ID V2TKX7_9GAMM Unreviewed; 432 AA.
AC V2TKX7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=P256_01955 {ECO:0000313|EMBL:ESK38416.1};
OS Acinetobacter nectaris CIP 110549.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1392540 {ECO:0000313|EMBL:ESK38416.1, ECO:0000313|Proteomes:UP000023785};
RN [1] {ECO:0000313|EMBL:ESK38416.1, ECO:0000313|Proteomes:UP000023785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110549 {ECO:0000313|EMBL:ESK38416.1,
RC ECO:0000313|Proteomes:UP000023785};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C.,
RA Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter nectaris CIP 110549.";
RL Submitted (OCT-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 -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
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:ESK38416.1}.
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DR EMBL; AYER01000007; ESK38416.1; -; Genomic_DNA.
DR RefSeq; WP_023273573.1; NZ_KI530734.1.
DR AlphaFoldDB; V2TKX7; -.
DR STRING; 1392540.P256_01955; -.
DR PATRIC; fig|1392540.3.peg.1885; -.
DR eggNOG; COG3392; Bacteria.
DR HOGENOM; CLU_034356_0_0_6; -.
DR OrthoDB; 9805629at2; -.
DR Proteomes; UP000023785; Unassembled WGS sequence.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF02086; MethyltransfD12; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000023785}.
SQ SEQUENCE 432 AA; 48968 MW; E58E2CFFA6F2E538 CRC64;
MSSETTVYHK RRHAARTTDE YLFHQLVPYL GNKRRLLHLI LEALEMTGTL NTDGKKKRAP
IFADFFAGSG VVSRLARQNG YRVIANDWEP YSHALNHAIL SCVEAPAFKE LGGYQKAIDY
LNRLPLAKGW VTHNLCPRND EEYDPARDRL FFKRRNGMRI DAIRQQIATW QAEGAIDDVE
MSALLAPLLY SASFVSNTSG VFKSFHHGWG GKTQTALERI ESLLWLTPSR FCEIGRPNQA
AAEMWCVDAQ HLANQMSDFE VDVAYLDPPY NQHAYSSNYH VLNSLTLWDQ TDLPSPDTKG
FKSGIDRAWR KERPSLYNSS KYAKEAYEKL LATVNARFIL TSYSTDGNIS ATDLLKANLE
RGKVTLLTQD VPRYRVSKQR QSERARVLEF IVITDTKAKS GPPLRQLLGQ LYHYAELGGV
DTTGVSSQLA LW
//
