GenomeNet

Database: UniProt
Entry: S2F6T5_9PSED
LinkDB: S2F6T5_9PSED
Original site: S2F6T5_9PSED 
ID   S2F6T5_9PSED            Unreviewed;       833 AA.
AC   S2F6T5;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-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=PG5_15330 {ECO:0000313|EMBL:EPA97804.1};
OS   Pseudomonas sp. G5(2012).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1268068 {ECO:0000313|EMBL:EPA97804.1, ECO:0000313|Proteomes:UP000014290};
RN   [1] {ECO:0000313|EMBL:EPA97804.1, ECO:0000313|Proteomes:UP000014290}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G5(2012) {ECO:0000313|Proteomes:UP000014290};
RA   Park S., Lee J.-H., Cho Y.-J., Chun J., Hur H.-G.;
RT   "Draft Genome Sequence of Pseudomonas sp. Strain G5, Isolated from a
RT   Traditional Indigo Fermentation Dye Vat.";
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:EPA97804.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; APIO01000025; EPA97804.1; -; Genomic_DNA.
DR   RefSeq; WP_020796508.1; NZ_APIO01000025.1.
DR   AlphaFoldDB; S2F6T5; -.
DR   PATRIC; fig|1268068.3.peg.1461; -.
DR   eggNOG; COG0286; Bacteria.
DR   Proteomes; UP000014290; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 1.20.1260.30; -; 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   InterPro; IPR038333; T1MK-like_N_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   Hydrolase {ECO:0000313|EMBL:EPA97804.1};
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          8..149
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          163..487
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   REGION          696..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..723
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   833 AA;  93681 MW;  C96BA19B770C06B2 CRC64;
     MPLTLPQLER HLFKAADILR GKMDASEFKE YIFGMLFLKR CSDMFEQRRE EVIRLEMEGG
     KSKVQAQVSS EISRWYKIEG SFWVPPQSRY EFLLNDAHQN VGDFLNKALT GIETANTSLY
     DVLEHIDFTR KVGQSKISDI KLRQLITHFG VFRLRNEDFE FPDLLGAAYE YLIGEFADSA
     GKKGGEFYTP RSVVRMMVRL IKPELKHDIY DPCCGSGGML IAAKEYIDEH GEDGRKANLF
     GQEFNGTVWS IAKMNMLLHG ISNADLHNED TLAEPQHVEG GELKHFDRVL TNPPFSIQWG
     NTEKDADGKP AWKPKFEAER FSYGQVPLGA KKADMMFLQH MLAVTRDGGM VATVLPHGVL
     FRGGEERIIR KGIIEDDLLE AVIGVAPNLF YGTSIPACIL VLRQRVQKGA NRVSGKPTER
     RGKVLFINAD RELFEGRAQN YLLPEHIEKI VTTFDEFRAI DGFSAIVDYA TLKANDYNLN
     IRRYADNSPP PEPHDVRAHL VGGIPKAEVA DKAGLFSAHG LNPMDLLVER EAKYLDFAPV
     LDKRQALKPT IESNSGLVAK EAAIRTAFEE WWQTHSARIT ALSGQMDNAA SLVALRNELL
     ASFSQSLETV GLLNPFQVRG IVAGFWYQTK YDFLTLMARG AKGVADAWRT SIVTALEDKA
     SKESPLEHKL VKFLMSDFVE VITELEAKKA ELDSQIKAAS PKDVEGEDGE TVEAGEHEAD
     EESVVDEAQL KAWKKELTAI KKQLKAKNDS FKQHINTAVK GLAPEAADDL LLTILHNDMQ
     TIVERYMAAQ RKEIVASFEN WWDKYRMTLT EIEGKRDAAA KALQGFLKGL RYV
//
DBGET integrated database retrieval system