd:pfam00067 391 NGKFRK-SFAFLPFGAGPRNCLGERLARMEMKLfLATLL---QNFEVELPPGtdppDIDETPGLLLPPKPYKLKF 461
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
71-487 9.59e-44

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: 159.73  E-value: 9.59e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  71 GFHASRRQkYGNVFKTHLLGRPLIRVTGAENVRKVLMGE-HSLVTVDWPQSTSTLLGpNSLANSIGDIHRKRRKIFAKVF 149
Cdd:cd11049   4 GFLSSLRA-HGDLVRIRLGPRPAYVVTSPELVRQVLVNDrVFDKGGPLFDRARPLLG-NGLATCPGEDHRRQRRLMQPAF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 150 SHEALESYLPKIQQVIQETLRVWSsNPDPINVYRESQRLSFNMAVRVLLGFRIPEEEM----HCLFSTFQEFVENVFSLP 225
Cdd:cd11049  82 HRSRIPAYAEVMREEAEALAGSWR-PGRVVDVDAEMHRLTLRVVARTLFSTDLGPEAAaelrQALPVVLAGMLRRAVPPK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 226 I--DLPFSGYRKGIRARDSLQKSIEKAIREkpLHTQGKDYTDALDVLLESAKENNTELTMQELKESTIELIFAAFATTAS 303
Cdd:cd11049 161 FleRLPTPGNRRFDRALARLRELVDEIIAE--YRASGTDRDDLLSLLLAARDEEGRPLSDEELRDQVITLLTAGTETTAS 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 304 ASTSLVMQLLRHPAVLEKLREELrscgllhDGCLCQGELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGV 383
Cdd:cd11049 239 TLAWAFHLLARHPEVERRLHAEL-------DAVLGGRPATFEDLPRLTYTRRVVTEALRLYPPVWLLTRRTTADVELGGH 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 384 QVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREgRFHYLPFGGGVRSCLGKQLATLFLKLLAVELAGGSRF 463
Cdd:cd11049 312 RLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVP-RGAFIPFGAGARKCIGDTFALTELTLALATIASRWRL 390
                       410       420
                ....*....|....*....|....
gi 47086709 464 ELSTRTFPRMISVPVVHPtDGLRV 487
Cdd:cd11049 391 RPVPGRPVRPRPLATLRP-RRLRM 413
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
16-453 2.44e-43

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 160.14  E-value: 2.44e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   16 AACLVSMALLLAVSqqLWQLRWTATRdkscKLPMPKGSMGFPIIGETchwfFQGAGFHAS---------RRQKYGNVFKT 86
Cdd:PLN02987   4 SAFLLLLSSLAAIF--FLLLRRTRYR----RMRLPPGSLGLPLVGET----LQLISAYKTenpepfideRVARYGSLFMT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   87 HLLGRPLIRVTGAENVRKVLMGEHSLVTVDWPQSTSTLLGPNSLANSIGDIHRKRRKIFAKVFSHEALESYL-PKIQQVI 165
Cdd:PLN02987  74 HLFGEPTVFSADPETNRFILQNEGKLFECSYPGSISNLLGKHSLLLMKGNLHKKMHSLTMSFANSSIIKDHLlLDIDRLI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  166 QETLRVWSSNpdpINVYRESQRLSFNMAVRVLLGFRiPEEEMHCLFSTFQEFVENVFSLPIDLPFSGYRKGIRARDSLQK 245
Cdd:PLN02987 154 RFNLDSWSSR---VLLMEEAKKITFELTVKQLMSFD-PGEWTESLRKEYVLVIEGFFSVPLPLFSTTYRRAIQARTKVAE 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  246 SIEKAIREKPLHTQ--GKDYTDALDVLLESAKENNTEltmqELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLR 323
Cdd:PLN02987 230 ALTLVVMKRRKEEEegAEKKKDMLAALLASDDGFSDE----EIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLK 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  324 EELRSC-GLLHDgclcQGELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTHDTS 402
Cdd:PLN02987 306 EEHEKIrAMKSD----SYSLEWSDYKSMPFTQCVVNETLRVANIIGGIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDH 381
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 47086709  403 AVFKDVEAFDPDRFSPERSEDREGRFhYLPFGGGVRSCLGKQLATLFLKLL 453
Cdd:PLN02987 382 EYFKDARTFNPWRWQSNSGTTVPSNV-FTPFGGGPRLCPGYELARVALSVF 431
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
81-487 2.76e-43

cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the omega-hydroxylation of the terminal carbon of fatty acids, including essential signaling molecules such as eicosanoids, prostaglandins and leukotrienes, and they are important for chemical defense. There are seven vertebrate family 4 subfamilies: CYP4A, CYP4B, CYP4F, CYP4T, CYP4V, CYP4X, and CYP4Z; three (CYP4X, CYP4A, CYP4Z) are specific to mammals. CYP4 enzymes metabolize fatty acids off various length, level of saturation, and branching. Specific subfamilies show preferences for the length of fatty acids; CYP4B, CYP4A and CYP4V, and CYP4F preferentially metabolize short (C7-C10), medium (C10-C16), and long to very long (C18-C26) fatty acid chains, respectively. CYP4 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410721 [Multi-domain]  Cd Length: 426  Bit Score: 158.84  E-value: 2.76e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  81 GNVFKTHLLGRPLIRVTGAENVRKVLMGEHSLVTVDWPQSTSTLLGpNSLANSIGDIHRKRRKIFAKVFSHEALESYLPk 160
Cdd:cd20628   1 GGVFRLWIGPKPYVVVTNPEDIEVILSSSKLITKSFLYDFLKPWLG-DGLLTSTGEKWRKRRKLLTPAFHFKILESFVE- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 161 iqqVIQETLRVW------SSNPDPINVYRESQRLSFNMAVRVLLGFripeeEMHCLFSTFQEFVENV-----------FS 223
Cdd:cd20628  79 ---VFNENSKILveklkkKAGGGEFDIFPYISLCTLDIICETAMGV-----KLNAQSNEDSEYVKAVkrileiilkriFS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 224 LPIDLPF-----SGYRKGIRARDSLQKSIEKAIREK--PLHTQGKDYTDA-----------LDVLLESAKENNTeLTMQE 285
Cdd:cd20628 151 PWLRFDFifrltSLGKEQRKALKVLHDFTNKVIKERreELKAEKRNSEEDdefgkkkrkafLDLLLEAHEDGGP-LTDED 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 286 LKE--------------STIelifaafattasastSLVMQLL-RHPAVLEKLREELRScgllhdgcLCQGELRLDS---I 347
Cdd:cd20628 230 IREevdtfmfaghdttaSAI---------------SFTLYLLgLHPEVQEKVYEELDE--------IFGDDDRRPTledL 286
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 348 ISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREgR 427
Cdd:cd20628 287 NKMKYLERVIKETLRLYPSVPFIGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSAKRH-P 365
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47086709 428 FHYLPFGGGVRSCLGKQLATLFLK-LLAVELaggSRFELSTR-TFPRMISVP--VVHPTDGLRV 487
Cdd:cd20628 366 YAYIPFSAGPRNCIGQKFAMLEMKtLLAKIL---RNFRVLPVpPGEDLKLIAeiVLRSKNGIRV 426
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
88-457 8.71e-42

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: 154.33  E-value: 8.71e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  88 LLGRPLIRVTGAENVRKVLMGEHS----LVTVDwpqSTSTLLGPNSLANSIGDIHRKRRKIFAKVFSHEALESYLPKIQQ 163
Cdd:cd11082   7 LVGKFIVFVTDAELSRKIFSNNRPdafhLCLHP---NAKKILGEDNLIFMFGEEHKELRKSLLPLFTRKALGLYLPIQER 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 164 VIQETLRVW----SSNPDPINVyresqRLSF---NMAV--RVLLGFRIPEEEMHclFST-FQEFVENVFSLPIDLPFSGY 233
Cdd:cd11082  84 VIRKHLAKWlensKSGDKPIEM-----RPLIrdlNLETsqTVFVGPYLDDEARR--FRIdYNYFNVGFLALPVDFPGTAL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 234 RKGIRARDSLQKSIEKAIREKPLHTQ-GKDYTDALDV----LLESAKENnTELTMQELKESTIELIFAAFA-----TTAS 303
Cdd:cd11082 157 WKAIQARKRIVKTLEKCAAKSKKRMAaGEEPTCLLDFwtheILEEIKEA-EEEGEPPPPHSSDEEIAGTLLdflfaSQDA 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 304 ASTSLVM--QLL-RHPAVLEKLREELRScgllhdgcLCQGE---LRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQT 377
Cdd:cd11082 236 STSSLVWalQLLaDHPDVLAKVREEQAR--------LRPNDeppLTLDLLEEMKYTRQVVKEVLRYRPPAPMVPHIAKKD 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 378 FEL-DGVQVPKGWSVMYSIRDT-HDTsavFKDVEAFDPDRFSPERSEDREGRFHYLPFGGGVRSCLGKQLA----TLFLK 451
Cdd:cd11082 308 FPLtEDYTVPKGTIVIPSIYDScFQG---FPEPDKFDPDRFSPERQEDRKYKKNFLVFGAGPHQCVGQEYAinhlMLFLA 384

                ....*.
gi 47086709 452 LLAVEL 457
Cdd:cd11082 385 LFSTLV 390
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
77-489 1.93e-38

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: 145.05  E-value: 1.93e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  77 RQKYGNVFKTHLLGRPLIRVTGAENVRKVLMGEHSlvtvDWPQS-----TSTLLGPNSLANSIGDIHRKRRKIFAKVFSH 151
Cdd:cd11042   2 RKKYGDVFTFNLLGKKVTVLLGPEANEFFFNGKDE----DLSAEevygfLTPPFGGGVVYYAPFAEQKEQLKFGLNILRR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 152 EALESYLPKIQQVIQETLRVWSsNPDPINVYRESQRLSFNMAVRVLLG--FRipeeEMhcLFSTFQEFVE---------N 220
Cdd:cd11042  78 GKLRGYVPLIVEEVEKYFAKWG-ESGEVDLFEEMSELTILTASRCLLGkeVR----EL--LDDEFAQLYHdldggftpiA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 221 VFSLPIDLPfsGYRKGIRARDSLQKSIEKAIREKPLHTQgKDYTDALDVLLESAKENNTELTMQELKESTIELIFAAFAT 300
Cdd:cd11042 151 FFFPPLPLP--SFRRRDRARAKLKEIFSEIIQKRRKSPD-KDEDDMLQTLMDAKYKDGRPLTDDEIAGLLIALLFAGQHT 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 301 TASASTSLVMQLLRHPAVLEKLREELRScgLLHDGclcQGELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFEL 380
Cdd:cd11042 228 SSATSAWTGLELLRNPEHLEALREEQKE--VLGDG---DDPLTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKPFEV 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 381 DGVQ--VPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREG-RFHYLPFGGGVRSCLGKQLATLFLKLLAVEL 457
Cdd:cd11042 303 EGGGyvIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAEDSKGgKFAYLPFGAGRHRCIGENFAYLQIKTILSTL 382
                       410       420       430
                ....*....|....*....|....*....|....*.
gi 47086709 458 AGGSRFELSTRTFP----RMISVPVVHPTdglRVKF 489
Cdd:cd11042 383 LRNFDFELVDSPFPepdyTTMVVWPKGPA---RVRY 415
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
83-489 5.46e-38

cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is composed of CYPs from unicellular ciliates similar to Tetrahymena thermophila CYP5011A1, whose function is still unknown. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410714 [Multi-domain]  Cd Length: 427  Bit Score: 144.32  E-value: 5.46e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  83 VFKTHLLGRPLIRVTGAENVRKVLMGEHSLVTVDWPQSTSTLLGpNSLANSIGDIHRKRRKIFAKVFSHEALESYLPKIQ 162
Cdd:cd20621   5 IIVSNLGSKPLISLVDPEYIKEFLQNHHYYKKKFGPLGIDRLFG-KGLLFSEGEEWKKQRKLLSNSFHFEKLKSRLPMIN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 163 QVIQETLRvwSSNPDPINVYRESQRLSFNMAVRVLLGFRIPE------EEMHCLFSTFQEFVENVFSLPID--------- 227
Cdd:cd20621  84 EITKEKIK--KLDNQNVNIIQFLQKITGEVVIRSFFGEEAKDlkingkEIQVELVEILIESFLYRFSSPYFqlkrlifgr 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 228 -----LPFSGYRKGIRARDSLQKSIEKAI-----REKPLHTQGKDYTDALDVLLESAKENNTELTMQEL----------- 286
Cdd:cd20621 162 kswklFPTKKEKKLQKRVKELRQFIEKIIqnrikQIKKNKDEIKDIIIDLDLYLLQKKKLEQEITKEEIiqqfitfffag 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 287 KESTIELIFAAfattasastsLVMqLLRHPAVLEKLREELRSCgllhdgCLCQGELRLDSIISLKYLDCVIKEVLRLFAP 366
Cdd:cd20621 242 TDTTGHLVGMC----------LYY-LAKYPEIQEKLRQEIKSV------VGNDDDITFEDLQKLNYLNAFIKEVLRLYNP 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 367 VSGG-YRIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSpERSEDREGRFHYLPFGGGVRSCLGKQL 445
Cdd:cd20621 305 APFLfPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWL-NQNNIEDNPFVFIPFSAGPRNCIGQHL 383
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 47086709 446 ATLFLKLLAVELAggSRFELSTRTFP--RMISVPVVHPTDGLRVKF 489
Cdd:cd20621 384 ALMEAKIILIYIL--KNFEIEIIPNPklKLIFKLLYEPVNDLLLKL 427
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
79-457 2.90e-37

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: 141.95  E-value: 2.90e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  79 KYGNVFKTHLLGRPLIRVTGAENVRKVLMGE-------HSLVTVDWPQsTSTLLgpnslanSIGDIHRKR-RKIFAKVFS 150
Cdd:cd11055   1 KYGKVFGLYFGTIPVIVVSDPEMIKEILVKEfsnftnrPLFILLDEPF-DSSLL-------FLKGERWKRlRTTLSPTFS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 151 HEALESYLPKIQQVIQETLRVWSSNPD---PINVYRESQRLSFNMAVRVLLGFRIPEEEM--HCLFSTFQEFVENVFSLP 225
Cdd:cd11055  73 SGKLKLMVPIINDCCDELVEKLEKAAEtgkPVDMKDLFQGFTLDVILSTAFGIDVDSQNNpdDPFLKAAKKIFRNSIIRL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 226 IDLP-----------FSGYRKGIRARDSLQKSIEKAIREKpLHTQGKDYTDALDVLLESAKENNTE----LTMQELKE-- 288
Cdd:cd11055 153 FLLLllfplrlflflLFPFVFGFKSFSFLEDVVKKIIEQR-RKNKSSRRKDLLQLMLDAQDSDEDVskkkLTDDEIVAqs 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 289 ------------STIelifaafattasastSLVMQLL-RHPAVLEKLREELRSCglLHDgclcQGELRLDSIISLKYLDC 355
Cdd:cd11055 232 fifllagyettsNTL---------------SFASYLLaTNPDVQEKLIEEIDEV--LPD----DGSPTYDTVSKLKYLDM 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 356 VIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREgRFHYLPFGG 435
Cdd:cd11055 291 VINETLRLYPPAFFISRECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKAKRH-PYAYLPFGA 369
                       410       420
                ....*....|....*....|..
gi 47086709 436 GVRSCLGKQLATLFLKLLAVEL 457
Cdd:cd11055 370 GPRNCIGMRFALLEVKLALVKI 391
PLN02500 PLN02500
cytochrome P450 90B1
24-465 4.97e-37

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 142.69  E-value: 4.97e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   24 LLLAVSQQLWQLRWTATRDKSCKLPMPKGSMGFPIIGETCHWFFQGAG-----FHASRRQKYGNVFKTHLLGRPLIRVTG 98
Cdd:PLN02500  14 LLPSILSLLLVFILTKRRPKQKRFNLPPGNMGWPFLGETIGYLKPYSAtsigeFMEQHISRYGKIYRSNLFGEPTIVSAD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   99 AENVRKVLMGEHSLVTVDWPQSTSTLLGPNSLANSIGDIHRKRRKIFAKVFSHEALESYLpkIQQVIQETLRVWSSNPD- 177
Cdd:PLN02500  94 AGLNRFILQNEGRLFECSYPRSIGGILGKWSMLVLVGDMHRDMRSISLNFLSHARLRTHL--LKEVERHTLLVLDSWKEn 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  178 -PINVYRESQRLSFNMAVRVLLGFRIPEEEMHCLFSTFQEFVENVFSLPIDLPFSGYRKGIRARDSLQKSIEKAIREKPL 256
Cdd:PLN02500 172 sTFSAQDEAKKFTFNLMAKHIMSMDPGEEETEQLKKEYVTFMKGVVSAPLNFPGTAYRKALKSRATILKFIERKMEERIE 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  257 HTQGKDYTDALDVLLESA-KENNteLTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRSCGLLHDG 335
Cdd:PLN02500 252 KLKEEDESVEEDDLLGWVlKHSN--LSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEHLEIARAKKQ 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  336 cLCQGELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDR 415
Cdd:PLN02500 330 -SGESELNWEDYKKMEFTQCVINETLRLGNVVRFLHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWR 408
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 47086709  416 F---SPERSEDREGRF---HYLPFGGGVRSCLGKQLATLFLKLLAVELAGGSRFEL 465
Cdd:PLN02500 409 WqqnNNRGGSSGSSSAttnNFMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFNWEL 464
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
78-446 5.44e-36

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: 138.81  E-value: 5.44e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  78 QKYGNVFKTHLLGRPLIRVTGAENVRKVLMGEHsLVTVDWPQST-STLLGPNSLANSI-----GDIHRKRRKIFAKVFSH 151
Cdd:cd20613   9 KEYGPVFVFWILHRPIVVVSDPEAVKEVLITLN-LPKPPRVYSRlAFLFGERFLGNGLvtevdHEKWKKRRAILNPAFHR 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 152 EALESYLPKIQQVIQ---ETLRVWSSNPDPINVYRESQRLSFNMAVRVLLG--FRIPEEEMH----CLFSTFQEFVENVF 222
Cdd:cd20613  88 KYLKNLMDEFNESADllvEKLSKKADGKTEVNMLDEFNRVTLDVIAKVAFGmdLNSIEDPDSpfpkAISLVLEGIQESFR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 223 SLPIDLPFS--GYRKGIRA-----RDSLQKSIEKAIREKplhtQGKDYTDAlDVL--LESAKENNTELTMQEL------- 286
Cdd:cd20613 168 NPLLKYNPSkrKYRREVREaikflRETGRECIEERLEAL----KRGEEVPN-DILthILKASEEEPDFDMEELlddfvtf 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 287 ----KESTIELIFAafattasastsLVMQLLRHPAVLEKLREELrscgllhDGCL-CQGELRLDSIISLKYLDCVIKEVL 361
Cdd:cd20613 243 fiagQETTANLLSF-----------TLLELGRHPEILKRLQAEV-------DEVLgSKQYVEYEDLGKLEYLSQVLKETL 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 362 RLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREgRFHYLPFGGGVRSCL 441
Cdd:cd20613 305 RLYPPVPGTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEAPEKIP-SYAYFPFSLGPRSCI 383

                ....*
gi 47086709 442 GKQLA 446
Cdd:cd20613 384 GQQFA 388
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
80-485 5.01e-35

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: 136.25  E-value: 5.01e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  80 YGNVFKTH-LLGRPLIRVTGAENVRKVLMgEHSLVTVDWPQ--STSTLLGPNSLANSIGDIHRKRRKIFAKVFSHEALES 156
Cdd:cd11069   1 YGGLIRYRgLFGSERLLVTDPKALKHILV-TNSYDFEKPPAfrRLLRRILGDGLLAAEGEEHKRQRKILNPAFSYRHVKE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 157 YLPKIQQVIQETLRVWS----SNPDP---INVYRESQRLSFNMAVRVLLG--FRIPEEEMHCLFSTFQEFVENVFSLPI- 226
Cdd:cd11069  80 LYPIFWSKAEELVDKLEeeieESGDEsisIDVLEWLSRATLDIIGLAGFGydFDSLENPDNELAEAYRRLFEPTLLGSLl 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 227 -------------DLPFSGYRKGIRARDSLQKSIEKAIREK------PLHTQGKDytdALDVLLES-AKENNTELTMQEL 286
Cdd:cd11069 160 filllflprwlvrILPWKANREIRRAKDVLRRLAREIIREKkaalleGKDDSGKD---ILSILLRAnDFADDERLSDEEL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 287 K-----------ESTielifaafattASASTSLVMQLLRHPAVLEKLREELRScgllHDGCLCQGELRLDSIISLKYLDC 355
Cdd:cd11069 237 IdqiltflaaghETT-----------STALTWALYLLAKHPDVQERLREEIRA----ALPDPPDGDLSYDDLDRLPYLNA 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 356 VIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTH-DTSAVFKDVEAFDPDRF-SPERSEDREGR---FHY 430
Cdd:cd11069 302 VCRETLRLYPPVPLTSREATKDTVIKGVPIPKGTVVLIPPAAINrSPEIWGPDAEEFNPERWlEPDGAASPGGAgsnYAL 381
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 47086709 431 LPFGGGVRSCLGKQLATLFLKLLAVELAGGSRFELST-RTFPRMISVPVVHPTDGL 485
Cdd:cd11069 382 LTFLHGPRSCIGKKFALAEMKVLLAALVSRFEFELDPdAEVERPIGIITRPPVDGL 437
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
81-450 5.80e-34

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: 132.72  E-value: 5.80e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  81 GNVFKTHLLGRPLIRVTGAENVRKVLMgEHSLVTVDWPQSTSTLLGPNS--LANSIGDIHRKRRKIFAKVFS-HEALESY 157
Cdd:cd20617   1 GGIFTLWLGDVPTVVLSDPEIIKEAFV-KNGDNFSDRPLLPSFEIISGGkgILFSNGDYWKELRRFALSSLTkTKLKKKM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 158 LPKI-QQVIQ--ETLRVWSSNPDPINVYRESQRLSFNMAVRVLLGFRIP---EEEMHCLFSTFQEFVENV--------FS 223
Cdd:cd20617  80 EELIeEEVNKliESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGKRFPdedDGEFLKLVKPIEEIFKELgsgnpsdfIP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 224 LPIDLPFSGYRKGIRARDSLQKSIEKAIREkplHTQGKDYTDALD-----VLLESAKENNTELTMQELKESTIELIFAAF 298
Cdd:cd20617 160 ILLPFYFLYLKKLKKSYDKIKDFIEKIIEE---HLKTIDPNNPRDliddeLLLLLKEGDSGLFDDDSIISTCLDLFLAGT 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 299 ATTASASTSLVMQLLRHPAVLEKLREELRSCGllhdgclcqGELRLDSI---ISLKYLDCVIKEVLRLFAPVS-GGYRIA 374
Cdd:cd20617 237 DTTSTTLEWFLLYLANNPEIQEKIYEEIDNVV---------GNDRRVTLsdrSKLPYLNAVIKEVLRLRPILPlGLPRVT 307
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47086709 375 TQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREGRFhyLPFGGGVRSCLGKQLAT--LFL 450
Cdd:cd20617 308 TEDTEIGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDGNKLSEQF--IPFGIGKRNCVGENLARdeLFL 383
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
77-477 8.10e-33

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: 129.57  E-value: 8.10e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  77 RQKYGNVFKTHLLGRPLIRVTGAENVRKVLMGEHslvtvDWP------------QSTSTLLGpnsLANSIGDIHRKRRKI 144
Cdd:cd11054   1 HKKYGPIVREKLGGRDIVHLFDPDDIEKVFRNEG-----KYPirpsleplekyrKKRGKPLG---LLNSNGEEWHRLRSA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 145 FAKVFSH-EALESYLPKIQQVIQETLRVW-----SSNPDPINVYRESQRLSFNMAVRVLLGFRI------PEEEMHCLFS 212
Cdd:cd11054  73 VQKPLLRpKSVASYLPAINEVADDFVERIrrlrdEDGEEVPDLEDELYKWSLESIGTVLFGKRLgclddnPDSDAQKLIE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 213 TFQEFVENVFSLPIDLPFS------GYRKGIRARDSLQKSIEKAIREKPLHTQGKDYTDALDV-LLESAKENNtELTMQE 285
Cdd:cd11054 153 AVKDIFESSAKLMFGPPLWkyfptpAWKKFVKAWDTIFDIASKYVDEALEELKKKDEEDEEEDsLLEYLLSKP-GLSKKE 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 286 LKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRScgLLHDGclcqGELRLDSIISLKYLDCVIKEVLRLFA 365
Cdd:cd11054 232 IVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRS--VLPDG----EPITAEDLKKMPYLKACIKESLRLYP 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 366 PVSGGYRIATQTFELDGVQVPKGWSVMYSirdthdTSAVFKDVEAF-DPDRFSPER---SEDREGRFH---YLPFGGGVR 438
Cdd:cd11054 306 VAPGNGRILPKDIVLSGYHIPKGTLVVLS------NYVMGRDEEYFpDPEEFIPERwlrDDSENKNIHpfaSLPFGFGPR 379
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 47086709 439 SCLGKQLATLFLKLLAVELAggSRFELSTRTFP-----RMISVP 477
Cdd:cd11054 380 MCIGRRFAELEMYLLLAKLL--QNFKVEYHHEElkvktRLILVP 421
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
237-488 4.04e-32

