ID N9R0H4_9GAMM Unreviewed; 430 AA.
AC N9R0H4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=F890_00226 {ECO:0000313|EMBL:ENX32662.1};
OS Acinetobacter sp. CIP 64.7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1144673 {ECO:0000313|EMBL:ENX32662.1, ECO:0000313|Proteomes:UP000013258};
RN [1] {ECO:0000313|EMBL:ENX32662.1, ECO:0000313|Proteomes:UP000013258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 64.7 {ECO:0000313|EMBL:ENX32662.1,
RC ECO:0000313|Proteomes:UP000013258};
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 sp. CIP 64.7.";
RL Submitted (FEB-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:ENX32662.1}.
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DR EMBL; APRY01000018; ENX32662.1; -; Genomic_DNA.
DR RefSeq; WP_004732518.1; NZ_KB850177.1.
DR AlphaFoldDB; N9R0H4; -.
DR PATRIC; fig|1144673.3.peg.208; -.
DR HOGENOM; CLU_034356_0_0_6; -.
DR OrthoDB; 9805629at2; -.
DR Proteomes; UP000013258; 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;
SQ SEQUENCE 430 AA; 48668 MW; 492A6E9258753264 CRC64;
MSSESTVYHK RRHAARTTDE YLFHQLVPYL GNKRRLLHLI LEALESTGTL KRSDGRAPIF
ADFFAGSGVV SRLARQNGYR VIANDWEPYS HALNHAVLAC TEAPAFKELG GYQKAIDYLN
RLPEVKGWVT HNLCPRNDEI YDPARDRLFF KRRNGMRIDA IRQQIAAWQA QGAIDDVEMS
ALLAPLLYSA SFVSNTSGVF KSFHHGWGGK TQTALERIES LLWLTPSRFC ESDQKKGMAA
EMWCVDAQHL ANQMNGFEVD VAYLDPPYNQ HAYSSNYHVL NALTLWDQAD LPTPDTKGFK
SGIDRAWRKE RPSQYNSSKY AKEAYESLLA TINARFILTS YSTDGNISAT DLLQANLKRG
RVTLLTQDVP RYRVSKQRQS ERARVLEFIV ITDTHAKSGP PIRQLLSQLH HYAELGGVDT
TGVSTQLALW
//
