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Database: UniProt
Entry: R9B473_9GAMM
LinkDB: R9B473_9GAMM
Original site: R9B473_9GAMM 
ID   R9B473_9GAMM            Unreviewed;       545 AA.
AC   R9B473;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
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=I593_02073 {ECO:0000313|EMBL:EOR07186.1};
OS   Acinetobacter tandoii DSM 14970 = CIP 107469.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1120927 {ECO:0000313|EMBL:EOR07186.1, ECO:0000313|Proteomes:UP000016201};
RN   [1] {ECO:0000313|EMBL:EOR07186.1, ECO:0000313|Proteomes:UP000016201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 107469 {ECO:0000313|EMBL:EOR07186.1,
RC   ECO:0000313|Proteomes:UP000016201};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter tandoii CIP 107469.";
RL   Submitted (MAR-2013) 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   -!- 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:EOR07186.1}.
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DR   EMBL; AQFM01000037; EOR07186.1; -; Genomic_DNA.
DR   RefSeq; WP_016167126.1; NZ_KE007366.1.
DR   AlphaFoldDB; R9B473; -.
DR   PATRIC; fig|1120927.3.peg.2010; -.
DR   eggNOG; COG0286; Bacteria.
DR   OrthoDB; 9784823at2; -.
DR   Proteomes; UP000016201; 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:0009007; F:site-specific DNA-methyltransferase (adenine-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; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          180..497
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   COILED          499..533
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   545 AA;  62345 MW;  E4519962FC3EF728 CRC64;
     MVEIQFQQKV RELIDGLKAI CANYGLGNDG NEFKIITQAF LYKFLNDKFA YEAKKVEPSL
     AEAEKWEDVL SNMSEDELEM LALQMPADTA ILKPQHFISY LFSQQNEPDF SKLFDDTLRD
     ISIQNNEIFA VQTDGGAKIK LFDELSQFIS DPSKRDEFCK AIINELVEFS FERIFDQKFD
     FYASIFEYLV KDYNSNSGGK YAEYYTPHAV ARIMAEILVP KDMQGQVKNV TCYDPAAGSG
     TLLMNVAHVI GETRCAIYTQ DISQKSSNLL RLNLILNNLV HSIPNVIQGN TMLHPYHKDG
     SELKKFDYIV SNPPFKLDFS DFRDNLDTKV NKERFFAGIP KIKPKDTDKM EIYQLFLQHI
     IFSLKENGKA AVVVPTGFIS AQSGIDRNIR EHLIKNKMLA GVISMPSNIF ATTGTNVSII
     FIDATNKEKV ILIDASNLGD KVKEGKNQKT LLTLEEEMQI IELFNSKTEK DRFSVLVEYD
     EIEAKNYSLS AGQYFDIKIE FSELTNEDFN LKLKEYEKDL DALFLQSREL EKELKKQLSS
     LSYDH
//
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