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Conserved domains on  [gi|1063706895|ref|NP_001325389|]
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cytochrome P450, family 76, subfamily C, polypeptide 1 [Arabidopsis thaliana]

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 ...
66-240 3.16e-86

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 cd11073:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 435  Bit Score: 262.47  E-value: 3.16e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  66 SKTYGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLVWLPSSsARWRLLRRLSVTQLLSP 145
Cdd:cd11073     1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPPYG-PRWRMLRKICTTELFSP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 146 QRIEATKALRMNKVKELVSFISESSDREESVDISRVAFITTLNIISNILFSVDLGSYNAKASiNGVQDTVISVMDAAGTP 225
Cdd:cd11073    80 KRLDATQPLRRRKVRELVRYVREKAGSGEAVDIGRAAFLTSLNLISNTLFSVDLVDPDSESG-SEFKELVREIMELAGKP 158
                         170
                  ....*....|....*
gi 1063706895 226 DAANYFPFLRFLDLQ 240
Cdd:cd11073   159 NVADFFPFLKFLDLQ 173
cytochrome_P450 super family cl41757
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
1-117 1.46e-07

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 PLN02196:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 463  Bit Score: 51.47  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895   1 MDIiSGQALLL----LFCFILSCFLIFTTTRSGRISrgataLPPGPPRLPIIG-NIHLVGKHPHRSFAELSKTYGPVMSL 75
Cdd:PLN02196    1 MDF-SALFLTLfagaLFLCLLRFLAGFRRSSSTKLP-----LPPGTMGWPYVGeTFQLYSQDPNVFFASKQKRYGSVFKT 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1063706895  76 KLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQ 117
Cdd:PLN02196   75 HVLGCPCVMISSPEAAKFVLVTKSHLFKPTFPASKERMLGKQ 116
 
Name Accession Description Interval E-value
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
66-240 3.16e-86

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: 262.47  E-value: 3.16e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  66 SKTYGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLVWLPSSsARWRLLRRLSVTQLLSP 145
Cdd:cd11073     1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPPYG-PRWRMLRKICTTELFSP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 146 QRIEATKALRMNKVKELVSFISESSDREESVDISRVAFITTLNIISNILFSVDLGSYNAKASiNGVQDTVISVMDAAGTP 225
Cdd:cd11073    80 KRLDATQPLRRRKVRELVRYVREKAGSGEAVDIGRAAFLTSLNLISNTLFSVDLVDPDSESG-SEFKELVREIMELAGKP 158
                         170
                  ....*....|....*
gi 1063706895 226 DAANYFPFLRFLDLQ 240
Cdd:cd11073   159 NVADFFPFLKFLDLQ 173
PLN02687 PLN02687
flavonoid 3'-monooxygenase
11-240 8.73e-38

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 138.02  E-value: 8.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  11 LLFCFILSCFLifttTRSGRISRGATALPPGPPRLPIIGNIHLVGKHPHRSFAELSKTYGPVMSLKLGSLNTVVIASPEA 90
Cdd:PLN02687   12 VAVSVLVWCLL----LRRGGSGKHKRPLPPGPRGWPVLGNLPQLGPKPHHTMAALAKTYGPLFRLRFGFVDVVVAASASV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  91 AREVLRTHDQILSARSPTNAVRSI--NHQDasLVWLPSSSaRWRLLRRLSVTQLLSPQRIEATKALRMNKVKELVSFISE 168
Cdd:PLN02687   88 AAQFLRTHDANFSNRPPNSGAEHMayNYQD--LVFAPYGP-RWRALRKICAVHLFSAKALDDFRHVREEEVALLVRELAR 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063706895 169 sSDREESVDISRVAFITTLNIISNI-----LFSVDlGSYNAKAsingVQDTVISVMDAAGTPDAANYFPFLRFLDLQ 240
Cdd:PLN02687  165 -QHGTAPVNLGQLVNVCTTNALGRAmvgrrVFAGD-GDEKARE----FKEMVVELMQLAGVFNVGDFVPALRWLDLQ 235
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
39-237 7.78e-32

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: 120.85  E-value: 7.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  39 PPGPPRLPIIGNIHLVG--KHPHRSFAELSKTYGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSAR--SPTNAVRSI 114
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGrkGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRpdEPWFATSRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 115 NHQDASLVwlPSSSARWRLLRRLSVTQLLSPqrieatKALRMNKV-----KELVSFISESSDREESVDISRVAFITTLNI 189
Cdd:pfam00067  81 PFLGKGIV--FANGPRWRQLRRFLTPTFTSF------GKLSFEPRveeeaRDLVEKLRKTAGEPGVIDITDLLFRAALNV 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063706895 190 ISNILFSVDLGSYN---AKASINGVQDtvISVMDAAGTPDAANYFPFLRFL 237
Cdd:pfam00067 153 ICSILFGERFGSLEdpkFLELVKAVQE--LSSLLSSPSPQLLDLFPILKYF 201
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
56-150 2.63e-08

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: 53.74  E-value: 2.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  56 KHPHRSFAELSKtYGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLVWL-PsssARWRLL 134
Cdd:COG2124    19 RDPYPFYARLRE-YGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVLRPLPLLGDSLLTLdG---PEHTRL 94
                          90
                  ....*....|....*.
gi 1063706895 135 RRLsVTQLLSPQRIEA 150
Cdd:COG2124    95 RRL-VQPAFTPRRVAA 109
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
1-117 1.46e-07

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 51.47  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895   1 MDIiSGQALLL----LFCFILSCFLIFTTTRSGRISrgataLPPGPPRLPIIG-NIHLVGKHPHRSFAELSKTYGPVMSL 75
Cdd:PLN02196    1 MDF-SALFLTLfagaLFLCLLRFLAGFRRSSSTKLP-----LPPGTMGWPYVGeTFQLYSQDPNVFFASKQKRYGSVFKT 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1063706895  76 KLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQ 117
Cdd:PLN02196   75 HVLGCPCVMISSPEAAKFVLVTKSHLFKPTFPASKERMLGKQ 116
 
Name Accession Description Interval E-value
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
66-240 3.16e-86

