ID A0A1D5PVC3_CHICK Unreviewed; 197 AA.
AC A0A1D5PVC3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Methylated-DNA--protein-cysteine methyltransferase {ECO:0000256|ARBA:ARBA00015377};
DE EC=2.1.1.63 {ECO:0000256|ARBA:ARBA00011918};
DE AltName: Full=6-O-methylguanine-DNA methyltransferase {ECO:0000256|ARBA:ARBA00030795};
DE AltName: Full=O-6-methylguanine-DNA-alkyltransferase {ECO:0000256|ARBA:ARBA00031621};
GN Name=MGMT {ECO:0000313|Ensembl:ENSGALP00010001568.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00010001568.1, ECO:0000313|Proteomes:UP000000539};
RN [1] {ECO:0000313|Ensembl:ENSGALP00010001568.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010001568.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Involved in the cellular defense against the biological
CC effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in
CC DNA. Repairs the methylated nucleobase in DNA by stoichiometrically
CC transferring the methyl group to a cysteine residue in the enzyme. This
CC is a suicide reaction: the enzyme is irreversibly inactivated.
CC {ECO:0000256|ARBA:ARBA00003317}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a
CC thymidine in DNA + S-methyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:53428, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132,
CC Rhea:RHEA-COMP:13555, Rhea:RHEA-COMP:13556, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:82612, ChEBI:CHEBI:137386, ChEBI:CHEBI:137387;
CC EC=2.1.1.63; Evidence={ECO:0000256|ARBA:ARBA00001286};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein]
CC = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:24000, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132,
CC Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:11368, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:82612, ChEBI:CHEBI:85445, ChEBI:CHEBI:85448; EC=2.1.1.63;
CC Evidence={ECO:0000256|ARBA:ARBA00001596};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MGMT family.
CC {ECO:0000256|ARBA:ARBA00008711}.
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DR AlphaFoldDB; A0A1D5PVC3; -.
DR Ensembl; ENSGALT00010003037.1; ENSGALP00010001568.1; ENSGALG00010001308.1.
DR VEuPathDB; HostDB:geneid_423965; -.
DR GeneTree; ENSGT00390000015799; -.
DR Proteomes; UP000000539; Chromosome 6.
DR Bgee; ENSGALG00000042949; Expressed in heart and 14 other cell types or tissues.
DR ExpressionAtlas; A0A1D5PVC3; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006304; P:DNA modification; IEA:UniProt.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd06445; ATase; 1.
DR Gene3D; 3.30.160.70; Methylated DNA-protein cysteine methyltransferase domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR001497; MethylDNA_cys_MeTrfase_AS.
DR InterPro; IPR014048; MethylDNA_cys_MeTrfase_DNA-bd.
DR InterPro; IPR036217; MethylDNA_cys_MeTrfase_DNAb.
DR InterPro; IPR008332; MethylG_MeTrfase_N.
DR InterPro; IPR036631; MGMT_N_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00589; ogt; 1.
DR PANTHER; PTHR46460; METHYLATED-DNA--PROTEIN-CYSTEINE METHYLTRANSFERASE; 1.
DR PANTHER; PTHR46460:SF1; METHYLATED-DNA--PROTEIN-CYSTEINE METHYLTRANSFERASE; 1.
DR Pfam; PF01035; DNA_binding_1; 1.
DR Pfam; PF02870; Methyltransf_1N; 1.
DR SUPFAM; SSF53155; Methylated DNA-protein cysteine methyltransferase domain; 1.
DR SUPFAM; SSF46767; Methylated DNA-protein cysteine methyltransferase, C-terminal domain; 1.
DR PROSITE; PS00374; MGMT; 1.
PE 1: Evidence at protein level;
KW DNA damage {ECO:0000256|ARBA:ARBA00023204};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A1D5PVC3};
KW Reference proteome {ECO:0000313|Proteomes:UP000000539};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 24..104
FT /note="Methylguanine DNA methyltransferase ribonuclease-
FT like"
FT /evidence="ECO:0000259|Pfam:PF02870"
FT DOMAIN 112..189
FT /note="Methylated-DNA-[protein]-cysteine S-
FT methyltransferase DNA binding"
FT /evidence="ECO:0000259|Pfam:PF01035"
SQ SEQUENCE 197 AA; 21708 MW; D15BAAD4A1D47E1C CRC64;
MASRRVPKMT SKEGTSQCQE KHAVLLSPVG KLEISGCETG VHEIKLPRLS VLPNGTEAAM
RCELSGSVTS MPEPLQQCAA WLNAYFCEPS RTEQLPLPPF HHPMLQQDSF TKEVLWTLLR
EVKFGEAISY QQLAERAGNS RAARAVGGAM RSNPIPIIIP CHRVICSSGQ IGNYGGGNVM
KEWLLSHEKL QKEKLAD
//