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: 127.67  E-value: 4.04e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 237 IRARdslQKSIEKAIREKPlhtQGKDYTDALDVLLESAKENNTELTMQELKE--------------STIelifaafatta 302
Cdd:cd20659 185 IKKR---RKELEDNKDEAL---SKRKYLDFLDILLTARDEDGKGLTDEEIRDevdtflfaghdttaSGI----------- 247
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 303 sasTSLVMQLLRHPAVLEKLREELRScgLLHDgclcQGELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDG 382
Cdd:cd20659 248 ---SWTLYSLAKHPEHQQKCREEVDE--VLGD----RDDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPITIDG 318
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 383 VQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREGrFHYLPFGGGVRSCLGKQLATLFLKL-LAVELaggS 461
Cdd:cd20659 319 VTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIKKRDP-FAFIPFSAGPRNCIGQNFAMNEMKVvLARIL---R 394
                       250       260       270
                ....*....|....*....|....*....|
gi 47086709 462 RFELS---TRTFPRMISVpVVHPTDGLRVK 488
Cdd:cd20659 395 RFELSvdpNHPVEPKPGL-VLRSKNGIKLK 423
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
138-473 5.88e-32

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: 127.03  E-value: 5.88e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 138 HRKRRKIFAKVFSHEALesYLPKIQQVIQETLRVW-------SSNPDPINVYRE--------SQRLSFNMAVRVLLGFRI 202
Cdd:cd11059  55 HSARRRLLSGVYSKSSL--LRAAMEPIIRERVLPLidriakeAGKSGSVDVYPLftalamdvVSHLLFGESFGTLLLGDK 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 203 PEEEMHCLFSTFQEFVENVFSLPIDLPFSGYRKGIRARDSLQKSIEK-AIR-----EKPLHTQGKDYTDALDVLLESAKE 276
Cdd:cd11059 133 DSRERELLRRLLASLAPWLRWLPRYLPLATSRLIIGIYFRAFDEIEEwALDlcaraESSLAESSDSESLTVLLLEKLKGL 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 277 NNTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRScgllHDGCLCQGELrLDSIISLKYLDCV 356
Cdd:cd11059 213 KKQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELAG----LPGPFRGPPD-LEDLDKLPYLNAV 287
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 357 IKEVLRLFAPVSGGY-RIATQTFE-LDGVQVPKGWSVM---YSIrdtHDTSAVFKDVEAFDPDRF-SPERSEDREGRFHY 430
Cdd:cd11059 288 IRETLRLYPPIPGSLpRVVPEGGAtIGGYYIPGGTIVStqaYSL---HRDPEVFPDPEEFDPERWlDPSGETAREMKRAF 364
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 47086709 431 LPFGGGVRSCLGKQLATLFLKLLAVELAggSRFELSTRTFPRM 473
Cdd:cd11059 365 WPFGSGSRMCIGMNLALMEMKLALAAIY--RNYRTSTTTDDDM 405
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
77-466 1.34e-31

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: 126.30  E-value: 1.34e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  77 RQKYGNVFkTHLLG-RPLIRVTGAENVRKVLMGEHSLVTVDWPQS-TSTLLGpNSLANSIGDIHRKRRKIFAKVFSHEAL 154
Cdd:cd11052   8 IKQYGKNF-LYWYGtDPRLYVTEPELIKELLSKKEGYFGKSPLQPgLKKLLG-RGLVMSNGEKWAKHRRIANPAFHGEKL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 155 ESYLPKIQQVIQETLRVW----SSNPDPINVYRESQRLSFNMAVRVLLG---------FRIPEEEMHCLFSTFQE-FVEN 220
Cdd:cd11052  86 KGMVPAMVESVSDMLERWkkqmGEEGEEVDVFEEFKALTADIISRTAFGssyeegkevFKLLRELQKICAQANRDvGIPG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 221 VFSLPidlpfsgYRKGIRA-------RDSLQKSIEKaiREKPL-HTQGKDY-TDALDVLLESAK--ENNTELTMQEL--- 286
Cdd:cd11052 166 SRFLP-------TKGNKKIkkldkeiEDSLLEIIKK--REDSLkMGRGDDYgDDLLGLLLEANQsdDQNKNMTVQEIvde 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 287 --------KESTIELIFAAfattasastslVMQLLRHPAVLEKLREELRS-CGllhdgclcQGELRLDSIISLKYLDCVI 357
Cdd:cd11052 237 cktfffagHETTALLLTWT-----------TMLLAIHPEWQEKAREEVLEvCG--------KDKPPSDSLSKLKTVSMVI 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 358 KEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVF-KDVEAFDPDRFSPERSEDREGRFHYLPFGGG 436
Cdd:cd11052 298 NESLRLYPPAVFLTRKAKEDIKLGGLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFADGVAKAAKHPMAFLPFGLG 377
                       410       420       430
                ....*....|....*....|....*....|.
gi 47086709 437 VRSCLGKQLATLFLKL-LAVELaggSRFELS 466
Cdd:cd11052 378 PRNCIGQNFATMEAKIvLAMIL---QRFSFT 405
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
312-486 8.72e-30

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: 121.11  E-value: 8.72e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 312 LLRHPAVLEKLREELRSCGLLHDGclcqgELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDG--VQVPKGW 389
Cdd:cd11056 256 LAKNPEIQEKLREEIDEVLEKHGG-----ELTYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGtdVVIEKGT 330
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 390 SVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREgRFHYLPFGGGVRSCLGKQLATLFLKLLAVELAGGSRFELSTRT 469
Cdd:cd11056 331 PVIIPVYALHHDPKYYPEPEKFDPERFSPENKKKRH-PYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSSKT 409
                       170       180
                ....*....|....*....|
gi 47086709 470 FPRMI---SVPVVHPTDGLR 486
Cdd:cd11056 410 KIPLKlspKSFVLSPKGGIW 429
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
80-455 6.10e-29

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: 118.45  E-value: 6.10e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  80 YGNVFKTHLLGRPLIRVTGAENVRKvLMGEHSLVTVDWPQSTSTLL----GPNSLANSIGDIHRKRRKIFAKVFSHEALE 155
Cdd:cd11065   1 YGPIISLKVGGQTIIVLNSPKAAKD-LLEKRSAIYSSRPRMPMAGElmgwGMRLLLMPYGPRWRLHRRLFHQLLNPSAVR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 156 SYLPKIQQVIQETLRVWSSNPDpiNVYRESQRLSFNMAVRVLLGFRIPE---EEMHCLFSTFQEFVE---------NVF- 222
Cdd:cd11065  80 KYRPLQELESKQLLRDLLESPD--DFLDHIRRYAASIILRLAYGYRVPSyddPLLRDAEEAMEGFSEagspgaylvDFFp 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 223 ---SLPIDLPFSGYRKGIRARDSLQKSIEKAIRE-KPLHTQGKDYTDALDVLLESaKENNTELTMQELKESTIELIFAAF 298
Cdd:cd11065 158 flrYLPSWLGAPWKRKARELRELTRRLYEGPFEAaKERMASGTATPSFVKDLLEE-LDKEGGLSEEEIKYLAGSLYEAGS 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 299 ATTASASTSLVMQLLRHPAVLEKLREEL-RSCGllhDGCLcqgeLRLDSIISLKYLDCVIKEVLRlFAPVS--GGYRIAT 375
Cdd:cd11065 237 DTTASTLQTFILAMALHPEVQKKAQEELdRVVG---PDRL----PTFEDRPNLPYVNAIVKEVLR-WRPVAplGIPHALT 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 376 QTFELDGVQVPKGWSVM---YSIrdTHDtSAVFKDVEAFDPDRF--SPERSEDREGRFHYlPFGGGVRSCLGKQLA--TL 448
Cdd:cd11065 309 EDDEYEGYFIPKGTTVIpnaWAI--HHD-PEVYPDPEEFDPERYldDPKGTPDPPDPPHF-AFGFGRRICPGRHLAenSL 384
                       410
                ....*....|
gi 47086709 449 FL---KLLAV 455
Cdd:cd11065 385 FIaiaRLLWA 394
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
127-467 6.77e-29

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: 118.47  E-value: 6.77e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 127 PNSLANSIGDIHRKRRKIFAKVFSHEALESYLPKIQQVIQETLRVWSSNPD--PINVYRESQRLSFNMAVRVLLGF--RI 202
Cdd:cd11057  44 GRGLFSAPYPIWKLQRKALNPSFNPKILLSFLPIFNEEAQKLVQRLDTYVGggEFDILPDLSRCTLEMICQTTLGSdvND 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 203 PEEEMHCLFSTFQEFVENVF------SLPIDLP---FSGYRKGIRARDSLQKS----IEKAIREKPLHTQGKDYTDALDV 269
Cdd:cd11057 124 ESDGNEEYLESYERLFELIAkrvlnpWLHPEFIyrlTGDYKEEQKARKILRAFsekiIEKKLQEVELESNLDSEEDEENG 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 270 --------LLESAKENNTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRS-CGllhdgcLCQG 340
Cdd:cd11057 204 rkpqifidQLLELARNGEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEvFP------DDGQ 277
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 341 ELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELD-GVQVPKGWSVMYSIRDTHDTSAVF-KDVEAFDPDRFSP 418
Cdd:cd11057 278 FITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLSnGVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLP 357
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 47086709 419 ERSEDREgRFHYLPFGGGVRSCLGKQLATLFLKLLAVELAggSRFELST 467
Cdd:cd11057 358 ERSAQRH-PYAFIPFSAGPRNCIGWRYAMISMKIMLAKIL--RNYRLKT 403
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
129-489 9.36e-29

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: 117.93  E-value: 9.36e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 129 SLANSIGDIHRKRRKIFAKVFSHEALESylPKIQQVIQET----LRVWSSNPDpINVYRESQRLSFNMAVRVLlgfRIPE 204
Cdd:cd20614  57 TMAAQDGALHRRARAASNPSFTPKGLSA--AGVGALIAEViearIRAWLSRGD-VAVLPETRDLTLEVIFRIL---GVPT 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 205 EEMHCLFSTFQEFVENVFSLPIDLPFSGYRKGIRARDSLQKSIEKAIREKplhTQGKDYTDALDVLLESAKENNTELTMQ 284
Cdd:cd20614 131 DDLPEWRRQYRELFLGVLPPPVDLPGMPARRSRRARAWIDARLSQLVATA---RANGARTGLVAALIRARDDNGAGLSEQ 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 285 ELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRSCGllhDGCLCQGELRldsiiSLKYLDCVIKEVLRLF 364
Cdd:cd20614 208 ELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAAG---DVPRTPAELR-----RFPLAEALFRETLRLH 279
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 365 APVSGGYRIATQTFELDGVQVPKGwsVMYSIRDTHdtsaVFKDVEAF-DPDRFSPERSEDREGR---FHYLPFGGGVRSC 440
Cdd:cd20614 280 PPVPFVFRRVLEEIELGGRRIPAG--THLGIPLLL----FSRDPELYpDPDRFRPERWLGRDRApnpVELLQFGGGPHFC 353
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 47086709 441 LGKQLA----TLFLKLLAVEL-AGGSRFELSTRtFPRMISVPVVHPTDGLRVKF 489
Cdd:cd20614 354 LGYHVAcvelVQFIVALARELgAAGIRPLLVGV-LPGRRYFPTLHPSNKTRVAF 406
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
136-466 1.03e-27

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: 115.01  E-value: 1.03e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 136 DIHRKRRKIFAKVFSHEALESYLPKIQQVIQETLRVWSSNPD-----PINVYRESQRLSFN-MAVrvlLGFRIP-----E 204
Cdd:cd11061  52 AEHARRRRVWSHAFSDKALRGYEPRILSHVEQLCEQLDDRAGkpvswPVDMSDWFNYLSFDvMGD---LAFGKSfgmleS 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 205 EEMHCLFSTFQEFVE--NVFSLPIDL-PFSGYR----KGIRARDSLQKSIEKAIREKpLHTQGKDYTDALDVLLE-SAKE 276
Cdd:cd11061 129 GKDRYILDLLEKSMVrlGVLGHAPWLrPLLLDLplfpGATKARKRFLDFVRAQLKER-LKAEEEKRPDIFSYLLEaKDPE 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 277 NNTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRSCGLLHDgclcqgELRLDSII-SLKYLDC 355
Cdd:cd11061 208 TGEGLDLEELVGEARLLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDD------EIRLGPKLkSLPYLRA 281
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 356 VIKEVLRLFAPVSGG-YRiatQT----FELDGVQVPKGWSVM---YSI-RDthdtSAVFKDVEAFDPDRFSPERSEDREG 426
Cdd:cd11061 282 CIDEALRLSPPVPSGlPR---ETppggLTIDGEYIPGGTTVSvpiYSIhRD----ERYFPDPFEFIPERWLSRPEELVRA 354
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 47086709 427 RFHYLPFGGGVRSCLGKQLATLFLKLLAVELAggSRFELS 466
Cdd:cd11061 355 RSAFIPFSIGPRGCIGKNLAYMELRLVLARLL--HRYDFR 392
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
126-446 3.08e-25

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: 107.67  E-value: 3.08e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 126 GPNSLANSIGDIHRKRRKIFAKVFSHEALESYLPKIQQVIQ---ETLRVWSSNPDPINVYRESQRLSFNMAVRVLLGfri 202
Cdd:cd11058  46 GPPSISTADDEDHARLRRLLAHAFSEKALREQEPIIQRYVDllvSRLRERAGSGTPVDMVKWFNFTTFDIIGDLAFG--- 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 203 peEEMHCL-FSTFQEFVENVF----SLPIDLPFSGY------------RKGIRAR-DSLQKSIEKAIREKPLHTQGKDYt 264
Cdd:cd11058 123 --ESFGCLeNGEYHPWVALIFdsikALTIIQALRRYpwllrllrllipKSLRKKRkEHFQYTREKVDRRLAKGTDRPDF- 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 265 daLDVLLEsAKENNTELTMQELK-----------ESTIELIFAafattasastsLVMQLLRHPAVLEKLREELRSCgllh 333
Cdd:cd11058 200 --MSYILR-NKDEKKGLTREELEanaslliiagsETTATALSG-----------LTYYLLKNPEVLRKLVDEIRSA---- 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 334 dgCLCQGELRLDSIISLKYLDCVIKEVLRLFAPVSGGY-RIATQ-TFELDGVQVPKGWSVMYSIRDTHDTSAVFKdveaf 411
Cdd:cd11058 262 --FSSEDDITLDSLAQLPYLNAVIQEALRLYPPVPAGLpRVVPAgGATIDGQFVPGGTSVSVSQWAAYRSPRNFH----- 334
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 47086709 412 DPDRFSPER-SEDREGRFH------YLPFGGGVRSCLGKQLA 446
Cdd:cd11058 335 DPDEFIPERwLGDPRFEFDndkkeaFQPFSVGPRNCIGKNLA 376
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
139-452 3.77e-25

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: 107.64  E-value: 3.77e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 139 RKRRKIFA-KVFSHEALESYLP----KIQQVIQETLRVwSSNPDPINVYRESQRLSFNMAVRVLLGFR-------IPEEE 206
Cdd:cd20618  62 RHLRKICTlELFSAKRLESFQGvrkeELSHLVKSLLEE-SESGKPVNLREHLSDLTLNNITRMLFGKRyfgesekESEEA 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 207 MHclfstFQEFVENVFSL--------------PIDLpfSGYRKGIRA----RDS-LQKSIEKAIREKPLHTQGKDYTDAL 267
Cdd:cd20618 141 RE-----FKELIDEAFELagafnigdyipwlrWLDL--QGYEKRMKKlhakLDRfLQKIIEEHREKRGESKKGGDDDDDL 213
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 268 DVLLESAKENNteLTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREElrscgllhdgclcqgelrLDSI 347
Cdd:cd20618 214 LLLLDLDGEGK--LSDDNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEE------------------LDSV 273
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 348 I------------SLKYLDCVIKEVLRLFAPVSGGY-RIATQTFELDGVQVPKGWSVM---YSI-RDThdtsAVFKDVEA 410
Cdd:cd20618 274 VgrerlveesdlpKLPYLQAVVKETLRLHPPGPLLLpHESTEDCKVAGYDIPAGTRVLvnvWAIgRDP----KVWEDPLE 349
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 47086709 411 FDPDRFSPERSEDREGR-FHYLPFGGGVRSCLGKQLATLFLKL 452
Cdd:cd20618 350 FKPERFLESDIDDVKGQdFELLPFGSGRRMCPGMPLGLRMVQL 392
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
153-457 4.14e-25

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: 107.76  E-value: 4.14e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 153 ALESYLPKIQQVIQETL-RVWSSNPD--PINVYRESQRLSFNMAVRVLLGFRI--PEEEMHCLFSTFQEFVENVFSL--- 224
Cdd:cd11041  79 NLPKLLPDLQEELRAALdEELGSCTEwtEVNLYDTVLRIVARVSARVFVGPPLcrNEEWLDLTINYTIDVFAAAAALrlf 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 225 -PIDLPFSGY-----RKGIRARDSLQKSIEKAIREKPLHTQGKDYT---DALDVLLESAKENNtELTMQELKESTIELIF 295
Cdd:cd11041 159 pPFLRPLVAPflpepRRLRRLLRRARPLIIPEIERRRKLKKGPKEDkpnDLLQWLIEAAKGEG-ERTPYDLADRQLALSF 237
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 296 AAFATTASASTSLVMQLLRHPAVLEKLREELRSCGLLHdgclcqGELRLDSIISLKYLDCVIKEVLRLFAPVSGGY-RIA 374
Cdd:cd11041 238 AAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEH------GGWTKAALNKLKKLDSFMKESQRLNPLSLVSLrRKV 311
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 375 TQTFEL-DGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREGRFH--------YLPFGGGVRSCLGKQL 445
Cdd:cd11041 312 LKDVTLsDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYRLREQPGQEKKHqfvstspdFLGFGHGRHACPGRFF 391
                       330
                ....*....|..
gi 47086709 446 ATLFLKLLAVEL 457
Cdd:cd11041 392 ASNEIKLILAHL 403
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
237-488 4.72e-25

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: 107.36  E-value: 4.72e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 237 IRAR-DSLQKSIEkaiREKplhTQGKDYTDALDVLLESAKENNTELTMQELKE--------------STIELIFAAfatt 301
Cdd:cd20678 196 IQQRkEQLQDEGE---LEK---IKKKRHLDFLDILLFAKDENGKSLSDEDLRAevdtfmfeghdttaSGISWILYC---- 265
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 302 asastslvmqLLRHPAVLEKLREELRscGLLHDGCLCQGElRLDSIislKYLDCVIKEVLRLFAPVSGGYRIATQ--TFE 379
Cdd:cd20678 266 ----------LALHPEHQQRCREEIR--EILGDGDSITWE-HLDQM---PYTTMCIKEALRLYPPVPGISRELSKpvTFP 329
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 380 lDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREGrFHYLPFGGGVRSCLGKQLATLFLKL-LAVELa 458
Cdd:cd20678 330 -DGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSSKRHS-HAFLPFSAGPRNCIGQQFAMNEMKVaVALTL- 406
                       250       260       270
                ....*....|....*....|....*....|...
gi 47086709 459 ggSRFELS---TRTfPRMISVPVVHPTDGLRVK 488
Cdd:cd20678 407 --LRFELLpdpTRI-PIPIPQLVLKSKNGIHLY 436
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
310-448 3.74e-24

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: 104.65  E-value: 3.74e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 310 MQLL-RHPAVLEKLREELrscgllhDGCLCQGELRL--DSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVP 386
Cdd:cd20660 256 LYLIgSHPEVQEKVHEEL-------DRIFGDSDRPAtmDDLKEMKYLECVIKEALRLFPSVPMFGRTLSEDIEIGGYTIP 328
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47086709 387 KGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREGrFHYLPFGGGVRSCLGKQLATL 448
Cdd:cd20660 329 KGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAGRHP-YAYIPFSAGPRNCIGQKFALM 389
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
308-446 4.67e-24

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: 104.18  E-value: 4.67e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 308 LVMQLLRHPAVLEKLREELRSCGLLHDgclcqgELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFEL------D 381
Cdd:cd11063 239 LFYELARHPEVWAKLREEVLSLFGPEP------TPTYEDLKNMKYLRAVINETLRLYPPVPLNSRVAVRDTTLprgggpD 312
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47086709 382 GVQ---VPKGWSVMYSIRDTH-DTSAVFKDVEAFDPDRFspeRSEDREGrFHYLPFGGGVRSCLGKQLA 446
Cdd:cd11063 313 GKSpifVPKGTRVLYSVYAMHrRKDIWGPDAEEFRPERW---EDLKRPG-WEYLPFNGGPRICLGQQFA 377
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
138-492 7.81e-24

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: 103.82  E-value: 7.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 138 HRKRRKIFAKVFSHEALESYLPKIQQVIQETLRVWSS---NPDPINVYRESQRLSFNMAVRVL----LGFRIPEEEMHCL 210
Cdd:cd11060  57 HAALRRKVASGYSMSSLLSLEPFVDECIDLLVDLLDEkavSGKEVDLGKWLQYFAFDVIGEITfgkpFGFLEAGTDVDGY 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 211 FSTFQEFVENVF---SLP-ID-----LPFSGYRKGIRARDSLQKSIEKAI--REKPLHTQGKDYTDALDVLLESAKENNT 279
Cdd:cd11060 137 IASIDKLLPYFAvvgQIPwLDrlllkNPLGPKRKDKTGFGPLMRFALEAVaeRLAEDAESAKGRKDMLDSFLEAGLKDPE 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 280 ELTMQELK-----------EST-IELifaafattasasTSLVMQLLRHPAVLEKLREELRSCGLlhdgclcqgELRLDSI 347
Cdd:cd11060 217 KVTDREVVaealsnilagsDTTaIAL------------RAILYYLLKNPRVYAKLRAEIDAAVA---------EGKLSSP 275
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 348 IS------LKYLDCVIKEVLRLFAPVSGGY-RIATQT-FELDGVQVPKGWSVMYSI----RDThdtsAVF-KDVEAFDPD 414
Cdd:cd11060 276 ITfaeaqkLPYLQAVIKEALRLHPPVGLPLeRVVPPGgATICGRFIPGGTIVGVNPwvihRDK----EVFgEDADVFRPE 351
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47086709 415 RFSPERSEDREGRFHY-LPFGGGVRSCLGKQLATLFLKLLAVELAggSRFELStrtfprmisvpVVHPTDGLRVKFFGL 492
Cdd:cd11060 352 RWLEADEEQRRMMDRAdLTFGAGSRTCLGKNIALLELYKVIPELL--RRFDFE-----------LVDPEKEWKTRNYWF 417
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
77-447 7.96e-24

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: 103.77  E-value: 7.96e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  77 RQKYGNVFKTHLLGRPLIRVTGAENVRKVLMG-EHSLVTVDWPQSTSTLL-GPNSLA-NSIGDIHRKRRKIFA-KVFSHE 152
Cdd:cd11073   1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKThDRVLSGRDVPDAVRALGhHKSSIVwPPYGPRWRMLRKICTtELFSPK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 153 ALESYLPKIQQVIQETLRvW----SSNPDPINVYRESQRLSFNMAVRVLLGFRIPEEEMHcLFSTFQEFVENVFSL---- 224
Cdd:cd11073  81 RLDATQPLRRRKVRELVR-YvrekAGSGEAVDIGRAAFLTSLNLISNTLFSVDLVDPDSE-SGSEFKELVREIMELagkp 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 225 ----------PIDLpfSGYRKgiRARDSLQKS---IEKAIREKPLHTQGKDY---TDALDVLLESAKENNTELTMQELK- 287
Cdd:cd11073 159 nvadffpflkFLDL--QGLRR--RMAEHFGKLfdiFDGFIDERLAEREAGGDkkkDDDLLLLLDLELDSESELTRNHIKa 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 288 -------------ESTIELifaafattasastslVM-QLLRHPAVLEKLREELRScgllhdgclcqgELRLDSII----- 348
Cdd:cd11073 235 llldlfvagtdttSSTIEW---------------AMaELLRNPEKMAKARAELDE------------VIGKDKIVeesdi 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 349 -SLKYLDCVIKEVLRLFAPVSG-GYRIATQTFELDGVQVPKGWSVM---YSI-RDthdtSAVFKDVEAFDPDRFSpERSE 422
Cdd:cd11073 288 sKLPYLQAVVKETLRLHPPAPLlLPRKAEEDVEVMGYTIPKGTQVLvnvWAIgRD----PSVWEDPLEFKPERFL-GSEI 362
                       410       420
                ....*....|....*....|....*.
gi 47086709 423 DREGR-FHYLPFGGGVRSCLGKQLAT 447
Cdd:cd11073 363 DFKGRdFELIPFGSGRRICPGLPLAE 388
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
141-450 8.51e-24