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: 262.47  E-value: 3.16e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  66 SKTYGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLVWLPSSsARWRLLRRLSVTQLLSP 145
Cdd:cd11073     1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPPYG-PRWRMLRKICTTELFSP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 146 QRIEATKALRMNKVKELVSFISESSDREESVDISRVAFITTLNIISNILFSVDLGSYNAKASiNGVQDTVISVMDAAGTP 225
Cdd:cd11073    80 KRLDATQPLRRRKVRELVRYVREKAGSGEAVDIGRAAFLTSLNLISNTLFSVDLVDPDSESG-SEFKELVREIMELAGKP 158
                         170
                  ....*....|....*
gi 1063706895 226 DAANYFPFLRFLDLQ 240
Cdd:cd11073   159 NVADFFPFLKFLDLQ 173
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
70-240 7.34e-45

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: 155.40  E-value: 7.34e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  70 GPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLVWLPsSSARWRLLRRLSVTQLLSPQRIE 149
Cdd:cd20618     1 GPLMYLRLGSVPTVVVSSPEMAKEVLKTQDAVFASRPRTAAGKIFSYNGQDIVFAP-YGPHWRHLRKICTLELFSAKRLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 150 ATKALRMNKVKELVSFISESSDREESVDISRVAFITTLNIISNILFSVDLGSYNAKASINGV--QDTVISVMDAAGTPDA 227
Cdd:cd20618    80 SFQGVRKEELSHLVKSLLEESESGKPVNLREHLSDLTLNNITRMLFGKRYFGESEKESEEARefKELIDEAFELAGAFNI 159
                         170
                  ....*....|...
gi 1063706895 228 ANYFPFLRFLDLQ 240
Cdd:cd20618   160 GDYIPWLRWLDLQ 172
PLN02687 PLN02687
flavonoid 3'-monooxygenase
11-240 8.73e-38

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 138.02  E-value: 8.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  11 LLFCFILSCFLifttTRSGRISRGATALPPGPPRLPIIGNIHLVGKHPHRSFAELSKTYGPVMSLKLGSLNTVVIASPEA 90
Cdd:PLN02687   12 VAVSVLVWCLL----LRRGGSGKHKRPLPPGPRGWPVLGNLPQLGPKPHHTMAALAKTYGPLFRLRFGFVDVVVAASASV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  91 AREVLRTHDQILSARSPTNAVRSI--NHQDasLVWLPSSSaRWRLLRRLSVTQLLSPQRIEATKALRMNKVKELVSFISE 168
Cdd:PLN02687   88 AAQFLRTHDANFSNRPPNSGAEHMayNYQD--LVFAPYGP-RWRALRKICAVHLFSAKALDDFRHVREEEVALLVRELAR 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063706895 169 sSDREESVDISRVAFITTLNIISNI-----LFSVDlGSYNAKAsingVQDTVISVMDAAGTPDAANYFPFLRFLDLQ 240
Cdd:PLN02687  165 -QHGTAPVNLGQLVNVCTTNALGRAmvgrrVFAGD-GDEKARE----FKEMVVELMQLAGVFNVGDFVPALRWLDLQ 235
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
68-240 3.43e-35

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: 129.50  E-value: 3.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  68 TYGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSI--NHQDasLVWLPsSSARWRLLRRLSVTQLLSP 145
Cdd:cd11072     1 KYGPLMLLRLGSVPTVVVSSPEAAKEVLKTHDLVFASRPKLLAARILsyGGKD--IAFAP-YGEYWRQMRKICVLELLSA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 146 QRIEATKALRMNKVKELVSFISESSDREESVDISRVAFITTLNIISNILFSVDLGSYNAkasiNGVQDTVISVMDAAGTP 225
Cdd:cd11072    78 KRVQSFRSIREEEVSLLVKKIRESASSSSPVNLSELLFSLTNDIVCRAAFGRKYEGKDQ----DKFKELVKEALELLGGF 153
                         170
                  ....*....|....*
gi 1063706895 226 DAANYFPFLRFLDLQ 240
Cdd:cd11072   154 SVGDYFPSLGWIDLL 168
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
31-240 3.79e-34

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 128.05  E-value: 3.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  31 ISRGATALPPGPPRLPIIGNIHLVGKHPHRSFAELSKTYGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNA 110
Cdd:PLN00110   25 LPKPSRKLPPGPRGWPLLGALPLLGNMPHVALAKMAKRYGPVMFLKMGTNSMVVASTPEAARAFLKTLDINFSNRPPNAG 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 111 VRSINHQDASLVWlPSSSARWRLLRRLSVTQLLSPQRIEATKALRMNKVKELVSFISESSDREESVDISRVAFITTLNII 190
Cdd:PLN00110  105 ATHLAYGAQDMVF-ADYGPRWKLLRKLSNLHMLGGKALEDWSQVRTVELGHMLRAMLELSQRGEPVVVPEMLTFSMANMI 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063706895 191 SNILFSVDLgsYNAKAS-INGVQDTVISVMDAAGTPDAANYFPFLRFLDLQ 240
Cdd:PLN00110  184 GQVILSRRV--FETKGSeSNEFKDMVVELMTTAGYFNIGDFIPSIAWMDIQ 232
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
39-237 7.78e-32

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: 120.85  E-value: 7.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  39 PPGPPRLPIIGNIHLVG--KHPHRSFAELSKTYGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSAR--SPTNAVRSI 114
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGrkGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRpdEPWFATSRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 115 NHQDASLVwlPSSSARWRLLRRLSVTQLLSPqrieatKALRMNKV-----KELVSFISESSDREESVDISRVAFITTLNI 189
Cdd:pfam00067  81 PFLGKGIV--FANGPRWRQLRRFLTPTFTSF------GKLSFEPRveeeaRDLVEKLRKTAGEPGVIDITDLLFRAALNV 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063706895 190 ISNILFSVDLGSYN---AKASINGVQDtvISVMDAAGTPDAANYFPFLRFL 237
Cdd:pfam00067 153 ICSILFGERFGSLEdpkFLELVKAVQE--LSSLLSSPSPQLLDLFPILKYF 201
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
10-240 8.08e-32

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 121.47  E-value: 8.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  10 LLLFCFILSCFLIFTTTRSGRISRgatALPPGPPRLPIIGNIHLVGKHPHRSFAELSKTYGPVMSLKLGSLNTVVIASPE 89
Cdd:PLN03112    8 LLFSVLIFNVLIWRWLNASMRKSL---RLPPGPPRWPIVGNLLQLGPLPHRDLASLCKKYGPLVYLRLGSVDAITTDDPE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  90 AAREVLRTHDQILSARSPTNAVRSINHqDASLVWLPSSSARWRLLRRLSVTQLLSPQRIEATKALRMNKVKELVSFISES 169
Cdd:PLN03112   85 LIREILLRQDDVFASRPRTLAAVHLAY-GCGDVALAPLGPHWKRMRRICMEHLLTTKRLESFAKHRAEEARHLIQDVWEA 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063706895 170 SDREESVDISRVAFITTLNIISNILfsvdLGSYNAKASINGVQDT------VISVMDAAGTPDAANYFPFLRFLDLQ 240
Cdd:PLN03112  164 AQTGKPVNLREVLGAFSMNNVTRML----LGKQYFGAESAGPKEAmefmhiTHELFRLLGVIYLGDYLPAWRWLDPY 236
PLN02183 PLN02183
ferulate 5-hydroxylase
3-241 1.14e-27

