ID   MTD5_DACSA              Reviewed;         351 AA.
AC   P50185;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Type II methyltransferase M.DsaV {ECO:0000303|PubMed:12654995};
DE            Short=M.DsaV {ECO:0000303|PubMed:7971279};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase DsaV;
DE   AltName: Full=Modification methylase DsaV;
GN   Name=dsaVm {ECO:0000303|PubMed:7971279};
OS   Dactylococcopsis salina (Myxobaktron salinum).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Dactylococcopsis.
OX   NCBI_TaxID=292566;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=DSM 4880;
RX   PubMed=7971279; DOI=10.1093/nar/22.21.4482;
RA   Gopal J., Yebra M.J., Bhagwat A.S.;
RT   "DsaV methyltransferase and its isoschizomers contain a conserved segment
RT   that is similar to the segment in Hhai methyltransferase that is in contact
RT   with DNA bases.";
RL   Nucleic Acids Res. 22:4482-4488(1994).
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, recognizes the double-stranded sequence 5'-
CC       CCNGG-3', methylates C-2 on both strands, and protects the DNA from
CC       cleavage by the DsaV endonuclease. {ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:7971279}.
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; U10528; AAA86046.1; -; Genomic_DNA.
DR   PIR; S50098; S50098.
DR   AlphaFoldDB; P50185; -.
DR   SMR; P50185; -.
DR   REBASE; 3361; M.DsaV.
DR   PRO; PR:P50185; -.
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..351
FT                   /note="Type II methyltransferase M.DsaV"
FT                   /id="PRO_0000087872"
FT   DOMAIN          6..312
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        75
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   351 AA;  40499 MW;  68B048AC0B8B2E5B CRC64;
     MEKKQLKFID LFAGIGGMRI PFEELGGKCV FSSEIDKHCQ RTYEANFGEM PTGDITKLSA
     DSIPYHDLLL AGFPCQAFSQ GGRKQGFQDE RGQLFFQVAK ILNDHRPQAI LLENVKGLRG
     HDKGRTLQMI LYVLEKLNYV VSWKIISATD FNLPQKRERI FIVGFQDKNN KNLIFDFPKP
     IELTAKVGDL LEKEVDEKYT ITDRMWEGHQ NRKKAHRKRG NGFGFSLVNR NSSYTRTISA
     RYYKDGSEVL VEQANKNPRV LTPRECARLQ GFPESFVIPV SDCQAWRQFG NSVPVSVIRA
     IAQKMLSYID LTEQQKEFKK VDLDQVITQK KKQLYPEDYQ EQFIQKELAL L