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: 103.83  E-value: 8.51e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 141 RRKIFAKVFSHEALESYLPkIQQviQETLRVW------SSNPDPINVYRESQRLSFNMAVRVLLGFRIPEE--------- 205
Cdd:cd20655  65 KKLCMTELLGPRALERFRP-IRA--QELERFLrrlldkAEKGESVDIGKELMKLTNNIICRMIMGRSCSEEngeaeevrk 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 206 ---EMHCLFSTFqeFVENVFSLPIDLPFSGYRKgiRARDSLQKS---IEKAIR---EKPLHTQGKDYTDALDVLLESAKE 276
Cdd:cd20655 142 lvkESAELAGKF--NASDFIWPLKKLDLQGFGK--RIMDVSNRFdelLERIIKeheEKRKKRKEGGSKDLLDILLDAYED 217
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 277 NNTE--LTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRSCgllhdgclcQGELRL----DsIISL 350
Cdd:cd20655 218 ENAEykITRNHIKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSV---------VGKTRLvqesD-LPNL 287
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 351 KYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKG-------WSVMysiRDthdtSAVFKDVEAFDPDRF----SPE 419
Cdd:cd20655 288 PYLQAVVKETLRLHPPGPLLVRESTEGCKINGYDIPEKttlfvnvYAIM---RD----PNYWEDPLEFKPERFlassRSG 360
                       330       340       350
                ....*....|....*....|....*....|..
gi 47086709 420 RSEDREGR-FHYLPFGGGVRSCLGKQLATLFL 450
Cdd:cd20655 361 QELDVRGQhFKLLPFGSGRRGCPGASLAYQVV 392
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
79-455 1.72e-23

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: 102.79  E-value: 1.72e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  79 KYGNVFktHLLGRP-LIRVTGAENVRKVLMGEHslvtvDWPQSTS-----TLLGPNsLANSIGDIHRKRRKIFAKVFSHe 152
Cdd:cd11070   1 KLGAVK--ILFVSRwNILVTKPEYLTQIFRRRD-----DFPKPGNqykipAFYGPN-VISSEGEDWKRYRKIVAPAFNE- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 153 alesylPKIQQVIQETLR-------VWSSNPDPINVYRES-----QRLSFNMAVRVLLGFRIP-----EEEMHCLFSTF- 214
Cdd:cd11070  72 ------RNNALVWEESIRqaqrlirYLLEEQPSAKGGGVDvrdllQRLALNVIGEVGFGFDLPaldeeESSLHDTLNAIk 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 215 QEFVENVF-SLPIdLPFSGYR---KGIRARDS----LQKSIEKAIREKPLHTQGKDYTDALDVLLESAKENNTELTMQEL 286
Cdd:cd11070 146 LAIFPPLFlNFPF-LDRLPWVlfpSRKRAFKDvdefLSELLDEVEAELSADSKGKQGTESVVASRLKRARRSGGLTEKEL 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 287 K-----------ESTIELIFAafattasastsLVMQLLRHPAVLEKLREELRSCGLLHDGCLCQGELRLdsiiSLKYLDC 355
Cdd:cd11070 225 LgnlfiffiaghETTANTLSF-----------ALYLLAKHPEVQDWLREEIDSVLGDEPDDWDYEEDFP----KLPYLLA 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 356 VIKEVLRLFAPVSGGYRIATQ-----TFELDGVQVPKGWSVMYSIRDTH-DTSAVFKDVEAFDPDRF-SPERSEDREGRF 428
Cdd:cd11070 290 VIYETLRLYPPVQLLNRKTTEpvvviTGLGQEIVIPKGTYVGYNAYATHrDPTIWGPDADEFDPERWgSTSGEIGAATRF 369
                       410       420       430
                ....*....|....*....|....*....|...
gi 47086709 429 H-----YLPFGGGVRSCLGKQLATL-FLKLLAV 455
Cdd:cd11070 370 TpargaFIPFSAGPRACLGRKFALVeFVAALAE 402
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
72-484 2.29e-23

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: 102.53  E-value: 2.29e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  72 FHASRRQKYGNVFKTHLLGRPLIRVTGAENVRKVLM---------GEHSLVTvdwpqststLLGPNSLANSIGDIHRKRR 142
Cdd:cd20639   3 FYHHWRKIYGKTFLYWFGPTPRLTVADPELIREILLtradhfdryEAHPLVR---------QLEGDGLVSLRGEKWAHHR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 143 KIFAKVFSHEALESYLPKIQQVIQETLRVW-----SSNPDPINVYRESQRLSFNMAVRVLLG---------FRIPEEEMh 208
Cdd:cd20639  74 RVITPAFHMENLKRLVPHVVKSVADMLDKWeamaeAGGEGEVDVAEWFQNLTEDVISRTAFGssyedgkavFRLQAQQM- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 209 cLFSTfqEFVENVFslpidLPfsGYR----KGIRARDSLQKSIEKAIR--------EKPLHTQGKDYTDALDVLLESAKE 276
Cdd:cd20639 153 -LLAA--EAFRKVY-----IP--GYRflptKKNRKSWRLDKEIRKSLLklierrqtAADDEKDDEDSKDLLGLMISAKNA 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 277 NNTE-LTMQEL-----------KESTIELIFAAFATtasastsLVMqllrHPAVLEKLREE-LRSCGllhdgclcQGEL- 342
Cdd:cd20639 223 RNGEkMTVEEIieecktfffagKETTSNLLTWTTVL-------LAM----HPEWQERARREvLAVCG--------KGDVp 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 343 RLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTH-DTSAVFKDVEAFDPDRFSPERS 421
Cdd:cd20639 284 TKDHLPKLKTLGMILNETLRLYPPAVATIRRAKKDVKLGGLDIPAGTELLIPIMAIHhDAELWGNDAAEFNPARFADGVA 363
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47086709 422 EDREGRFHYLPFGGGVRSCLGKQLATLFLKL-LAVELaggSRFELstRTFPRMISVPVV----HPTDG 484
Cdd:cd20639 364 RAAKHPLAFIPFGLGPRTCVGQNLAILEAKLtLAVIL---QRFEF--RLSPSYAHAPTVlmllQPQHG 426
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
230-450 3.70e-23

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: 101.53  E-value: 3.70e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 230 FSGYRKGIRARDSLQKSIEKAIRE--KPLHT-QGKDYTDALDVLLESAKENNTELTMQELKESTIELIFAAFATTASAST 306
Cdd:cd20651 167 FSGYNLLVELNQKLIEFLKEEIKEhkKTYDEdNPRDLIDAYLREMKKKEPPSSSFTDDQLVMICLDLFIAGSETTSNTLG 246
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 307 SLVMQLLRHPAVLEKLREELRSCglLHDGCLCQgelrLDSIISLKYLDCVIKEVLRLFAPV-SGGYRIATQTFELDGVQV 385
Cdd:cd20651 247 FAFLYLLLNPEVQRKVQEEIDEV--VGRDRLPT----LDDRSKLPYTEAVILEVLRIFTLVpIGIPHRALKDTTLGGYRI 320
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47086709 386 PKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSperseDREGRF----HYLPFGGGVRSCLGKQLA--TLFL 450
Cdd:cd20651 321 PKDTTILASLYSVHMDPEYWGDPEEFRPERFL-----DEDGKLlkdeWFLPFGAGKRRCLGESLArnELFL 386
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
241-457 7.46e-23

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: 100.95  E-value: 7.46e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 241 DSLQKSIEKaIREKPLHTQGKDYTDALDVLLESAKENNTE----LTMQELKESTIELIFAAFATTASASTSLVMQLLRHP 316
Cdd:cd20650 181 NFFYKSVKK-IKESRLDSTQKHRVDFLQLMIDSQNSKETEshkaLSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHP 259
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 317 AVLEKLREELrscgllhDGCL-CQGELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSI 395
Cdd:cd20650 260 DVQQKLQEEI-------DAVLpNKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKDVEINGVFIPKGTVVMIPT 332
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47086709 396 RDTHDTSAVFKDVEAFDPDRFSPErSEDREGRFHYLPFGGGVRSCLGKQLATLFLKLLAVEL 457
Cdd:cd20650 333 YALHRDPQYWPEPEEFRPERFSKK-NKDNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRV 393
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
312-486 8.91e-23

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: 100.90  E-value: 8.91e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 312 LLRHPAVLEKLREELRScgLLHDGcLCQGelrLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDG--VQVPKGW 389
Cdd:cd11046 267 LSQNPELMAKVQAEVDA--VLGDR-LPPT---YEDLKKLKYTRRVLNESLRLYPQPPVLIRRAVEDDKLPGggVKVPAGT 340
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 390 SVMYSIRDTHDTSAVFKDVEAFDPDRFSP-------ERSEDregrFHYLPFGGGVRSCLGKQLATLFLKL-LAVELaggS 461
Cdd:cd11046 341 DIFISVYNLHRSPELWEDPEEFDPERFLDpfinppnEVIDD----FAFLPFGGGPRKCLGDQFALLEATVaLAMLL---R 413
                       170       180
                ....*....|....*....|....*...
gi 47086709 462 RFELSTRTFPR---MISVPVVHPTDGLR 486
Cdd:cd11046 414 RFDFELDVGPRhvgMTTGATIHTKNGLK 441
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
116-450 1.21e-22

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: 100.02  E-value: 1.21e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 116 DWPQSTSTLLGPNSLANSIG-DIHRKRRKIFAKVFSHEALESYLPKIQQVIQET---LRVWSSNPDPINVYRESQRLSFN 191
Cdd:cd11062  32 DPPYFYGAFGAPGSTFSTVDhDLHRLRRKALSPFFSKRSILRLEPLIQEKVDKLvsrLREAKGTGEPVNLDDAFRALTAD 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 192 MAVRVLLGFR---IPEEEMHC-LFSTFQEFVEN---------VFSLPIDLPFSGYRKGIRARDS---LQKSIEKAIRE-- 253
Cdd:cd11062 112 VITEYAFGRSygyLDEPDFGPeFLDALRALAEMihllrhfpwLLKLLRSLPESLLKRLNPGLAVfldFQESIAKQVDEvl 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 254 -KPLHTQGKDYTDALDVLLESAKENNTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRScgLL 332
Cdd:cd11062 192 rQVSAGDPPSIVTSLFHALLNSDLPPSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKT--AM 269
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 333 HDGclcQGELRLDSIISLKYLDCVIKEVLRLFAPVSG-GYRIATQ-TFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEA 410
Cdd:cd11062 270 PDP---DSPPSLAELEKLPYLTAVIKEGLRLSYGVPTrLPRVVPDeGLYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHE 346
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 47086709 411 FDPDR-FSPERSEDREgrfHYL-PFGGGVRSCLGKQLATLFL 450
Cdd:cd11062 347 FRPERwLGAAEKGKLD---RYLvPFSKGSRSCLGINLAYAEL 385
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
173-458 2.24e-21

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: 96.38  E-value: 2.24e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 173 SSNPDPINVYRESQRLSFNMAVRVLLGFRIPEEEMhclfSTFQEFVENVFSL--------------PIDLPFSGYRKGIR 238
Cdd:cd11072 102 ASSSSPVNLSELLFSLTNDIVCRAAFGRKYEGKDQ----DKFKELVKEALELlggfsvgdyfpslgWIDLLTGLDRKLEK 177
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 239 ARDSLQKSIEKAIRE--KPLHTQGKDYTDALDVLLESAKENNTE--LTMQELK--------------ESTIELifaafat 300
Cdd:cd11072 178 VFKELDAFLEKIIDEhlDKKRSKDEDDDDDDLLDLRLQKEGDLEfpLTRDNIKaiildmflagtdtsATTLEW------- 250
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 301 tasastslVM-QLLRHPAVLEKLREELRSCgllhdgclcqgeLRLDSIIS------LKYLDCVIKEVLRLFAPVSG-GYR 372
Cdd:cd11072 251 --------AMtELIRNPRVMKKAQEEVREV------------VGGKGKVTeedlekLKYLKAVIKETLRLHPPAPLlLPR 310
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 373 IATQTFELDGVQVPKGWSVM---YSI-RDthdtSAVFKDVEAFDPDRFSpERSEDREGR-FHYLPFGGGVRSCLGKQLAt 447
Cdd:cd11072 311 ECREDCKINGYDIPAKTRVIvnaWAIgRD----PKYWEDPEEFRPERFL-DSSIDFKGQdFELIPFGAGRRICPGITFG- 384
                       330
                ....*....|.
gi 47086709 448 lflkLLAVELA 458
Cdd:cd11072 385 ----LANVELA 391
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
139-467 2.50e-21

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: 96.53  E-value: 2.50e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 139 RKRRKIFA-KVFSHEALES----YLPKIQQVIQETLRVWSSNPD-----PINVYRESQRLSFNMAVRVLLGFRI------ 202
Cdd:cd20654  62 RELRKIATlELLSNRRLEKlkhvRVSEVDTSIKELYSLWSNNKKggggvLVEMKQWFADLTFNVILRMVVGKRYfggtav 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 203 --PEEEMHCLfSTFQEFVeNVFSLPID---------LPFSGYRKGIR--ARD---SLQKSIEKAIREKPLHTQGKDYTDA 266
Cdd:cd20654 142 edDEEAERYK-KAIREFM-RLAGTFVVsdaipflgwLDFGGHEKAMKrtAKEldsILEEWLEEHRQKRSSSGKSKNDEDD 219
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 267 LDVLLESAKE------NNTELTmqeLKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRScgllHDGclcQG 340
Cdd:cd20654 220 DDVMMLSILEdsqisgYDADTV---IKATCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDT----HVG---KD 289
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 341 ELRLDSIIS-LKYLDCVIKEVLRLFAPVS-GGYRIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRF-S 417
Cdd:cd20654 290 RWVEESDIKnLVYLQAIVKETLRLYPPGPlLGPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFlT 369
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 47086709 418 PERSEDREGR-FHYLPFGGGVRSCLGKQLATLFLKL-LAVELAGgsrFELST 467
Cdd:cd20654 370 THKDIDVRGQnFELIPFGSGRRSCPGVSFGLQVMHLtLARLLHG---FDIKT 418
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
75-473 3.89e-21

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


Pssm-ID: 410666 [Multi-domain]  Cd Length: 432  Bit Score: 95.90  E-value: 3.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  75 SRRQKYGN---VFKTHLLGRPLIRVTGAENV------RKVLMGEHSLVTVdwpqsTSTLLGPNSLANSIGDIHRKRRKIF 145
Cdd:cd11040   3 RNGKKYFSggpIFTIRLGGQKIYVITDPELIsavfrnPKTLSFDPIVIVV-----VGRVFGSPESAKKKEGEPGGKGLIR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 146 AKV-FSHEAL----------ESYLPKIQQVIQETLRVWSSNPDPINVYRESQRLSFNMAVRVLLGFRIPEEEmHCLFSTF 214
Cdd:cd11040  78 LLHdLHKKALsggegldrlnEAMLENLSKLLDELSLSGGTSTVEVDLYEWLRDVLTRATTEALFGPKLPELD-PDLVEDF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 215 QEFVENVFSLPIDLPFSGYRKGIRARDSLQKSIEKAIREK-PLHTQGKDYTDALDVLLESAKENNTELTMQELKestieL 293
Cdd:cd11040 157 WTFDRGLPKLLLGLPRLLARKAYAARDRLLKALEKYYQAArEERDDGSELIRARAKVLREAGLSEEDIARAELA-----L 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 294 IFAAFATTASASTSLVMQLLRHPAVLEKLREELRSCglLHDGCLCQGELRLDSII-SLKYLDCVIKEVLRLFAPVSGGYR 372
Cdd:cd11040 232 LWAINANTIPAAFWLLAHILSDPELLERIREEIEPA--VTPDSGTNAILDLTDLLtSCPLLDSTYLETLRLHSSSTSVRL 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 373 IATQTFELDGVQVPKGWSVMYSIRDTHDTSAVF-KDVEAFDPDRF--SPERSEDREGRFHYLPFGGGVRSCLGKQLATLF 449
Cdd:cd11040 310 VTEDTVLGGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFlkKDGDKKGRGLPGAFRPFGGGASLCPGRHFAKNE 389
                       410       420
                ....*....|....*....|....*....
gi 47086709 450 LKLLAVELAggSRFELS-----TRTFPRM 473
Cdd:cd11040 390 ILAFVALLL--SRFDVEpvgggDWKVPGM 416
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
77-487 1.47e-20

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: 94.02  E-value: 1.47e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  77 RQKYGNVFKTHLLGRPLIRVTGAENVRKVL------MGEHSLVTvdwpQSTSTLLGpNSLANSIGDIHRKRRKIFAKVFS 150
Cdd:cd20640   8 RKQYGPIFTYSTGNKQFLYVSRPEMVKEINlcvsldLGKPSYLK----KTLKPLFG-GGILTSNGPHWAHQRKIIAPEFF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 151 HEALESYLPKIQQVIQETLRVWSSNPD-------PINVYRESQRLSFNMAVRVLLGFRIPE-EEMHCLFSTFQEFV--EN 220
Cdd:cd20640  83 LDKVKGMVDLMVDSAQPLLSSWEERIDraggmaaDIVVDEDLRAFSADVISRACFGSSYSKgKEIFSKLRELQKAVskQS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 221 VFsLPIDLPFSGYRKGIRARDSLQKSIEKAIRE--KPLHTQGKDYTDALDVLLESAKENNTELTMQEL------------ 286
Cdd:cd20640 163 VL-FSIPGLRHLPTKSNRKIWELEGEIRSLILEivKEREEECDHEKDLLQAILEGARSSCDKKAEAEDfivdnckniyfa 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 287 -KESTielifaafattASASTSLVMQLLRHPAVLEKLREELRScgllhdgcLCQGEL-RLDSIISLKYLDCVIKEVLRLF 364
Cdd:cd20640 242 gHETT-----------AVTAAWCLMLLALHPEWQDRVRAEVLE--------VCKGGPpDADSLSRMKTVTMVIQETLRLY 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 365 APVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTH-DTSAVFKDVEAFDPDRFSPERSEDREGRFHYLPFGGGVRSCLGK 443
Cdd:cd20640 303 PPAAFVSREALRDMKLGGLVVPKGVNIWVPVSTLHlDPEIWGPDANEFNPERFSNGVAAACKPPHSYMPFGAGARTCLGQ 382
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 47086709 444 QLATLFLK-LLAVELaggSRFELSTRtfPRMISVP----VVHPTDGLRV 487
Cdd:cd20640 383 NFAMAELKvLVSLIL---SKFSFTLS--PEYQHSPafrlIVEPEFGVRL 426
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
138-446 1.89e-20

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: 93.79  E-value: 1.89e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 138 HRkrrkIFAKVFSHEALESYLPKIQQVIQETLRVWSS-NPD-PINVYRESQRLSFNMAVRVLLGFR---IPEEEMH---- 208
Cdd:cd11068  76 HR----ILMPAFGPLAMRGYFPMMLDIAEQLVLKWERlGPDePIDVPDDMTRLTLDTIALCGFGYRfnsFYRDEPHpfve 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 209 CLFSTFQEFVENVFSLPIDLPF-----SGYRKGIRARDSLQKSIEKAIREKPlhTQGKDytDALDVLLESAKENNTE-LT 282
Cdd:cd11068 152 AMVRALTEAGRRANRPPILNKLrrrakRQFREDIALMRDLVDEIIAERRANP--DGSPD--DLLNLMLNGKDPETGEkLS 227
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 283 MQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELrscgllhDGCLCQGELRLDSIISLKYLDCVIKEVLR 362
Cdd:cd11068 228 DENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEV-------DEVLGDDPPPYEQVAKLRYIRRVLDETLR 300
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 363 LFAPVSGGYRIATQTFELDGV-QVPKGWSVMYSIRDTH-DTSAVFKDVEAFDPDRFSPERsEDREGRFHYLPFGGGVRSC 440
Cdd:cd11068 301 LWPTAPAFARKPKEDTVLGGKyPLKKGDPVLVLLPALHrDPSVWGEDAEEFRPERFLPEE-FRKLPPNAWKPFGNGQRAC 379

                ....*.
gi 47086709 441 LGKQLA 446
Cdd:cd11068 380 IGRQFA 385
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
80-467 2.22e-20

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: 93.43  E-value: 2.22e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  80 YGNVFKTHLLGRPLIRVTGAENVRKVLMGEHslvtVDW---PQSTSTLL---GPNSLAnsIGDIHRK---RRKIFakvfs 150
Cdd:cd11027   1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKKS----ADFagrPKLFTFDLfsrGGKDIA--FGDYSPTwklHRKLA----- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 151 HEALESYL-------PKIQQVIQETLRVWSSNPD-PINVYRESQRLSFNMAVRVLLG--FRIPEEEMHCLFSTFQEFVE- 219
Cdd:cd11027  70 HSALRLYAsggprleEKIAEEAEKLLKRLASQEGqPFDPKDELFLAVLNVICSITFGkrYKLDDPEFLRLLDLNDKFFEl 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 220 -------NVFSLPIDLPFSGYRKGIRARDSLQKSIEKAIREKPLHTQGK---DYTDALDVLLESAKENNTE--------- 280
Cdd:cd11027 150 lgagsllDIFPFLKYFPNKALRELKELMKERDEILRKKLEEHKETFDPGnirDLTDALIKAKKEAEDEGDEdsglltddh 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 281 --LTMQEL----KESTIELIFAAfattasastslVMQLLRHPAVLEKLREELrscgllhdgclcqgelrlDSII------ 348
Cdd:cd11027 230 lvMTISDIfgagTETTATTLRWA-----------IAYLVNYPEVQAKLHAEL------------------DDVIgrdrlp 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 349 ------SLKYLDCVIKEVLRL--FAPVSGGYRiATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDveafdPDRFSPER 420
Cdd:cd11027 281 tlsdrkRLPYLEATIAEVLRLssVVPLALPHK-TTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDD-----PDEFRPER 354
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....
gi 47086709 421 SEDREGRFH-----YLPFGGGVRSCLGKQLA--TLFLkLLAVELaggSRFELST 467
Cdd:cd11027 355 FLDENGKLVpkpesFLPFSAGRRVCLGESLAkaELFL-FLARLL---QKFRFSP 404
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
78-466 2.29e-20

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: 93.50  E-value: 2.29e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  78 QKYGNVFKTHLLGRPLIRVTGAENVRKVLmGEHSLVTVDWPQSTSTLLGpNSLANSIGDIHRKRRKIFAKVFSHEALESY 157
Cdd:cd20642   9 KTYGKNSFTWFGPIPRVIIMDPELIKEVL-NKVYDFQKPKTNPLTKLLA-TGLASYEGDKWAKHRKIINPAFHLEKLKNM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 158 LPKIQQVIQETLRVW-----SSNPDPINVYRESQRLSFNMAVRVLLGFRIpeEEMHCLFSTFQEFVENVFSLPIDLPFSG 232
Cdd:cd20642  87 LPAFYLSCSEMISKWeklvsSKGSCELDVWPELQNLTSDVISRTAFGSSY--EEGKKIFELQKEQGELIIQALRKVYIPG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 233 YR----KGIR--------ARDSLQKSIEKaiREKPLHTQGKDYTDALDVLLES----AKENN-------TELTMQELK-- 287
Cdd:cd20642 165 WRflptKRNRrmkeiekeIRSSLRGIINK--REKAMKAGEATNDDLLGILLESnhkeIKEQGnknggmsTEDVIEECKlf 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 288 -----ESTIELifaafattasastsLV--MQLL-RHPAVLEKLREE-LRSCGllhdgclcQGELRLDSIISLKYLDCVIK 358
Cdd:cd20642 243 yfagqETTSVL--------------LVwtMVLLsQHPDWQERAREEvLQVFG--------NNKPDFEGLNHLKVVTMILY 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 359 EVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTH-DTSAVFKDVEAFDPDRFSPERSEDREGRFHYLPFGGGV 437
Cdd:cd20642 301 EVLRLYPPVIQLTRAIHKDTKLGDLTLPAGVQVSLPILLVHrDPELWGDDAKEFNPERFAEGISKATKGQVSYFPFGWGP 380
                       410       420       430
                ....*....|....*....|....*....|
gi 47086709 438 RSCLGKQLATLFLKL-LAVELAGGSrFELS 466
Cdd:cd20642 381 RICIGQNFALLEAKMaLALILQRFS-FELS 409
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
69-465 2.99e-20