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 109.94  E-value: 1.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895   3 IISGQALLLLFCFILSCFLIFTTTRsgRISRgATALPPGPPRLPIIGNIHLVGKHPHRSFAELSKTYGPVMSLKLGSLNT 82
Cdd:PLN02183    5 LQSLLTSPSFFLILISLFLFLGLIS--RLRR-RLPYPPGPKGLPIIGNMLMMDQLTHRGLANLAKQYGGLFHMRMGYLHM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  83 VVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLVWlPSSSARWRLLRRLSVTQLLSPQRIEATKALRmNKVKEL 162
Cdd:PLN02183   82 VAVSSPEVARQVLQVQDSVFSNRPANIAISYLTYDRADMAF-AHYGPFWRQMRKLCVMKLFSRKRAESWASVR-DEVDSM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 163 VSFISESSDreESVDISRVAFITTLNIISNILFSvdlgsynakASINGVQDTVISVMDA----AGTPDAANYFPFLRFLD 238
Cdd:PLN02183  160 VRSVSSNIG--KPVNIGELIFTLTRNITYRAAFG---------SSSNEGQDEFIKILQEfsklFGAFNVADFIPWLGWID 228

                  ...
gi 1063706895 239 LQE 241
Cdd:PLN02183  229 PQG 231
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
70-240 3.34e-27

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: 107.89  E-value: 3.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  70 GPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSI--NHQDasLVWLPSSsARWRLLRRLSVTQLLSPQR 147
Cdd:cd20657     1 GPIMYLKVGSCGVVVASSPPVAKAFLKTHDANFSNRPPNAGATHMayNAQD--MVFAPYG-PRWRLLRKLCNLHLFGGKA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 148 IEATKALRMNKVKELVSFISESSDREESVDISRVAFITTLNIISNILFSVDLGSYNAKASINGVQDTVISVMDAAGTPDA 227
Cdd:cd20657    78 LEDWAHVRENEVGHMLKSMAEASRKGEPVVLGEMLNVCMANMLGRVMLSKRVFAAKAGAKANEFKEMVVELMTVAGVFNI 157
                         170
                  ....*....|...
gi 1063706895 228 ANYFPFLRFLDLQ 240
Cdd:cd20657   158 GDFIPSLAWMDLQ 170
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
3-238 3.34e-25

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 103.23  E-value: 3.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895   3 IISGQALLLLFCFILScflifTTTRSGRisrgataLPPGPPRLPIIGNIHLVGK-HPHRSFAELSKTYGPVMSLKLGSLN 81
Cdd:PLN03234    6 IIAALVAAAAFFFLRS-----TTKKSLR-------LPPGPKGLPIIGNLHQMEKfNPQHFLFRLSKLYGPIFTMKIGGRR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  82 TVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLvWLPSSSARWRLLRRLSVTQLLSPQRIEATKALRMNKVKE 161
Cdd:PLN03234   74 LAVISSAELAKELLKTQDLNFTARPLLKGQQTMSYQGREL-GFGQYTAYYREMRKMCMVNLFSPNRVASFRPVREEECQR 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063706895 162 LVSFISESSDREESVDISRVAFITTLNIISNILFSVDLGSYNAKasINGVQDTVISVMDAAGTPDAANYFPFLRFLD 238
Cdd:PLN03234  153 MMDKIYKAADQSGTVDLSELLLSFTNCVVCRQAFGKRYNEYGTE--MKRFIDILYETQALLGTLFFSDLFPYFGFLD 227
PLN02966 PLN02966
cytochrome P450 83A1
17-238 7.02e-24

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 99.44  E-value: 7.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  17 LSCFLIFTTTRSGRISRgaTALPPGPPRLPIIGNIHLVGK-HPHRSFAELSKTYGPVMSLKLGSLNTVVIASPEAAREVL 95
Cdd:PLN02966   11 LAAVLLFFLYQKPKTKR--YKLPPGPSPLPVIGNLLQLQKlNPQRFFAGWAKKYGPILSYRIGSRTMVVISSAELAKELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  96 RTHDQILSARSPTNAVRSINHQDASLVwLPSSSARWRLLRRLSVTQLLSPQRIEATKALRMNKVKELVSFISESSDREES 175
Cdd:PLN02966   89 KTQDVNFADRPPHRGHEFISYGRRDMA-LNHYTPYYREIRKMGMNHLFSPTRVATFKHVREEEARRMMDKINKAADKSEV 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063706895 176 VDISRVAFITTLNIISNILFSvdlGSYNAKA-SINGVQDTVISVMDAAGTPDAANYFPFLRFLD 238
Cdd:PLN02966  168 VDISELMLTFTNSVVCRQAFG---KKYNEDGeEMKRFIKILYGTQSVLGKIFFSDFFPYCGFLD 228
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
70-240 4.88e-23

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: 4.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  70 GPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLVWLPsSSARWRLLRRLSVTQLLSPQRIE 149
Cdd:cd20654     1 GPIFTLRLGSHPTLVVSSWEMAKECFTTNDKAFSSRPKTAAAKLMGYNYAMFGFAP-YGPYWRELRKIATLELLSNRRLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 150 ATKALRM----NKVKELVSFISESSDREES--VDISRVAFITTLNIISNILFSVDLGSYNAKASINGVQ---DTVISVMD 220
Cdd:cd20654    80 KLKHVRVsevdTSIKELYSLWSNNKKGGGGvlVEMKQWFADLTFNVILRMVVGKRYFGGTAVEDDEEAErykKAIREFMR 159
                         170       180
                  ....*....|....*....|
gi 1063706895 221 AAGTPDAANYFPFLRFLDLQ 240
Cdd:cd20654   160 LAGTFVVSDAIPFLGWLDFG 179
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
70-240 5.84e-23

