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Conserved domains on  [gi|1958642105|ref|XP_038946894|]
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cytochrome P450 2C13, male-specific isoform X7 [Rattus norvegicus]

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 ...
61-273 2.25e-153

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 cd20665:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 425  Bit Score: 434.77  E-value: 2.25e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQGIAFSHGNVWKATRHFTVKTLRNLGMGKGT 140
Cdd:cd20665     1 YGPVFTLYLGMKPTVVLHGYEAVKEALIDLGEEFSGRGRFPIFEKVNKGLGIVFSNGERWKETRRFSLMTLRNFGMGKRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 141 IEDKVQEEAKWLVKELKKTNGSPCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIISSPGIQVFNIFP 220
Cdd:cd20665    81 IEDRVQEEARCLVEELRKTNGSPCDPTFILGCAPCNVICSIIFQNRFDYKDQDFLNLMEKLNENFKILSSPWLQVCNNFP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958642105 221 ILLDYCPGNHNIYLKNYTWVKSYLLEKIKEHEESLDVSNPRDFIDYFLIERNQ 273
Cdd:cd20665   161 ALLDYLPGSHNKLLKNVAYIKSYILEKVKEHQESLDVNNPRDFIDCFLIKMEQ 213
 
Name Accession Description Interval E-value
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
61-273 2.25e-153

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: 434.77  E-value: 2.25e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQGIAFSHGNVWKATRHFTVKTLRNLGMGKGT 140
Cdd:cd20665     1 YGPVFTLYLGMKPTVVLHGYEAVKEALIDLGEEFSGRGRFPIFEKVNKGLGIVFSNGERWKETRRFSLMTLRNFGMGKRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 141 IEDKVQEEAKWLVKELKKTNGSPCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIISSPGIQVFNIFP 220
Cdd:cd20665    81 IEDRVQEEARCLVEELRKTNGSPCDPTFILGCAPCNVICSIIFQNRFDYKDQDFLNLMEKLNENFKILSSPWLQVCNNFP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958642105 221 ILLDYCPGNHNIYLKNYTWVKSYLLEKIKEHEESLDVSNPRDFIDYFLIERNQ 273
Cdd:cd20665   161 ALLDYLPGSHNKLLKNVAYIKSYILEKVKEHQESLDVNNPRDFIDCFLIKMEQ 213
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
30-275 3.69e-69

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: 221.00  E-value: 3.69e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  30 PPGPTPLPIIGNFFQVDMKDIRQS-LTNFSKTYGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLP---ICEK 105
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRKGNLHSvFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPwfaTSRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 106 VAKGQGIAFSHGNVWKATRHFTVKTLRNLgmGKGTIEDKVQEEAKWLVKELKKTNGSP--CDPQFIMGCAPGNVICCIIL 183
Cdd:pfam00067  81 PFLGKGIVFANGPRWRQLRRFLTPTFTSF--GKLSFEPRVEEEARDLVEKLRKTAGEPgvIDITDLLFRAALNVICSILF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 184 QNRFD-YEDKDFLNLIEKVNEAVKIISSPGIQVFNIFPILLdYCPGNHNIYLKNyTW--VKSYLLEKIKEHEESLD--VS 258
Cdd:pfam00067 159 GERFGsLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPILK-YFPGPHGRKLKR-ARkkIKDLLDKLIEERRETLDsaKK 236
                         250
                  ....*....|....*..
gi 1958642105 259 NPRDFIDYFLIERNQME 275
Cdd:pfam00067 237 SPRDFLDALLLAKEEED 253
PTZ00404 PTZ00404
cytochrome P450; Provisional
31-270 2.90e-21

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 92.86  E-value: 2.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  31 PGPTPLPIIGNFFQVDmKDIRQSLTNFSKTYGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQ 110
Cdd:PTZ00404   32 KGPIPIPILGNLHQLG-NLPHRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHGTFYH 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 111 GIAFSHGNVWKATRHFTVKTLR--NLGMGKGTIEDKVQEeakwLVKELKK--TNGSPCDPQFIMGCapgnviccIILQNR 186
Cdd:PTZ00404  111 GIVTSSGEYWKRNREIVGKAMRktNLKHIYDLLDDQVDV----LIESMKKieSSGETFEPRYYLTK--------FTMSAM 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 187 FDY---EDKDFLNLIEKVNEAvKIISsPGIQVFNIFPI--LLDYCPGNHNIYL-------KNYTWVKSYLLEKIKEHEES 254
Cdd:PTZ00404  179 FKYifnEDISFDEDIHNGKLA-ELMG-PMEQVFKDLGSgsLFDVIEITQPLYYqylehtdKNFKKIKKFIKEKYHEHLKT 256
                         250
                  ....*....|....*.
gi 1958642105 255 LDVSNPRDFIDYFLIE 270
Cdd:PTZ00404  257 IDPEVPRDLLDLLIKE 272
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
61-156 6.41e-06

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: 46.81  E-value: 6.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHgEEFSGRGRLP--ICEKVAKGQGIAFSHGNVWKATR-----HFTVKTLRN 133
Cdd:COG2124    31 YGPVFRVRLPGGGAWLVTRYEDVREVLRDP-RTFSSDGGLPevLRPLPLLGDSLLTLDGPEHTRLRrlvqpAFTPRRVAA 109
                          90       100
                  ....*....|....*....|...
gi 1958642105 134 LgmgkgtiEDKVQEEAKWLVKEL 156
Cdd:COG2124   110 L-------RPRIREIADELLDRL 125
 
Name Accession Description Interval E-value
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
61-273 2.25e-153

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: 434.77  E-value: 2.25e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQGIAFSHGNVWKATRHFTVKTLRNLGMGKGT 140
Cdd:cd20665     1 YGPVFTLYLGMKPTVVLHGYEAVKEALIDLGEEFSGRGRFPIFEKVNKGLGIVFSNGERWKETRRFSLMTLRNFGMGKRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 141 IEDKVQEEAKWLVKELKKTNGSPCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIISSPGIQVFNIFP 220
Cdd:cd20665    81 IEDRVQEEARCLVEELRKTNGSPCDPTFILGCAPCNVICSIIFQNRFDYKDQDFLNLMEKLNENFKILSSPWLQVCNNFP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958642105 221 ILLDYCPGNHNIYLKNYTWVKSYLLEKIKEHEESLDVSNPRDFIDYFLIERNQ 273
Cdd:cd20665   161 ALLDYLPGSHNKLLKNVAYIKSYILEKVKEHQESLDVNNPRDFIDCFLIKMEQ 213
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
61-270 8.58e-106

