MTA1_THAGE
ID MTA1_THAGE Reviewed; 429 AA.
AC P94147;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Type II methyltransferase M.AgeI {ECO:0000303|PubMed:12654995};
DE Short=M.AgeI {ECO:0000303|PubMed:8901102};
DE EC=2.1.1.37;
DE AltName: Full=Cytosine-specific methyltransferase AgeI;
DE AltName: Full=Modification methylase AgeI;
GN Name=ageIM;
OS Thalassobius gelatinovorus (Ruegeria gelatinovora).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Thalassobius.
OX NCBI_TaxID=53501;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 25655 / DSM 5887 / IAM 12617 / JCM 20688 / NBRC 15761 / NCIMB
RC 2206 / B6;
RX PubMed=8901102; DOI=10.1271/bbb.60.444;
RA Suzuki T., Sugimoto E., Tahara Y., Yamada Y.;
RT "Cloning and nucleotide sequence of the AgeI methylase gene from
RT Agrobacterium gelatinovorum IAM 12617, a marine bacterium.";
RL Biosci. Biotechnol. Biochem. 60:444-447(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25655 / DSM 5887 / IAM 12617 / JCM 20688 / NBRC 15761 / NCIMB
RC 2206 / B6;
RA Xu S.-Y., Maunus R.E., Lunnen K.D., Allen R.;
RT "Method for cloning and producing AgeI restriction endonuclease in
RT E.coli.";
RL Patent number EP0959131, 26-APR-1999.
RN [3]
RP NOMENCLATURE.
RX PubMed=12654995; DOI=10.1093/nar/gkg274;
RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT endonucleases and their genes.";
RL Nucleic Acids Res. 31:1805-1812(2003).
CC -!- FUNCTION: A methylase, recognizes the double-stranded sequence 5'-
CC ACCGGT-3', methylates C-3 on both strands, and protects the DNA from
CC cleavage by the AgeI endonuclease. {ECO:0000269|PubMed:8901102,
CC ECO:0000303|PubMed:12654995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01016}.
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DR EMBL; D78259; BAA11333.1; -; Genomic_DNA.
DR EMBL; AF247972; AAF71525.1; -; Genomic_DNA.
DR PIR; JC4656; JC4656.
DR RefSeq; WP_058263201.1; NZ_FOFW01000005.1.
DR AlphaFoldDB; P94147; -.
DR SMR; P94147; -.
DR STRING; 53501.SAMN04488043_1052; -.
DR REBASE; 203781; M1.Lbr1106ORF1748P.
DR REBASE; 3276; M.AgeI.
DR OrthoDB; 1178320at2; -.
DR PRO; PR:P94147; -.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR031303; C5_meth_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF00145; DNA_methylase; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00675; dcm; 1.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS00095; C5_MTASE_2; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 3: Inferred from homology;
KW DNA-binding; Methyltransferase; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..429
FT /note="Type II methyltransferase M.AgeI"
FT /id="PRO_0000087856"
FT DOMAIN 1..429
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT ACT_SITE 80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018"
SQ SEQUENCE 429 AA; 47359 MW; 97C5EC5414B02FD3 CRC64;
MKTIDLFCGA GGLGEGFRQA GFSALYANDH ETPALATYKE NHPDAVCSTD SIETVDPKKI
REDLGVAPGQ VDVVMGGPPC QGFSTYGQRR DDDARNQLYV PYFGFVEEFR PKAFLIENVV
GLLSMSGGAV LADMVARAEA LGYAADVVTL DACEYGVPQH RRRVFIFGAA DGQRIDPPQP
SHVNGKRSGV VLNDQPSLFF DGPSIQPALT VRDAISDLPD EVLVPRDTQK PMEYPEPPKT
EYQRLMRGNS TELTHHSAKR MLGIRRLRLA MLHPGDYGTK IEERLADGGL NDELIDLMMG
GAGMRDAAEC RTQDREKEAA LREVLKGGHT TPAKVMEFLD SQGFANKYRR LRWDAPSHTV
VAHMARDCSD FVHPGIDRFV SVREAARFQS FPDTYRFPGS QFRQFRQIGN AVPPLLGRAM
AETIKVAIS