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: 92.59  E-value: 2.99e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  69 GAGFHASRRQKYG-NVFKTHLLGRPLIRVTGAE-------------------NVRKVLMGEHSLVTVDwpqststllgpn 128
Cdd:cd11067  10 GYRFISNRCRRLGsDAFRTRLMGRPAICLRGPEaarlfydedrftrkgamppRVQKTLFGKGGVQGLD------------ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 129 slansiGDIHRKRRKIFAKVFSHEALESYLPKIQQVIQETLRVWSSnPDPINVYRESQRLsFNMAVRVLLGFRIPEEEMH 208
Cdd:cd11067  78 ------GEAHRHRKAMFMSLMTPERVARLARLFRREWRAALARWEG-RDEVVLFDEAQEV-LTRAACRWAGVPLPEEDVE 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 209 CLFSTFQEFVENVFSlpidlPFSGYRKGIRARDSLQKSIE---KAIREKPLHTQGkdyTDALDVLLesakeNNTELTMQE 285
Cdd:cd11067 150 RRARDLAAMIDGAGA-----VGPRHWRARLARRRAERWAAeliEDVRAGRLAPPE---GTPLAAIA-----HHRDPDGEL 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 286 LKEST--IELIFAafattasastsL-------------VMQLLRHPAVLEKLREElrscgllhdgclcqgelrldsiiSL 350
Cdd:cd11067 217 LPERVaaVELLNL-----------LrptvavarfvtfaALALHEHPEWRERLRSG-----------------------DE 262
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 351 KYLDCVIKEVLRL--FAPVSGGyrIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFspersEDREG-R 427
Cdd:cd11067 263 DYAEAFVQEVRRFypFFPFVGA--RARRDFEWQGYRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERF-----LGWEGdP 335
                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 47086709 428 FHYLPFGGG-VRS---CLGKQLATLFLKLLAVELAGGSRFEL 465
Cdd:cd11067 336 FDFIPQGGGdHATghrCPGEWITIALMKEALRLLARRDYYDV 377
PLN02183 PLN02183
ferulate 5-hydroxylase
22-458 7.60e-20

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 92.61  E-value: 7.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   22 MALLLAVSQQLWQLRWTATRDKsckLPMPKGSMGFPIIGeTCHWFFQGAgfH---ASRRQKYGNVFKTHLLGRPLIRVTG 98
Cdd:PLN02183  13 SFFLILISLFLFLGLISRLRRR---LPYPPGPKGLPIIG-NMLMMDQLT--HrglANLAKQYGGLFHMRMGYLHMVAVSS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   99 AENVRKVLMGEHSLVTvDWPQSTSTLLGPNSLAN----SIGDIHRKRRKI-FAKVFSHEALESYlPKIQQVIQETLRVWS 173
Cdd:PLN02183  87 PEVARQVLQVQDSVFS-NRPANIAISYLTYDRADmafaHYGPFWRQMRKLcVMKLFSRKRAESW-ASVRDEVDSMVRSVS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  174 SN-PDPINVYRESQRLSFNMAVRVLLGFRiPEEEMHCLFSTFQEFVE--NVFSLPIDLPFSGY-------RKGIRARDSL 243
Cdd:PLN02183 165 SNiGKPVNIGELIFTLTRNITYRAAFGSS-SNEGQDEFIKILQEFSKlfGAFNVADFIPWLGWidpqglnKRLVKARKSL 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  244 QKSIEKAIRE---KPLHTQGKDY-----TDALDVLL----ESAKENNTE-------LTMQELKESTIELIFAAFATTASA 304
Cdd:PLN02183 244 DGFIDDIIDDhiqKRKNQNADNDseeaeTDMVDDLLafysEEAKVNESDdlqnsikLTRDNIKAIIMDVMFGGTETVASA 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  305 STSLVMQLLRHPAVLEKLREELRSC-GLlhdgclcqgELRLDS--IISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELD 381
Cdd:PLN02183 324 IEWAMAELMKSPEDLKRVQQELADVvGL---------NRRVEEsdLEKLTYLKCTLKETLRLHPPIPLLLHETAEDAEVA 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  382 GVQVPKGWSVM---YSI-RDTHDtsavFKDVEAFDPDRFSPERSEDREG-RFHYLPFGGGVRSCLGKQLAtlflkLLAVE 456
Cdd:PLN02183 395 GYFIPKRSRVMinaWAIgRDKNS----WEDPDTFKPSRFLKPGVPDFKGsHFEFIPFGSGRRSCPGMQLG-----LYALD 465

                 ..
gi 47086709  457 LA 458
Cdd:PLN02183 466 LA 467
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
252-465 1.44e-19

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: 90.91  E-value: 1.44e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 252 REKPLHTQGKD----------YTDALDVLLESAKENNTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEK 321
Cdd:cd20679 201 RRRTLPSQGVDdflkakakskTLDFIDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQER 280
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 322 LREELRScgLLHDGCLcqGELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFEL-DGVQVPKGWSVMYSIRDTHD 400
Cdd:cd20679 281 CRQEVQE--LLKDREP--EEIEWDDLAQLPFLTMCIKESLRLHPPVTAISRCCTQDIVLpDGRVIPKGIICLISIYGTHH 356
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47086709 401 TSAVFKDVEAFDPDRFSPERSEDREGrFHYLPFGGGVRSCLGKQLATLFLKL-LAVELAggsRFEL 465
Cdd:cd20679 357 NPTVWPDPEVYDPFRFDPENSQGRSP-LAFIPFSAGPRNCIGQTFAMAEMKVvLALTLL---RFRV 418
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
80-454 3.06e-19

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: 90.07  E-value: 3.06e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  80 YGNVFKTHLLGRPLIRVTGAENVRKvLMGEHSLVTVDWPQS-TSTLLGPNSLANSIG-----DIHRKRRKIFAKVFSHEA 153
Cdd:cd11066   1 NGPVFQIRLGNKRIVVVNSFASVRD-LWIKNSSALNSRPTFyTFHKVVSSTQGFTIGtspwdESCKRRRKAAASALNRPA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 154 LESYLPKIQQ----VIQETLRVWSSNPDPINVYRESQRLSFNMAVRVLLGFRIPEEEMHCLFSTFQEFVENVFS------ 223
Cdd:cd11066  80 VQSYAPIIDLesksFIRELLRDSAEGKGDIDPLIYFQRFSLNLSLTLNYGIRLDCVDDDSLLLEIIEVESAISKfrstss 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 224 -----LPI--DLPFSGYRKGIRA--RDSLQKSIEKAIREkpLHTQGKDYTDALDVLLESAKENNTELTMQELKESTIELI 294
Cdd:cd11066 160 nlqdyIPIlrYFPKMSKFRERADeyRNRRDKYLKKLLAK--LKEEIEDGTDKPCIVGNILKDKESKLTDAELQSICLTMV 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 295 FAAFATTASASTSLVMQLLRHP--AVLEKLREELRSCGLLHDGCLCqgelrlDSIISLK--YLDCVIKEVLRLFAPVSGG 370
Cdd:cd11066 238 SAGLDTVPLNLNHLIGHLSHPPgqEIQEKAYEEILEAYGNDEDAWE------DCAAEEKcpYVVALVKETLRYFTVLPLG 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 371 Y-RIATQTFELDGVQVPKG-WSVMYSIRDTHDtSAVFKDVEAFDPDRFSPERSEDREGRFHYlPFGGGVRSCLGKQLA-- 446
Cdd:cd11066 312 LpRKTTKDIVYNGAVIPAGtILFMNAWAANHD-PEHFGDPDEFIPERWLDASGDLIPGPPHF-SFGAGSRMCAGSHLAnr 389
                       410
                ....*....|.
gi 47086709 447 ---TLFLKLLA 454
Cdd:cd11066 390 elyTAICRLIL 400
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
124-487 1.54e-18

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: 87.69  E-value: 1.54e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 124 LLGPNSLANSIGDIHRKRRKIFAKVFSHEALESYLPKIqqvIQET------LRVWSSNPDPINVYRESQRLSFNMAVRVL 197
Cdd:cd11051  43 LTGGSSLISMEGEEWKRLRKRFNPGFSPQHLMTLVPTI---LDEVeifaaiLRELAESGEVFSLEELTTNLTFDVIGRVT 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 198 LGFRIP----EEEMHCLFSTFQEFVENVFSLPIDLPFSGYRKGIRARDSLQKSIEKAIREKPlhtqgkdytdaldvlles 273
Cdd:cd11051 120 LDIDLHaqtgDNSLLTALRLLLALYRSLLNPFKRLNPLRPLRRWRNGRRLDRYLKPEVRKRF------------------ 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 274 akenNTELTMQELK-------ESTIELIFAafattasastsLVMQLLRHPAVLEKLREEL---------RSCGLLHDGcl 337
Cdd:cd11051 182 ----ELERAIDQIKtflfaghDTTSSTLCW-----------AFYLLSKHPEVLAKVRAEHdevfgpdpsAAAELLREG-- 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 338 cqgelrlDSII-SLKYLDCVIKEVLRLFaPVSGGYRIATQTFEL---DGVQVP-KGWSVMYSIRDTHDTSAVFKDVEAFD 412
Cdd:cd11051 245 -------PELLnQLPYTTAVIKETLRLF-PPAGTARRGPPGVGLtdrDGKEYPtDGCIVYVCHHAIHRDPEYWPRPDEFI 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 413 PDRFSPERSED-REGRFHYLPFGGGVRSCLGKQLATLFLKL-LAVELaggSRFELST-----------RTFPRMISVPVV 479
Cdd:cd11051 317 PERWLVDEGHElYPPKSAWRPFERGPRNCIGQELAMLELKIiLAMTV---RRFDFEKaydewdakggyKGLKELFVTGQG 393
                       410
                ....*....|
gi 47086709 480 --HPTDGLRV 487
Cdd:cd11051 394 taHPVDGMPC 403
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
79-452 1.56e-18

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: 87.68  E-value: 1.56e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  79 KYGNVFKTHLLGRPLIRVTGAENVRKVLMgEHSLVTVDWPQS--TSTLLGPN--SLANSI-GDIHRK-RRKIFAKVFSHE 152
Cdd:cd11075   1 KYGPIFTLRMGSRPLIVVASRELAHEALV-QKGSSFASRPPAnpLRVLFSSNkhMVNSSPyGPLWRTlRRNLVSEVLSPS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 153 ALESYLPKIQQVIQ---ETLRVWS-SNPDPINVYRESQRLSFNMAVRVLLG-------FRIPEEEMHCLFSTFQEFveNV 221
Cdd:cd11075  80 RLKQFRPARRRALDnlvERLREEAkENPGPVNVRDHFRHALFSLLLYMCFGerldeetVRELERVQRELLLSFTDF--DV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 222 FS-LPI--DLPFSGYRKGIRARDSLQKSIEKA-IREKPLHTQGK----DYTDALDVLLESAKE--NNTELTMQELKESTI 291
Cdd:cd11075 158 RDfFPAltWLLNRRRWKKVLELRRRQEEVLLPlIRARRKRRASGeadkDYTDFLLLDLLDLKEegGERKLTDEELVSLCS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 292 ELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRSCgllhdgCLCQGELRLDSIISLKYLDCVIKEVLRLFAPVS-GG 370
Cdd:cd11075 238 EFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEV------VGDEAVVTEEDLPKMPYLKAVVLETLRRHPPGHfLL 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 371 YRIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDRE----GRFHYLPFGGGVRSCLGKQLA 446
Cdd:cd11075 312 PHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGGEAADIdtgsKEIKMMPFGAGRRICPGLGLA 391

                ....*.
gi 47086709 447 TLFLKL 452
Cdd:cd11075 392 TLHLEL 397
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
124-465 2.30e-18

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: 87.26  E-value: 2.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 124 LLGpNSLANSIGDIHRKRRKIFAKVFSHEAL-ESYLPKIQQVIQETLRVW----SSNPDPINVYRESQRLSF----NMAV 194
Cdd:cd11064  46 LLG-DGIFNVDGELWKFQRKTASHEFSSRALrEFMESVVREKVEKLLVPLldhaAESGKVVDLQDVLQRFTFdvicKIAF 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 195 RVLLGFRIPEEEMHCLFSTFQEFVENVFSLPIDLPFS---------GYRKGIRA-----RDSLQKSIEKAIREK-PLHTQ 259
Cdd:cd11064 125 GVDPGSLSPSLPEVPFAKAFDDASEAVAKRFIVPPWLwklkrwlniGSEKKLREairviDDFVYEVISRRREELnSREEE 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 260 GKDYTDALDVLLESAKENNTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRScgllHDGCLCQ 339
Cdd:cd11064 205 NNVREDLLSRFLASEEEEGEPVSDKFLRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKS----KLPKLTT 280
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 340 GELR---LDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQ-TFELDGVQVPKGWSVMYSI----RdthDTSAVFKDVEAF 411
Cdd:cd11064 281 DESRvptYEELKKLVYLHAALSESLRLYPPVPFDSKEAVNdDVLPDGTFVKKGTRIVYSIyamgR---MESIWGEDALEF 357
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 47086709 412 DPDRF-SPERSEDREGRFHYLPFGGGVRSCLGKQLATLFLKLLAVELAggSRFEL 465
Cdd:cd11064 358 KPERWlDEDGGLRPESPYKFPAFNAGPRICLGKDLAYLQMKIVAAAIL--RRFDF 410
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
72-466 1.11e-17

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: 85.19  E-value: 1.11e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  72 FHASRRQkYGNVFKTHLLGRPLIRVTGAENVRKVLMGEHSLVTVDWPQSTSTLLGPNSLANSIGDIHRKRRKIFAKVFSH 151
Cdd:cd20641   4 YQQWKSQ-YGETFLYWQGTTPRICISDHELAKQVLSDKFGFFGKSKARPEILKLSGKGLVFVNGDDWVRHRRVLNPAFSM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 152 EALESYLPKIQQVIQETLRVW-------SSNPDPINVYRESQRLSFNMAVRVLLG---------FRIPEEEMHCLFSTFq 215
Cdd:cd20641  83 DKLKSMTQVMADCTERMFQEWrkqrnnsETERIEVEVSREFQDLTADIIATTAFGssyaegievFLSQLELQKCAAASL- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 216 efveNVFSLPID--LPFSGYRKGIRARDSLQKSIeKAIREKPLHTQGKDY-TDALDVLLESAKENNTELTmQELKESTIE 292
Cdd:cd20641 162 ----TNLYIPGTqyLPTPRNLRVWKLEKKVRNSI-KRIIDSRLTSEGKGYgDDLLGLMLEAASSNEGGRR-TERKMSIDE 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 293 LIFAAFA------TTASASTSLVMQLLR-HPAVLEKLREE-LRSCG--LLHDGclcqgelrlDSIISLKYLDCVIKEVLR 362
Cdd:cd20641 236 IIDECKTfffaghETTSNLLTWTMFLLSlHPDWQEKLREEvFRECGkdKIPDA---------DTLSKLKLMNMVLMETLR 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 363 LFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVF-KDVEAFDPDRFSPERSEDREGRFHYLPFGGGVRSCL 441
Cdd:cd20641 307 LYGPVINIARRASEDMKLGGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGVSRAATHPNALLSFSLGPRACI 386
                       410       420
                ....*....|....*....|....*.
gi 47086709 442 GKQLATLFLKL-LAVELaggSRFELS 466
Cdd:cd20641 387 GQNFAMIEAKTvLAMIL---QRFSFS 409
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
79-464 1.22e-17

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: 85.28  E-value: 1.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  79 KYGNVFKTHLLGRPLIRVTGAENVRKVLMGEHSlvtvDWPQSTSTLLGPNSLANSI----GDIHRKRRKIFAKVFSHEAL 154
Cdd:cd20649   1 KYGPICGYYIGRRMFVVIAEPDMIKQVLVKDFN----NFTNRMKANLITKPMSDSLlclrDERWKRVRSILTPAFSAAKM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 155 ESYLPKIQQ---VIQETLRVWSSNPDPINVYRESQRLSFNMAVRVLLGFRI-----PEEEM--HCL----FSTFQEFVEN 220
Cdd:cd20649  77 KEMVPLINQacdVLLRNLKSYAESGNAFNIQRCYGCFTMDVVASVAFGTQVdsqknPDDPFvkNCKrffeFSFFRPILIL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 221 VFSLP-IDLPFSGY-----------------RKGI----------RARDSLQKSIEkaIREKPLHTQGKDYTDALDVLLE 272
Cdd:cd20649 157 FLAFPfIMIPLARIlpnksrdelnsfftqciRNMIafrdqqspeeRRRDFLQLMLD--ARTSAKFLSVEHFDIVNDADES 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 273 SAKENNTE--------------LTMQE-LKESTIELIFAAFATTASASTSLVMqLLRHPAVLEKLREELRSCGLLH---D 334
Cdd:cd20649 235 AYDGHPNSpaneqtkpskqkrmLTEDEiVGQAFIFLIAGYETTTNTLSFATYL-LATHPECQKKLLREVDEFFSKHemvD 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 335 GCLCQGelrldsiisLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPD 414
Cdd:cd20649 314 YANVQE---------LPYLDMVIAETLRMYPPAFRFAREAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPE 384
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 47086709 415 RFSPERSEDREgRFHYLPFGGGVRSCLGKQLATLFLKLLAVELAGGSRFE 464
Cdd:cd20649 385 RFTAEAKQRRH-PFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQ 433
PLN02687 PLN02687
flavonoid 3'-monooxygenase
20-492 1.26e-17

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 85.63  E-value: 1.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   20 VSMALLL---AVSQQLWQLRWTATRDKSCKLPMPKGSMGFPIIGETCHWffqGAGFH---ASRRQKYGNVFktHL-LGRP 92
Cdd:PLN02687   3 LPLPLLLgtvAVSVLVWCLLLRRGGSGKHKRPLPPGPRGWPVLGNLPQL---GPKPHhtmAALAKTYGPLF--RLrFGFV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   93 LIRVTGAENVRKVLMGEHSLVTVDWPqststllgPNSLANSI------------GDIHRKRRKIFA-KVFSHEALESYLP 159
Cdd:PLN02687  78 DVVVAASASVAAQFLRTHDANFSNRP--------PNSGAEHMaynyqdlvfapyGPRWRALRKICAvHLFSAKALDDFRH 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  160 KIQQVIQETLRVWSSNPD--PINVYRESQRLSFNMAVRVLLGFRIPEEEMHCLFSTFQEFVENVFSLP------------ 225
Cdd:PLN02687 150 VREEEVALLVRELARQHGtaPVNLGQLVNVCTTNALGRAMVGRRVFAGDGDEKAREFKEMVVELMQLAgvfnvgdfvpal 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  226 --IDLP-FSGYRKGIRAR-DSLQKSIEKAiREKPLHTQGKDYTDALDVLL-----ESAKENNTELTMQELKESTIELIFA 296
Cdd:PLN02687 230 rwLDLQgVVGKMKRLHRRfDAMMNGIIEE-HKAAGQTGSEEHKDLLSTLLalkreQQADGEGGRITDTEIKALLLNLFTA 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  297 AFATTASASTSLVMQLLRHPAVLEKLREELrscgllhDGCLCQGELRLDSIIS-LKYLDCVIKEVLRLF--APVSGGyRI 373
Cdd:PLN02687 309 GTDTTSSTVEWAIAELIRHPDILKKAQEEL-------DAVVGRDRLVSESDLPqLTYLQAVIKETFRLHpsTPLSLP-RM 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  374 ATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSE---DREGR-FHYLPFGGGVRSCLGKQLATLF 449
Cdd:PLN02687 381 AAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLPGGEHagvDVKGSdFELIPFGAGRRICAGLSWGLRM 460
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 47086709  450 LKLLAVELAGGSRFELSTRTFPRMI------------SVP-VVHPTDGLRVKFFGL 492
Cdd:PLN02687 461 VTLLTATLVHAFDWELADGQTPDKLnmeeaygltlqrAVPlMVHPRPRLLPSAYGI 516
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
81-466 2.65e-17

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: 83.91  E-value: 2.65e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  81 GNVFKTHLLGRPLIRVTGAENVRKVLMgehslvtvDWPQS---TSTL------LGPNSLANSIGDIHRKRRKIFAKVFSH 151
Cdd:cd11083   1 GSAYRFRLGRQPVLVISDPELIREVLR--------RRPDEfrrISSLesvfreMGINGVFSAEGDAWRRQRRLVMPAFSP 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 152 EALESYLPKIQQVIQETLRVW---SSNPDPINVYRESQR--------LSFNMAVRVLLGFRIP-EEEMHCLFSTFQEFVE 219
Cdd:cd11083  73 KHLRYFFPTLRQITERLRERWeraAAEGEAVDVHKDLMRytvdvttsLAFGYDLNTLERGGDPlQEHLERVFPMLNRRVN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 220 NVF------SLPIDLPFSGYRKGIRARdsLQKSIEKAIREKPLHTQGKDYTDALDVLLESAKENNTELTMQELKESTIEL 293
Cdd:cd11083 153 APFpywrylRLPADRALDRALVEVRAL--VLDIIAAARARLAANPALAEAPETLLAMMLAEDDPDARLTDDEIYANVLTL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 294 IFAAFATTASASTSLVMQLLRHPAVLEKLREELRSCGLLHDGCLCQGELRldsiiSLKYLDCVIKEVLRLFAPVSGGYRI 373
Cdd:cd11083 231 LLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPLLEALD-----RLPYLEAVARETLRLKPVAPLLFLE 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 374 ATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRF-SPERSEDREGRFHYLPFGGGVRSCLGKQLATLFLKL 452
Cdd:cd11083 306 PNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWlDGARAAEPHDPSSLLPFGAGPRLCPGRSLALMEMKL 385
                       410
                ....*....|....
gi 47086709 453 LAVELAggSRFELS 466
Cdd:cd11083 386 VFAMLC--RNFDIE 397
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
267-448 2.19e-16

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: 81.35  E-value: 2.19e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 267 LDVLLESAKENNTELTMQELKEStIELIFAAFATTASASTSLVMQLL-RHPAVLEKLREELrscgllhDGCLCQGE--LR 343
Cdd:cd20680 225 LDMLLSVTDEEGNKLSHEDIREE-VDTFMFEGHDTTAAAMNWSLYLLgSHPEVQRKVHKEL-------DEVFGKSDrpVT 296
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 344 LDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSED 423
Cdd:cd20680 297 MEDLKKLRYLECVIKESLRLFPSVPLFARSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSG 376
                       170       180
                ....*....|....*....|....*
gi 47086709 424 REgRFHYLPFGGGVRSCLGKQLATL 448
Cdd:cd20680 377 RH-PYAYIPFSAGPRNCIGQRFALM 400
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
80-450 2.26e-16

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: 81.31  E-value: 2.26e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  80 YGNVFKTHLLGRPLIRVTGAENVRKVLMGEHslvtVDW---PQS-TSTLLGPNSLANSIGD------IHRKrrkifakvF 149
Cdd:cd20674   1 YGPIYRLRLGLQDVVVLNSKRTIREALVRKW----ADFagrPHSyTGKLVSQGGQDLSLGDysllwkAHRK--------L 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 150 SHEAL-----ESYLPKIQQVIQETL-RVWSSNPDPINVYRESQRLSFNMAVRVLLGFRIPEE-EMHCLFSTFQEFVE--- 219
Cdd:cd20674  69 TRSALqlgirNSLEPVVEQLTQELCeRMRAQAGTPVDIQEEFSLLTCSIICCLTFGDKEDKDtLVQAFHDCVQELLKtwg 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 220 -------NVFSLPIDLPFSGYRKGIRA---RDSLqksIEKAIREKPLHTQGKDYTDALDVLLESAKENNTELTMQELKE- 288
Cdd:cd20674 149 hwsiqalDSIPFLRFFPNPGLRRLKQAvenRDHI---VESQLRQHKESLVAGQWRDMTDYMLQGLGQPRGEKGMGQLLEg 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 289 ----STIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELrsCGLLHDGCLCQGELRLdsiiSLKYLDCVIKEVLRL- 363
Cdd:cd20674 226 hvhmAVVDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEEL--DRVLGPGASPSYKDRA----RLPLLNATIAEVLRLr 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 364 -FAPVSGGYRiATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRF-SPERSEDRegrfhYLPFGGGVRSCL 441
Cdd:cd20674 300 pVVPLALPHR-TTRDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFlEPGAANRA-----LLPFGCGARVCL 373

                ....*....
gi 47086709 442 GKQLATLFL 450
Cdd:cd20674 374 GEPLARLEL 382
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
80-471 4.17e-16