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: 313.73  E-value: 8.58e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQGIAFSHGNVWKATRHFTVKTLRNLGMGKGT 140
Cdd:cd11026     1 YGPVFTVYLGSKPVVVLCGYEAVKEALVDQAEEFSGRPPVPLFDRVTKGYGVVFSNGERWKQLRRFSLTTLRNFGMGKRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 141 IEDKVQEEAKWLVKELKKTNGSPCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIISSPGIQVFNIFP 220
Cdd:cd11026    81 IEERIQEEAKFLVEAFRKTKGKPFDPTFLLSNAVSNVICSIVFGSRFDYEDKEFLKLLDLINENLRLLSSPWGQLYNMFP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958642105 221 ILLDYCPGNHNIYLKNYTWVKSYLLEKIKEHEESLDVSNPRDFIDYFLIE 270
Cdd:cd11026   161 PLLKHLPGPHQKLFRNVEEIKSFIRELVEEHRETLDPSSPRDFIDCFLLK 210
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
61-273 3.26e-88

cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members are selectively expressed in lung tissues. They are responsible for the bioactivation of several pneumotoxic and carcinogenic chemicals such as benzene, styrene, naphthalene, and 1,1-dichloroethylene. CYP2F1 and CYP2F3 selectively catalyzes the 3-methyl dehydrogenation of 3-methylindole, forming toxic reactive intermediates that can form adducts with proteins and DNA. The CYP2F subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410762 [Multi-domain]  Cd Length: 425  Bit Score: 268.94  E-value: 3.26e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQGIAFSHGNVWKATRHFTVKTLRNLGMGKGT 140
Cdd:cd20669     1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRGDYPVFFNFTKGNGIAFSNGERWKILRRFALQTLRNFGMGKRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 141 IEDKVQEEAKWLVKELKKTNGSPCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIISSPGIQVFNIFP 220
Cdd:cd20669    81 IEERILEEAQFLLEELRKTKGAPFDPTFLLSRAVSNIICSVVFGSRFDYDDKRLLTILNLINDNFQIMSSPWGELYNIFP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958642105 221 ILLDYCPGNHNIYLKNYTWVKSYLLEKIKEHEESLDVSNPRDFIDYFLIERNQ 273
Cdd:cd20669   161 SVMDWLPGPHQRIFQNFEKLRDFIAESVREHQESLDPNSPRDFIDCFLTKMAE 213
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
61-273 1.07e-73

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: 231.74  E-value: 1.07e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQGIAFSHGNVWKATRHFTVKTLRNLGMGKGT 140
Cdd:cd20670     1 YGPVFTVYMGPRPVVVLCGHEAVKEALVDQADEFSGRGELATIERNFQGHGVALANGERWRILRRFSLTILRNFGMGKRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 141 IEDKVQEEAKWLVKELKKTNGSPCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIISSPGIQVFNIFP 220
Cdd:cd20670    81 IEERIQEEAGYLLEEFRKTKGAPIDPTFFLSRTVSNVISSVVFGSRFDYEDKQFLSLLRMINESFIEMSTPWAQLYDMYS 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958642105 221 ILLDYCPGNHNIYLKNYTWVKSYLLEKIKEHEESLDVSNPRDFIDYFLIERNQ 273
Cdd:cd20670   161 GIMQYLPGRHNRIYYLIEELKDFIASRVKINEASLDPQNPRDFIDCFLIKMHQ 213
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
61-275 1.30e-70

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: 223.89  E-value: 1.30e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQGIAFSHGNVWKATRHFTVKTLRNLGMGKGT 140
Cdd:cd20672     1 YGDVFTVHLGPRPVVMLCGTDAIREALVDQAEAFSGRGTIAVVDPIFQGYGVIFANGERWKTLRRFSLATMRDFGMGKRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 141 IEDKVQEEAKWLVKELKKTNGSPCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIISSPGIQVFNIFP 220
Cdd:cd20672    81 VEERIQEEAQCLVEELRKSKGALLDPTFLFQSITANIICSIVFGERFDYKDPQFLRLLDLFYQTFSLISSFSSQVFELFS 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958642105 221 ILLDYCPGNHNIYLKNYTWVKSYLLEKIKEHEESLDVSNPRDFIDYFLIernQME 275
Cdd:cd20672   161 GFLKYFPGAHRQIYKNLQEILDYIGHSVEKHRATLDPSAPRDFIDTYLL---RME 212
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
61-275 2.19e-69

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: 220.45  E-value: 2.19e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQGIAFSHGNVWKATRHFTVKTLRNLGMGKGT 140
Cdd:cd20664     1 YGSIFTVQMGTKKVVVLAGYKTVKEALVNHAEAFGGRPIIPIFEDFNKGYGILFSNGENWKEMRRFTLTTLRDFGMGKKT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 141 IEDKVQEEAKWLVKELKKTNGSPCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIISSPGIQVFNIFP 220
Cdd:cd20664    81 SEDKILEEIPYLIEVFEKHKGKPFETTLSMNVAVSNIIASIVLGHRFEYTDPTLLRMVDRINENMKLTGSPSVQLYNMFP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958642105 221 ILLDYcPGNHNIYLKNYTWVKSYLLEKIKEHEESLDVSNPRDFIDYFLIERNQME 275
Cdd:cd20664   161 WLGPF-PGDINKLLRNTKELNDFLMETFMKHLDVLEPNDQRGFIDAFLVKQQEEE 214
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
30-275 3.69e-69

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: 221.00  E-value: 3.69e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  30 PPGPTPLPIIGNFFQVDMKDIRQS-LTNFSKTYGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLP---ICEK 105
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRKGNLHSvFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPwfaTSRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 106 VAKGQGIAFSHGNVWKATRHFTVKTLRNLgmGKGTIEDKVQEEAKWLVKELKKTNGSP--CDPQFIMGCAPGNVICCIIL 183
Cdd:pfam00067  81 PFLGKGIVFANGPRWRQLRRFLTPTFTSF--GKLSFEPRVEEEARDLVEKLRKTAGEPgvIDITDLLFRAALNVICSILF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 184 QNRFD-YEDKDFLNLIEKVNEAVKIISSPGIQVFNIFPILLdYCPGNHNIYLKNyTW--VKSYLLEKIKEHEESLD--VS 258
Cdd:pfam00067 159 GERFGsLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPILK-YFPGPHGRKLKR-ARkkIKDLLDKLIEERRETLDsaKK 236
                         250
                  ....*....|....*..
gi 1958642105 259 NPRDFIDYFLIERNQME 275
Cdd:pfam00067 237 SPRDFLDALLLAKEEED 253
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
61-279 5.64e-67

cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes CYP2A1, 2A2, and 2A3 in rats; CYP2A4, 2A5, 2A12, 2A20p, 2A21p, 2A22, and 2A23p in mice; CYP2A6, 2A7, 2A13, 2A18P in humans; CYP2A8, 2A9, 2A14, 2A15, 2A16, and 2A17 in hamsters; CYP2A10 and 2A11 in rabbits; and CYP2A19 in pigs. CYP2A enzymes metabolize numerous xenobiotic compounds, including coumarin, aflatoxin B1, nicotine, cotinine, 1,3-butadiene, and acetaminophen, among others, as well as endogenous compounds, including testosterone, progesterone, and other steroid hormones. Human CYP2A6 is responsible for the systemic clearance of nicotine, while CYP2A13 activates the nicotine-derived procarcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) into DNA-altering compounds that cause lung cancer. The CYP2A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410761 [Multi-domain]  Cd Length: 425  Bit Score: 214.28  E-value: 5.64e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQGIAFSHGNVWKATRHFTVKTLRNLGMGKGT 140
Cdd:cd20668     1 YGPVFTIHLGPRRVVVLCGYDAVKEALVDQAEEFSGRGEQATFDWLFKGYGVAFSNGERAKQLRRFSIATLRDFGVGKRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 141 IEDKVQEEAKWLVKELKKTNGSPCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIISSPGIQVFNIFP 220
Cdd:cd20668    81 IEERIQEEAGFLIDALRGTGGAPIDPTFYLSRTVSNVISSIVFGDRFDYEDKEFLSLLRMMLGSFQFTATSTGQLYEMFS 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642105 221 ILLDYCPGNHNIYLKNYTWVKSYLLEKIKEHEESLDVSNPRDFIDYFLIERNQ------MEFYYK 279
Cdd:cd20668   161 SVMKHLPGPQQQAFKELQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEekknpnTEFYMK 225
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
61-270 3.37e-65

cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in mice and humans. They function as catalysts of arachidonic acid metabolism and are active in the metabolism of fatty acids to generate bioactive compounds. Human CYP2J2, also called arachidonic acid epoxygenase or albendazole monooxygenase (hydroxylating), is a membrane-bound cytochrome P450 primarily expressed in the heart and plays a significant role in cardiovascular diseases. The CYP2J subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410755 [Multi-domain]  Cd Length: 421  Bit Score: 209.65  E-value: 3.37e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQGIAFSHGNVWKATRHFTVKTLRNLGMGKGT 140
Cdd:cd20662     1 YGNIFSLQLGSISSVIVTGLPLIKEALVTQEQNFMNRPETPLRERIFNKNGLIFSSGQTWKEQRRFALMTLRNFGLGKKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 141 IEDKVQEEAKWLVKELKKTNGSPCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIISSPGIQVFNIFP 220
Cdd:cd20662    81 LEERIQEECRHLVEAIREEKGNPFNPHFKINNAVSNIICSVTFGERFEYHDEWFQELLRLLDETVYLEGSPMSQLYNAFP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958642105 221 ILLDYCPGNHNIYLKNYTWVKSYLLEKIKEHEESLDVSNPRDFIDYFLIE 270
Cdd:cd20662   161 WIMKYLPGSHQTVFSNWKKLKLFVSDMIDKHREDWNPDEPRDFIDAYLKE 210
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
61-275 6.43e-54

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: 180.38  E-value: 6.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQGIAFSHGNVWKATRHFTVKTLRNLGMGKGT 140
Cdd:cd20671     1 YGPVFTIHLGMQKTVVLTGYEAVKEALVGTGDEFADRPPIPIFQAIQHGNGVFFSSGERWRTTRRFTVRSMKSLGMGKRT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 141 IEDKVQEEAKWLVKELKKTNGSPCdPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIISSPGIQVFNIFP 220
Cdd:cd20671    81 IEDKILEELQFLNGQIDSFNGKPF-PLRLLGWAPTNITFAMLFGRRFDYKDPTFVSLLDLIDEVMVLLGSPGLQLFNLYP 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958642105 221 ILLDYCPgNHNIYLKNYTWVKSYLLEKIKEHEESLDVSNPRDFIDYfLIERNQME 275
Cdd:cd20671   160 VLGAFLK-LHKPILDKVEEVCMILRTLIEARRPTIDGNPLHSYIEA-LIQKQEED 212
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
62-271 2.66e-53

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: 178.56  E-value: 2.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  62 GPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQGIAFSHGNVWKATRHFTVKTLRNLGMGKgTI 141
Cdd:cd20617     1 GGIFTLWLGDVPTVVLSDPEIIKEAFVKNGDNFSDRPLLPSFEIISGGKGILFSNGDYWKELRRFALSSLTKTKLKK-KM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 142 EDKVQEEAKWLVKELKKT--NGSPCDPQFIMGCAPGNVICCIILQNRFD-YEDKDFLNLIEKVNEAVKIISSPGIQVFni 218
Cdd:cd20617    80 EELIEEEVNKLIESLKKHskSGEPFDPRPYFKKFVLNIINQFLFGKRFPdEDDGEFLKLVKPIEEIFKELGSGNPSDF-- 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958642105 219 FPILLDYCPGNHNIYLKNYTWVKSYLLEKIKEHEESLDVSNPRDFIDYFLIER 271
Cdd:cd20617   158 IPILLPFYFLYLKKLKKSYDKIKDFIEKIIEEHLKTIDPNNPRDLIDDELLLL 210
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
61-270 5.02e-53

