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Database: UniProt
Entry: M0JJ62_9EURY
LinkDB: M0JJ62_9EURY
Original site: M0JJ62_9EURY 
ID   M0JJ62_9EURY            Unreviewed;       308 AA.
AC   M0JJ62;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   ORFNames=C436_19493 {ECO:0000313|EMBL:EMA09177.1}, KDQ40_17265
GN   {ECO:0000313|EMBL:QUJ74205.1};
OS   Haloarcula sinaiiensis ATCC 33800.
OG   Plasmid pHsi540 {ECO:0000313|EMBL:QUJ74205.1,
OG   ECO:0000313|Proteomes:UP000682967}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=662476 {ECO:0000313|EMBL:EMA09177.1, ECO:0000313|Proteomes:UP000011659};
RN   [1] {ECO:0000313|EMBL:EMA09177.1, ECO:0000313|Proteomes:UP000011659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33800 {ECO:0000313|EMBL:EMA09177.1,
RC   ECO:0000313|Proteomes:UP000011659};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
RN   [2] {ECO:0000313|EMBL:QUJ74205.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 33800 {ECO:0000313|EMBL:QUJ74205.1};
RC   PLASMID=pHsi540 {ECO:0000313|EMBL:QUJ74205.1};
RA   Fomenkov A., DasSarma P., DasSarma S., Roberts R.J.;
RT   "Complete Genome sequence and Methylome Analysis of the Haloarchaeon
RT   Haloarcula sinaiiensis.";
RL   Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC         COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC         Evidence={ECO:0000256|ARBA:ARBA00001279};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594}.
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DR   EMBL; AOLR01000051; EMA09177.1; -; Genomic_DNA.
DR   EMBL; CP073368; QUJ74205.1; -; Genomic_DNA.
DR   RefSeq; WP_004966496.1; NZ_CP073368.1.
DR   AlphaFoldDB; M0JJ62; -.
DR   GeneID; 64824743; -.
DR   KEGG; hsin:KDQ40_17265; -.
DR   PATRIC; fig|662476.7.peg.3883; -.
DR   OrthoDB; 372040at2157; -.
DR   Proteomes; UP000011659; Unassembled WGS sequence.
DR   Proteomes; UP000682967; Plasmid pHsi540.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   Gene3D; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR012263; M_m6A_EcoRV.
DR   InterPro; IPR012327; MeTrfase_D12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00571; dam; 1.
DR   PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR   PANTHER; PTHR30481:SF3; DNA ADENINE METHYLASE; 1.
DR   Pfam; PF02086; MethyltransfD12; 1.
DR   PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR   PRINTS; PR00505; D12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EMA09177.1}; Plasmid {ECO:0000313|EMBL:QUJ74205.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:QUJ74205.1}.
FT   REGION          79..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..98
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   308 AA;  35049 MW;  7761DC2E908EE657 CRC64;
     MAAPVLKWAG GKRQLLDELQ SRFPKEYNHF HEPFLGGGAL FFELEPEDGT INDTNTRLIN
     FYRQVRDNPE ELIDKLESFD DPESKVNPDN DYSETSHTGR EIKNYYYQQR ARFNKRPYGE
     SFDPLTEAAL LMYLNRTCYN GLYRENNSGG YNVPIGDFTD PDWVQHERIH KASTVLTGTD
     IRNDDFTYIL DAAEPGDLVY FDPPYKPMSS TAYFTDYSAD GFDQDDQKRL LEVVQTLAEQ
     DVHVIVSNSG VMYEMYEDAG LQVDKEGATR AINSDGDSRG EVDEIIATTV EPANRATKGQ
     TSLGQYNS
//
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