MTS2_SHISO
ID MTS2_SHISO Reviewed; 379 AA.
AC P34879;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Type II methyltransferase M.SsoII {ECO:0000303|PubMed:12654995};
DE Short=M.SsoII {ECO:0000303|PubMed:7916706};
DE EC=2.1.1.37;
DE AltName: Full=Cytosine-specific methyltransferase SsoII;
DE AltName: Full=Modification methylase SsoII;
GN Name=ssoIIM;
OS Shigella sonnei.
OG Plasmid P4.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=624;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=47;
RX PubMed=7916706; DOI=10.1016/0378-1119(93)90756-s;
RA Karyagina A.S., Lunin V.G., Degtyarenko K.N., Uvarov V.Y., Nikolskaya I.I.;
RT "Analysis of the nucleotide and derived amino acid sequences of the SsoII
RT restriction endonuclease and methyltransferase.";
RL Gene 124:13-19(1993).
RN [2]
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 that recognizes the double-stranded sequence 5'-
CC CCNGG-3', methylates C-2 on both strands, and protects the DNA from
CC cleavage by the SsoII endonuclease. {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; M86545; AAA98279.1; -; Genomic_DNA.
DR PIR; JT0744; JT0744.
DR RefSeq; WP_000131511.1; NZ_UEDG01000221.1.
DR AlphaFoldDB; P34879; -.
DR SASBDB; P34879; -.
DR SMR; P34879; -.
DR REBASE; 3509; M.SsoII.
DR PRIDE; P34879; -.
DR BRENDA; 2.1.1.37; 5713.
DR PRO; PR:P34879; -.
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 CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
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; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF00145; DNA_methylase; 1.
DR Pfam; PF01381; HTH_3; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
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; PS50943; HTH_CROC1; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 3: Inferred from homology;
KW DNA-binding; Methyltransferase; Plasmid; Restriction system;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..379
FT /note="Type II methyltransferase M.SsoII"
FT /id="PRO_0000087906"
FT DOMAIN 9..66
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT DOMAIN 72..379
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT ACT_SITE 142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018"
SQ SEQUENCE 379 AA; 42890 MW; 97440A79FC6AB275 CRC64;
MTDNIAATIK EKRERLHMTQ KEFADALGLS KYGDRTIRRW ERGETKPTGA ELKAVIDFPD
TPPYPNNENG RYRMIDLFAG IGGTRLGFHQ TNAVNVVFSS EWDKFAQKTY HANYGDFPDG
DITKIDEKDI PDHEILVGGF PCVAFSQAGL KKGFNDTRGT LFFDIARIIK EKKPHAFLLE
NVKNLLGHDK GRTFSIIKNT LEELNYTVYY NIFAAKDFGV PQNRERIYIV GFNKEKVRNH
EHFTFPTPLK TKTRVGDILE KSVDNKYTLS DALWNGHQRR KLVNAAAGKG FGYGLFNENS
PYTNTISARY YKDGSEILIE QKGSNPRKIT PREASRLQGF PSDFIIPVSD TQAYKQFGNS
VAVPVINAIA EKIISTLDS