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


Pssm-ID: 410759 [Multi-domain]  Cd Length: 426  Bit Score: 178.05  E-value: 5.02e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQGIAFSH-GNVWKATRHFTVKTLRNLGMGKG 139
Cdd:cd20666     1 YGNIFSLFIGSQLVVVLNDFESVREALVQKAEVFSDRPSVPLVTILTKGKGIVFAPyGPVWRQQRKFSHSTLRHFGLGKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 140 TIEDKVQEEAKWLVKELKKTNGSPCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIISSPGIQVFNIF 219
Cdd:cd20666    81 SLEPKIIEEFRYVKAEMLKHGGDPFNPFPIVNNAVSNVICSMSFGRRFDYQDVEFKTMLGLMSRGLEISVNSAAILVNIC 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958642105 220 PILLdYCP-GNHNIYLKNYTWVKSYLLEKIKEHEESLDVSNPRDFIDYFLIE 270
Cdd:cd20666   161 PWLY-YLPfGPFRELRQIEKDITAFLKKIIADHRETLDPANPRDFIDMYLLH 211
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
61-268 1.81e-47

cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The function of CYP2AB1 is unknown. CYP2AB1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410760 [Multi-domain]  Cd Length: 423  Bit Score: 163.47  E-value: 1.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQGIAFSHGNVWKATRHFTVKTLRNLGMGKGT 140
Cdd:cd20667     1 YGNIYTLWLGSTPIVVLSGFKAVKEGLVSHSEEFSGRPLTPFFRDLFGEKGIICTNGLTWKQQRRFCMTTLRELGLGKQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 141 IEDKVQEEAKWLVKELKKTNGSPCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIISSPGIQVFNIFP 220
Cdd:cd20667    81 LESQIQHEAAELVKVFAQENGRPFDPQDPIVHATANVIGAVVFGHRFSSEDPIFLELIRAINLGLAFASTIWGRLYDAFP 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958642105 221 ILLDYCPGNHNIYLKNYTWVKSYLLEKIKEHEESlDVSNPRDFIDYFL 268
Cdd:cd20667   161 WLMRYLPGPHQKIFAYHDAVRSFIKKEVIRHELR-TNEAPQDFIDCYL 207
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
61-270 4.68e-46

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: 159.86  E-value: 4.68e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVA---KGQGIAFS-HGNVWKATRHFTVKTLRNLGM 136
Cdd:cd20663     1 FGDVFSLQMAWKPVVVLNGLKAVREALVTCGEDTADRPPVPIFEHLGfgpKSQGVVLArYGPAWREQRRFSVSTLRNFGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 137 GKGTIEDKVQEEAKWLVKELKKTNGSPCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIISSPGIQVF 216
Cdd:cd20663    81 GKKSLEQWVTEEAGHLCAAFTDQAGRPFNPNTLLNKAVCNVIASLIFARRFEYEDPRFIRLLKLLEESLKEESGFLPEVL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958642105 217 NIFPILLdYCPGNHNIYLKNYTWVKSYLLEKIKEHEESLDVSN-PRDFIDYFLIE 270
Cdd:cd20663   161 NAFPVLL-RIPGLAGKVFPGQKAFLALLDELLTEHRTTWDPAQpPRDLTDAFLAE 214
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
62-270 6.79e-44

cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This subfamily is composed of insect and crustacean cytochrome P450s including Diploptera punctata cytochrome P450 15A1 (CYP15A1 or CYP15A1), Panulirus argus CYP2L1, and CYP303A1, CYP304A1, and CYP305A1 from Drosophila melanogaster. CYP15A1, also called methyl farnesoate epoxidase, catalyzes the conversion of methyl farnesoate to juvenile hormone III acid during juvenile hormone biosynthesis. CYP303A1, CYP304A1, and CYP305A1 may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. The CYP15A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410744 [Multi-domain]  Cd Length: 423  Bit Score: 153.91  E-value: 6.79e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  62 GPVYTLYVGSQPTVVLHGYEALKEALvdHGEEFSGRGRLPICEKVAKGQ--GIAFSHGNVWKATRHFTVKTLRNLGMGKG 139
Cdd:cd20651     1 GDVVGLKLGKDKVVVVSGYEAVREVL--SREEFDGRPDGFFFRLRTFGKrlGITFTDGPFWKEQRRFVLRHLRDFGFGRR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 140 TIEDKVQEEAKWLVKELKKTNGSPCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVK-IISSPGIqvFNI 218
Cdd:cd20651    79 SMEEVIQEEAEELIDLLKKGEKGPIQMPDLFNVSVLNVLWAMVAGERYSLEDQKLRKLLELVHLLFRnFDMSGGL--LNQ 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958642105 219 FPILLDYCPG--NHNIYLKNYTWVKSYLLEKIKEHEESLDVSNPRDFIDYFLIE 270
Cdd:cd20651   157 FPWLRFIAPEfsGYNLLVELNQKLIEFLKEEIKEHKKTYDEDNPRDLIDAYLRE 210
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
61-275 9.34e-44

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: 153.90  E-value: 9.34e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKG-QGIAFS-HGNVWKATRHFTVKTLRNLGMGK 138
Cdd:cd11027     1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKKSADFAGRPKLFTFDLFSRGgKDIAFGdYSPTWKLHRKLAHSALRLYASGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 139 GTIEDKVQEEAKWLVKELKKTNGSPCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIISSPGIqvFNI 218
Cdd:cd11027    81 PRLEEKIAEEAEKLLKRLASQEGQPFDPKDELFLAVLNVICSITFGKRYKLDDPEFLRLLDLNDKFFELLGAGSL--LDI 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642105 219 FPiLLDYCPgnhniyLKNYTWVK-------SYLLEKIKEHEESLDVSNPRDFIDYFLIERNQME 275
Cdd:cd11027   159 FP-FLKYFP------NKALRELKelmkerdEILRKKLEEHKETFDPGNIRDLTDALIKAKKEAE 215
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
61-267 8.45e-39

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: 140.90  E-value: 8.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQGIAFSH-GNVWKATRHFTVKTLRNL--GMG 137
Cdd:cd11028     1 YGDVFQIRMGSRPVVVLNGLETIKQALVRQGEDFAGRPDFYSFQFISNGKSMAFSDyGPRWKLHRKLAQNALRTFsnART 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 138 KGTIEDKVQEEAKWLVKELKKTNGS--PCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIISSpGIQV 215
Cdd:cd11028    81 HNPLEEHVTEEAEELVTELTENNGKpgPFDPRNEIYLSVGNVICAICFGKRYSRDDPEFLELVKSNDDFGAFVGA-GNPV 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958642105 216 fNIFPILLDYCPGNHNIYLKNYTWVKSYLLEKIKEHEESLDVSNPRDFIDYF 267
Cdd:cd11028   160 -DVMPWLRYLTRRKLQKFKELLNRLNSFILKKVKEHLDTYDKGHIRDITDAL 210
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
58-275 7.43e-34

