ID E7G370_9HELI Unreviewed; 391 AA.
AC E7G370;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Methyltransferase {ECO:0000256|RuleBase:RU362026};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU362026};
GN ORFNames=HSUHS5_0378 {ECO:0000313|EMBL:EFX42183.1};
OS Helicobacter suis HS5.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=710394 {ECO:0000313|EMBL:EFX42183.1, ECO:0000313|Proteomes:UP000054093};
RN [1] {ECO:0000313|EMBL:EFX42183.1, ECO:0000313|Proteomes:UP000054093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS5 {ECO:0000313|EMBL:EFX42183.1,
RC ECO:0000313|Proteomes:UP000054093};
RX PubMed=21414191; DOI=10.1186/1297-9716-42-51;
RA Vermoote M., Vandekerckhove T.T., Flahou B., Pasmans F., Smet A.,
RA De Groote D., Van Criekinge W., Ducatelle R., Haesebrouck F.;
RT "Genome sequence of Helicobacter suis supports its role in gastric
RT pathology.";
RL Vet. Res. 42:51-51(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 -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC subfamily. {ECO:0000256|ARBA:ARBA00010203}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFX42183.1}.
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DR EMBL; ADHO01000061; EFX42183.1; -; Genomic_DNA.
DR RefSeq; WP_006564106.1; NZ_ADHO01000061.1.
DR AlphaFoldDB; E7G370; -.
DR Proteomes; UP000054093; Unassembled WGS sequence.
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 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 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 Methyltransferase {ECO:0000313|EMBL:EFX42183.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054093};
KW Transferase {ECO:0000313|EMBL:EFX42183.1}.
FT DOMAIN 160..382
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
SQ SEQUENCE 391 AA; 45908 MW; 9D2296AC3792C30B CRC64;
MNNPTKKSKS LFEPLTIEFI KKLGAEKSDT NLYLLMELFK KDGVEIGIKR EIVSSIGRQK
DNDAIFAFLN QEALKGWCVD ICCQMLRTCL YKAKQDSRFI ALRDKILKHY DNEVMHKMVA
YHEFRQNKHS LKKQSPQIKR PTLLVGDNRL TLNKIRQGQI QLVFTSPPYY NARTYSSYKN
YKEYLKQMQE SLAQAYRILE EGRFIIINVS PVIVKRAGRE FESIRYPIHF DFHSILVQSG
FYFIDEIIWI KPEVCVPNRI AGYLQTKRPL SYKPNCITES LLVYRKNTPF LLDRNMKRYN
KRLKNDGAVD STNCWFITPK SDKDHPAVFP EELVARVLRY YSFEGDVVCD PFAGSGTLAR
VAQRMKRIAL LCEQNEEFVK RLKREGFFEL R
//