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: 80.21  E-value: 4.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  80 YGNVFKTHLLGRPLIRVTGAENVRKVLMgEHSLVTVDWPQSTSTLL---GPNSLANSIGDIHRKRRKifakvFSHEAL-- 154
Cdd:cd20666   1 YGNIFSLFIGSQLVVVLNDFESVREALV-QKAEVFSDRPSVPLVTIltkGKGIVFAPYGPVWRQQRK-----FSHSTLrh 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 155 -----ESYLPKIQQ----VIQETLRVWSS--NPDPI------NVYresqrLSFNMAVRvllgFRIPEEEMHCLFSTFQEF 217
Cdd:cd20666  75 fglgkLSLEPKIIEefryVKAEMLKHGGDpfNPFPIvnnavsNVI-----CSMSFGRR----FDYQDVEFKTMLGLMSRG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 218 VE----------NVFSLPIDLPFSGYR------KGIRArdSLQKSIEKAiREKPLHTQGKDYTDALDVLLESAKENNTEL 281
Cdd:cd20666 146 LEisvnsaailvNICPWLYYLPFGPFRelrqieKDITA--FLKKIIADH-RETLDPANPRDFIDMYLLHIEEEQKNNAES 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 282 TMQELKESTI--ELIFAAFATTASASTSLVMQLLRHPAVLEKLREELrscgllhDGCLCQGEL-RLDSIISLKYLDCVIK 358
Cdd:cd20666 223 SFNEDYLFYIigDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEI-------DTVIGPDRApSLTDKAQMPFTEATIM 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 359 EVLRLFAPVSGGY-RIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREGRFhYLPFGGGV 437
Cdd:cd20666 296 EVQRMTVVVPLSIpHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLIKKEA-FIPFGIGR 374
                       410       420       430
                ....*....|....*....|....*....|....
gi 47086709 438 RSCLGKQLATLFLKLLAVELAGGSRFELSTRTFP 471
Cdd:cd20666 375 RVCMGEQLAKMELFLMFVSLMQSFTFLLPPNAPK 408
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
142-482 4.63e-16

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: 80.16  E-value: 4.63e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 142 RKIFA-KVFSHEALESYLPKIQQVIQETLRVW---SSNPDPINVyreSQRLSF---NMAVRVLLGFRIPEEEMHCLFSTF 214
Cdd:cd20657  65 RKLCNlHLFGGKALEDWAHVRENEVGHMLKSMaeaSRKGEPVVL---GEMLNVcmaNMLGRVMLSKRVFAAKAGAKANEF 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 215 QEFV------ENVFSLPIDLPFSGYR--KGIRAR-DSLQKSIE----KAIREKPLHTQ-GKDYTDALDVLLESAKENNT- 279
Cdd:cd20657 142 KEMVvelmtvAGVFNIGDFIPSLAWMdlQGVEKKmKRLHKRFDalltKILEEHKATAQeRKGKPDFLDFVLLENDDNGEg 221
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 280 -ELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELrscgllhDGCLCQGELRLDSIIS-LKYLDCVI 357
Cdd:cd20657 222 eRLTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEM-------DQVIGRDRRLLESDIPnLPYLQAIC 294
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 358 KEVLRLF--APVSGGyRIATQTFELDGVQVPKGWSVMYSI----RDthdtSAVFKDVEAFDPDRFSPERSEDREGR---F 428
Cdd:cd20657 295 KETFRLHpsTPLNLP-RIASEACEVDGYYIPKGTRLLVNIwaigRD----PDVWENPLEFKPERFLPGRNAKVDVRgndF 369
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47086709 429 HYLPFGGGVRSCLGKQLATLFLKLLAVELAGGSRFELSTRTFPRMI------------SVP-VVHPT 482
Cdd:cd20657 370 ELIPFGAGRRICAGTRMGIRMVEYILATLVHSFDWKLPAGQTPEELnmeeafglalqkAVPlVAHPT 436
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
96-458 5.95e-16

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: 79.53  E-value: 5.95e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  96 VTGAENVRKVL----MGEHSLVTVDWPQSTSTLLGPNSLANSIGDIHRKRRKIFAKVFSHEALESYLPKIQQVIQETLRV 171
Cdd:cd11031  28 VTRYADVRQVLadprFSRAAAAPPDAPRLTPEPLLPGSLMSMDPPEHTRLRRLVAKAFTARRVERLRPRIEEIADELLDA 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 172 WSSNPDPINVYREsqrLSFNMAVRV---LLGfrIPEEEMHclfsTFQEFVENVFSLPIDLPfsgyRKGIRARDSLQKSIE 248
Cdd:cd11031 108 MEAQGPPADLVEA---LALPLPVAViceLLG--VPYEDRE----RFRAWSDALLSTSALTP----EEAEAARQELRGYMA 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 249 KAIREKPlhtqgKDYTDalDVL--LESAKENNTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREEL 326
Cdd:cd11031 175 ELVAARR-----AEPGD--DLLsaLVAARDDDDRLSEEELVTLAVGLLVAGHETTASQIGNGVLLLLRHPEQLARLRADP 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 327 rscgllhdgclcqgELrldsiislkyLDCVIKEVLRLFAPVSGG--YRIATQTFELDGVQVPKGWSVMYSIrdthdTSAV 404
Cdd:cd11031 248 --------------EL----------VPAAVEELLRYIPLGAGGgfPRYATEDVELGGVTIRAGEAVLVSL-----NAAN 298
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47086709 405 FkDVEAF-DPDRFSPERSEDRegrfHyLPFGGGVRSCLGKQLA---------TLFLKLLAVELA 458
Cdd:cd11031 299 R-DPEVFpDPDRLDLDREPNP----H-LAFGHGPHHCLGAPLArlelqvalgALLRRLPGLRLA 356
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
312-450 8.25e-16

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: 79.30  E-value: 8.25e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 312 LLRHPAVLEKLREELrscgllhDGCLCQGELRLDS-IISLKYLDCVIKEVLRLFAP---VSGGyRIATQTFELDGVQVPK 387
Cdd:cd11076 251 MVLHPDIQSKAQAEI-------DAAVGGSRRVADSdVAKLPYLQAVVKETLRLHPPgplLSWA-RLAIHDVTVGGHVVPA 322
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47086709 388 GWSVM---YSIrdTHDtSAVFKDVEAFDPDRFSPERSED----REGRFHYLPFGGGVRSCLGKQ--LATLFL 450
Cdd:cd11076 323 GTTAMvnmWAI--THD-PHVWEDPLEFKPERFVAAEGGAdvsvLGSDLRLAPFGAGRRVCPGKAlgLATVHL 391
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
138-446 1.10e-15

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: 78.75  E-value: 1.10e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 138 HRKRRKIFAKVFSHEALESYLPKIQQVIQETL-RVWSsnPDPINVYREsqrLSFNMAVRV---LLGfrIPEEEMHclfsT 213
Cdd:cd20625  65 HTRLRRLVSKAFTPRAVERLRPRIERLVDELLdRLAA--RGRVDLVAD---FAYPLPVRViceLLG--VPEEDRP----R 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 214 FQEFVENVFSL--PIDLPfSGYRKGIRARDSLQKSIEKAIREKPLHTQgkdyTDALDVLLeSAKENNTELTMQELK---- 287
Cdd:cd20625 134 FRGWSAALARAldPGPLL-EELARANAAAAELAAYFRDLIARRRADPG----DDLISALV-AAEEDGDRLSEDELVanci 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 288 -------ESTIELIFAAfattasastslVMQLLRHPAVLEKLREELRscglLHDGclcqgelrldsiislkyldcVIKEV 360
Cdd:cd20625 208 lllvaghETTVNLIGNG-----------LLALLRHPEQLALLRADPE----LIPA--------------------AVEEL 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 361 LRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSI----RDthdtSAVFkdveaFDPDRFSPERSEDRegrfhYLPFGGG 436
Cdd:cd20625 253 LRYDSPVQLTARVALEDVEIGGQTIPAGDRVLLLLgaanRD----PAVF-----PDPDRFDITRAPNR-----HLAFGAG 318
                       330
                ....*....|
gi 47086709 437 VRSCLGKQLA 446
Cdd:cd20625 319 IHFCLGAPLA 328
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
80-450 3.50e-15

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: 77.72  E-value: 3.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  80 YGNVFKTHLLGRPLIRVTGAENVRKVLM--GEHslvTVDWPQSTSTLLGPN--SLA-NSIGDIHRKRRKI-------FAK 147
Cdd:cd11028   1 YGDVFQIRMGSRPVVVLNGLETIKQALVrqGED---FAGRPDFYSFQFISNgkSMAfSDYGPRWKLHRKLaqnalrtFSN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 148 VFSHEALESylpKIQQVIQETLRVW---SSNPDPINVYRESQRLSFNMAVRVLLGFRIPE--EEMHCLFSTFQEFVENVF 222
Cdd:cd11028  78 ARTHNPLEE---HVTEEAEELVTELtenNGKPGPFDPRNEIYLSVGNVICAICFGKRYSRddPEFLELVKSNDDFGAFVG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 223 SL-PID-LPFSGY------RKGIRARDSLQKSIEKAIREKpLHTQGKDYT-DALDVLLESAKENNTELTMQ-ELKESTI- 291
Cdd:cd11028 155 AGnPVDvMPWLRYltrrklQKFKELLNRLNSFILKKVKEH-LDTYDKGHIrDITDALIKASEEKPEEEKPEvGLTDEHIi 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 292 ----ELIFAAFATTASASTSLVMQLLRHPAVLEKLREELrscgllhDGCLCQGEL-RLDSIISLKYLDCVIKEVLRL--F 364
Cdd:cd11028 234 stvqDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAEL-------DRVIGRERLpRLSDRPNLPYTEAFILETMRHssF 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 365 APVSGGyRIATQTFELDGVQVPKGWSV---MYSIrdTHDTSaVFKDVEAFDPDRF-SPERSEDREGRFHYLPFGGGVRSC 440
Cdd:cd11028 307 VPFTIP-HATTRDTTLNGYFIPKGTVVfvnLWSV--NHDEK-LWPDPSVFRPERFlDDNGLLDKTKVDKFLPFGAGRRRC 382
                       410
                ....*....|..
gi 47086709 441 LGKQLA--TLFL 450
Cdd:cd11028 383 LGEELArmELFL 394
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
18-454 5.46e-15

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 77.56  E-value: 5.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   18 CLVSMALLLAV---SQQLWQLRWTATRdKSCKLPmpKGSMGFPIIGEtchwFFQ-GAGFH---ASRRQKYGNVFKTHLLG 90
Cdd:PLN03112   2 DSFLLSLLFSVlifNVLIWRWLNASMR-KSLRLP--PGPPRWPIVGN----LLQlGPLPHrdlASLCKKYGPLVYLRLGS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   91 RPLIRVTGAENVRKVLMgEHSLVTVDWPQSTSTLLgpnsLANSIGDI---------HRKRRKIFAKVFSHEALESYLPKI 161
Cdd:PLN03112  75 VDAITTDDPELIREILL-RQDDVFASRPRTLAAVH----LAYGCGDValaplgphwKRMRRICMEHLLTTKRLESFAKHR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  162 QQVIQETLR-VW--SSNPDPINVYRESQRLSFNMAVRVLLGFRI----------PEEEMHCLFSTFqeFVENVFSLPIDL 228
Cdd:PLN03112 150 AEEARHLIQdVWeaAQTGKPVNLREVLGAFSMNNVTRMLLGKQYfgaesagpkeAMEFMHITHELF--RLLGVIYLGDYL 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  229 PF------SGYRKGIR-----ARDSLQKSIEKAIREKPLHTQGKDYTDALDVLLESAKENNTE-LTMQELKESTIELIFA 296
Cdd:PLN03112 228 PAwrwldpYGCEKKMRevekrVDEFHDKIIDEHRRARSGKLPGGKDMDFVDVLLSLPGENGKEhMDDVEIKALMQDMIAA 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  297 AFATTASASTSLVMQLLRHPAVLEKLREELrscgllhDGCLCQGELRLDS-IISLKYLDCVIKEVLRLFApvSGGYRIAT 375
Cdd:PLN03112 308 ATDTSAVTNEWAMAEVIKNPRVLRKIQEEL-------DSVVGRNRMVQESdLVHLNYLRCVVRETFRMHP--AGPFLIPH 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  376 QTFE---LDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSP------ERSEDREgrFHYLPFGGGVRSCLGKQLA 446
Cdd:PLN03112 379 ESLRattINGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERHWPaegsrvEISHGPD--FKILPFSAGKRKCPGAPLG 456

                 ....*....
gi 47086709  447 -TLFLKLLA 454
Cdd:PLN03112 457 vTMVLMALA 465
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
96-479 6.77e-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: 76.42  E-value: 6.77e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  96 VTGAENVRKVL------------MGEHSLVTVDWPQSTSTLLGPNsLANSIGDIHRKRRKIFAKVFSHEALESYLPKIQQ 163
Cdd:cd11029  28 VTRYDDARAALadprlskdprkaWPAFRGRAPGAPPDLPPVLSDN-MLTSDPPDHTRLRRLVAKAFTPRRVEALRPRIEE 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 164 VIQETLRVWSSnpdpinvyRES----QRLSFNMAVRV---LLGfrIPEEEMhclfSTFQEFVENVFSlpIDLPFSGYRKG 236
Cdd:cd11029 107 ITDELLDALAA--------RGVvdlvADFAYPLPITViceLLG--VPEEDR----DRFRRWSDALVD--TDPPPEEAAAA 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 237 IRA-RDSLQKSIEKAiREKPlhtqGKDYTDALdVlleSAKENNTELTMQEL-----------KESTIELIFAAfattasa 304
Cdd:cd11029 171 LRElVDYLAELVARK-RAEP----GDDLLSAL-V---AARDEGDRLSEEELvstvflllvagHETTVNLIGNG------- 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 305 stslVMQLLRHPAVLEKLREelrscgllhdgclcqGELRLDSiislkyldcVIKEVLRLFAPVS-GGYRIATQTFELDGV 383
Cdd:cd11029 235 ----VLALLTHPDQLALLRA---------------DPELWPA---------AVEELLRYDGPVAlATLRFATEDVEVGGV 286
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 384 QVPKGWSVMYSIrdthdtSAVFKDVEAF-DPDRFSPERSEDRegrfHyLPFGGGVRSCLGKQLA---------TLFLKLL 453
Cdd:cd11029 287 TIPAGEPVLVSL------AAANRDPARFpDPDRLDITRDANG----H-LAFGHGIHYCLGAPLArleaeialgALLTRFP 355
                       410       420
                ....*....|....*....|....*....
gi 47086709 454 AVELAGGSRfELSTRTFPRM---ISVPVV 479
Cdd:cd11029 356 DLRLAVPPD-ELRWRPSFLLrglRALPVR 383
PLN02290 PLN02290
cytokinin trans-hydroxylase
309-494 7.20e-15

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 77.16  E-value: 7.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  309 VMQLLRHPAVLEKLREELRScgllhdgcLCQGEL-RLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPK 387
Cdd:PLN02290 340 LMLLASNPTWQDKVRAEVAE--------VCGGETpSVDHLSKLTLLNMVINESLRLYPPATLLPRMAFEDIKLGDLHIPK 411
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  388 GWSVMYSIRDTHDTSAVF-KDVEAFDPDRFSperSEDREGRFHYLPFGGGVRSCLGKQLATLFLKLLAVELAGGSRFELS 466
Cdd:PLN02290 412 GLSIWIPVLAIHHSEELWgKDANEFNPDRFA---GRPFAPGRHFIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSFTIS 488
                        170       180
                 ....*....|....*....|....*...
gi 47086709  467 TRTFPRMISVPVVHPTDGLRVKFFGLDS 494
Cdd:PLN02290 489 DNYRHAPVVVLTIKPKYGVQVCLKPLNP 516
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
124-446 1.44e-14

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: 75.03  E-value: 1.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 124 LLGPNSLAnSIGDIHRKRRKIFAKVFSHEALESYLPKIQQVIQETL---RVWSSNPDPINVYresqrlSFNMAVRV---L 197
Cdd:cd20629  43 FLGHSILA-MDGEEHRRRRRLLQPAFAPRAVARWEEPIVRPIAEELvddLADLGRADLVEDF------ALELPARViyaL 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 198 LGFriPEEEMHclfsTFQEFVENVFSLPIDLPFSGYRKGIRARDSLQKSIEKAIREKplhtQGKDYTDALDVLL----ES 273
Cdd:cd20629 116 LGL--PEEDLP----EFTRLALAMLRGLSDPPDPDVPAAEAAAAELYDYVLPLIAER----RRAPGDDLISRLLraevEG 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 274 AKENNTELTMQelkesTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREElRScgllhdgclcqgelrldsiislkYL 353
Cdd:cd20629 186 EKLDDEEIISF-----LRLLLPAGSDTTYRALANLLTLLLQHPEQLERVRRD-RS-----------------------LI 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 354 DCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRfspersedreGRFHYLPF 433
Cdd:cd20629 237 PAAIEEGLRWEPPVASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDIDR----------KPKPHLVF 306
                       330
                ....*....|...
gi 47086709 434 GGGVRSCLGKQLA 446
Cdd:cd20629 307 GGGAHRCLGEHLA 319
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
138-488 1.65e-14

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: 74.94  E-value: 1.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 138 HRKRRKIFAKVFSHEALESYLPKIQQVIQETLrvwssnpDPINVYRES---QRLSFNMAVRV---LLGfrIPEEEMHclf 211
Cdd:cd11032  61 HRKLRKLVSQAFTPRLIADLEPRIAEITDELL-------DAVDGRGEFdlvEDLAYPLPVIViaeLLG--VPAEDRE--- 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 212 sTFQEFVENVFSLPIDLPF--SGYRKGIRARDSLQKSIEKAIREKPLHTQGkdytDALDVLLEsAKENNTELTMQELKES 289
Cdd:cd11032 129 -LFKKWSDALVSGLGDDSFeeEEVEEMAEALRELNAYLLEHLEERRRNPRD----DLISRLVE-AEVDGERLTDEEIVGF 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 290 TIELIFAAFATTASASTSLVMQLLRHPAVLEKLREElrscgllhdgclcqGELRLDsiislkyldcVIKEVLRLFAPVSG 369
Cdd:cd11032 203 AILLLIAGHETTTNLLGNAVLCLDEDPEVAARLRAD--------------PSLIPG----------AIEEVLRYRPPVQR 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 370 GYRIATQTFELDGVQVPKGWSVMYSI----RDthdtSAVFKdveafDPDRFSPERSEDRegrfHyLPFGGGVRSCLGKQL 445
Cdd:cd11032 259 TARVTTEDVELGGVTIPAGQLVIAWLasanRD----ERQFE-----DPDTFDIDRNPNP----H-LSFGHGIHFCLGAPL 324
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 47086709 446 ATL----FLKLLAvelaggSRFELSTRTF---PRMISVPVVHPTDGLRVK 488
Cdd:cd11032 325 ARLeariALEALL------DRFPRIRVDPdvpLELIDSPVVFGVRSLPVR 368
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
135-445 2.22e-14

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: 75.21  E-value: 2.22e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 135 GDIHRKRRKIFA-KVFSHEALESYLP----KIQQVIQETLRVWSSNPD---PINVYRESQRLSFNMAVRVLLGFRIPEEE 206
Cdd:cd20656  59 GPHYVKVRKLCTlELFTPKRLESLRPiredEVTAMVESIFNDCMSPENegkPVVLRKYLSAVAFNNITRLAFGKRFVNAE 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 207 MHCLFS--TFQEFVENVFSLPIDLPFSGYRKGIR---------------ARDSLQKSI--EKAIREKPLHTqGKDYTDAL 267
Cdd:cd20656 139 GVMDEQgvEFKAIVSNGLKLGASLTMAEHIPWLRwmfplsekafakhgaRRDRLTKAImeEHTLARQKSGG-GQQHFVAL 217
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 268 dvllesakennteLTMQE---LKESTI-----ELIFAAFATTASASTSLVMQLLRHPAVLEKLREELrscgllhDGCLCQ 339
Cdd:cd20656 218 -------------LTLKEqydLSEDTVigllwDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEEL-------DRVVGS 277
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 340 GELRLDSIIS-LKYLDCVIKEVLRLF--APVSGGYRiATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRF 416
Cdd:cd20656 278 DRVMTEADFPqLPYLQCVVKEALRLHppTPLMLPHK-ASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERF 356
                       330       340
                ....*....|....*....|....*....
gi 47086709 417 SPERSEDREGRFHYLPFGGGVRSCLGKQL 445
Cdd:cd20656 357 LEEDVDIKGHDFRLLPFGAGRRVCPGAQL 385
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
280-485 9.76e-14

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: 73.03  E-value: 9.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 280 ELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRScgLLHDGCLCQGElrldSIISLKYLDCVIKE 359
Cdd:cd20647 232 ELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVR--NLGKRVVPTAE----DVPKLPLIRALLKE 305
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 360 VLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREGRFHYLPFGGGVRS 439
Cdd:cd20647 306 TLRLFPVLPGNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKDALDRVDNFGSIPFGYGIRS 385
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 47086709 440 CLGKQLATLFLKLLAVELAGGSRFELSTRTFPrmisvpvVHP-TDGL 485
Cdd:cd20647 386 CIGRRIAELEIHLALIQLLQNFEIKVSPQTTE-------VHAkTHGL 425
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
139-468 1.08e-13

cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or estrogen synthetase (EC 1.14.14.14), catalyzes the formation of aromatic C18 estrogens from C19 androgens. The CYP19A1 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410709 [Multi-domain]  Cd Length: 414  Bit Score: 72.78  E-value: 1.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 139 RKRRKIFAKVFSHEALE-----------SYLPKIQQVIQEtlrvwSSNPDPINVYResqRLSFNMAVRVLLGfrIPEEE- 206
Cdd:cd20616  71 KKVRPFFAKALTGPGLVrmvtvcvestnTHLDNLEEVTNE-----SGYVDVLTLMR---RIMLDTSNRLFLG--VPLNEk 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 207 -----MHCLFSTFQEFV--ENVFslpidLPFSG-YRKGIRARDSLQKSIEKAIREKPLHTQG----KDYTD-ALDVLLes 273
Cdd:cd20616 141 aivlkIQGYFDAWQALLikPDIF-----FKISWlYKKYEKAVKDLKDAIEILIEQKRRRISTaeklEDHMDfATELIF-- 213
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 274 aKENNTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRSCgllhdgcLCQGELRLDSIISLKYL 353
Cdd:cd20616 214 -AQKRGELTAENVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTV-------LGERDIQNDDLQKLKVL 285
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 354 DCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTHDTsavfkdvEAF-DPDRFSPERSEDREGRFHYLP 432
Cdd:cd20616 286 ENFINESMRYQPVVDFVMRKALEDDVIDGYPVKKGTNIILNIGRMHRL-------EFFpKPNEFTLENFEKNVPSRYFQP 358
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 47086709 433 FGGGVRSCLGKQLATLFLKLLAVELAggSRFELSTR 468
Cdd:cd20616 359 FGFGPRSCVGKYIAMVMMKAILVTLL--RRFQVCTL 392
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
315-455 1.53e-13

fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 monooxygenase TRI13, also called core trichothecene cluster (CTC) protein 13, and similar proteins. The tri13 gene is located in the trichothecene biosynthesis gene cluster in Fusarium species, which produce a great diversity of agriculturally important trichothecene toxins that differ from each other in their pattern of oxygenation and esterification. Trichothecenes comprise a large family of chemically related bicyclic sesquiterpene compounds acting as mycotoxins, including the T2-toxin; TRI13 is required for the addition of the C-4 oxygen of T-2 toxin. The TRI13-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410715 [Multi-domain]  Cd Length: 494  Bit Score: 72.72  E-value: 1.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 315 HPAVLEKLREELRSCgllhdgcLCQG--ELRLDS---IIS--LKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPK 387
Cdd:cd20622 292 NQDVQSKLRKALYSA-------HPEAvaEGRLPTaqeIAQarIPYLDAVIEEILRCANTAPILSREATVDTQVLGYSIPK 364
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 388 GWSVM----------------YSIRDTHDTSAVFKDV--EAFDPDRFSPER-----SEDREGRFH-----YLPFGGGVRS 439
Cdd:cd20622 365 GTNVFllnngpsylsppieidESRRSSSSAAKGKKAGvwDSKDIADFDPERwlvtdEETGETVFDpsagpTLAFGLGPRG 444
                       170
                ....*....|....*.
gi 47086709 440 CLGKQLATLFLKLLAV 455
Cdd:cd20622 445 CFGRRLAYLEMRLIIT 460
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
312-446 1.61e-13

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: 72.25  E-value: 1.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 312 LLRHPAVLEKLREELrscgllhDGCLCQGELRLDSIIS-LKYLDCVIKEVLRLFAPVSGGY-RIATQTFELDGVQVPKGW 389
Cdd:cd20653 254 LLNHPEVLKKAREEI-------DTQVGQDRLIEESDLPkLPYLQNIISETLRLYPAAPLLVpHESSEDCKIGGYDIPRGT 326
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 47086709 390 SVMYSIRDTHDTSAVFKdveafDPDRFSPERSEDRE-GRFHYLPFGGGVRSCLGKQLA 446
Cdd:cd20653 327 MLLVNAWAIHRDPKLWE-----DPTKFKPERFEGEErEGYKLIPFGLGRRACPGAGLA 379
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
138-473 1.63e-13