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


Pssm-ID: 410754 [Multi-domain]  Cd Length: 436  Bit Score: 127.62  E-value: 7.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  58 SKTYGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQGIAFS-HGNVWKATRHFTVKTLRNLGM 136
Cdd:cd20661     9 SQIHGQIFSLDLGGISTVVLNGYDAVKECLVHQSEIFADRPSLPLFMKLTNMGGLLNSkYGRGWTEHRKLAVNCFRYFGY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 137 GKGTIEDKVQEEAKWLVKELKKTNGSPCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIISSPGIQVF 216
Cdd:cd20661    89 GQKSFESKISEECKFFLDAIDTYKGKPFDPKHLITNAVSNITNLIIFGERFTYEDTDFQHMIEIFSENVELAASAWVFLY 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 217 NIFPiLLDYCP-GNHNIYLKNYTWVKSYLLEKIKEHEESLDVSNPRDFIDYFLIERNQME 275
Cdd:cd20661   169 NAFP-WIGILPfGKHQQLFRNAAEVYDFLLRLIERFSENRKPQSPRHFIDAYLDEMDQNK 227
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
61-273 1.32e-30

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


Pssm-ID: 410769 [Multi-domain]  Cd Length: 437  Bit Score: 118.58  E-value: 1.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQGIAFSH--GNVWKATRHFTVKTLRNLGMGK 138
Cdd:cd20676     1 YGDVLQIQIGSRPVVVLSGLDTIRQALVKQGDDFKGRPDLYSFRFISDGQSLTFSTdsGPVWRARRKLAQNALKTFSIAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 139 GT-------IEDKVQEEAKWLVKELK---KTNGSpCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKII 208
Cdd:cd20676    81 SPtssssclLEEHVSKEAEYLVSKLQelmAEKGS-FDPYRYIVVSVANVICAMCFGKRYSHDDQELLSLVNLSDEFGEVA 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642105 209 SSPGIQVFniFPIlLDYCPGNHNIYLKNYTWVKSYLLEKI-KEHEESLDVSNPRDFIDYfLIERNQ 273
Cdd:cd20676   160 GSGNPADF--IPI-LRYLPNPAMKRFKDINKRFNSFLQKIvKEHYQTFDKDNIRDITDS-LIEHCQ 221
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
62-262 5.27e-28

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: 111.35  E-value: 5.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  62 GPVYTLYVGSQPTVVLHGYEALKEALvdHGEEFSGRGRLPICEKVAKGQGIAFSHGNVWKATRHFTVKTLRNLGM----- 136
Cdd:cd20652     1 GSIFSLKMGSVYTVVLSDPKLIRDTF--RRDEFTGRAPLYLTHGIMGGNGIICAEGDLWRDQRRFVHDWLRQFGMtkfgn 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 137 GKGTIEDKVQEEAKWLVKELKKTNGSPCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIISSPGiqVF 216
Cdd:cd20652    79 GRAKMEKRIATGVHELIKHLKAESGQPVDPSPVLMHSLGNVINDLVFGFRYKEDDPTWRWLRFLQEEGTKLIGVAG--PV 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642105 217 NIFPILLdycpgnhniYLKNYTWVKSYLLEK-----------IKEHEESLDVSNPRD 262
Cdd:cd20652   157 NFLPFLR---------HLPSYKKAIEFLVQGqakthaiyqkiIDEHKRRLKPENPRD 204
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
61-265 1.10e-26

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: 107.87  E-value: 1.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQGIAFS--HGNVWKATRHFTVKTLRNLGMGK 138
Cdd:cd20677     1 YGDVFQIKLGMLPVVVVSGLETIKQVLLKQGESFAGRPDFYTFSLIANGKSMTFSekYGESWKLHKKIAKNALRTFSKEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 139 GT-------IEDKVQEEAKWLVKELK---KTNGSpCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKii 208
Cdd:cd20677    81 AKsstcsclLEEHVCAEASELVKTLVelsKEKGS-FDPVSLITCAVANVVCALCFGKRYDHSDKEFLTIVEINNDLLK-- 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642105 209 SSPGIQVFNIFPIlLDYCPGNH-NIYLKNYTWVKSYLLEKIKEHEESLDVSNPRDFID 265
Cdd:cd20677   158 ASGAGNLADFIPI-LRYLPSPSlKALRKFISRLNNFIAKSVQDHYATYDKNHIRDITD 214
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
61-268 2.67e-23

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: 98.54  E-value: 2.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQGIAF-SHGNVWKATRHFTVKTLRNLGMG-- 137
Cdd:cd20675     1 YGDVFQIRLGSRPVVVLNGERAIRQALVQQGTDFAGRPDFASFRVVSGGRSLAFgGYSERWKAHRRVAHSTVRAFSTRnp 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 138 --KGTIEDKVQEEAKWLVKEL--KKTNGSPCDPQFIMGCAPGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIISS--- 210
Cdd:cd20675    81 rtRKAFERHVLGEARELVALFlrKSAGGAYFDPAPPLVVAVANVMSAVCFGKRYSHDDAEFRSLLGRNDQFGRTVGAgsl 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 211 ----PGIQ--------VFNIFPILldycpgNHNIYLknytwvksYLLEKIKEHEESLDVSNPRDFIDYFL 268
Cdd:cd20675   161 vdvmPWLQyfpnpvrtVFRNFKQL------NREFYN--------FVLDKVLQHRETLRGGAPRDMMDAFI 216
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
61-268 5.48e-23

cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), also called steroid 21-hydroxylase (EC 1.14.14.16) or cytochrome P-450c21 or CYP21A2 (in humans), catalyzes the 21-hydroxylation of steroids such as progesterone and 17-alpha-hydroxyprogesterone (17-alpha-OH-progesterone) to form 11-deoxycorticosterone and 11-deoxycortisol, respectively. It is required for the adrenal synthesis of mineralocorticoids and glucocorticoids. Deficiency of this CYP is involved in ~95% of cases of human congenital adrenal hyperplasia, a disorder of adrenal steroidogenesis. There are two CYP21 genes in the human genome, CYP21A1 (a pseudogene) and CYP21A2 (the functional gene). Deficiencies in steroid 21-hydroxylase activity lead to a type of congenital adrenal hyperplasia, which has three clinical forms: a severe form with concurrent defects in both cortisol and aldosterone biosynthesis; a form with adequate aldosterone biosynthesis; and a mild, non-classic form that can be asymptomatic or associated with signs of postpubertal androgen excess without cortisol deficiency. CYP21A2 is also the major autoantigen in autoimmune Addison disease. Cyp21 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410767 [Multi-domain]  Cd Length: 424  Bit Score: 97.48  E-value: 5.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGqGIAFSHGN---VWKATRHFTVKTLRnLGMg 137
Cdd:cd20674     1 YGPIYRLRLGLQDVVVLNSKRTIREALVRKWADFAGRPHSYTGKLVSQG-GQDLSLGDyslLWKAHRKLTRSALQ-LGI- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 138 KGTIEDKVQEEAKWLVKELKKTNGSPCDPQFIMGCAPGNVICCIILQNRFDyEDKDFLNLIEKVNEAVKIISSPGIQVFN 217
Cdd:cd20674    78 RNSLEPVVEQLTQELCERMRAQAGTPVDIQEEFSLLTCSIICCLTFGDKED-KDTLVQAFHDCVQELLKTWGHWSIQALD 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642105 218 IFPILLdycpgnhniYLKNYTW-------------VKSYLlekiKEHEESLDVSNPRDFIDYFL 268
Cdd:cd20674   157 SIPFLR---------FFPNPGLrrlkqavenrdhiVESQL----RQHKESLVAGQWRDMTDYML 207
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
61-275 7.26e-23

