ID   MTV1_VIBS3              Reviewed;         408 AA.
AC   Q03055;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=Type II methyltransferase M.VspI {ECO:0000303|PubMed:12654995};
DE            Short=M.VspI {ECO:0000303|PubMed:8493116};
DE            EC=2.1.1.72 {ECO:0000269|PubMed:7607528};
DE   AltName: Full=Adenine-specific methyltransferase VspI;
DE   AltName: Full=Modification methylase VspI;
GN   Name=vspIM {ECO:0000303|PubMed:7607528};
OS   Vibrio sp. (strain 343).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=29496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=343;
RX   PubMed=8493116; DOI=10.1093/nar/21.8.2015;
RA   Degtyarev S.K., Prikhod'Ko E.A., Prikhod'Ko G.G., Krasnykh V.N.;
RT   "Vspl methylase belongs to m6A-gamma class of adenine methylases.";
RL   Nucleic Acids Res. 21:2015-2015(1993).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=7607528; DOI=10.1016/0378-1119(94)00710-a;
RA   Degtyarev S.K., Prikhod'Ko E.A., Rechkunova N.I., Prikhod'Ko G.G.,
RA   Krasnykh V.N.;
RT   "Biochemical characterization of VspI methyltransferase.";
RL   Gene 157:65-66(1995).
RN   [3]
RP   NOMENCLATURE, AND SUBTYPE.
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 gamma subtype methylase, recognizes the double-stranded
CC       sequence 5'-ATTAAT-3', methylates A-5 on both strands, and protects the
CC       DNA from cleavage by the VspI endonuclease.
CC       {ECO:0000269|PubMed:7607528, ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:8493116}.
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:0000269|PubMed:7607528};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; X68658; CAA48625.1; -; Genomic_DNA.
DR   PIR; S33683; S33683.
DR   AlphaFoldDB; Q03055; -.
DR   SMR; Q03055; -.
DR   REBASE; 3525; M.VspI.
DR   PRO; PR:Q03055; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR   PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..408
FT                   /note="Type II methyltransferase M.VspI"
FT                   /id="PRO_0000087982"
SQ   SEQUENCE   408 AA;  45507 MW;  31283121D15299A7 CRC64;
     MKQSALFEAD DVEAISIDDV AFSLNVSSAS VRNWIKTGYL HKATKNSVTA ESFVAFKDEI
     LGTEKLNQRA NKSLKDQHDH SGLEEMIHNI IRSNEVHPEG LSDIYEESLS ESYKNKEGVF
     YTPKEIAADF FDYLPKDCSE LTFCDPCCGT GNFLIEAVKR GFKPCNIYGY DIDEVALEIS
     RSRLKELCGV AESNIEKRDF LSASYQIEQK YDVIFTNPPW GKKLPKKDKD SLADSLATGN
     SKDTSAIFFF ASMKILNSSG YLGFLLQDAF FNIASYESVR KAALANQIVA LIDFGKPFKG
     LLTKAKGIIL RKQCPDDQHA TICVSGNTKN EVSQRVFEKN PKSIFNFTCS ELDLEVVEHI
     LSIPHKTLRG SARWGLGIVT GNNKKFCLPE ARGGYIPVYK GSDITRKG
//