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Database: UniProt
Entry: C3QN25_9BACE
LinkDB: C3QN25_9BACE
Original site: C3QN25_9BACE 
ID   C3QN25_9BACE            Unreviewed;      1215 AA.
AC   C3QN25;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 47.
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=BSCG_00284 {ECO:0000313|EMBL:EEO53359.1};
OS   Bacteroides sp. 2_2_4.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=469590 {ECO:0000313|EMBL:EEO53359.1};
RN   [1] {ECO:0000313|EMBL:EEO53359.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2_2_4 {ECO:0000313|EMBL:EEO53359.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA   Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA   White J., Yandava C., Allen-Vercoe E., Strauss J., Ambrose C., Lander E.,
RA   Nusbaum C., Ilzarbe M., Galagan J., Birren B.;
RT   "The Genome Sequence of Bacteroides sp. strain 2_2_4.";
RL   Submitted (DEC-2008) 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}.
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DR   EMBL; EQ973355; EEO53359.1; -; Genomic_DNA.
DR   AlphaFoldDB; C3QN25; -.
DR   HOGENOM; CLU_002539_0_0_10; -.
DR   Proteomes; UP000003969; 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   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR   InterPro; IPR046816; MmeI_Mtase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR025931; TaqI_C.
DR   PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR   PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR   Pfam; PF07669; Eco57I; 1.
DR   Pfam; PF20473; MmeI_Mtase; 1.
DR   Pfam; PF12950; TaqI_C; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          564..767
FT                   /note="MmeI-like DNA-methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF20473"
FT   DOMAIN          860..967
FT                   /note="Type II methyltransferase M.TaqI-like"
FT                   /evidence="ECO:0000259|Pfam:PF07669"
FT   DOMAIN          1076..1206
FT                   /note="TaqI-like C-terminal specificity"
FT                   /evidence="ECO:0000259|Pfam:PF12950"
FT   COILED          807..834
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1215 AA;  140924 MW;  EE21CB86F68E6713 CRC64;
     MAVEQTFVKP IRSFFIIKFL DYLCILLTHL PNIMGLLKPN QVLNKAYRQV AIETTDFDLF
     KNALRTLRDN IVDGQREHTQ KEHLRNFLSE TFYKPYYMAP EEDIDLAIRL DKTIKSNIGL
     LIEVKSTTNK GEMISNDNLN RKALQELLLY YLKERVNKKN NDIKYLIATN IHEFFIFDAH
     EFERKFYQNK QLRREFQDFV DGRKTSNKTD FFYTEIATTY IEEVKDSLEY TYFNLQDYQH
     LLDRTDSSAS RKLIELYKIF SDTHLLKLSF QNDSNSLNRG FYTELLHIIG IEERKENNKT
     VIVRKAVERR DEASLLENTI NQLDAEDCLR HINGRLYGND YEERLFNVAM ELCITWMNRI
     LFLKLLEAQM LKYHNGDAIY KFLSITKIHD YDDLNTLFFQ VLARDMGSRT HSIMRDFAYV
     PYLNSSLFEV TDLESKTIKI NSLSQRTVLP VLASSVLRNK KRNLQVNALP TLQYLFAFLD
     AYNFASEGSE EVQEEAKTLI NASVLGLIFE KINGHKDGSV FTPGFITMFM CREAITKTVL
     QKFNGYYGWN CTTRIELYNH IDNIVEANEL INSLRLCDPA VGSGHFLVSA LNELILLKYE
     LGILVDATGK RIRKADYQLA IENDELIVTD TEGNLFAYNP LNAESRRMQE TLFKEKRQII
     ENCLFGVDIN PNSVKICRLR LWIELLKNAY YTAESNYTYL ETLPNIDINI KCGNSLLHRF
     ALTDSIQTVL RESSISISQY KEAVAKYKNA QSKSEKQDLE TFITEIKSKL KTEINRRDAR
     LVRLNKRRSE LANLQAPQLF EPTKKEKKAS DKRIADLKKE IATLENIFEE IRSNKIYLGA
     FEWRIEFPEV LDAEGNFLGF DCIIGNPPYI QLQSMGKSAD VLECMGYITY ARTGDIYCLF
     YELGMNLLTP NGFLCYITSN KWMRAGYGEA LRGYFASKTN PIMLVDFAGI KIFDAITVEA
     NILLSQKAAN IFNTQACLVQ DSNGLNNLSD FVQQQGVKCN FADSIPWVIL SPIEQSIKQK
     IESVGIPLKD WNIQINYGIK TGFNDAFIIS TEKRDEILAN CQTEDERVRT AELIRPILRG
     RDIKRYEYEW ADLWIIATFP SRHYDIESYP AVKNYLLSIG IERLEQTGET HIVNGKKIKA
     RKKTSNEWFE TQDSISYWED FSKPKIVWKI IGNQMAFAYD ANNYVMNNAC YIMTGDHLDY
     LLAVLNFPIT EVTFV
//
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