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: 97.01  E-value: 7.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAK-GQGIAF-SHGNVWKATRHFTVKTLRNLGMGK 138
Cdd:cd20673     1 YGPIYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGRPRMVTTDLLSRnGKDIAFaDYSATWQLHRKLVHSAFALFGEGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 139 GTIEDKVQEEAKWLVKELKKTNGSPCDPQFIMGCAPGNVICCIILQNRFDYEDKDFlNLIEKVNEA-VKIISSPGIqvFN 217
Cdd:cd20673    81 QKLEKIICQEASSLCDTLATHNGESIDLSPPLFRAVTNVICLLCFNSSYKNGDPEL-ETILNYNEGiVDTVAKDSL--VD 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 218 IFPILLDYcPgNHNI-YLKNYTWVKSYLL-EKIKEHEESLDVSNPRDFIDYFLIERNQME 275
Cdd:cd20673   158 IFPWLQIF-P-NKDLeKLKQCVKIRDKLLqKKLEEHKEKFSSDSIRDLLDALLQAKMNAE 215
PTZ00404 PTZ00404
cytochrome P450; Provisional
31-270 2.90e-21

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 92.86  E-value: 2.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  31 PGPTPLPIIGNFFQVDmKDIRQSLTNFSKTYGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVAKGQ 110
Cdd:PTZ00404   32 KGPIPIPILGNLHQLG-NLPHRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHGTFYH 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 111 GIAFSHGNVWKATRHFTVKTLR--NLGMGKGTIEDKVQEeakwLVKELKK--TNGSPCDPQFIMGCapgnviccIILQNR 186
Cdd:PTZ00404  111 GIVTSSGEYWKRNREIVGKAMRktNLKHIYDLLDDQVDV----LIESMKKieSSGETFEPRYYLTK--------FTMSAM 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 187 FDY---EDKDFLNLIEKVNEAvKIISsPGIQVFNIFPI--LLDYCPGNHNIYL-------KNYTWVKSYLLEKIKEHEES 254
Cdd:PTZ00404  179 FKYifnEDISFDEDIHNGKLA-ELMG-PMEQVFKDLGSgsLFDVIEITQPLYYqylehtdKNFKKIKKFIKEKYHEHLKT 256
                         250
                  ....*....|....*.
gi 1958642105 255 LDVSNPRDFIDYFLIE 270
Cdd:PTZ00404  257 IDPEVPRDLLDLLIKE 272
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
28-268 6.68e-14

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 71.39  E-value: 6.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  28 KLPPGPTPLPIIGNFFQVDMKDIRqSLTNFSKTYGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVA 107
Cdd:PLN03112   32 RLPPGPPRWPIVGNLLQLGPLPHR-DLASLCKKYGPLVYLRLGSVDAITTDDPELIREILLRQDDVFASRPRTLAAVHLA 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 108 KGQG-IAFS-HGNVWKATRHFTVKTLRNLGMGKGTIEDKVqEEAKWLVKEL--KKTNGSPCDPQFIMGCAPGNVICCIIL 183
Cdd:PLN03112  111 YGCGdVALApLGPHWKRMRRICMEHLLTTKRLESFAKHRA-EEARHLIQDVweAAQTGKPVNLREVLGAFSMNNVTRMLL 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 184 QNRF-------DYEDKDFLNLIEKVNEAVKIISspgiqvfnifpiLLDYCPGnhniylknYTWVKSYLLEK--------- 247
Cdd:PLN03112  190 GKQYfgaesagPKEAMEFMHITHELFRLLGVIY------------LGDYLPA--------WRWLDPYGCEKkmrevekrv 249
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958642105 248 -------IKEH----EESLDVSNPRDFIDYFL 268
Cdd:PLN03112  250 defhdkiIDEHrrarSGKLPGGKDMDFVDVLL 281
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
28-158 7.84e-14

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 70.92  E-value: 7.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  28 KLPPGPTPLPIIGNFFQV--DMKdiRQSLTNFSKTYGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEK 105
Cdd:PLN02394   30 KLPPGPAAVPIFGNWLQVgdDLN--HRNLAEMAKKYGDVFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDI 107
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642105 106 -VAKGQGIAFS-HGNVWKATRH------FTVKTLRNLGMGkgtiedkVQEEAKWLVKELKK 158
Cdd:PLN02394  108 fTGKGQDMVFTvYGDHWRKMRRimtvpfFTNKVVQQYRYG-------WEEEADLVVEDVRA 161
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
62-268 1.71e-12

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: 66.81  E-value: 1.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  62 GPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVA-KGQGIAFS-HGNVWKATRH------FTVKTLRN 133
Cdd:cd20618     1 GPLMYLRLGSVPTVVVSSPEMAKEVLKTQDAVFASRPRTAAGKIFSyNGQDIVFApYGPHWRHLRKictlelFSAKRLES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 134 LgmgkgtiEDKVQEEAKWLVKELKK--TNGSPCDPQFIMGCAPGNVICCIILQNRF-------DYEDKDFLNLIEkvnEA 204
Cdd:cd20618    81 F-------QGVRKEELSHLVKSLLEesESGKPVNLREHLSDLTLNNITRMLFGKRYfgesekeSEEAREFKELID---EA 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642105 205 VKIISspgiqVFNI---FPIL--LDYcPGNHNIYLKNYTWVKSYLLEKIKEHEESLDVSNPRDFIDYFL 268
Cdd:cd20618   151 FELAG-----AFNIgdyIPWLrwLDL-QGYEKRMKKLHAKLDRFLQKIIEEHREKRGESKKGGDDDDDL 213
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
60-273 1.52e-11

