GenomeNet

Database: UniProt
Entry: C9RMT1_FIBSS
LinkDB: C9RMT1_FIBSS
Original site: C9RMT1_FIBSS 
ID   C9RMT1_FIBSS            Unreviewed;       894 AA.
AC   C9RMT1;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   OrderedLocusNames=FSU_1135 {ECO:0000313|EMBL:ADL24987.1};
OS   Fibrobacter succinogenes (strain ATCC 19169 / S85).
OC   Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC   Fibrobacter.
OX   NCBI_TaxID=59374 {ECO:0000313|EMBL:ADL24987.1, ECO:0000313|Proteomes:UP000000517};
RN   [1] {ECO:0000313|Proteomes:UP000000517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19169 / S85 {ECO:0000313|Proteomes:UP000000517};
RA   Durkin A.S., Nelson K.E., Morrison M., Forsberg C.W., Wilson D.B.,
RA   Russell J.B., Cann I.K.O., Mackie R.I., White B.A.;
RT   "Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85.";
RL   Submitted (AUG-2010) 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   ---------------------------------------------------------------------------
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; CP002158; ADL24987.1; -; Genomic_DNA.
DR   RefSeq; WP_014545471.1; NC_017448.1.
DR   AlphaFoldDB; C9RMT1; -.
DR   STRING; 59374.FSU_1135; -.
DR   REBASE; 22227; Fsu85ORF699P.
DR   REBASE; 27332; FssORF1135P.
DR   GeneID; 34755056; -.
DR   KEGG; fsc:FSU_1135; -.
DR   PATRIC; fig|59374.8.peg.1096; -.
DR   eggNOG; COG0286; Bacteria.
DR   HOGENOM; CLU_015410_1_0_0; -.
DR   OrthoDB; 9814572at2; -.
DR   Proteomes; UP000000517; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006306; P:DNA methylation; IEA:InterPro.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.220.20; DNA methylase specificity domains; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
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; SSF116734; DNA methylase specificity domain; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Endonuclease {ECO:0000313|EMBL:ADL24987.1};
KW   Hydrolase {ECO:0000313|EMBL:ADL24987.1};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:ADL24987.1}; Nuclease {ECO:0000313|EMBL:ADL24987.1};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADL24987.1}.
FT   DOMAIN          353..481
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   DOMAIN          487..582
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   COILED          172..206
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   894 AA;  101419 MW;  0A80BF8119D47AC7 CRC64;
     MAKSIEEQVE DWCKNQLENY FTKTESINSE IDKALKTAPS KKGGSGQNLP DIKCFVSVGF
     RNIPVMIECK GTKGDFAKTD ENGLISNTNK KGETDYTAIT KYAVNGAIHY AKSILDFTET
     YKETIAIGVN GYKQDNDLQL EIGVYYLSKD NLAIPKKVGD FSDLSFLKKK NLKEFFEKID
     ELKLTLEEIE SRKLALEDEI ETKLKRLNQT MHDDLSITVK SRVMLIVGLI MAGLGVEDVS
     EGLKVEELKG ELGPKSNDAQ KIINKVEDFL RMKNLPEEKR EAIMHELSNV FKNEDLYKPK
     NGESKLRKVY VIVHKDILPY LTSDLPNIDF TGRLFNVLND WVDVPDGAEN DVVLTPRYVT
     ELMAKLTEVN MNSYVWDYAT GSAGFLISAM HLMIADAKNK IKSPEELRKT IAKIKAEKLL
     GIEKLPEIYI LAVLNMILMG DGSSNIINGD STQFDGKYKQ GKMKDKEFPA NVFLLNPPYS
     APGKGLNFVE KALSKMKSGK AAVLIQENAG STQGDGYTKK ILNKNTLIAS IHMSTDLFIG
     KSSVQTAIYV FDVGIPHDTE KLVKFIDFSN DGYARQNRKK SSQSVNLKDA DNAKERYAEL
     VNLVVRGKGK DDKNLNYYKD CYVEDYITSE GNDWTYSQHK KIDIKPTEND FKKIIKEYMA
     WQISNLIRNE DIYPWTNKSP EQSNCILSKK ERDCIQMKNA TFKAITIGSL FDIHPTKAYK
     ATNKDLFKEK GKVPVVANSS VDNGIGGWTN LKATEKGNKV VFSDTTTSDS IFYQPNDFVG
     YPHVQGLYPY CNKWDENSLL YFITCFRKSA SGLFNYGNKF TRKNALKMKV FLPEKNKEDI
     DFSFMETFIS AQKKLIIQKL SCWLEQQKIN NEIYIIEKEI PQDTLSMIAE KKHH
//
DBGET integrated database retrieval system