ID B0VVF7_ACIBS Unreviewed; 390 AA.
AC B0VVF7;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=site-specific DNA-methyltransferase (cytosine-N(4)-specific) {ECO:0000256|ARBA:ARBA00012185};
DE EC=2.1.1.113 {ECO:0000256|ARBA:ARBA00012185};
GN ORFNames=ABSDF_p30013 {ECO:0000313|EMBL:CAP02987.1};
OS Acinetobacter baumannii (strain SDF).
OG Plasmid p3ABSDF {ECO:0000313|EMBL:CAP02987.1,
OG ECO:0000313|Proteomes:UP000001741}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509170 {ECO:0000313|EMBL:CAP02987.1, ECO:0000313|Proteomes:UP000001741};
RN [1] {ECO:0000313|EMBL:CAP02987.1, ECO:0000313|Proteomes:UP000001741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDF {ECO:0000313|EMBL:CAP02987.1,
RC ECO:0000313|Proteomes:UP000001741};
RC PLASMID=p3ABSDF {ECO:0000313|Proteomes:UP000001741};
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(2008).
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; CU468233; CAP02987.1; -; Genomic_DNA.
DR AlphaFoldDB; B0VVF7; -.
DR REBASE; 17289; M1.AbaSORF13P.
DR KEGG; abm:ABSDF_p30013; -.
DR HOGENOM; CLU_027633_1_1_6; -.
DR Proteomes; UP000001741; Plasmid p3ABSDF.
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; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00093; N4_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:CAP02987.1}; Plasmid {ECO:0000313|EMBL:CAP02987.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAP02987.1}.
FT DOMAIN 32..105
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
SQ SEQUENCE 390 AA; 44310 MW; F5704CFE97B93E15 CRC64;
MVCVNNLNLF EESNCNLVKD LDIKSQLNNI DWSFANREKA HPIESLHPYP AKFIGELPRS
LIKTFNNGLP VLDPFAGSGT TLMEAQRLGL EAVGIDLNPI ACLITKVKTS ATPAKLLEHA
DDIVMSAQGR FSELELDIPN IDHWFKKDIQ EAIVVLLEEI QKFKDDEGLF NVLRLSLSSI
LVKVSNQDSD TRYAAVEKNI TAKDVFSNFL NAVKKIHKSL LARTWTLKDV QLIHANTLEV
KAEDFKKDIG MVVTSPPYPN AYEYWLYHKY RMWWLGFDPL KVKEKEIGAR AHFFKKNAHT
EENFWHQMDG TFDLIDNVLV DKGYTAFVIG RSKIKGKIID NADIIQDVAS QHGYTETARI
ERVIASKSKS FNPSYGNIKT ETVLVLQKQK
//
