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}.
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; 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
//