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: 72.07  E-value: 1.63e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 138 HRKRRKIFAKVFSHEALESYLPKIQQVIQETLRVwSSNPDPINVYRE-SQRLSFNMAVRVLlgfRIPEEEmHCLFSTFQE 216
Cdd:cd20630  66 HARVRKLVAPAFTPRAIDRLRAEIQAIVDQLLDE-LGEPEEFDVIREiAEHIPFRVISAML---GVPAEW-DEQFRRFGT 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 217 FVENVFsLPIDLP--FSGYRKGIRARDSLQKSIEKAIREKPLHtqgkdytDALDVLLESAKENNTELTMQELKESTIELI 294
Cdd:cd20630 141 ATIRLL-PPGLDPeeLETAAPDVTEGLALIEEVIAERRQAPVE-------DDLLTTLLRAEEDGERLSEDELMALVAALI 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 295 FAAFATTASASTSLVMQLLRHPAVLEKLREElrscgllhdgclcqGELrldsiislkyLDCVIKEVLRL-FAPVSGGYRI 373
Cdd:cd20630 213 VAGTDTTVHLITFAVYNLLKHPEALRKVKAE--------------PEL----------LRNALEEVLRWdNFGKMGTARY 268
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 374 ATQTFELDGVQVPKGWSVMYSIrdthdtSAVFKDVEAF-DPDRFSPERSEDREgrfhyLPFGGGVRSCLGKQLATlflkl 452
Cdd:cd20630 269 ATEDVELCGVTIRKGQMVLLLL------PSALRDEKVFsDPDRFDVRRDPNAN-----IAFGYGPHFCIGAALAR----- 332
                       330       340
                ....*....|....*....|.
gi 47086709 453 LAVELAGGSRFelstRTFPRM 473
Cdd:cd20630 333 LELELAVSTLL----RRFPEM 349
PLN02936 PLN02936
epsilon-ring hydroxylase
312-488 3.37e-13

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 71.75  E-value: 3.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  312 LLRHPAVLEKLREELrscgllhDGCLCQGELRLDSIISLKYLDCVIKEVLRLFA--PVSggYRIATQTFEL-DGVQVPKG 388
Cdd:PLN02936 305 LSKNPEALRKAQEEL-------DRVLQGRPPTYEDIKELKYLTRCINESMRLYPhpPVL--IRRAQVEDVLpGGYKVNAG 375
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  389 WSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREGR--FHYLPFGGGVRSCLGKQLATL--------FLKLLAVELA 458
Cdd:PLN02936 376 QDIMISVYNIHRSPEVWERAEEFVPERFDLDGPVPNETNtdFRYIPFSGGPRKCVGDQFALLeaivalavLLQRLDLELV 455
                        170       180       190
                 ....*....|....*....|....*....|
gi 47086709  459 GGSRFelstrtfpRMISVPVVHPTDGLRVK 488
Cdd:PLN02936 456 PDQDI--------VMTTGATIHTTNGLYMT 477
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
138-466 4.68e-13

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: 70.78  E-value: 4.68e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 138 HRKR-RKIFAKVFSHEALESYLPKIQQVIQETLRVWSSNPDP-----INVYRESQRLSFNMAVRVLLGfripeeemhclf 211
Cdd:cd20615  59 DWKRvRKVFDPAFSHSAAVYYIPQFSREARKWVQNLPTNSGDgrrfvIDPAQALKFLPFRVIAEILYG------------ 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 212 STFQEFVENVFSL-PIDLPFSGYR-KGIRARDSLQK----SIEKAIREkpLHTQGKDY-TDALDVLLESAKENNTE---- 280
Cdd:cd20615 127 ELSPEEKEELWDLaPLREELFKYViKGGLYRFKISRylptAANRRLRE--FQTRWRAFnLKIYNRARQRGQSTPIVklye 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 281 ------LTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRSCgllhdgcLCQGELRLDSIISLK--Y 352
Cdd:cd20615 205 avekgdITFEELLQTLDEMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEISAA-------REQSGYPMEDYILSTdtL 277
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 353 LDCVIKEVLRL--FAPVSGGYRIATQTFeLDGVQVPKGWSVM---YSIRDTHDTSAVfkDVEAFDPDRF-SPERSEdreG 426
Cdd:cd20615 278 LAYCVLESLRLrpLLAFSVPESSPTDKI-IGGYRIPANTPVVvdtYALNINNPFWGP--DGEAYRPERFlGISPTD---L 351
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 47086709 427 RFHYLPFGGGVRSCLGKQLATLFLKLLAVELAggSRFELS 466
Cdd:cd20615 352 RYNFWRFGFGPRKCLGQHVADVILKALLAHLL--EQYELK 389
PLN02655 PLN02655
ent-kaurene oxidase
228-448 7.39e-13

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 70.54  E-value: 7.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  228 LPFSGYRKGIRARDSLQKSIEKAI--REKPLHTQGKDYTDALDVLLEsakeNNTELTMQELKESTIELIFAAFATTASAS 305
Cdd:PLN02655 207 IPNKSFETRVQTTEFRRTAVMKALikQQKKRIARGEERDCYLDFLLS----EATHLTDEQLMMLVWEPIIEAADTTLVTT 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  306 TSLVMQLLRHPAVLEKLREELRScgllhdgcLCQGE-LRLDSIISLKYLDCVIKEVLRLFAPVSG-GYRIATQTFELDGV 383
Cdd:PLN02655 283 EWAMYELAKNPDKQERLYREIRE--------VCGDErVTEEDLPNLPYLNAVFHETLRKYSPVPLlPPRFVHEDTTLGGY 354
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47086709  384 QVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREgRFHYLPFGGGVRSCLGKQLATL 448
Cdd:PLN02655 355 DIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLGEKYESAD-MYKTMAFGAGKRVCAGSLQAML 418
PLN02738 PLN02738
carotene beta-ring hydroxylase
312-487 9.04e-13

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 70.71  E-value: 9.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  312 LLRHPAVLEKLREELrscgllhDGCLCQGELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSV 391
Cdd:PLN02738 418 LSKEPSVVAKLQEEV-------DSVLGDRFPTIEDMKKLKYTTRVINESLRLYPQPPVLIRRSLENDMLGGYPIKRGEDI 490
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  392 MYSIRDTHDTSAVFKDVEAFDPDRF---SPERSEDREGrFHYLPFGGGVRSCLGKQLATlFLKLLAVE-LAGGSRFELST 467
Cdd:PLN02738 491 FISVWNLHRSPKHWDDAEKFNPERWpldGPNPNETNQN-FSYLPFGGGPRKCVGDMFAS-FENVVATAmLVRRFDFQLAP 568
                        170       180
                 ....*....|....*....|.
gi 47086709  468 RTFP-RMISVPVVHPTDGLRV 487
Cdd:PLN02738 569 GAPPvKMTTGATIHTTEGLKM 589
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
234-450 8.14e-12

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: 66.96  E-value: 8.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 234 RKGIRARDS-LQKSIEKAiREKplhTQGKDYTDALDVLLE---SAKENNTELTMQE--LKESTI-----ELIFAAFATTA 302
Cdd:cd20673 174 KQCVKIRDKlLQKKLEEH-KEK---FSSDSIRDLLDALLQakmNAENNNAGPDQDSvgLSDDHIlmtvgDIFGAGVETTT 249
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 303 SASTSLVMQLLRHPAVLEKLREELRSCgllhdgclcQGELRLDSII---SLKYLDCVIKEVLRlFAPVSGGY--RIATQT 377
Cdd:cd20673 250 TVLKWIIAFLLHNPEVQKKIQEEIDQN---------IGFSRTPTLSdrnHLPLLEATIREVLR-IRPVAPLLipHVALQD 319
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 378 FELDGVQVPKGWSV---MYSIRdtHDTSavfkdvEAFDPDRFSPERSEDREGRF------HYLPFGGGVRSCLGKQLA-- 446
Cdd:cd20673 320 SSIGEFTIPKGTRVvinLWALH--HDEK------EWDQPDQFMPERFLDPTGSQlispslSYLPFGAGPRVCLGEALArq 391

                ....
gi 47086709 447 TLFL 450
Cdd:cd20673 392 ELFL 395
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
259-450 8.49e-12

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: 67.17  E-value: 8.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 259 QGKDYTDALDVLLESAkenntELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRSCGLLHDGCLC 338
Cdd:cd20644 211 RPQHYTGIVAELLLQA-----ELSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQ 285
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 339 QgelrldSIISLKYLDCVIKEVLRLFaPVSGGY-RIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFS 417
Cdd:cd20644 286 K------ALTELPLLKAALKETLRLY-PVGITVqRVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWL 358
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 47086709 418 PERSEDREgrFHYLPFGGGVRSCLGKQLA----TLFL 450
Cdd:cd20644 359 DIRGSGRN--FKHLAFGFGMRQCLGRRLAeaemLLLL 393
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
129-446 1.56e-11

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: 66.09  E-value: 1.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 129 SLANSIGDIHRKRRKIFAKVFSHEALESYLPKIQQVIQETLrvwssnpDPInVYRES----QRLSFNMAVRV---LLGfr 201
Cdd:cd11078  63 SLVNEDPPRHTRLRRLVSRAFTPRRIAALEPRIRELAAELL-------DRL-AEDGRadfvADFAAPLPALViaeLLG-- 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 202 IPEEEMHCLFSTFQEFVENVFSLPIDLPFSGYRKGIrarDSLQKSIEKAIREKPLHTQGKDYTDaldvLLESAKENNTEL 281
Cdd:cd11078 133 VPEEDMERFRRWADAFALVTWGRPSEEEQVEAAAAV---GELWAYFADLVAERRREPRDDLISD----LLAAADGDGERL 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 282 TMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREElRScgllhdgclcqgelRLDSIISlkyldcvikEVL 361
Cdd:cd11078 206 TDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLRAD-PS--------------LIPNAVE---------ETL 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 362 RLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIrdthdTSAVfKDVEAF-DPDRFSPerseDREGRFHYLPFGGGVRSC 440
Cdd:cd11078 262 RYDSPVQGLRRTATRDVEIGGVTIPAGARVLLLF-----GSAN-RDERVFpDPDRFDI----DRPNARKHLTFGHGIHFC 331

                ....*.
gi 47086709 441 LGKQLA 446
Cdd:cd11078 332 LGAALA 337
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
308-478 2.65e-11

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


Pssm-ID: 410701 [Multi-domain]  Cd Length: 350  Bit Score: 65.07  E-value: 2.65e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 308 LVMQLLRHPAVLEKLREelrscglLHDGclcqgelrldsiislkyLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPK 387
Cdd:cd11079 206 LVHYLARHPELQARLRA-------NPAL-----------------LPAAIDEILRLDDPFVANRRITTRDVELGGRTIPA 261
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 388 GWSVMysirdTHDTSAVfKDVEAF-DPDRFSPERSEDREgrfhyLPFGGGVRSCLGKQLATLFLKLLAVEL-AGGSRFEL 465
Cdd:cd11079 262 GSRVT-----LNWASAN-RDERVFgDPDEFDPDRHAADN-----LVYGRGIHVCPGAPLARLELRILLEELlAQTEAITL 330
                       170
                ....*....|...
gi 47086709 466 STRTFPRMISVPV 478
Cdd:cd11079 331 AAGGPPERATYPV 343
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
39-452 2.74e-11

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 65.87  E-value: 2.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   39 ATRDKSCKLPmpKGSMGFPIIGeTCHWF--FQGAGFHASRRQKYGNVFKTHLLGRPLIRVTGAEnVRKVLMGEHSLVTVD 116
Cdd:PLN03234  21 STTKKSLRLP--PGPKGLPIIG-NLHQMekFNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAE-LAKELLKTQDLNFTA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  117 WP----QSTSTLLGPNSLANSIGDIHRKRRKI-FAKVFSHEALESYLPKIQQVIQETL-RVWSSNPDPINVYRESQRLSF 190
Cdd:PLN03234  97 RPllkgQQTMSYQGRELGFGQYTAYYREMRKMcMVNLFSPNRVASFRPVREEECQRMMdKIYKAADQSGTVDLSELLLSF 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  191 NMAV--RVLLGFRIPE--EEMH----CLFSTfQEFVENVFSLPIdLPFSGYR---KGIRAR-----DSLQKSIEKAIREK 254
Cdd:PLN03234 177 TNCVvcRQAFGKRYNEygTEMKrfidILYET-QALLGTLFFSDL-FPYFGFLdnlTGLSARlkkafKELDTYLQELLDET 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  255 PLHTQGKDYTDA-LDVLLESAKEN--NTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRScgL 331
Cdd:PLN03234 255 LDPNRPKQETESfIDLLMQIYKDQpfSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRN--V 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  332 LHDgclcQGELRLDSIISLKYLDCVIKEVLRLfAPV--------------SGGYRIATQTFeldgVQVpKGWSVmysird 397
Cdd:PLN03234 333 IGD----KGYVSEEDIPNLPYLKAVIKESLRL-EPVipillhretiadakIGGYDIPAKTI----IQV-NAWAV------ 396
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 47086709  398 THDTSAVFKDVEAFDPDRFSPE-RSEDREGR-FHYLPFGGGVRSCLGKQLATLFLKL 452
Cdd:PLN03234 397 SRDTAAWGDNPNEFIPERFMKEhKGVDFKGQdFELLPFGSGRRMCPAMHLGIAMVEI 453
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
138-453 3.51e-11

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: 65.07  E-value: 3.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 138 HRKRRKIFAKVFSHEALESYLPKIQQVIQ------ETLRVWSSNPDPIN-VYRESQRLSFNMAVRVLLGFR-------IP 203
Cdd:cd20646  67 YRLRSVLNQRMLKPKEVSLYADAINEVVSdlmkriEYLRERSGSGVMVSdLANELYKFAFEGISSILFETRigclekeIP 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 204 EEEMHCLFSTFQEFVENV-------FSLPIdLPFsgYRKGIRARDSLQKSIEKAIREKPLHTQGKDYTDA------LDVL 270
Cdd:cd20646 147 EETQKFIDSIGEMFKLSEivtllpkWTRPY-LPF--WKRYVDAWDTIFSFGKKLIDKKMEEIEERVDRGEpvegeyLTYL 223
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 271 LESAKennteLTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRScgllhdgcLCQGElRL---DSI 347
Cdd:cd20646 224 LSSGK-----LSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVIS--------VCPGD-RIptaEDI 289
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 348 ISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQV-PKgwsvMYSIRDTHdtSAVFKDVEAF-DPDRFSPER----S 421
Cdd:cd20646 290 AKMPLLKAVIKETLRLYPVVPGNARVIVEKEVVVGDYLfPK----NTLFHLCH--YAVSHDETNFpEPERFKPERwlrdG 363
                       330       340       350
                ....*....|....*....|....*....|..
gi 47086709 422 EDREGRFHYLPFGGGVRSCLGKQLATLFLKLL 453
Cdd:cd20646 364 GLKHHPFGSIPFGYGVRACVGRRIAELEMYLA 395
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
212-450 4.87e-11

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: 64.50  E-value: 4.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 212 STFQEFVENVFSlPIDLPFSGYRKGIRardSLQKSIEKAIREKPLHTQG-------KDYTDALdvLLESAKEN---NTEL 281
Cdd:cd11026 149 SSPWGQLYNMFP-PLLKHLPGPHQKLF---RNVEEIKSFIRELVEEHREtldpsspRDFIDCF--LLKMEKEKdnpNSEF 222
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 282 TMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELrscgllhDGCLCQGEL-RLDSIISLKYLDCVIKEV 360
Cdd:cd11026 223 HEENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEI-------DRVIGRNRTpSLEDRAKMPYTDAVIHEV 295
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 361 LRL--FAPVsGGYRIATQTFELDGVQVPKGWSVMYSIrdthdtSAVFKDVEAF-DPDRFSPERSEDREGRFH----YLPF 433
Cdd:cd11026 296 QRFgdIVPL-GVPHAVTRDTKFRGYTIPKGTTVIPNL------TSVLRDPKQWeTPEEFNPGHFLDEQGKFKkneaFMPF 368
                       250
                ....*....|....*....
gi 47086709 434 GGGVRSCLGKQLA--TLFL 450
Cdd:cd11026 369 SAGKRVCLGEGLArmELFL 387
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
261-476 4.97e-11

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: 64.56  E-value: 4.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 261 KDYTDALDVLLESAKEN-NTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRScgllhdgclCQ 339
Cdd:cd20670 201 RDFIDCFLIKMHQDKNNpHTEFNLKNLVLTTLNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQ---------VI 271
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 340 GELRLDSI---ISLKYLDCVIKEVLRL--FAPVSGGYRIATQTfELDGVQVPKGWSVMYSIrdthdtSAVFKDVEAF-DP 413
Cdd:cd20670 272 GPHRLPSVddrVKMPYTDAVIHEIQRLtdIVPLGVPHNVIRDT-QFRGYLLPKGTDVFPLL------GSVLKDPKYFrYP 344
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47086709 414 DRFSPERSEDREGRFH----YLPFGGGVRSCLGKQLATLFLKLLAVELAggSRFELSTRTFPRMISV 476
Cdd:cd20670 345 EAFYPQHFLDEQGRFKkneaFVPFSSGKRVCLGEAMARMELFLYFTSIL--QNFSLRSLVPPADIDI 409
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
20-458 5.17e-11

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 64.75  E-value: 5.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   20 VSMALLLAVSQQLwqlrwTATRDKSCKLPMPKGSMGFPIIGetcHWFFQGAGFH----ASRRQKYGNVFKTHLLGRPLIR 95
Cdd:PLN02394   7 TLLGLFVAIVLAL-----LVSKLRGKKLKLPPGPAAVPIFG---NWLQVGDDLNhrnlAEMAKKYGDVFLLRMGQRNLVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   96 VTGAENVRKVLMGEhslvTVDWPQSTSTLL-------GPNSLANSIGDIHRKRRKIFA-KVFSHEALESYLPKIQQVIQE 167
Cdd:PLN02394  79 VSSPELAKEVLHTQ----GVEFGSRTRNVVfdiftgkGQDMVFTVYGDHWRKMRRIMTvPFFTNKVVQQYRYGWEEEADL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  168 TLRVWSSNPDP----INVYRESQRLSFNMAVRVLLGFRIpEEEMHCLFSTF-----------QEFVENV--FsLPIDLPF 230
Cdd:PLN02394 155 VVEDVRANPEAategVVIRRRLQLMMYNIMYRMMFDRRF-ESEDDPLFLKLkalngersrlaQSFEYNYgdF-IPILRPF 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  231 -SGYRKGIR----ARDSLQKS--IEKaiREKPLHTQGKDYTD---ALDVLLESAK-----ENNTELTMQELKESTIELIF 295
Cdd:PLN02394 233 lRGYLKICQdvkeRRLALFKDyfVDE--RKKLMSAKGMDKEGlkcAIDHILEAQKkgeinEDNVLYIVENINVAAIETTL 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  296 AAFATTasastslVMQLLRHPAVLEKLREELrscgllhDGCLCQGELRLDSII-SLKYLDCVIKEVLRLFAPVS------ 368
Cdd:PLN02394 311 WSIEWG-------IAELVNHPEIQKKLRDEL-------DTVLGPGNQVTEPDThKLPYLQAVVKETLRLHMAIPllvphm 376
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  369 -------GGYRIatqtfeldgvqvPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERS--EDREGRFHYLPFGGGVRS 439
Cdd:PLN02394 377 nledaklGGYDI------------PAESKILVNAWWLANNPELWKNPEEFRPERFLEEEAkvEANGNDFRFLPFGVGRRS 444
                        490
                 ....*....|....*....
gi 47086709  440 CLGKQLAtlfLKLLAVELA 458
Cdd:PLN02394 445 CPGIILA---LPILGIVLG 460
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
320-457 5.51e-11

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


Pssm-ID: 410694 [Multi-domain]  Cd Length: 424  Bit Score: 64.59  E-value: 5.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 320 EKLREELRSCGLLHDGclcqgeLRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFEL---DGV-QVPKGWSVMYSI 395
Cdd:cd11071 261 ARLAEEIRSALGSEGG------LTLAALEKMPLLKSVVYETLRLHPPVPLQYGRARKDFVIeshDASyKIKKGELLVGYQ 334
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47086709 396 ----RDthdtSAVFKDVEAFDPDRFsperSEDREGRFHYLPFGGGV---------RSCLGKQLATLFLKLLAVEL 457
Cdd:cd11071 335 platRD----PKVFDNPDEFVPDRF----MGEEGKLLKHLIWSNGPeteeptpdnKQCPGKDLVVLLARLFVAEL 401
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
96-446 6.28e-11

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: 64.08  E-value: 6.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  96 VTGAENVRKVL-------MGEHSLVTVDWPQSTSTLLGPNSLANSIGDIHRKRRKIFAKVFSHEALESYLPKIQQVIQET 168
Cdd:cd11030  28 VTGHDEVRAVLadprfssDRTRPGFPALSPEGKAAAALPGSFIRMDPPEHTRLRRMLAPEFTVRRVRALRPRIQEIVDEL 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 169 LRVWSSNPDPINVYREsqrLSFNMAVRV---LLGfrIPEEEMHclfsTFQEFVENVFSLPIDLpfsgyRKGIRARDSLQK 245
Cdd:cd11030 108 LDAMEAAGPPADLVEA---FALPVPSLViceLLG--VPYEDRE----FFQRRSARLLDLSSTA-----EEAAAAGAELRA 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 246 SIEKAIREKplHTQGKDytDALDVLLESAKENNtELTMQELK-----------ESTIELIFAAfattasastslVMQLLR 314
Cdd:cd11030 174 YLDELVARK--RREPGD--DLLSRLVAEHGAPG-ELTDEELVgiavlllvaghETTANMIALG-----------TLALLE 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 315 HPAVLEKLREElrscgllhdgclcqgelrldsiISLkyLDCVIKEVLRLFAPVSGG-YRIATQTFELDGVQVPKGWSVMY 393
Cdd:cd11030 238 HPEQLAALRAD----------------------PSL--VPGAVEELLRYLSIVQDGlPRVATEDVEIGGVTIRAGEGVIV 293
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 47086709 394 SI----RDthdtSAVFKDVEAFDPDRfspersedrEGRFHyLPFGGGVRSCLGKQLA 446
Cdd:cd11030 294 SLpaanRD----PAVFPDPDRLDITR---------PARRH-LAFGHGVHQCLGQNLA 336
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
217-485 7.12e-11

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


Pssm-ID: 410754 [Multi-domain]  Cd Length: 436  Bit Score: 64.06  E-value: 7.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 217 FVENVFSLPIDLPFSG----YRKGIRARDSLQKSIEK-AIREKPLHTQgkDYTDA-LDVLLESAKENNTELTMQELKEST 290
Cdd:cd20661 166 FLYNAFPWIGILPFGKhqqlFRNAAEVYDFLLRLIERfSENRKPQSPR--HFIDAyLDEMDQNKNDPESTFSMENLIFSV 243
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 291 IELIFAAFATTASASTSLVMQLLRHPAVLEKLREELrscgllhDGCLCQGEL-RLDSIISLKYLDCVIKEVLRL--FAPV 367
Cdd:cd20661 244 GELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEI-------DLVVGPNGMpSFEDKCKMPYTEAVLHEVLRFcnIVPL 316
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 368 sGGYRIATQTFELDGVQVPKGWSVMYSIRDTHdtsavFKDVEAFDPDRFSPERSEDREGRF----HYLPFGGGVRSCLGK 443
Cdd:cd20661 317 -GIFHATSKDAVVRGYSIPKGTTVITNLYSVH-----FDEKYWSDPEVFHPERFLDSNGQFakkeAFVPFSLGRRHCLGE 390
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 47086709 444 QLATLFLKLLAVELAggSRFELStrtFPRMiSVPVVHPTDGL 485
Cdd:cd20661 391 QLARMEMFLFFTALL--QRFHLH---FPHG-LIPDLKPKLGM 426
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
138-457 7.29e-11