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: 64.02  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  60 TYGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKVA-KGQGIAFS-HGNVWKATRHFT---------V 128
Cdd:cd11072     1 KYGPLMLLRLGSVPTVVVSSPEAAKEVLKTHDLVFASRPKLLAARILSyGGKDIAFApYGEYWRQMRKICvlellsakrV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 129 KTLRNLgmgkgtiedkVQEEAKWLVKELKKTNGSPcDP----QFIMGCApGNVICCIILQNRFDYEDKDflNLIEKVNEA 204
Cdd:cd11072    81 QSFRSI----------REEEVSLLVKKIRESASSS-SPvnlsELLFSLT-NDIVCRAAFGRKYEGKDQD--KFKELVKEA 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642105 205 VKIISspGIQVFNIFPIL--LDYCPGNHNIYLKNYTWVKSYLLEKIKEHEESLDVSNPRDFIDYFLIERNQ 273
Cdd:cd11072   147 LELLG--GFSVGDYFPSLgwIDLLTGLDRKLEKVFKELDAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRLQ 215
PLN02655 PLN02655
ent-kaurene oxidase
31-97 8.87e-11

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 62.07  E-value: 8.87e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642105  31 PGptpLPIIGNFFQVDMKDIRQSLTNFSKTYGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGR 97
Cdd:PLN02655    5 PG---LPVIGNLLQLKEKKPHRTFTKWSEIYGPIYTIRTGASSVVVLNSTEVAKEAMVTKFSSISTR 68
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
61-222 1.45e-10

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: 61.05  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPI-CEKVAKGQGIAF-SHGNVWKATR-----HFTVKTLRN 133
Cdd:cd11065     1 YGPIISLKVGGQTIIVLNSPKAAKDLLEKRSAIYSSRPRMPMaGELMGWGMRLLLmPYGPRWRLHRrlfhqLLNPSAVRK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 134 LGmgkgtiedKVQE-EAKWLVKELKKtngspcDPQFIMGCA---PGNVICCIILQNRFDYEDKDFLNLIEKVNEAVKIIS 209
Cdd:cd11065    81 YR--------PLQElESKQLLRDLLE------SPDDFLDHIrryAASIILRLAYGYRVPSYDDPLLRDAEEAMEGFSEAG 146
                         170
                  ....*....|...
gi 1958642105 210 SPGIQVFNIFPIL 222
Cdd:cd11065   147 SPGAYLVDFFPFL 159
PLN02687 PLN02687
flavonoid 3'-monooxygenase
25-162 1.77e-10

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 60.98  E-value: 1.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  25 GRGKLPPGPTPLPIIGNFFQVDMKDiRQSLTNFSKTYGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICE 104
Cdd:PLN02687   31 HKRPLPPGPRGWPVLGNLPQLGPKP-HHTMAALAKTYGPLFRLRFGFVDVVVAASASVAAQFLRTHDANFSNRPPNSGAE 109
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642105 105 KVA-KGQGIAFS-HGNVWKATRH------FTVKTLRNLgmgkgtiEDKVQEEAKWLVKELKKTNGS 162
Cdd:PLN02687  110 HMAyNYQDLVFApYGPRWRALRKicavhlFSAKALDDF-------RHVREEEVALLVRELARQHGT 168
PLN02966 PLN02966
cytochrome P450 83A1
26-158 2.23e-09

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 57.84  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  26 RGKLPPGPTPLPIIGNFFQVDMKDIRQSLTNFSKTYGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRgrlpicek 105
Cdd:PLN02966   27 RYKLPPGPSPLPVIGNLLQLQKLNPQRFFAGWAKKYGPILSYRIGSRTMVVISSAELAKELLKTQDVNFADR-------- 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642105 106 vAKGQGIAF-SHGNVWKATRHFT--VKTLRNLGMGK-------GTIEDKVQEEAKWLVKELKK 158
Cdd:PLN02966   99 -PPHRGHEFiSYGRRDMALNHYTpyYREIRKMGMNHlfsptrvATFKHVREEEARRMMDKINK 160
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
28-97 3.45e-09

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 57.01  E-value: 3.45e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  28 KLPPGPTPLPIIGNFFQVDMKDIRQSLTNFSKTYGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGR 97
Cdd:PLN03234   28 RLPPGPKGLPIIGNLHQMEKFNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTAR 97
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
60-125 7.11e-08

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: 53.02  E-value: 7.11e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642105  60 TYGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRL-PICEKVAKGQ-GIAFS-HGNVWKATRH 125
Cdd:cd11075     1 KYGPIFTLRMGSRPLIVVASRELAHEALVQKGSSFASRPPAnPLRVLFSSNKhMVNSSpYGPLWRTLRR 69
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
61-268 8.73e-08

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


Pssm-ID: 410678 [Multi-domain]  Cd Length: 422  Bit Score: 52.59  E-value: 8.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRgRLPICEKVAKGQGIAFSHGNVWKATRH-----FTVKTLRNLg 135
Cdd:cd11055     2 YGKVFGLYFGTIPVIVVSDPEMIKEILVKEFSNFTNR-PLFILLDEPFDSSLLFLKGERWKRLRTtlsptFSSGKLKLM- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 136 mgKGTIEDKVQEeakwLVKELKK--TNGSPCD-----PQF----IMGCAPGnvicciILQNRFDYEDKDFLNLIEKV--N 202
Cdd:cd11055    80 --VPIINDCCDE----LVEKLEKaaETGKPVDmkdlfQGFtldvILSTAFG------IDVDSQNNPDDPFLKAAKKIfrN 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642105 203 EAVKIISSPGIQVFNIFPILLDYC--PGNHNIYLKNytwvksyLLEKIKEHEESLDVSNPRDFIDYFL 268
Cdd:cd11055   148 SIIRLFLLLLLFPLRLFLFLLFPFvfGFKSFSFLED-------VVKKIIEQRRKNKSSRRKDLLQLML 208
PLN00168 PLN00168
Cytochrome P450; Provisional
25-220 9.76e-08

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 52.64  E-value: 9.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  25 GRGKLPPGPTPLPIIGNFFQV--DMKDIRQSLTNFSKTYGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPI 102
Cdd:PLN00168   32 KGRRLPPGPPAVPLLGSLVWLtnSSADVEPLLRRLIARYGPVVSLRVGSRLSVFVADRRLAHAALVERGAALADRPAVAS 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 103 CEKVAKGQGIAF--SHGNVWKATRHFTVKTLRNLGMGKGTIEDKVQEEAKwLVKELKKTNGSPCDPQfIMGCAPGNVICC 180
Cdd:PLN00168  112 SRLLGESDNTITrsSYGPVWRLLRRNLVAETLHPSRVRLFAPARAWVRRV-LVDKLRREAEDAAAPR-VVETFQYAMFCL 189
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958642105 181 IILQNRFDYEDKDFLNLIEKVNEAVKIISSPGIQVFNIFP 220
Cdd:PLN00168  190 LVLMCFGERLDEPAVRAIAAAQRDWLLYVSKKMSVFAFFP 229
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
58-222 4.72e-07

