ID C9MPH0_9BACT Unreviewed; 683 AA.
AC C9MPH0;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=HMPREF0973_01511 {ECO:0000313|EMBL:EEX18567.1};
OS Prevotella veroralis F0319.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=649761 {ECO:0000313|EMBL:EEX18567.1, ECO:0000313|Proteomes:UP000003327};
RN [1] {ECO:0000313|EMBL:EEX18567.1, ECO:0000313|Proteomes:UP000003327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0319 {ECO:0000313|EMBL:EEX18567.1,
RC ECO:0000313|Proteomes:UP000003327};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) 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:EEX18567.1}.
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DR EMBL; ACVA01000033; EEX18567.1; -; Genomic_DNA.
DR AlphaFoldDB; C9MPH0; -.
DR STRING; 649761.HMPREF0973_01511; -.
DR eggNOG; COG0286; Bacteria.
DR HOGENOM; CLU_015410_1_0_10; -.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000003327; 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:0006306; P:DNA methylation; IEA:InterPro.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
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; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EEX18567.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003327};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 362..491
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT DOMAIN 498..608
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 683 AA; 76596 MW; A1294DE87D01BB69 CRC64;
MIMAKSVQSI EPNIADLANG WLKSYKLDYK LEQESLNTEI DKALADYFSK NGGSGANRPD
AKLLLQDKKL NYYPVLIEYK GYKDKLVKLD AEGRVENKNA KNEPNFKNIN SYAVNGAVHY
ANALLHYTSY TEIIAIGMTG YKDEFGKIQH EIGVYYVSRK NLGIGQEVGK FTDLSFLAPN
NFDAFIEKVE SLSLTQEELD NLKAKREQEI TASLVKLNNH IYQNEKGLGE NDRVYLVAAS
IIATLGIAGK VSPLEKEDLK SSVEQGNTDG EIILRKIIAF LKEKNLPDAK RDLIIRTLQN
TLTAENVNKV ENGESQLKRV FTNIVDDLGI YYKIGLTTDF TGKLFNEMYG WLGFSQDKLN
DVVLTPSYVA TLLVKLARVN KDSYVWDFAT GSAGLLVAAM NEMLIDAKNN IDSPNELAIK
EAHIKAEQLL GIELLPSVYM LAILNMILMG DGSSNILNKD SLKDFDGKYG YGRPKEQFPA
DAFVLNPPYS SLGNGMNFVE KALSMMQKGY AAIIIQNSAG SGRATEYNKR ILKRNTLLAS
IKMPIDLFIG KSSVQTNIYV FRVNEAHKKD DVVKFIDFSN DGYTRTNRKK ASVNLRDTDH
AKERYEEVFN LVRFGKSKLN FLTEKEYYEG TIDPNSGADW NQTAPIDTKP TLADFKKTVS
DYLAWEVSNL LKQKADEEDS LGK
//
