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Database: UniProt
Entry: U1JMK0_9GAMM
LinkDB: U1JMK0_9GAMM
Original site: U1JMK0_9GAMM 
ID   U1JMK0_9GAMM            Unreviewed;       825 AA.
AC   U1JMK0;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=PCIT_14159 {ECO:0000313|EMBL:ERG17885.1};
OS   Pseudoalteromonas citrea DSM 8771.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1117314 {ECO:0000313|EMBL:ERG17885.1, ECO:0000313|Proteomes:UP000016487};
RN   [1] {ECO:0000313|EMBL:ERG17885.1, ECO:0000313|Proteomes:UP000016487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8771 {ECO:0000313|Proteomes:UP000016487};
RX   PubMed=22535931; DOI=10.1128/JB.00265-12;
RA   Xie B.B., Shu Y.L., Qin Q.L., Rong J.C., Zhang X.Y., Chen X.L., Shi M.,
RA   He H.L., Zhou B.C., Zhang Y.Z.;
RT   "Genome sequences of type strains of seven species of the marine bacterium
RT   Pseudoalteromonas.";
RL   J. Bacteriol. 194:2746-2747(2012).
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:ERG17885.1}.
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DR   EMBL; AHBZ02000147; ERG17885.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1JMK0; -.
DR   STRING; 1117314.PCIT_14159; -.
DR   eggNOG; COG0286; Bacteria.
DR   OrthoDB; 9784823at2; -.
DR   Proteomes; UP000016487; 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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR022749; D12N6_MeTrfase_N.
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; SLR6095 PROTEIN; 1.
DR   PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 1.
DR   Pfam; PF12161; HsdM_N; 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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:ERG17885.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016487};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ERG17885.1}.
FT   DOMAIN          9..149
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          177..490
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   825 AA;  93613 MW;  DC1061EA2E44A821 CRC64;
     MDHSAHNKLI SFIWSIADDC LRDVYVRGKY RDVILPMVVL RRLDTLLEPT KKAVLDEVKF
     QVEEMEATEL DDAPLIDAAG YVFYNTSKWT LTSIKETATN NRQIILANIE EYLNGFSANV
     KEIIECFNLK SQFQHMAGKD VLLDVLEKFV SPTINLTPDE VEDPEGNKLP ALSNLGMGYV
     FEELIRKFNE DNNEEAGEHF TPREVIELMT HLVFDPIKSD LPLTLTVYDP ACGSGGMLTE
     TQNFINENYP VENTTRDINL YGKEINDETY AICKSDMMIK GNDPKNIKVG STLSTDEFAG
     QRFDFCLSNP PYGKSWASEQ KHIKEGSDVI DSRFQVVLKD YWGNLPKEGF VDATPRSSDG
     QLLFLMEMVS KMKSIATSPL GSRIASVHNG SSLFTGDAGS GESNIRRYII ENDMLDAIVQ
     LPNNLFYNTG ITTYIWLLNN SKPDQRKGKV QLIDASLLFK KLRKNLGNKN CEFSPEHITE
     ITQTYLDAAS VERQLTQEKG PTGIAAKVFN NDDFGYYKVN IERPDRRSAQ FKDDLIAPLR
     FDKTLREPME HLYVEYGDKV YQADFFTADN KAMEKDVIAW CEDNDINLNA KAKAKLLATD
     TWLNGKLLVE LANKLAETII AEYNDYNLFK ADVEAQFKQI SADVLADIKP NKRKAFYITV
     VNAMSWYDEN AEKVIKKVVK FKQDKLDELL HHLGCEQAGS LSEVMADFGY YAIEDKKLEF
     TTYESNSDLR DAESVPLTYN EGNDSDNSEI HQYFLDEVQP HVSEAWINLD STKIGYEISF
     NKYFYQHKPL RAMDEVATDI INLEQKAEGL IADILGVDIA KVHGA
//
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