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: 96.13  E-value: 5.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  70 GPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLVWLPSSSaRWRLLRRLSVTQLLSPQRIE 149
Cdd:cd20655     1 GPLLHLRIGSVPCVVVSSASVAKEILKTHDLNFSSRPVPAAAESLLYGSSGFAFAPYGD-YWKFMKKLCMTELLGPRALE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 150 ATKALRMNKVKELVSFISESSDREESVDISRVAFITTLNIISNILFSVDLGSYNAKASinGVQDTVISVMDAAGTPDAAN 229
Cdd:cd20655    80 RFRPIRAQELERFLRRLLDKAEKGESVDIGKELMKLTNNIICRMIMGRSCSEENGEAE--EVRKLVKESAELAGKFNASD 157
                         170
                  ....*....|.
gi 1063706895 230 YFPFLRFLDLQ 240
Cdd:cd20655   158 FIWPLKKLDLQ 168
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
70-240 4.98e-20

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: 87.66  E-value: 4.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  70 GPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLVWLPsSSARWRLLRRLSVTQLLSPQRIE 149
Cdd:cd20653     1 GPIFSLRFGSRLVVVVSSPSAAEECFTKNDIVLANRPRFLTGKHIGYNYTTVGSAP-YGDHWRNLRRITTLEIFSSHRLN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 150 ATKALRMNKVKELVSFISESSDRE-ESVDISRVAFITTLNIISNIL----FSVDLGSYNAKASIngVQDTVISVMDAAGT 224
Cdd:cd20653    80 SFSSIRRDEIRRLLKRLARDSKGGfAKVELKPLFSELTFNNIMRMVagkrYYGEDVSDAEEAKL--FRELVSEIFELSGA 157
                         170
                  ....*....|....*.
gi 1063706895 225 PDAANYFPFLRFLDLQ 240
Cdd:cd20653   158 GNPADFLPILRWFDFQ 173
PLN02655 PLN02655
ent-kaurene oxidase
40-237 2.66e-19

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 85.95  E-value: 2.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  40 PGPPRLPIIGNIH-LVGKHPHRSFAELSKTYGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHqD 118
Cdd:PLN02655    2 PAVPGLPVIGNLLqLKEKKPHRTFTKWSEIYGPIYTIRTGASSVVVLNSTEVAKEAMVTKFSSISTRKLSKALTVLTR-D 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 119 ASLVWLPSSSARWRLLRRLSVTQLLSPQRIEATKALRMNKVKELVS-FISESSDREESVDISRVAFITTL---------- 187
Cdd:PLN02655   81 KSMVATSDYGDFHKMVKRYVMNNLLGANAQKRFRDTRDMLIENMLSgLHALVKDDPHSPVNFRDVFENELfglsliqalg 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063706895 188 NIISNIlFSVDLGSYNAKASINGVqdTVISVMDAAGTPDAANYFPFLRFL 237
Cdd:PLN02655  161 EDVESV-YVEELGTEISKEEIFDV--LVHDMMMCAIEVDWRDFFPYLSWI 207
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
70-237 1.27e-18

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: 83.80  E-value: 1.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  70 GPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINhQDASLVWlpSSSARWRLLRRLSVTQLLSPQRIE 149
Cdd:cd20617     1 GGIFTLWLGDVPTVVLSDPEIIKEAFVKNGDNFSDRPLLPSFEIIS-GGKGILF--SNGDYWKELRRFALSSLTKTKLKK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 150 ATKALRMNKVKELVSFISESSDREESVDISRVAFITTLNIISNILFSVDLGSYNaKASINGVQDTVISVMDAAGTPDAAN 229
Cdd:cd20617    78 KMEELIEEEVNKLIESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGKRFPDED-DGEFLKLVKPIEEIFKELGSGNPSD 156

                  ....*...
gi 1063706895 230 YFPFLRFL 237
Cdd:cd20617   157 FIPILLPF 164
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
10-137 1.39e-17

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 81.32  E-value: 1.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  10 LLLFCFILSCFLIFTTTRSGRisrgATALPPGPPRLPIIGNIHLVGKH-PHRSFAELSKTYGPVMSLKLGSLNTVVIASP 88
Cdd:PLN02394    7 TLLGLFVAIVLALLVSKLRGK----KLKLPPGPAAVPIFGNWLQVGDDlNHRNLAEMAKKYGDVFLLRMGQRNLVVVSSP 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063706895  89 EAAREVLRTHDQILSARsPTNAVRSI---NHQDasLVWlPSSSARWRLLRRL 137
Cdd:PLN02394   83 ELAKEVLHTQGVEFGSR-TRNVVFDIftgKGQD--MVF-TVYGDHWRKMRRI 130
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
69-237 9.13e-17

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: 78.68  E-value: 9.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  69 YGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLVWlPSSSARWRLLRRLSVTQLLSPQRI 148
Cdd:cd20656     1 YGPIISVWIGSTLNVVVSSSELAKEVLKEKDQQLADRHRTRSAARFSRNGQDLIW-ADYGPHYVKVRKLCTLELFTPKRL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 149 EATKALRMNKVKELVSFI----SESSDREESVDISRVAFITTLNIISNILFSVDLGSYNAKASINGVQ--DTVISVMDAA 222
Cdd:cd20656    80 ESLRPIREDEVTAMVESIfndcMSPENEGKPVVLRKYLSAVAFNNITRLAFGKRFVNAEGVMDEQGVEfkAIVSNGLKLG 159
                         170
                  ....*....|....*
gi 1063706895 223 GTPDAANYFPFLRFL 237
Cdd:cd20656   160 ASLTMAEHIPWLRWM 174
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
68-235 1.12e-15

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: 75.36  E-value: 1.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  68 TYGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLVwlpSSSA---RWRLLRRLSVTQLLS 144
Cdd:cd11075     1 KYGPIFTLRMGSRPLIVVASRELAHEALVQKGSSFASRPPANPLRVLFSSNKHMV---NSSPygpLWRTLRRNLVSEVLS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 145 PQRIEATKALRMNKVKELVSFISESSDREESVdisrvafITTLNIISNILFSVDL----GSYNAKASINGVQDTVISVMD 220
Cdd:cd11075    78 PSRLKQFRPARRRALDNLVERLREEAKENPGP-------VNVRDHFRHALFSLLLymcfGERLDEETVRELERVQRELLL 150
                         170
                  ....*....|....*
gi 1063706895 221 AAGTPDAANYFPFLR 235
Cdd:cd11075   151 SFTDFDVRDFFPALT 165
PLN00168 PLN00168
Cytochrome P450; Provisional
7-163 9.02e-15

