MTV1_VIBS3
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 03-AUG-2022, entry version 81.
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; Proteobacteria; 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 Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF02384; N6_Mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 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