ID Q7VHC9_HELHP Unreviewed; 411 AA.
AC Q7VHC9;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Methyltransferase {ECO:0000256|RuleBase:RU362026};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU362026};
GN OrderedLocusNames=HH_1038 {ECO:0000313|EMBL:AAP77635.1};
OS Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=235279 {ECO:0000313|EMBL:AAP77635.1, ECO:0000313|Proteomes:UP000002495};
RN [1] {ECO:0000313|EMBL:AAP77635.1, ECO:0000313|Proteomes:UP000002495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51449 / 3B1 {ECO:0000313|Proteomes:UP000002495};
RX PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA Shen Z., Weber J., Frosch M., Fox J.G.;
RT "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT hepaticus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
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}.
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DR EMBL; AE017125; AAP77635.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7VHC9; -.
DR STRING; 235279.HH_1038; -.
DR REBASE; 7195; M.HheORF1038P.
DR KEGG; hhe:HH_1038; -.
DR eggNOG; COG0863; Bacteria.
DR HOGENOM; CLU_027633_2_0_7; -.
DR OrthoDB; 8901552at2; -.
DR Proteomes; UP000002495; 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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
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; 2.
DR PRINTS; PR00508; S21N4MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR PROSITE; PS00093; N4_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:AAP77635.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002495};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAP77635.1}.
FT DOMAIN 31..84
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
FT DOMAIN 263..372
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
SQ SEQUENCE 411 AA; 48059 MW; 03D1D7DA150F7C40 CRC64;
MGNSSILSDE INTNDYKQYF CRDFSKIHQI TAYLAMFPPN LPYHFIKKYS QKGDLVFDPF
SGRGTTAFEA CRMGRKGIGN DLNPLAVCLT KSKIDIPKKH NIQKRLEKLK QDFTTTRITN
KQIKNISDDI KMLYEESETL PQLVYLKNNL NKNRKIDNFI LAVLTGIMHG KHRKDGTSIY
CSIDMPNTFS MSPNYIRNFI AKHHLKKIKQ NVFELLQQRI EHLFQNQTKE FQSLDSYQKG
DCFNKDAIKS TKKIIKKYGE NSVQLIITSP PYLKNINYGK YNWIRLWLLN KEVKEVDKNV
SIYHNMQKIK GLKDNLAFEN YAKYMQELFK SWEKILKPKS YAFVVIGDID KRNLAKDTWD
YIQNNGGCKL RLKHIAEDVI ANDKEKKVTR IWGAKKGKAT KIDRILVLQK E
//