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 73.06  E-value: 9.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895   7 QALLLLFCFILSCFLIFTTTRSGRISRGATALPPGPPRLPIIGNIHLVGKHP---HRSFAELSKTYGPVMSLKLGSLNTV 83
Cdd:PLN00168    5 QLLLLAALLLLPLLLLLLGKHGGRGGKKGRRLPPGPPAVPLLGSLVWLTNSSadvEPLLRRLIARYGPVVSLRVGSRLSV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  84 VIASPEAAREVLRTHDQILSARsPTNAVRSINHQDASLVWLPSSSARWRLLRRLSVTQLLSPQRIEATKALRMNKVKELV 163
Cdd:PLN00168   85 FVADRRLAHAALVERGAALADR-PAVASSRLLGESDNTITRSSYGPVWRLLRRNLVAETLHPSRVRLFAPARAWVRRVLV 163
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
76-240 2.17e-13

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: 68.93  E-value: 2.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  76 KLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLVWLPsSSARWRLLRRLSVTQLLSPQRIEATKALR 155
Cdd:cd20658     7 RLGNTHVIPVTCPKIAREILRKQDAVFASRPLTYATEIISGGYKTTVISP-YGEQWKKMRKVLTTELMSPKRHQWLHGKR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 156 MNKVKELVSFI---SESSDREESVDISRVAFITTLNIISNILFSVdlgSYNAKASING------VQ--DTVISVMDAAGT 224
Cdd:cd20658    86 TEEADNLVAYVynmCKKSNGGGLVNVRDAARHYCGNVIRKLMFGT---RYFGKGMEDGgpgleeVEhmDAIFTALKCLYA 162
                         170
                  ....*....|....*.
gi 1063706895 225 PDAANYFPFLRFLDLQ 240
Cdd:cd20658   163 FSISDYLPFLRGLDLD 178
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
69-237 6.15e-13

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: 67.22  E-value: 6.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  69 YGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLVWLPsSSARWRLLRRLsVTQLLSPQRI 148
Cdd:cd11065     1 YGPIISLKVGGQTIIVLNSPKAAKDLLEKRSAIYSSRPRMPMAGELMGWGMRLLLMP-YGPRWRLHRRL-FHQLLNPSAV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 149 EATKALRMNKVKELVSFISESSDREESVdISRVAFittlNIISNILFSVDLGSYNAKASIngVQDTVISVMDAAGTPDAA 228
Cdd:cd11065    79 RKYRPLQELESKQLLRDLLESPDDFLDH-IRRYAA----SIILRLAYGYRVPSYDDPLLR--DAEEAMEGFSEAGSPGAY 151
                         170
                  ....*....|.
gi 1063706895 229 --NYFPFLRFL 237
Cdd:cd11065   152 lvDFFPFLRYL 162
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
71-240 2.00e-12

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: 65.81  E-value: 2.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  71 PVMSLKLGSLNTVVIASPEAAREVLRthdqilsarSPTNAVRSINHQDASLVW-----LPSSSARWRLLRRLSVTQLLSP 145
Cdd:cd11076     4 RLMAFSLGETRVVITSHPETAREILN---------SPAFADRPVKESAYELMFnraigFAPYGEYWRNLRRIASNHLFSP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 146 QRIEATKALRMNKVKELVSFISESSDREESVDISRVAFITTLNiisNILFSV-----DLGSYNAKAsiNGVQDTVISVMD 220
Cdd:cd11076    75 RRIAASEPQRQAIAAQMVKAIAKEMERSGEVAVRKHLQRASLN---NIMGSVfgrryDFEAGNEEA--EELGEMVREGYE 149
                         170       180
                  ....*....|....*....|
gi 1063706895 221 AAGTPDAANYFPFLRFLDLQ 240
Cdd:cd11076   150 LLGAFNWSDHLPWLRWLDLQ 169
PLN03018 PLN03018
homomethionine N-hydroxylase
7-195 3.96e-12

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 65.03  E-value: 3.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895   7 QALLLLFCFILSCFLIFTT-TRSGRISRGATALPPGPPRLPIIGNI-HLVGKHPHRSFAELS----KTygPVMSLKLGSL 80
Cdd:PLN03018    9 QILLGFIVFIASITLLGRIlSRPSKTKDRSRQLPPGPPGWPILGNLpELIMTRPRSKYFHLAmkelKT--DIACFNFAGT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  81 NTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLVWLPSSSaRWRLLRRLSVTQLLSPQRIEATKALRMNKVK 160
Cdd:PLN03018   87 HTITINSDEIAREAFRERDADLADRPQLSIMETIGDNYKSMGTSPYGE-QFMKMKKVITTEIMSVKTLNMLEAARTIEAD 165
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063706895 161 ELVSFISESSDREESVDISRVAFITTLNIISNILF 195
Cdd:PLN03018  166 NLIAYIHSMYQRSETVDVRELSRVYGYAVTMRMLF 200
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
69-237 4.93e-12

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: 64.54  E-value: 4.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  69 YGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSAR--SPTNAVRSINHQDASlvwLPSSSARWRLLRRLsvtqllspq 146
Cdd:cd11027     1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKKSADFAGRpkLFTFDLFSRGGKDIA---FGDYSPTWKLHRKL--------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 147 rieATKALRMNK-------------VKELVSFISESSDReeSVDISRVAFITTLNIISNILF----SVDLGSYNA--KAS 207
Cdd:cd11027    69 ---AHSALRLYAsggprleekiaeeAEKLLKRLASQEGQ--PFDPKDELFLAVLNVICSITFgkryKLDDPEFLRllDLN 143
                         170       180       190
                  ....*....|....*....|....*....|
gi 1063706895 208 INGVQDTVISvmdaagtpDAANYFPFLRFL 237
Cdd:cd11027   144 DKFFELLGAG--------SLLDIFPFLKYF 165
PTZ00404 PTZ00404
cytochrome P450; Provisional
40-240 2.25e-10

