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Database: UniProt
Entry: G0LKS9_HALWC
LinkDB: G0LKS9_HALWC
Original site: G0LKS9_HALWC 
ID   G0LKS9_HALWC            Unreviewed;       284 AA.
AC   G0LKS9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Type II methyltransferase {ECO:0000256|RuleBase:RU362026};
DE            EC=2.1.1.113 {ECO:0000256|RuleBase:RU362026};
DE   AltName: Full=N-4 cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU362026};
GN   OrderedLocusNames=Hqrw_2138 {ECO:0000313|EMBL:CCC40037.1};
OS   Haloquadratum walsbyi (strain DSM 16854 / JCM 12705 / C23).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=768065 {ECO:0000313|EMBL:CCC40037.1, ECO:0000313|Proteomes:UP000007954};
RN   [1] {ECO:0000313|EMBL:CCC40037.1, ECO:0000313|Proteomes:UP000007954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16854 / JCM 12705 / C23
RC   {ECO:0000313|Proteomes:UP000007954};
RX   PubMed=21701686; DOI=10.1371/journal.pone.0020968;
RA   Dyall-Smith M., Pfeiffer F., Klee K., Palm P., Gross K., Schuster S.C.,
RA   Rampp M., Oesterhelt D.;
RT   "Haloquadratum walsbyi: limited diversity in a global pond.";
RL   PLoS ONE 6:E20968-E20968(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC         Evidence={ECO:0000256|ARBA:ARBA00001893,
CC         ECO:0000256|RuleBase:RU362026};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC       subfamily. {ECO:0000256|ARBA:ARBA00010203}.
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DR   EMBL; FR746099; CCC40037.1; -; Genomic_DNA.
DR   RefSeq; WP_014555762.1; NC_017459.1.
DR   AlphaFoldDB; G0LKS9; -.
DR   REBASE; 36620; M.HwaC23ORF2138P.
DR   GeneID; 12446872; -.
DR   KEGG; hwc:Hqrw_2138; -.
DR   HOGENOM; CLU_024927_2_2_2; -.
DR   OMA; LWNFSGE; -.
DR   OrthoDB; 38200at2157; -.
DR   Proteomes; UP000007954; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR002941; DNA_methylase_N4/N6.
DR   InterPro; IPR017985; MeTrfase_CN4_CS.
DR   InterPro; IPR001091; RM_Methyltransferase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR13370:SF32; DNA ADENINE METHYLTRANSFERASE YHDJ; 1.
DR   PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00093; N4_MTASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU362026};
KW   Restriction system {ECO:0000256|RuleBase:RU362026};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU362026};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCC40037.1}.
FT   DOMAIN          30..269
FT                   /note="DNA methylase N-4/N-6"
FT                   /evidence="ECO:0000259|Pfam:PF01555"
SQ   SEQUENCE   284 AA;  33380 MW;  93C6063A08FD1268 CRC64;
     MEEYELSNGV IHRGDCLDGL RELAEDAITL GFTSPPYFNA VNYEEHVEKV HGNTDHWERE
     EMSYDDYQDF LIKRFEEVFR VTRPGGHTIV NISPVHWEDE RVALPFHLVG WMEDIGWTFK
     EDIIWEKPVA KDRRSGVLLQ NPYPGYYYPS VVAEYVLVFQ KEADDENKNN IYWNRTEEEK
     TKNEISLDDY QGEKSKNVWK IRQVAPGENE HPAPFPRELA ERVIQFYSYQ DDTVMDIFAG
     SGQTLLAAQD LDREFIGFET QHEYVEYAKD RVIDESSQMT LEDI
//
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