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Database: UniProt
Entry: F9DFJ0_9BACT
LinkDB: F9DFJ0_9BACT
Original site: F9DFJ0_9BACT 
ID   F9DFJ0_9BACT            Unreviewed;       356 AA.
AC   F9DFJ0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   Name=hphIBM {ECO:0000313|EMBL:EGQ21661.1};
GN   ORFNames=HMPREF9144_0430 {ECO:0000313|EMBL:EGQ21661.1};
OS   Prevotella pallens ATCC 700821.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=997353 {ECO:0000313|EMBL:EGQ21661.1, ECO:0000313|Proteomes:UP000004123};
RN   [1] {ECO:0000313|EMBL:EGQ21661.1, ECO:0000313|Proteomes:UP000004123}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700821 {ECO:0000313|EMBL:EGQ21661.1,
RC   ECO:0000313|Proteomes:UP000004123};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (APR-2011) 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:EGQ21661.1}.
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DR   EMBL; AFPY01000017; EGQ21661.1; -; Genomic_DNA.
DR   RefSeq; WP_006044121.1; NZ_GL982513.1.
DR   AlphaFoldDB; F9DFJ0; -.
DR   eggNOG; COG3392; Bacteria.
DR   HOGENOM; CLU_749428_0_0_10; -.
DR   Proteomes; UP000004123; 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:UniProtKB-EC.
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   Methyltransferase {ECO:0000313|EMBL:EGQ21661.1};
KW   Transferase {ECO:0000313|EMBL:EGQ21661.1}.
SQ   SEQUENCE   356 AA;  41355 MW;  86DF82CDA1324B7F CRC64;
     MQGSLFSDYY LNYKFPEPQY LGSKYIHRAW IEQFIPVDTE VVLDAFGGSQ SIAYLMKQLG
     KTTYTNDFLN FNYQIGKALI ENAGELLTKE DIDILFSQNH NPSEYNLMEG LFSNLFFCPE
     EAALLDSFRS NVPRLQNTFK QALSLSVMCR SITRKVTMGH FAHTQALKYA ADPIRVKRNR
     SLIRPVRDIF LDILPDYNAA VFNNQKSNKS FHKNILELLP TLSNIDLVYF DPPYCNSHAD
     YQSFYHLLET FVEYWRDKEF VNGIKRYEPK RYSGFDKSSE AICSFKLLFK RAQHIPTWLV
     SYNDRSYPDI NTMIEMIEPY RNVRVEHKKY TNGRGGKGSV AGSSEILLIC TPKIKE
//
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