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 59.74  E-value: 2.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  40 PGPPRLPIIGNIHLVGKHPHRSFAELSKTYGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSAR--SPTNAVRSINHQ 117
Cdd:PTZ00404   32 KGPIPIPILGNLHQLGNLPHRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRpkIPSIKHGTFYHG 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 118 DASlvwlpSSSARWRLLRRLsVTQLLSPQRIEATKALRMNKVKELVSFISESSDREESVDISRVAFITTLNIISNILFSV 197
Cdd:PTZ00404  112 IVT-----SSGEYWKRNREI-VGKAMRKTNLKHIYDLLDDQVDVLIESMKKIESSGETFEPRYYLTKFTMSAMFKYIFNE 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1063706895 198 DLGSYN--AKASINGVQDTVISVMDAAGTPDAANYFPFLRFLDLQ 240
Cdd:PTZ00404  186 DISFDEdiHNGKLAELMGPMEQVFKDLGSGSLFDVIEITQPLYYQ 230
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
69-201 2.68e-10

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: 59.50  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  69 YGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARsPTNAVRSINHQDASLVWlpSSSARWRLLRRLSVTQL----LS 144
Cdd:cd11026     1 YGPVFTVYLGSKPVVVLCGYEAVKEALVDQAEEFSGR-PPVPLFDRVTKGYGVVF--SNGERWKQLRRFSLTTLrnfgMG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063706895 145 PQRIEatkalrmNKVKELVSFISESSDREESVDISRVAFITtlNIISNILFSVDLGS 201
Cdd:cd11026    78 KRSIE-------ERIQEEAKFLVEAFRKTKGKPFDPTFLLS--NAVSNVICSIVFGS 125
PLN02971 PLN02971
tryptophan N-hydroxylase
7-239 2.34e-09

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 56.97  E-value: 2.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895   7 QALLLLfCFILSCFLIFTTTRSGRISrgatALPPGPPRLPIIGNI-HLVGKHP-----HRSFAELSKTygpVMSLKLGSL 80
Cdd:PLN02971   32 QALVAI-TLLMILKKLKSSSRNKKLH----PLPPGPTGFPIVGMIpAMLKNRPvfrwlHSLMKELNTE---IACVRLGNT 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  81 NTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLVWLPSSSaRWRLLRRLSVTQLLSPQRIEATKALRMNKVK 160
Cdd:PLN02971  104 HVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGE-QFKKMRKVIMTEIVCPARHRWLHDNRAEETD 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 161 ELVSFISESSDREESVDISRVAFITTLNIISNILFSVDLGSYNAKASiNGVQDTVISVMDAA----GTPDA---ANYFPF 233
Cdd:PLN02971  183 HLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEPD-GGPTLEDIEHMDAMfeglGFTFAfciSDYLPM 261

                  ....*.
gi 1063706895 234 LRFLDL 239
Cdd:PLN02971  262 LTGLDL 267
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
69-237 1.60e-08

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: 54.25  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  69 YGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARsPTNAVRSINHQDASLVWLPSSSARWRLLRRLSVTQL------ 142
Cdd:cd20673     1 YGPIYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGR-PRMVTTDLLSRNGKDIAFADYSATWQLHRKLVHSAFalfgeg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 143 -LSPQRIEATKAlrmnkvKELVSFISESsdREESVDISRVAFITTLNIISNILFSVdlgSY-NAKASINGVQDTVISVMD 220
Cdd:cd20673    80 sQKLEKIICQEA------SSLCDTLATH--NGESIDLSPPLFRAVTNVICLLCFNS---SYkNGDPELETILNYNEGIVD 148
                         170
                  ....*....|....*..
gi 1063706895 221 AAGTPDAANYFPFLRFL 237
Cdd:cd20673   149 TVAKDSLVDIFPWLQIF 165
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
70-200 1.96e-08

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: 54.06  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  70 GPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLVwlpSSSARWRLLRRLsVTQLLSPQRIE 149
Cdd:cd00302     1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLT---LDGPEHRRLRRL-LAPAFTPRALA 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063706895 150 ATKALRMNKVKELVSFISESSDreESVDISRVAFITTLNIISNILFSVDLG 200
Cdd:cd00302    77 ALRPVIREIARELLDRLAAGGE--VGDDVADLAQPLALDVIARLLGGPDLG 125
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
56-150 2.63e-08

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: 53.74  E-value: 2.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  56 KHPHRSFAELSKtYGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLVWL-PsssARWRLL 134
Cdd:COG2124    19 RDPYPFYARLRE-YGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVLRPLPLLGDSLLTLdG---PEHTRL 94
                          90
                  ....*....|....*.
gi 1063706895 135 RRLsVTQLLSPQRIEA 150
Cdd:COG2124    95 RRL-VQPAFTPRRVAA 109
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
1-117 1.46e-07

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 51.47  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895   1 MDIiSGQALLL----LFCFILSCFLIFTTTRSGRISrgataLPPGPPRLPIIG-NIHLVGKHPHRSFAELSKTYGPVMSL 75
Cdd:PLN02196    1 MDF-SALFLTLfagaLFLCLLRFLAGFRRSSSTKLP-----LPPGTMGWPYVGeTFQLYSQDPNVFFASKQKRYGSVFKT 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1063706895  76 KLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQ 117
Cdd:PLN02196   75 HVLGCPCVMISSPEAAKFVLVTKSHLFKPTFPASKERMLGKQ 116
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
69-171 1.13e-06

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: 48.64  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  69 YGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLVwlpSSSARWRLLRRLSVTQLlspQRI 148
Cdd:cd20671     1 YGPVFTIHLGMQKTVVLTGYEAVKEALVGTGDEFADRPPIPIFQAIQHGNGVFF---SSGERWRTTRRFTVRSM---KSL 74
                          90       100
                  ....*....|....*....|...
gi 1063706895 149 EATKALRMNKVKELVSFISESSD 171
Cdd:cd20671    75 GMGKRTIEDKILEELQFLNGQID 97
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
69-236 2.40e-06

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: 47.88  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  69 YGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINHQDASLVwlpSSSARWRLLRRLSVTQL----LS 144
Cdd:cd20664     1 YGSIFTVQMGTKKVVVLAGYKTVKEALVNHAEAFGGRPIIPIFEDFNKGYGILF---SNGENWKEMRRFTLTTLrdfgMG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 145 PQRIEatkalrmNKVKELVSFISE--SSDREESVDISRVAFITTLNIISNILFSVDLGSYNAKasINGVQDTVISVMDAA 222
Cdd:cd20664    78 KKTSE-------DKILEEIPYLIEvfEKHKGKPFETTLSMNVAVSNIIASIVLGHRFEYTDPT--LLRMVDRINENMKLT 148
                         170
                  ....*....|....*.
gi 1063706895 223 GTPDAA--NYFPFLRF 236
Cdd:cd20664   149 GSPSVQlyNMFPWLGP 164
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
70-237 2.69e-06