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: 50.61  E-value: 4.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  58 SKTYGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRgRLPICEKVAKGQG--IAFSH-GNVWK------ATRHFTV 128
Cdd:cd11073     1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGR-DVPDAVRALGHHKssIVWPPyGPRWRmlrkicTTELFSP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 129 KTLRNLgmgKGTIEDKVQEEAKWLVKelKKTNGSPCDPQFIMGCAPGNVICCIIL-QNRFDYEDKDFLNLIEKVNEAVKI 207
Cdd:cd11073    80 KRLDAT---QPLRRRKVRELVRYVRE--KAGSGEAVDIGRAAFLTSLNLISNTLFsVDLVDPDSESGSEFKELVREIMEL 154
                         170
                  ....*....|....*
gi 1958642105 208 ISSPgiQVFNIFPIL 222
Cdd:cd11073   155 AGKP--NVADFFPFL 167
PLN02183 PLN02183
ferulate 5-hydroxylase
30-163 2.76e-06

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 48.31  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  30 PPGPTPLPIIGNFFQVDMKDIRqSLTNFSKTYGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGR-GRLPICEKVAK 108
Cdd:PLN02183   38 PPGPKGLPIIGNMLMMDQLTHR-GLANLAKQYGGLFHMRMGYLHMVAVSSPEVARQVLQVQDSVFSNRpANIAISYLTYD 116
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642105 109 GQGIAFSH-GNVWKATRHFTVKTLrnLGMGKGTIEDKVQEEAKWLVKELKKTNGSP 163
Cdd:PLN02183  117 RADMAFAHyGPFWRQMRKLCVMKL--FSRKRAESWASVRDEVDSMVRSVSSNIGKP 170
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
61-156 6.41e-06

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: 46.81  E-value: 6.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  61 YGPVYTLYVGSQPTVVLHGYEALKEALVDHgEEFSGRGRLP--ICEKVAKGQGIAFSHGNVWKATR-----HFTVKTLRN 133
Cdd:COG2124    31 YGPVFRVRLPGGGAWLVTRYEDVREVLRDP-RTFSSDGGLPevLRPLPLLGDSLLTLDGPEHTRLRrlvqpAFTPRRVAA 109
                          90       100
                  ....*....|....*....|...
gi 1958642105 134 LgmgkgtiEDKVQEEAKWLVKEL 156
Cdd:COG2124   110 L-------RPRIREIADELLDRL 125
PLN02290 PLN02290
cytokinin trans-hydroxylase
32-275 7.28e-05

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 44.03  E-value: 7.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  32 GPTPLPIIGNFFQV----------DMKDIRQSLTN--------FSKTYGPVYTLYVGSQPTVVLHGYEALKEALVDHGEE 93
Cdd:PLN02290   46 GPKPRPLTGNILDVsalvsqstskDMDSIHHDIVGrllphyvaWSKQYGKRFIYWNGTEPRLCLTETELIKELLTKYNTV 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  94 fSGRGRLPicEKVAK---GQGIAFSHGNVWKATRHFTVKTLrnlgMG---KGTIEDKVqEEAKWLVKELKKTNGSPCDpQ 167
Cdd:PLN02290  126 -TGKSWLQ--QQGTKhfiGRGLLMANGADWYHQRHIAAPAF----MGdrlKGYAGHMV-ECTKQMLQSLQKAVESGQT-E 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 168 FIMGCAPGNVICCIILQNRFD--YED-KDFLNLIEKVN----EAVKIISSPGIQVFnifpilldycPGNHNIYLKNY-TW 239
Cdd:PLN02290  197 VEIGEYMTRLTADIISRTEFDssYEKgKQIFHLLTVLQrlcaQATRHLCFPGSRFF----------PSKYNREIKSLkGE 266
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958642105 240 VKSYLLEKIKEHEESLDVSNPRDFIDYFL-IERNQME 275
Cdd:PLN02290  267 VERLLMEIIQSRRDCVEIGRSSSYGDDLLgMLLNEME 303
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
59-275 1.18e-04

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: 43.23  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  59 KTYGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEK-VAKGQGIAFS-HGNVWKATRH------FTVKT 130
Cdd:cd11074     1 KKFGDIFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDIfTGKGQDMVFTvYGEHWRKMRRimtvpfFTNKV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 131 LRNLGMGkgtiedkVQEEAKWLVKELKK-----TNGSPCDP--QFIMgcapGNVICCIILQNRFDYEDKDFLNLIEKVN- 202
Cdd:cd11074    81 VQQYRYG-------WEEEAARVVEDVKKnpeaaTEGIVIRRrlQLMM----YNNMYRIMFDRRFESEDDPLFVKLKALNg 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642105 203 EAVKIISSPGIQVFNIFPILLDYCPGnhniYLKnytwvksyLLEKIKEHEESLdvsnprdFIDYFLIERNQME 275
Cdd:cd11074   150 ERSRLAQSFEYNYGDFIPILRPFLRG----YLK--------ICKEVKERRLQL-------FKDYFVDERKKLG 203
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
28-218 1.70e-04

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 42.53  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105  28 KLPPGPTPLPIIGNF-FQVDMKDIrqSLTNFSKTYGPVYTLYVGSQPTVVLHGYEALKEALVDHGEEFSGRGRLPICEKV 106
Cdd:PLN00110   31 KLPPGPRGWPLLGALpLLGNMPHV--ALAKMAKRYGPVMFLKMGTNSMVVASTPEAARAFLKTLDINFSNRPPNAGATHL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642105 107 AKG-QGIAFS-HGNVWKATRHftvktLRNLGM-GKGTIEDKVQEEAKWLVKELK-----KTNGSPCDPQFIMGCAPGNVI 178
Cdd:PLN00110  109 AYGaQDMVFAdYGPRWKLLRK-----LSNLHMlGGKALEDWSQVRTVELGHMLRamlelSQRGEPVVVPEMLTFSMANMI 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1958642105 179 CCIILQNRF----DYEDKDFLNLIekvneaVKIISSPGIqvFNI 218
Cdd:PLN00110  184 GQVILSRRVfetkGSESNEFKDMV------VELMTTAGY--FNI 219
 
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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