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: 63.89  E-value: 7.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 138 HRKRRKIFAKVFSHEALESYLPKIQQVIQETLRV-----------WSSNPDPINVYREsqrlsfnmavrvLLGFriPEEe 206
Cdd:cd11034  61 HKKYRKLLNPFFTPEAVEAFRPRVRQLTNDLIDAfiergecdlvtELANPLPARLTLR------------LLGL--PDE- 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 207 mhcLFSTFQEFVENVFSLPidlpfsGYRKGIRARDSLQKSIEKAIREKplHTQGKDytDALDVLLEsAKENNTELTMQEL 286
Cdd:cd11034 126 ---DGERLRDWVHAILHDE------DPEEGAAAFAELFGHLRDLIAER--RANPRD--DLISRLIE-GEIDGKPLSDGEV 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 287 KESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELrscgllhdgclcqgelrldsiiSLkyLDCVIKEVLRLFAP 366
Cdd:cd11034 192 IGFLTLLLLGGTDTTSSALSGALLWLAQHPEDRRRLIADP----------------------SL--IPNAVEEFLRFYSP 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 367 VSGGYRIATQTFELDGVQVPKGWSVMYSIrdthdtSAVFKDVEAF-DPDRFSPERSEDRegrfhYLPFGGGVRSCLGKQL 445
Cdd:cd11034 248 VAGLARTVTQEVEVGGCRLKPGDRVLLAF------ASANRDEEKFeDPDRIDIDRTPNR-----HLAFGSGVHRCLGSHL 316
                       330
                ....*....|..
gi 47086709 446 ATLFLKLLAVEL 457
Cdd:cd11034 317 ARVEARVALTEV 328
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
210-483 1.46e-10

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: 63.05  E-value: 1.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 210 LFSTFQEFVENVFSLPID-LPFSgYRKGIRARDSLQKSIEKAIRE--KPL-HTQGKDYTDALDVLLESAKEN-NTELTMQ 284
Cdd:cd20665 147 ILSSPWLQVCNNFPALLDyLPGS-HNKLLKNVAYIKSYILEKVKEhqESLdVNNPRDFIDCFLIKMEQEKHNqQSEFTLE 225
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 285 ELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREEL-RSCGLLHDGCLcQGELRLdsiislKYLDCVIKEVLRL 363
Cdd:cd20665 226 NLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIdRVIGRHRSPCM-QDRSHM------PYTDAVIHEIQRY 298
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 364 --FAPvSGGYRIATQTFELDGVQVPKGWSVMYSIrdthdtSAVFKDVEAF-DPDRFSPERSEDREGRF----HYLPFGGG 436
Cdd:cd20665 299 idLVP-NNLPHAVTCDTKFRNYLIPKGTTVITSL------TSVLHDDKEFpNPEKFDPGHFLDENGNFkksdYFMPFSAG 371
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 47086709 437 VRSCLGKQLA--TLFLKLLAVElaggSRFELStrtfprmisvPVVHPTD 483
Cdd:cd20665 372 KRICAGEGLArmELFLFLTTIL----QNFNLK----------SLVDPKD 406
PTZ00404 PTZ00404
cytochrome P450; Provisional
51-446 1.51e-10

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 63.20  E-value: 1.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   51 KGSMGFPIIGETcHWFFQGAGFHASR-RQKYGNVFKTHLLGRPLIRVTGAENVRKVLMGEHSLVTvDWPQSTSTLLGPN- 128
Cdd:PTZ00404  32 KGPIPIPILGNL-HQLGNLPHRDLTKmSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFS-DRPKIPSIKHGTFy 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  129 -SLANSIGDIHRKRRKIFAKVFShealESYLPKIQQVIQ-------ETLRVWSSNPDPINVYRESQRLSFNMAVRVLLGF 200
Cdd:PTZ00404 110 hGIVTSSGEYWKRNREIVGKAMR----KTNLKHIYDLLDdqvdvliESMKKIESSGETFEPRYYLTKFTMSAMFKYIFNE 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  201 RIPEEE-------------MHCLFSTFQefVENVF-SLPIDLPFsgYRKGIRARDSLQKSIEKAIREKpLHTQGKDYT-- 264
Cdd:PTZ00404 186 DISFDEdihngklaelmgpMEQVFKDLG--SGSLFdVIEITQPL--YYQYLEHTDKNFKKIKKFIKEK-YHEHLKTIDpe 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  265 ---DALDVLLESAKENNTELtMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRSCGLLHDgclcqgE 341
Cdd:PTZ00404 261 vprDLLDLLIKEYGTNTDDD-ILSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRN------K 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  342 LRLDSIISLKYLDCVIKEVLRLFAPVSGGY-RIATQTFELDGVQ-VPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPE 419
Cdd:PTZ00404 334 VLLSDRQSTPYTVAIIKETLRYKPVSPFGLpRSTSNDIIIGGGHfIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNP 413
                        410       420
                 ....*....|....*....|....*..
gi 47086709  420 RSEDRegrfhYLPFGGGVRSCLGKQLA 446
Cdd:PTZ00404 414 DSNDA-----FMPFSIGPRNCVGQQFA 435
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
309-465 1.79e-10

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: 62.55  E-value: 1.79e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 309 VMQLLRHPAVLEKLREelrscgllhDGCLcqgelrldsiislkyLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKG 388
Cdd:cd11033 233 VLALAEHPDQWERLRA---------DPSL---------------LPTAVEEILRWASPVIHFRRTATRDTELGGQRIRAG 288
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 389 WSVMYSI----RDThdtsAVFKDVEAFDPDRfSPERsedregrfHyLPFGGGVRSCLGKQLATLFLKLLAVELAG-GSRF 463
Cdd:cd11033 289 DKVVLWYasanRDE----EVFDDPDRFDITR-SPNP--------H-LAFGGGPHFCLGAHLARLELRVLFEELLDrVPDI 354

                ..
gi 47086709 464 EL 465
Cdd:cd11033 355 EL 356
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
100-446 1.87e-10

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: 62.49  E-value: 1.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 100 ENVRKVLMGEHSLVTVDWPQSTSTLLGPNSLANSIGDIHRKRRKIFAKVFSHEALESYLPKIQQVIQETLRVWSS--NPD 177
Cdd:cd11080  18 EDVRRILKDPDGFTTKSLAERAEPVMRGPVLAQMTGKEHAAKRAIVVRAFRGDALDHLLPLIKENAEELIAPFLErgRVD 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 178 PINVYreSQRLSFNMAVRVLLGFRIPEEEMHCLFSTFQEFVENvfslpIDLPFSGYRKGIRARDSLQKSIEKAIREKPLH 257
Cdd:cd11080  98 LVNDF--GKPFAVNVTMDMLGLDKRDHEKIHEWHSSVAAFITS-----LSQDPEARAHGLRCAEQLSQYLLPVIEERRVN 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 258 TqGKDytdaLDVLLESAKENNTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREelrscgllhDGCL 337
Cdd:cd11080 171 P-GSD----LISILCTAEYEGEALSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPEQLAAVRA---------DRSL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 338 CQGelrldsiislkyldcVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIrdthdtSAVFKDVEAF-DPDRF 416
Cdd:cd11080 237 VPR---------------AIAETLRYHPPVQLIPRQASQDVVVSGMEIKKGTTVFCLI------GAANRDPAAFeDPDTF 295
                       330       340       350
                ....*....|....*....|....*....|....*
gi 47086709 417 SPERSE-----DREGRFHYLPFGGGVRSCLGKQLA 446
Cdd:cd11080 296 NIHREDlgirsAFSGAADHLAFGSGRHFCVGAALA 330
PLN02971 PLN02971
tryptophan N-hydroxylase
5-479 2.53e-10

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 62.75  E-value: 2.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709    5 SFDLVSALATLAAcLVSMALLLAVSQQLwqlrwTATRDKSCKlPMPKGSMGFPIIGETCHWFFQGAGF---HASRRQKYG 81
Cdd:PLN02971  21 SFTNMYLLTTLQA-LVAITLLMILKKLK-----SSSRNKKLH-PLPPGPTGFPIVGMIPAMLKNRPVFrwlHSLMKELNT 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   82 NVFKTHLLGRPLIRVTGAENVRKVLMGEHSLVT---VDWPQSTSTLLGPNSLANSIGDIHRKRRKIFAKVFSHEALESYL 158
Cdd:PLN02971  94 EIACVRLGNTHVIPVTCPKIAREIFKQQDALFAsrpLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  159 PKIQQVIQETLRVW----SSNPDPINVYRESQRLSFNMAVRVLLGFRI------PE--------EEMHCLFS----TFQE 216
Cdd:PLN02971 174 HDNRAEETDHLTAWlynmVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTfsektePDggptlediEHMDAMFEglgfTFAF 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  217 FVENVFSLPIDLPFSGYRKGIRARDSLQKSIEKAIREKPLHT--QGK--DYTDALDVLLESAKE-NNTELTMQELKESTI 291
Cdd:PLN02971 254 CISDYLPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMwrEGKrtQIEDFLDIFISIKDEaGQPLLTADEIKPTIK 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  292 ELIFAAFATTASASTSLVMQLLRHPAVLEKLREELrscgllhDGCLCQGELRLDS-IISLKYLDCVIKEVLRLFaPVSGG 370
Cdd:PLN02971 334 ELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEI-------DRVVGKERFVQESdIPKLNYVKAIIREAFRLH-PVAAF 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  371 Y--RIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSED--REGRFHYLPFGGGVRSCLGKQLA 446
Cdd:PLN02971 406 NlpHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVtlTENDLRFISFSTGKRGCAAPALG 485
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 47086709  447 TLFLKLLAVELAGG---------SRFELSTRTFPRMISVPVV 479
Cdd:PLN02971 486 TAITTMMLARLLQGfkwklagseTRVELMESSHDMFLSKPLV 527
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
311-452 3.05e-10

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: 62.08  E-value: 3.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 311 QLLRHPAVLEKLREELRScgLLHDGCLCQGElrldSIISLKYLDCVIKEVLRLFAPVSGGYR-IATQTFELDGVQVPKGW 389
Cdd:cd20648 260 ELSRHPDVQTALHREITA--ALKDNSVPSAA----DVARMPLLKAVVKEVLRLYPVIPGNARvIPDRDIQVGEYIIPKKT 333
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47086709 390 SVMYSIRDTHDTSAVFKDveafdPDRFSPERSEDREGRFH---YLPFGGGVRSCLGKQLATLFLKL 452
Cdd:cd20648 334 LITLCHYATSRDENQFPD-----PNSFRPERWLGKGDTHHpyaSLPFGFGKRSCIGRRIAELEVYL 394
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
245-450 4.89e-10

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: 61.66  E-value: 4.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 245 KSIEKAIREKPLHTQG-KDYTDALDVLLESAKennteLTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLR 323
Cdd:cd20643 198 KCIQNIYRDLRQKGKNeHEYPGILANLLLQDK-----LPIEDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLR 272
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 324 EELRSCGLLHDGCLCQgelRLDSIISLKyldCVIKEVLRLFaPVSGGY-RIATQTFELDGVQVPKGWSVMYSIRDTHDTS 402
Cdd:cd20643 273 AEVLAARQEAQGDMVK---MLKSVPLLK---AAIKETLRLH-PVAVSLqRYITEDLVLQNYHIPAGTLVQVGLYAMGRDP 345
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 47086709 403 AVFkdveaFDPDRFSPERSEDREGR-FHYLPFGGGVRSCLGKQLA----TLFL 450
Cdd:cd20643 346 TVF-----PKPEKYDPERWLSKDIThFRNLGFGFGPRQCLGRRIAetemQLFL 393
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
312-454 5.12e-10

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: 61.66  E-value: 5.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 312 LLRHPAVLEKLREELRSCGLLHDgclcqgELRLDSIISLKYLDCVIKEVLRLFAPVSGGY-RIATQTFELDGVQVPKGWS 390
Cdd:cd20652 261 MALFPKEQRRIQRELDEVVGRPD------LVTLEDLSSLPYLQACISESQRIRSVVPLGIpHGCTEDAVLAGYRIPKGSM 334
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47086709 391 VMYSIRDTHDTSAVFKDVEAFDPDRFSperseDREGRF----HYLPFGGGVRSCLGKQLATLFLKLLA 454
Cdd:cd20652 335 IIPLLWAVHMDPNLWEEPEEFRPERFL-----DTDGKYlkpeAFIPFQTGKRMCLGDELARMILFLFT 397
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
80-455 1.55e-09

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: 59.78  E-value: 1.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  80 YGNVFKTHLLGRPLIRVTGAENVRK--VLMGEHSLVTVDWPQSTSTLLGpNSLANSIGDIHRKRRKIFAKVFSH-----E 152
Cdd:cd20669   1 YGSVYTVYLGPRPVVVLCGYQAVKEalVDQAEEFSGRGDYPVFFNFTKG-NGIAFSNGERWKILRRFALQTLRNfgmgkR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 153 ALESYLPKIQQVIQETLRVWSSNP-DPINVYreSQRLSfNMAVRVLLGFRIPEE------------EMHCLFSTFQEFVE 219
Cdd:cd20669  80 SIEERILEEAQFLLEELRKTKGAPfDPTFLL--SRAVS-NIICSVVFGSRFDYDdkrlltilnlinDNFQIMSSPWGELY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 220 NVFSLPIDLPFSGYRKGIRARDSLQKSIEKAIRE-KPLHTQG--KDYTDALdvLLESAKENNTELT---MQELKESTIEL 293
Cdd:cd20669 157 NIFPSVMDWLPGPHQRIFQNFEKLRDFIAESVREhQESLDPNspRDFIDCF--LTKMAEEKQDPLShfnMETLVMTTHNL 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 294 IFAAFATTASASTSLVMQLLRHPAVLEKLREELrscgllhDGCLCQGEL-RLDSIISLKYLDCVIKEVLRlFA---PVSG 369
Cdd:cd20669 235 LFGGTETVSTTLRYGFLILMKYPKVAARVQEEI-------DRVVGRNRLpTLEDRARMPYTDAVIHEIQR-FAdiiPMSL 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 370 GYRIaTQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSEDREGRfHYLPFGGGVRSCLGKQLA--T 447
Cdd:cd20669 307 PHAV-TRDTNFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKND-AFMPFSAGKRICLGESLArmE 384

                ....*...
gi 47086709 448 LFLKLLAV 455
Cdd:cd20669 385 LFLYLTAI 392
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
356-482 1.81e-09

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: 59.53  E-value: 1.81e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 356 VIKEVLRLFAPVSGGyRIATQTFELDGVQVPKGWSVMYSirdthdTSAVFKDVEAF-DPDRFSPERSedregRFHYLPFG 434
Cdd:cd11035 237 AVEELLRRYPLVNVA-RIVTRDVEFHGVQLKAGDMVLLP------LALANRDPREFpDPDTVDFDRK-----PNRHLAFG 304
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 47086709 435 GGVRSCLGKQLATLFLKLLAVE-LAGGSRFELSTRTFPRMISVPVVHPT 482
Cdd:cd11035 305 AGPHRCLGSHLARLELRIALEEwLKRIPDFRLAPGAQPTYHGGSVMGLE 353
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
191-480 2.22e-09

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: 59.43  E-value: 2.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 191 NMAVRVLLGFR-------------IPEEEMHcLFSTFQEFVENVFslPIDLPFSGYRKGI-----RARDSLQKSIEKAIR 252
Cdd:cd20664 116 NIIASIVLGHRfeytdptllrmvdRINENMK-LTGSPSVQLYNMF--PWLGPFPGDINKLlrntkELNDFLMETFMKHLD 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 253 EKPLHTQgKDYTDALDVLLESAKENNTEL-TMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELrscgl 331
Cdd:cd20664 193 VLEPNDQ-RGFIDAFLVKQQEEEESSDSFfHDDNLTCSVGNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEI----- 266
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 332 lhDGCLCQGELRLDSIISLKYLDCVIKEVLRlFAPVS--GGYRIATQTFELDGVQVPKGWSVMYSIrdthdTSAVFKDVE 409
Cdd:cd20664 267 --DRVIGSRQPQVEHRKNMPYTDAVIHEIQR-FANIVpmNLPHATTRDVTFRGYFIPKGTYVIPLL-----TSVLQDKTE 338
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 410 AFDPDRFSPERSEDREGRF----HYLPFGGGVRSCLGKQLATLFLKLLAVEL---------AGGSRFELSTRTFPRMISV 476
Cdd:cd20664 339 WEKPEEFNPEHFLDSQGKFvkrdAFMPFSAGRRVCIGETLAKMELFLFFTSLlqrfrfqppPGVSEDDLDLTPGLGFTLN 418

                ....
gi 47086709 477 PVVH 480
Cdd:cd20664 419 PLPH 422
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
247-453 2.28e-09

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: 59.43  E-value: 2.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 247 IEKAIREKPLHTQGKDYTDALDVLLESAKENNTELTM---QELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLR 323
Cdd:cd20671 182 LRTLIEARRPTIDGNPLHSYIEALIQKQEEDDPKETLfhdANVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQ 261
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 324 EELRScgLLHDGCLCQGELRLdsiiSLKYLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIrdthdTSA 403
Cdd:cd20671 262 EEIDR--VLGPGCLPNYEDRK----ALPYTSAVIHEVQRFITLLPHVPRCTAADTQFKGYLIPKGTPVIPLL-----SSV 330
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 47086709 404 VFKDVEAFDPDRFSPERSEDREGRF----HYLPFGGGVRSCLGKQLATLFLKLL 453
Cdd:cd20671 331 LLDKTQWETPYQFNPNHFLDAEGKFvkkeAFLPFSAGRRVCVGESLARTELFIF 384
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
308-457 5.92e-09

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 58.16  E-value: 5.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  308 LVMQLLRHPAVLEKLREELRScgLLHDGclcQGELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFEL-DGVQVP 386
Cdd:PLN02426 316 FFWLLSKHPEVASAIREEADR--VMGPN---QEAASFEEMKEMHYLHAALYESMRLFPPVQFDSKFAAEDDVLpDGTFVA 390
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47086709  387 KGWSVMYSIRDTHDTSAVF-KDVEAFDPDR------FSPERSedregrFHYLPFGGGVRSCLGKQLATLFLKLLAVEL 457
Cdd:PLN02426 391 KGTRVTYHPYAMGRMERIWgPDCLEFKPERwlkngvFVPENP------FKYPVFQAGLRVCLGKEMALMEMKSVAVAV 462
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
352-450 6.23e-09

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: 58.17  E-value: 6.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 352 YLDCVIKEVLRL--FAPVsGGYRIATQTFELDGVQVPKGWSVMYSIrdthdtSAVFKDVEAFD-PDRFSPERSEDREGRF 428
Cdd:cd20663 291 YTNAVIHEVQRFgdIVPL-GVPHMTSRDIEVQGFLIPKGTTLITNL------SSVLKDETVWEkPLRFHPEHFLDAQGHF 363
                        90       100
                ....*....|....*....|....*...
gi 47086709 429 ----HYLPFGGGVRSCLGKQLA--TLFL 450
Cdd:cd20663 364 vkpeAFMPFSAGRRACLGEPLArmELFL 391
PLN02966 PLN02966
cytochrome P450 83A1
41-479 6.23e-09

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 58.22  E-value: 6.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   41 RDKSCKLPMPKGSMGFPIIGETCHW-FFQGAGFHASRRQKYGNVFKTHLLGRPLIRVTGAENVRKVLMGEHSLVTVDWPQ 119
Cdd:PLN02966  22 KPKTKRYKLPPGPSPLPVIGNLLQLqKLNPQRFFAGWAKKYGPILSYRIGSRTMVVISSAELAKELLKTQDVNFADRPPH 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  120 STSTLL--GPNSLA-NSIGDIHRKRRKI-FAKVFSHEALESYLPKIQQVIQETLRVWSSNPDPINVYRESQ-RLSFNMAV 194
Cdd:PLN02966 102 RGHEFIsyGRRDMAlNHYTPYYREIRKMgMNHLFSPTRVATFKHVREEEARRMMDKINKAADKSEVVDISElMLTFTNSV 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  195 --RVLLGFRIPE--EEMH----CLFSTfQEFVENVFSLPIdLPFSGYRKGIRARDSLQKS--------IEKAIREKPLHT 258
Cdd:PLN02966 182 vcRQAFGKKYNEdgEEMKrfikILYGT-QSVLGKIFFSDF-FPYCGFLDDLSGLTAYMKEcferqdtyIQEVVNETLDPK 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  259 QGKDYTDAL-DVLLESAKEN--NTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELRSCgLLHDG 335
Cdd:PLN02966 260 RVKPETESMiDLLMEIYKEQpfASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREY-MKEKG 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  336 CLCQGElrlDSIISLKYLDCVIKEVLR------LFAPvsggyRIATQTFELDGVQVPKGWSVmysirdTHDTSAVFKDVE 409
Cdd:PLN02966 339 STFVTE---DDVKNLPYFRALVKETLRiepvipLLIP-----RACIQDTKIAGYDIPAGTTV------NVNAWAVSRDEK 404
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47086709  410 AF--DPDRFSPERSEDREGRF-----HYLPFGGGVRSCLGKQLATLFLKLLAVELAGGSRFELSTRTFPRMISVPVV 479
Cdd:PLN02966 405 EWgpNPDEFRPERFLEKEVDFkgtdyEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFKLPNGMKPDDINMDVM 481
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
265-446 6.38e-09

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 58.33  E-value: 6.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  265 DALDVLLeSAKENNTE--LTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELrscgllhDGCLCQGEL 342
Cdd:PLN00110 268 DFLDVVM-ANQENSTGekLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEM-------DQVIGRNRR 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  343 RLDS-IISLKYLDCVIKEVLRLFAPVSGGY-RIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPER 420
Cdd:PLN00110 340 LVESdLPKLPYLQAICKESFRKHPSTPLNLpRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEK 419
                        170       180
                 ....*....|....*....|....*....
gi 47086709  421 SED---REGRFHYLPFGGGVRSCLGKQLA 446
Cdd:PLN00110 420 NAKidpRGNDFELIPFGAGRRICAGTRMG 448
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
152-452 1.35e-08

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: 57.12  E-value: 1.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 152 EALESYLPKIQQVIQETLRVwssnPDpinVYRESQRLSFNMAVRVLLGFR-------IPEEEMH------CLFSTFQEFV 218
Cdd:cd20645  92 EVLADFMGRIDELCDETGRV----ED---LYSELNKWSFETICLVLYDKRfgllqqnVEEEALNfikaikTMMSTFGKMM 164
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 219 ENVFSLPIDLPFSGYRKGIRARDSLQKSIEKAIrEKPL--HTQGKdytdALDVLLESAKENntELTMQELKESTIELIFA 296
Cdd:cd20645 165 VTPVELHKRLNTKVWQDHTEAWDNIFKTAKHCI-DKRLqrYSQGP----ANDFLCDIYHDN--ELSKKELYAAITELQIG 237
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 297 AFATTASASTSLVMQLLRHPAVLEKLREELRSCgllhdgCLCQGELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQ 376
Cdd:cd20645 238 GVETTANSLLWILYNLSRNPQAQQKLLQEIQSV------LPANQTPRAEDLKNMPYLKACLKESMRLTPSVPFTSRTLDK 311
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 377 TFELDGVQVPKGWSVMYsirdthDTSAVFKDVEAF-DPDRFSPER---SEDREGRFHYLPFGGGVRSCLGKQLATLFLKL 452
Cdd:cd20645 312 DTVLGDYLLPKGTVLMI------NSQALGSSEEYFeDGRQFKPERwlqEKHSINPFAHVPFGIGKRMCIGRRLAELQLQL 385
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
309-458 1.50e-08

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: 56.71  E-value: 1.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 309 VMQLLRHPAVLEKLREELrscgllhDGCLCQGELRLDS-IISLKYLDCVIKEVLRLfapvsggyRIATQTF--------- 378
Cdd:cd11074 257 IAELVNHPEIQKKLRDEL-------DTVLGPGVQITEPdLHKLPYLQAVVKETLRL--------RMAIPLLvphmnlhda 321
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 379 ELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSE-DREGR-FHYLPFGGGVRSCLGKQLAtlfLKLLAVE 456
Cdd:cd11074 322 KLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEESKvEANGNdFRYLPFGVGRRSCPGIILA---LPILGIT 398

                ..
gi 47086709 457 LA 458
Cdd:cd11074 399 IG 400
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
312-460 2.16e-08

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: 56.54  E-value: 2.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 312 LLRHPAVLEKLREElrscglLHDGCLCQG-ELRLDSII--------SLKYLDCVIKEVLRLFApVSGGYRIATQTFELD- 381
Cdd:cd20632 242 LLRHPEALAAVRDE------IDHVLQSTGqELGPDFDIhltreqldSLVYLESAINESLRLSS-ASMNIRVVQEDFTLKl 314
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 382 ----GVQVPKG-WSVMYSiRDTHDTSAVFKDVEAFDPDRFSPERSE-------DREGRFHYLPFGGGVRSCLG------- 442
Cdd:cd20632 315 esdgSVNLRKGdIVALYP-QSLHMDPEIYEDPEVFKFDRFVEDGKKkttfykrGQKLKYYLMPFGSGSSKCPGrffavne 393
                       170
                ....*....|....*....
gi 47086709 443 -KQLATLFLKLLAVELAGG 460
Cdd:cd20632 394 iKQFLSLLLLYFDLELLEE 412
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
80-450 2.82e-08