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: 47.79  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  70 GPVMSLKLGSLNTVVIASPEAAREVLRThdQILSARSPTNAVRSINHQDASLVwlpSSSARWRLLRRLSVTQL------- 142
Cdd:cd20652     1 GSIFSLKMGSVYTVVLSDPKLIRDTFRR--DEFTGRAPLYLTHGIMGGNGIIC---AEGDLWRDQRRFVHDWLrqfgmtk 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 143 LSPQRiEATKALRMNKVKELVSFISESSDREesVDISRVAFITTLNIISNILFSVdlgSYNAKAS----INGVQDTVISV 218
Cdd:cd20652    76 FGNGR-AKMEKRIATGVHELIKHLKAESGQP--VDPSPVLMHSLGNVINDLVFGF---RYKEDDPtwrwLRFLQEEGTKL 149
                         170
                  ....*....|....*....
gi 1063706895 219 MDAAGTpdaANYFPFLRFL 237
Cdd:cd20652   150 IGVAGP---VNFLPFLRHL 165
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
67-232 3.11e-06

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: 47.52  E-value: 3.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  67 KTYGPVMSLKLGSLNTVVIASPEAAREVLRtHDQILSARSPTNAV---RSINHQDASLvwLPSSSARWRLLRRLSVTQLL 143
Cdd:cd11054     2 KKYGPIVREKLGGRDIVHLFDPDDIEKVFR-NEGKYPIRPSLEPLekyRKKRGKPLGL--LNSNGEEWHRLRSAVQKPLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 144 SPQrieATKAL--RMNKV-KELVSFISESSDR--EESVDISRVAFITTLNIISNILFSVDLGSYN------AKASINGVQ 212
Cdd:cd11054    79 RPK---SVASYlpAINEVaDDFVERIRRLRDEdgEEVPDLEDELYKWSLESIGTVLFGKRLGCLDdnpdsdAQKLIEAVK 155
                         170       180
                  ....*....|....*....|
gi 1063706895 213 DTVISVMDAAGTPDAANYFP 232
Cdd:cd11054   156 DIFESSAKLMFGPPLWKYFP 175
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
69-237 9.29e-06

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: 46.14  E-value: 9.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  69 YGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINhqDASLVWLPSSSARWRLLRRLsvtqllspqri 148
Cdd:cd11028     1 YGDVFQIRMGSRPVVVLNGLETIKQALVRQGEDFAGRPDFYSFQFIS--NGKSMAFSDYGPRWKLHRKL----------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 149 eATKALRM---------------NKVKELVSFISESSDREESVDISRVAFITTLNIISNILFSVDLGSYNAKasingVQD 213
Cdd:cd11028    68 -AQNALRTfsnarthnpleehvtEEAEELVTELTENNGKPGPFDPRNEIYLSVGNVICAICFGKRYSRDDPE-----FLE 141
                         170       180
                  ....*....|....*....|....*..
gi 1063706895 214 TVISV---MDAAGTPDAANYFPFLRFL 237
Cdd:cd11028   142 LVKSNddfGAFVGAGNPVDVMPWLRYL 168
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
67-137 1.03e-05

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: 45.93  E-value: 1.03e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063706895  67 KTYGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARsPTNAVRSI---NHQDASLVwlpSSSARWRLLRRL 137
Cdd:cd11074     1 KKFGDIFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSR-TRNVVFDIftgKGQDMVFT---VYGEHWRKMRRI 70
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
69-200 1.11e-05

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: 45.90  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  69 YGPVMSLKLGSLNTVVIASPEAAREVLRT--HDQILSARSPTNAVRSINHQDASLvwLPSSSARWRLLRRLSVTQLLSPQ 146
Cdd:cd20648     5 YGPVWKASFGPILTVHVADPALIEQVLRQegKHPVRSDLSSWKDYRQLRGHAYGL--LTAEGEEWQRLRSLLAKHMLKPK 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063706895 147 RIEATKALRMNKVKELVSFISESSDREESVDISRVA---FITTLNIISNILFSVDLG 200
Cdd:cd20648    83 AVEAYAGVLNAVVTDLIRRLRRQRSRSSPGVVKDIAgefYKFGLEGISSVLFESRIG 139
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
69-195 1.57e-05

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: 45.30  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  69 YGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAV-RSINHQDASLvwlpSSSARWRLLRRLSVTQL----L 143
Cdd:cd20670     1 YGPVFTVYMGPRPVVVLCGHEAVKEALVDQADEFSGRGELATIeRNFQGHGVAL----ANGERWRILRRFSLTILrnfgM 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063706895 144 SPQRIEatkalrmNKVKELVSFISESSDREESVDISRVAFI--TTLNIISNILF 195
Cdd:cd20670    77 GKRSIE-------ERIQEEAGYLLEEFRKTKGAPIDPTFFLsrTVSNVISSVVF 123
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
70-200 5.82e-05

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: 43.34  E-value: 5.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  70 GPVMSLKLGSLNTVVIASPEAAREVLRTHDQilsarsptNAVRSINHQDASLVW----LPSSSARWRLLRRLsVTQLLSP 145
Cdd:cd20620     1 GDVVRLRLGPRRVYLVTHPDHIQHVLVTNAR--------NYVKGGVYERLKLLLgnglLTSEGDLWRRQRRL-AQPAFHR 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063706895 146 QRIEATKALRMNKVKELVSFISESSDREEsVDISRVAFITTLNIISNILFSVDLG 200
Cdd:cd20620    72 RRIAAYADAMVEATAALLDRWEAGARRGP-VDVHAEMMRLTLRIVAKTLFGTDVE 125
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
68-204 9.66e-05

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: 42.90  E-value: 9.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  68 TYGPVMSLKLGSLNTVVIASPEAAREVLRthdqilsarspTNAVRSINHQDASLVWLPSSSA-------RWRLLRRLsVT 140
Cdd:cd20649     1 KYGPICGYYIGRRMFVVIAEPDMIKQVLV-----------KDFNNFTNRMKANLITKPMSDSllclrdeRWKRVRSI-LT 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063706895 141 QLLSPQRIEATKALRMNKVKELVSFISESSDREESVDISRVAFITTLNIISNILFSVDLGSYNA 204
Cdd:cd20649    69 PAFSAAKMKEMVPLINQACDVLLRNLKSYAESGNAFNIQRCYGCFTMDVVASVAFGTQVDSQKN 132
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
69-142 1.27e-04

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: 42.63  E-value: 1.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063706895  69 YGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINhQDASLVWlpSSSARWRLLRRLSVTQL 142
Cdd:cd20665     1 YGPVFTLYLGMKPTVVLHGYEAVKEALIDLGEEFSGRGRFPIFEKVN-KGLGIVF--SNGERWKETRRFSLMTL 71
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
69-240 1.57e-04

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: 42.39  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  69 YGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARsPTNAVRSINHQDASLVWLPSSSARWRLLRRLSVTQLLSPQRI 148
Cdd:cd20677     1 YGDVFQIKLGMLPVVVVSGLETIKQVLLKQGESFAGR-PDFYTFSLIANGKSMTFSEKYGESWKLHKKIAKNALRTFSKE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 149 EA---TKALRMN-----KVKELVSFISESSDREESVDISRVAFITTLNIISNILFSVDLgSYNAKASINGVqDTVISVMD 220
Cdd:cd20677    80 EAkssTCSCLLEehvcaEASELVKTLVELSKEKGSFDPVSLITCAVANVVCALCFGKRY-DHSDKEFLTIV-EINNDLLK 157
                         170       180
                  ....*....|....*....|
gi 1063706895 221 AAGTPDAANYFPFLRFLDLQ 240
Cdd:cd20677   158 ASGAGNLADFIPILRYLPSP 177
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
69-195 4.04e-04

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: 41.14  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  69 YGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSINhQDASLVWlPSSSARWRLLRRL--SVTQLLSPQ 146
Cdd:cd20675     1 YGDVFQIRLGSRPVVVLNGERAIRQALVQQGTDFAGRPDFASFRVVS-GGRSLAF-GGYSERWKAHRRVahSTVRAFSTR 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063706895 147 RIEATKALR---MNKVKELVSFISESSDREESVDISRVAFITTLNIISNILF 195
Cdd:cd20675    79 NPRTRKAFErhvLGEARELVALFLRKSAGGAYFDPAPPLVVAVANVMSAVCF 130
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
69-142 4.17e-04

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: 40.83  E-value: 4.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063706895  69 YGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARS--PTNAVRSINHQDASLVWLPSSSArWRLLRRLSVTQL 142
Cdd:cd20663     1 FGDVFSLQMAWKPVVVLNGLKAVREALVTCGEDTADRPpvPIFEHLGFGPKSQGVVLARYGPA-WREQRRFSVSTL 75
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
8-107 5.58e-04

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 40.73  E-value: 5.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895   8 ALLLLFCFILSCFLIFTttRSGRISRgaTALPPGPPRLPIIG-NIHLVGKH----PHRSFAELSKTYGPVMSLKLGSLNT 82
Cdd:PLN02987    5 AFLLLLSSLAAIFFLLL--RRTRYRR--MRLPPGSLGLPLVGeTLQLISAYktenPEPFIDERVARYGSLFMTHLFGEPT 80
                          90       100
                  ....*....|....*....|....*
gi 1063706895  83 VVIASPEAAREVLRTHDQILSARSP 107
Cdd:PLN02987   81 VFSADPETNRFILQNEGKLFECSYP 105
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
67-198 1.33e-03

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: 39.47  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  67 KTYGPV--MSLkLGSlNTVVIASPEAAREVLrTHDQILSARSPTNAVRSINHQDaSLVWLPSSSARWrlLRRLsVTQLLS 144
Cdd:cd11043     3 KRYGPVfkTSL-FGR-PTVVSADPEANRFIL-QNEGKLFVSWYPKSVRKLLGKS-SLLTVSGEEHKR--LRGL-LLSFLG 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063706895 145 PqriEATKALRMNKVKELV--SFISESSDREESV--DISRVAFittlNIISNILFSVD 198
Cdd:cd11043    76 P---EALKDRLLGDIDELVrqHLDSWWRGKSVVVleLAKKMTF----ELICKLLLGID 126
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
69-142 1.57e-03

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: 38.99  E-value: 1.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063706895  69 YGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILSARSPTNAVRSInHQDASLVWlpSSSARWRLLRRLSVTQL 142
Cdd:cd20672     1 YGDVFTVHLGPRPVVMLCGTDAIREALVDQAEAFSGRGTIAVVDPI-FQGYGVIF--ANGERWKTLRRFSLATM 71
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
69-201 1.89e-03

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: 38.79  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  69 YGPVMSLK--LGSlNTVVIASPEAAREVLRTHDqilSARSPTNAVRSINHQ--DASLVWlpSSSARWRLLRRLsVTQLLS 144
Cdd:cd11069     1 YGGLIRYRglFGS-ERLLVTDPKALKHILVTNS---YDFEKPPAFRRLLRRilGDGLLA--AEGEEHKRQRKI-LNPAFS 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063706895 145 PQRIEATKALRMNKVKELVSFISE----SSDREESVDISRVAFITTLNIISNILFSVDLGS 201
Cdd:cd11069    74 YRHVKELYPIFWSKAEELVDKLEEeieeSGDESISIDVLEWLSRATLDIIGLAGFGYDFDS 134
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
64-103 2.07e-03

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: 38.84  E-value: 2.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1063706895  64 ELSKTYGPVMSLKLGSLNTVVIASPEAAREVLRTHDQILS 103
Cdd:cd11045     5 QRYRRYGPVSWTGMLGLRVVALLGPDANQLVLRNRDKAFS 44
PLN02302 PLN02302
ent-kaurenoic acid oxidase
38-200 5.45e-03

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 37.39  E-value: 5.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895  38 LPPGPPRLPIIGNI-----HLVGKHPHRSFAELSKTYGPVMSLK--LGSLNTVVIASPEAAREVLrTHDQILSARSPTNA 110
Cdd:PLN02302   43 LPPGDLGWPVIGNMwsflrAFKSSNPDSFIASFISRYGRTGIYKafMFGQPTVLVTTPEACKRVL-TDDDAFEPGWPEST 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706895 111 VRSINHQdaSLVWLPSSSArwRLLRRLSVTQLLSPQRIEAtkalrmnkvkeLVSFISES--SDREESVDISRVAFIT--- 185
Cdd:PLN02302  122 VELIGRK--SFVGITGEEH--KRLRRLTAAPVNGPEALST-----------YIPYIEENvkSCLEKWSKMGEIEFLTelr 186
                         170
                  ....*....|....*..
gi 1063706895 186 --TLNIISNILFSVDLG 200
Cdd:PLN02302  187 klTFKIIMYIFLSSESE 203
 
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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