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: 55.94  E-value: 2.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  80 YGNVFKTHLLGRPLIRVTGAENVRKVLMGEHSLVTvdwPQSTSTLLGPNSLANSIGDIHRKRRKIFAKvFS--------- 150
Cdd:cd20672   1 YGDVFTVHLGPRPVVMLCGTDAIREALVDQAEAFS---GRGTIAVVDPIFQGYGVIFANGERWKTLRR-FSlatmrdfgm 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 151 -HEALESYLPKIQQVIQETLRVWSSNP-DPINVYresQRLSFNMAVRVLLGFRI---PEEEMHCL------FSTFQEFVE 219
Cdd:cd20672  77 gKRSVEERIQEEAQCLVEELRKSKGALlDPTFLF---QSITANIICSIVFGERFdykDPQFLRLLdlfyqtFSLISSFSS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 220 NVFSLpidlpFSGYRK---GIRAR---------DSLQKSIEKAiREKPLHTQGKDYTDALDVLLESAKEN-NTELTMQEL 286
Cdd:cd20672 154 QVFEL-----FSGFLKyfpGAHRQiyknlqeilDYIGHSVEKH-RATLDPSAPRDFIDTYLLRMEKEKSNhHTEFHHQNL 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 287 KESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELrscgllhDGCLCQGEL-RLDSIISLKYLDCVIKEVLRL-- 363
Cdd:cd20672 228 MISVLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEI-------DQVIGSHRLpTLDDRAKMPYTDAVIHEIQRFsd 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 364 FAPVSGGYRIATQTFeLDGVQVPKGWSVmYSIrdthdTSAVFKDVEAFD-PDRFSPERSEDREGRFH----YLPFGGGVR 438
Cdd:cd20672 301 LIPIGVPHRVTKDTL-FRGYLLPKNTEV-YPI-----LSSALHDPQYFEqPDTFNPDHFLDANGALKkseaFMPFSTGKR 373
                       410
                ....*....|....
gi 47086709 439 SCLGKQLA--TLFL 450
Cdd:cd20672 374 ICLGEGIArnELFL 387
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
91-474 2.93e-08

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


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 55.81  E-value: 2.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  91 RPLIRVTGAENVRKVLMGEHSlVTVDWPQSTSTL--LGPNSLANSIGDIHRKRRKIFAKVFSHEALESYLPKIQQVIQET 168
Cdd:cd20612  11 PPPVIVTRYADVKKVLEDPES-FSVPWGPAMEDLtkGGPFFLLGGDTPANDRQRELMRKALYSPDLAKDVVFFYELQTRA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 169 LRVWSSNPDP----INVYRE-SQRLSFNMAVRvLLGFR----------IPEEEMHCLFSTFQEFVenVFSLPIDLPFSGY 233
Cdd:cd20612  90 LLVESSRLGGsggqVDIVRDvANLVPARFCAD-LFGLPlktkenprggYTEAELYRALAAIFAYI--FFDLDPAKSFQLR 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 234 RKGIRARDSLQKSIEKAIrekplhtqgKDYT-DALDVLLESAKENNTELTMQELKEstielifaafattasastslvmqL 312
Cdd:cd20612 167 RAAQAAAARLGALLDAAV---------ADEVrDNVLGTAVGGVPTQSQAFAQILDF-----------------------Y 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 313 LRHPAvlEKLREELRScgllhdgclcqgeLRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFELD-----GVQVPK 387
Cdd:cd20612 215 LRRPG--AAHLAEIQA-------------LARENDEADATLRGYVLEALRLNPIAPGLYRRATTDTTVAdgggrTVSIKA 279
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 388 GWSVMYSirdthdTSAVFKDVEAF-DPDRFSPERSEDRegrfhYLPFGGGVRSCLGKQLATLFL--------KLLAVELA 458
Cdd:cd20612 280 GDRVFVS------LASAMRDPRAFpDPERFRLDRPLES-----YIHFGHGPHQCLGEEIARAALtemlrvvlRLPNLRRA 348
                       410       420
                ....*....|....*....|..
gi 47086709 459 GGSRFEL------STRTFPRMI 474
Cdd:cd20612 349 PGPQGELkkiprgGFKAYLRED 370
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
173-453 7.09e-08

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: 54.68  E-value: 7.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 173 SSNPDPINVYRESQRLSFNMAVRVLLGFRI-----------PEEEMH---------CLFStfqefvenvFSLPIDLPF-- 230
Cdd:cd20658 103 SNGGGLVNVRDAARHYCGNVIRKLMFGTRYfgkgmedggpgLEEVEHmdaiftalkCLYA---------FSISDYLPFlr 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 231 ----SGYRKGIRARDSLQKSIEKAIREKPLHT----QGKDYTDALDVLLeSAKE--NNTELTMQELKESTIELIFAAFAT 300
Cdd:cd20658 174 gldlDGHEKIVREAMRIIRKYHDPIIDERIKQwregKKKEEEDWLDVFI-TLKDenGNPLLTPDEIKAQIKELMIAAIDN 252
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 301 TASASTSLVMQLLRHPAVLEKLREELrscgllhDGCLCQGELRLDSIIS-LKYLDCVIKEVLRL--FAPVSGGYrIATQT 377
Cdd:cd20658 253 PSNAVEWALAEMLNQPEILRKATEEL-------DRVVGKERLVQESDIPnLNYVKACAREAFRLhpVAPFNVPH-VAMSD 324
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 378 FELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPERSE----DREGRFhyLPFGGGVRSCLGKQLAT-----L 448
Cdd:cd20658 325 TTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSEvtltEPDLRF--ISFSTGRRGCPGVKLGTamtvmL 402

                ....*
gi 47086709 449 FLKLL 453
Cdd:cd20658 403 LARLL 407
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
80-450 8.13e-08

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: 54.42  E-value: 8.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  80 YGNVFKTHLLGRPLIRVTGAENVRKVL--MGEHSLVTVDWPQSTStLLGPNSLANSIGDIHRKRRKifakvFSHEALESY 157
Cdd:cd20662   1 YGNIFSLQLGSISSVIVTGLPLIKEALvtQEQNFMNRPETPLRER-IFNKNGLIFSSGQTWKEQRR-----FALMTLRNF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 158 -LPK--IQQVIQETLRVWssnpdpINVYRESQRLSF-----------NMAVRVLLGFRIPEEEmhclfSTFQEFVE---- 219
Cdd:cd20662  75 gLGKksLEERIQEECRHL------VEAIREEKGNPFnphfkinnavsNIICSVTFGERFEYHD-----EWFQELLRllde 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 220 -------------NVFSLPID-LP------FSGYRKgirARDSLQKSIEKAiREKPLHTQGKDYTDALDVLLESAKENNT 279
Cdd:cd20662 144 tvylegspmsqlyNAFPWIMKyLPgshqtvFSNWKK---LKLFVSDMIDKH-REDWNPDEPRDFIDAYLKEMAKYPDPTT 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 280 ELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELrscgllhDGCLCQGEL-RLDSIISLKYLDCVIK 358
Cdd:cd20662 220 SFNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEI-------DRVIGQKRQpSLADRESMPYTNAVIH 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 359 EVLRLFAPVSGGY-RIATQTFELDGVQVPKGWSVMYSIrdthdtSAVFKDVEAFD-PDRFSPERSEDrEGRFH----YLP 432
Cdd:cd20662 293 EVQRMGNIIPLNVpREVAVDTKLAGFHLPKGTMILTNL------TALHRDPKEWAtPDTFNPGHFLE-NGQFKkreaFLP 365
                       410       420
                ....*....|....*....|
gi 47086709 433 FGGGVRSCLGKQLA--TLFL 450
Cdd:cd20662 366 FSMGKRACLGEQLArsELFI 385
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
245-464 1.23e-07

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: 54.03  E-value: 1.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 245 KSIEKAIREKPLHTQG-------KDYTDALDVLLESAKEN-NTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHP 316
Cdd:cd20668 178 QGLEDFIAKKVEHNQRtldpnspRDFIDSFLIRMQEEKKNpNTEFYMKNLVMTTLNLFFAGTETVSTTLRYGFLLLMKHP 257
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 317 AVLEKLREEL-RSCGLlhdgclcQGELRLDSIISLKYLDCVIKEVLRL--FAPVSGGYRIATQTfELDGVQVPKGWSVMY 393
Cdd:cd20668 258 EVEAKVHEEIdRVIGR-------NRQPKFEDRAKMPYTEAVIHEIQRFgdVIPMGLARRVTKDT-KFRDFFLPKGTEVFP 329
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47086709 394 SIrdthdtSAVFKDVEAF-DPDRFSPERSEDREGRFH----YLPFGGGVRSCLGKQLATLFLKLLAVELAGGSRFE 464
Cdd:cd20668 330 ML------GSVLKDPKFFsNPKDFNPQHFLDDKGQFKksdaFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRFK 399
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
309-465 1.44e-07

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: 53.69  E-value: 1.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 309 VMQLLRHPAVLEKLREELRSC-GLLHDGCLCQGELrldsiisLKYLDCVIKEVLRLFAPVS-GGYRIATQTFELDGVQVP 386
Cdd:cd20667 249 LLYMVHHPEIQEKVQQELDEVlGASQLICYEDRKR-------LPYTNAVIHEVQRLSNVVSvGAVRQCVTSTTMHGYYVE 321
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 387 KGWSVMYSIrdthdtSAVFKDVEAFD-PDRFSPERSEDREGRF----HYLPFGGGVRSCLGKQLATLFLKLLAVELAGGS 461
Cdd:cd20667 322 KGTIILPNL------ASVLYDPECWEtPHKFNPGHFLDKDGNFvmneAFLPFSAGHRVCLGEQLARMELFIFFTTLLRTF 395

                ....
gi 47086709 462 RFEL 465
Cdd:cd20667 396 NFQL 399
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
308-458 2.05e-07

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


Pssm-ID: 410663 [Multi-domain]  Cd Length: 371  Bit Score: 52.97  E-value: 2.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 308 LVMQLLRHPAVLEKLREE---LRSCgllhdgclcqgelrldsiislkyldcvIKEVLRLFAPVSGGYRIATQTFELDGVQ 384
Cdd:cd11037 225 ALWLLARHPDQWERLRADpslAPNA---------------------------FEEAVRLESPVQTFSRTTTRDTELAGVT 277
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47086709 385 VPKGWSVMYSIrdthdtSAVFKDVEAF-DPDRFSPERSEDRegrfHyLPFGGGVRSCLGKQLATLFLKLLAVELA 458
Cdd:cd11037 278 IPAGSRVLVFL------GSANRDPRKWdDPDRFDITRNPSG----H-VGFGHGVHACVGQHLARLEGEALLTALA 341
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
116-464 2.15e-07

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: 53.14  E-value: 2.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 116 DWPQSTSTLLGP------NSLANSIGDIHRKRRKIFAKVFSHEALESYLPKIQQVIQETLrvwssnpDPInvyRESQRLS 189
Cdd:cd11038  51 RWLAMNGVTEGPfadwwvDFLLSLEGADHARLRGLVNPAFTPKAVEALRPRFRATANDLI-------DGF---AEGGECE 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 190 F---------NMAVRVLLGFriPEEEmHCLFSTFQEFVENVFSLPIdlpfsgyrKGIRARdslqksIEKAIREKplhtqg 260
Cdd:cd11038 121 FveafaepypARVICTLLGL--PEED-WPRVHRWSADLGLAFGLEV--------KDHLPR------IEAAVEEL------ 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 261 KDYTDAL----------DVL--LESAKENNTELTMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREElrs 328
Cdd:cd11038 178 YDYADALiearraepgdDLIstLVAAEQDGDRLSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPDQWRALRED--- 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 329 cgllhdgclcqGELrldsiislkyLDCVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTHdtsavfKDV 408
Cdd:cd11038 255 -----------PEL----------APAAVEEVLRWCPTTTWATREAVEDVEYNGVTIPAGTVVHLCSHAAN------RDP 307
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47086709 409 EAFDPDRFSPERSEDRegrfhYLPFGGGVRSCLGKQLATLFL---------KLLAVELAGGSRFE 464
Cdd:cd11038 308 RVFDADRFDITAKRAP-----HLGFGGGVHHCLGAFLARAELaealtvlarRLPTPAIAGEPTWL 367
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
313-457 2.67e-07

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: 52.70  E-value: 2.67e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 313 LRHPAVLEKLREELRScgLLHDGCLCQGELRLDSIISLKYLDCVIKEVLRLFAPvsgGY--RIATQTFELDGVQVPKGWS 390
Cdd:cd20635 238 LSHPSVYKKVMEEISS--VLGKAGKDKIKISEDDLKKMPYIKRCVLEAIRLRSP---GAitRKVVKPIKIKNYTIPAGDM 312
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47086709 391 VMYSIRDTHDTSAVFKDVEAFDPDRFS---PERSEDREGrfhYLPFGGGVRSCLGKQLA--------TLFLKLLAVEL 457
Cdd:cd20635 313 LMLSPYWAHRNPKYFPDPELFKPERWKkadLEKNVFLEG---FVAFGGGRYQCPGRWFAlmeiqmfvAMFLYKYDFTL 387
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
80-446 3.32e-07

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: 52.79  E-value: 3.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  80 YGNVFKTHLLGRPLIRVTGAENVRKVLM--GEHslvTVDWPQ--STSTLLGPNSLANSI--GD---IHRKRRKIFAKVFS 150
Cdd:cd20677   1 YGDVFQIKLGMLPVVVVSGLETIKQVLLkqGES---FAGRPDfyTFSLIANGKSMTFSEkyGEswkLHKKIAKNALRTFS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 151 HEA---------LESYL-PKIQQVIQETLRVWSSNP--DPINVYRESQRlsfNMAVRVLLGFRIP--EEEMHCLFSTFQE 216
Cdd:cd20677  78 KEEaksstcsclLEEHVcAEASELVKTLVELSKEKGsfDPVSLITCAVA---NVVCALCFGKRYDhsDKEFLTIVEINND 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 217 fVENVFS--LPID-------LPFSGYRKGIRARDSLQKSIEKAIREKpLHTQGK----DYTDALDVLLESAKE--NNTEL 281
Cdd:cd20677 155 -LLKASGagNLADfipilryLPSPSLKALRKFISRLNNFIAKSVQDH-YATYDKnhirDITDALIALCQERKAedKSAVL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 282 TMQELKESTIELIFAAFATTASASTSLVMQLLRHPAVLEKLREELrscgllhDGCLCQGEL-RLDSIISLKYLDCVIKEV 360
Cdd:cd20677 233 SDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEI-------DEKIGLSRLpRFEDRKSLHYTEAFINEV 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 361 LR--LFAPVSGGYRIATQTFeLDGVQVPKGWSV---MYSIrdTHDTSaVFKDVEAFDPDRFSPERSE-DREGRFHYLPFG 434
Cdd:cd20677 306 FRhsSFVPFTIPHCTTADTT-LNGYFIPKDTCVfinMYQV--NHDET-LWKDPDLFMPERFLDENGQlNKSLVEKVLIFG 381
                       410
                ....*....|..
gi 47086709 435 GGVRSCLGKQLA 446
Cdd:cd20677 382 MGVRKCLGEDVA 393
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
308-454 5.19e-07

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: 51.93  E-value: 5.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 308 LVMQLLRHPAVLEKLREELrscgllhDGCLcqGELRLDSI---ISLKYLDCVIKEVLRL--FAPVSGGYRIATQTFeLDG 382
Cdd:cd20675 258 ILLLLVRYPDVQARLQEEL-------DRVV--GRDRLPCIedqPNLPYVMAFLYEAMRFssFVPVTIPHATTADTS-ILG 327
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 383 VQVPKG-------WSVmysirdTHDTSAvFKDVEAFDPDRFSPER-SEDREGRFHYLPFGGGVRSCLGKQLAT----LFL 450
Cdd:cd20675 328 YHIPKDtvvfvnqWSV------NHDPQK-WPNPEVFDPTRFLDENgFLNKDLASSVMIFSVGKRRCIGEELSKmqlfLFT 400

                ....
gi 47086709 451 KLLA 454
Cdd:cd20675 401 SILA 404
PLN00168 PLN00168
Cytochrome P450; Provisional
19-451 7.42e-07

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 51.87  E-value: 7.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   19 LVSMALLLAVSQQLWQLRWTATRDKScKLPMPKGSMGFPIIGETCHWFFQGAGFHASRRQ---KYGNVFKTHLLGRPLIR 95
Cdd:PLN00168   7 LLLAALLLLPLLLLLLGKHGGRGGKK-GRRLPPGPPAVPLLGSLVWLTNSSADVEPLLRRliaRYGPVVSLRVGSRLSVF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709   96 VTGAENVRKVLMgEHSLVTVDWPQSTST-LLGPNS---LANSIGDIHRK-RRKIFAKVFSHEALESYLPK---IQQVIQE 167
Cdd:PLN00168  86 VADRRLAHAALV-ERGAALADRPAVASSrLLGESDntiTRSSYGPVWRLlRRNLVAETLHPSRVRLFAPArawVRRVLVD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  168 TLRVWSSNPDPINVYRESQRLSFNMAVRVLLGFRIPEEEMHC---------LFSTFQEFVENVFSLPIDLPFSGYRKGIR 238
Cdd:PLN00168 165 KLRREAEDAAAPRVVETFQYAMFCLLVLMCFGERLDEPAVRAiaaaqrdwlLYVSKKMSVFAFFPAVTKHLFRGRLQKAL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  239 ARDSLQKS----IEKAIREKPLH------------TQGKDYTDAL-DVLLEsaKENNTELTMQELKESTIELIFAAFATT 301
Cdd:PLN00168 245 ALRRRQKElfvpLIDARREYKNHlgqggeppkketTFEHSYVDTLlDIRLP--EDGDRALTDDEIVNLCSEFLNAGTDTT 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  302 ASASTSLVMQLLRHPAVLEKLREELRS-CGllhDGclcQGELRLDSIISLKYLDCVIKEVLRLFAPvsgGYRI----ATQ 376
Cdd:PLN00168 323 STALQWIMAELVKNPSIQSKLHDEIKAkTG---DD---QEEVSEEDVHKMPYLKAVVLEGLRKHPP---AHFVlphkAAE 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  377 TFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDRFSPerSEDREG-------RFHYLPFGGGVRSCLGKQLATLF 449
Cdd:PLN00168 394 DMEVGGYLIPKGATVNFMVAEMGRDEREWERPMEFVPERFLA--GGDGEGvdvtgsrEIRMMPFGVGRRICAGLGIAMLH 471

                 ..
gi 47086709  450 LK 451
Cdd:PLN00168 472 LE 473
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
309-448 1.22e-06

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: 50.57  E-value: 1.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 309 VMQLLRHPAvlekLREELRSCGLLHDGclcqgelrldsiislkyldcVIKEVLRLFAPVSGGYRIATQTFELDGVQVPKG 388
Cdd:cd11036 201 VLALLRRPA----QWARLRPDPELAAA--------------------AVAETLRYDPPVRLERRFAAEDLELAGVTLPAG 256
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47086709 389 WSVMYSIrdthdtSAVFKDVEAF-DPDRFSPERsedreGRFHYLPFGGGVRSCLGKQLATL 448
Cdd:cd11036 257 DHVVVLL------AAANRDPEAFpDPDRFDLGR-----PTARSAHFGLGRHACLGAALARA 306
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
309-465 2.72e-06

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 49.78  E-value: 2.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  309 VMQLLRHPAVLEKLREELRS--------CGLLHDGCLCQ------GELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIA 374
Cdd:PLN03195 316 VYMIMMNPHVAEKLYSELKAlekerakeEDPEDSQSFNQrvtqfaGLLTYDSLGKLQYLHAVITETLRLYPAVPQDPKGI 395
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  375 TQTFEL-DGVQVPKGWSVMYSIRDTHDTSAVF-KDVEAFDPDRFSPERSEDREGRFHYLPFGGGVRSCLGKQLATLFLKL 452
Cdd:PLN03195 396 LEDDVLpDGTKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERWIKDGVFQNASPFKFTAFQAGPRICLGKDSAYLQMKM 475
                        170
                 ....*....|...
gi 47086709  453 LAVELAGGSRFEL 465
Cdd:PLN03195 476 ALALLCRFFKFQL 488
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
312-465 1.11e-05

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 48.08  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  312 LLRHPAVLEKLREELRScgllhdgclcqgELRLDSIISLKYLDCVIKEVLRLFAPVSGGYRIATQTFEL-DGVQVPKGWS 390
Cdd:PLN02169 328 LSKHPQVMAKIRHEINT------------KFDNEDLEKLVYLHAALSESMRLYPPLPFNHKAPAKPDVLpSGHKVDAESK 395
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47086709  391 VMYSIRDTHDTSAVF-KDVEAFDPDRFSPERSEDR-EGRFHYLPFGGGVRSCLGKQLATLFLKLLAVELAGGSRFEL 465
Cdd:PLN02169 396 IVICIYALGRMRSVWgEDALDFKPERWISDNGGLRhEPSYKFMAFNSGPRTCLGKHLALLQMKIVALEIIKNYDFKV 472
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
311-446 7.52e-05

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


Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 45.06  E-value: 7.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 311 QLLRHPAVLEKLREELRScgLLH--------DG---CLCQGELRLDSIislkyLDCVIKEVLRLfAPVSGGYRIATQTFE 379
Cdd:cd20631 253 YLLRCPEAMKAATKEVKR--TLEktgqkvsdGGnpiVLTREQLDDMPV-----LGSIIKEALRL-SSASLNIRVAKEDFT 324
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 380 LdgvQVPKGWSvmYSIRDThDTSAVFKDVEAFDP-----------DRFSPERSED--------REGRFHYLPFGGGVRSC 440
Cdd:cd20631 325 L---HLDSGES--YAIRKD-DIIALYPQLLHLDPeiyedpltfkyDRYLDENGKEkttfykngRKLKYYYMPFGSGTSKC 398

                ....*.
gi 47086709 441 LGKQLA 446
Cdd:cd20631 399 PGRFFA 404
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
80-457 9.42e-04

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: 41.54  E-value: 9.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709  80 YGNVFKTHLLGRPLIRVTGAENVRKVL-------MGEHSLVTVDWPQSTSTL-LGPNSlansiGDIHRKRRKIfakvfsh 151
Cdd:cd20676   1 YGDVLQIQIGSRPVVVLSGLDTIRQALvkqgddfKGRPDLYSFRFISDGQSLtFSTDS-----GPVWRARRKL------- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 152 ealesylpkiqqvIQETLRVWSSNPDPINVY---------RESQRL------------SFN----MAVRV-------LLG 199
Cdd:cd20676  69 -------------AQNALKTFSIASSPTSSSsclleehvsKEAEYLvsklqelmaekgSFDpyryIVVSVanvicamCFG 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 200 FRIPE--EEMHCLFSTFQEFVENVFS-LPID-------LPFSGYRKGIRARDSLQKSIEKAIREkplHTQG------KDY 263
Cdd:cd20676 136 KRYSHddQELLSLVNLSDEFGEVAGSgNPADfipilryLPNPAMKRFKDINKRFNSFLQKIVKE---HYQTfdkdniRDI 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 264 TDALDVLLESAK-ENNTELTMQELKESTI--ELIFAAFATTASASTSLVMQLLRHPAVLEKLREEL-RSCGLLHdgclcq 339
Cdd:cd20676 213 TDSLIEHCQDKKlDENANIQLSDEKIVNIvnDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELdEVIGRER------ 286
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 340 gELRLDSIISLKYLDCVIKEVLR--LFAPvsggYRI---ATQTFELDGVQVPKG-------WSVmysirdTHDTSaVFKD 407
Cdd:cd20676 287 -RPRLSDRPQLPYLEAFILETFRhsSFVP----FTIphcTTRDTSLNGYYIPKDtcvfinqWQV------NHDEK-LWKD 354
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 47086709 408 VEAFDPDRF--SPERSEDREGRFHYLPFGGGVRSCLGKQLAT----LFLKLLAVEL 457
Cdd:cd20676 355 PSSFRPERFltADGTEINKTESEKVMLFGLGKRRCIGESIARwevfLFLAILLQQL 410
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
359-474 3.71e-03

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: 39.79  E-value: 3.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086709 359 EVLRLFAPVSGGYRIATQTFELDGVQVPKGWSVMYSIRDTHDTSAVFKDVEAFDPDR-FSPERSedregrfhylpFGGGV 437
Cdd:cd11039 252 EGLRWISPIGMSPRRVAEDFEIRGVTLPAGDRVFLMFGSANRDEARFENPDRFDVFRpKSPHVS-----------FGAGP 320
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 47086709 438 RSCLGKQLATLFLKLLAVELAggsrFelstRTFPRMI 474
Cdd:cd11039 321 HFCAGAWASRQMVGEIALPEL----F----RRLPNLI 349
 
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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