MTM5_METJA
ID MTM5_METJA Reviewed; 292 AA.
AC Q58893;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Type II methyltransferase M.MjaV {ECO:0000303|PubMed:12654995};
DE Short=M.MjaV {ECO:0000303|PubMed:12654995};
DE EC=2.1.1.113;
DE AltName: Full=N-4 cytosine-specific methyltransferase MjaV;
GN Name=mjaVM; OrderedLocusNames=MJ1498;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP CHARACTERIZATION.
RA Noren C.J., Roberts R.J., Patti J., Byrd D.R., Morgan R.D.;
RT "Method for screening restriction endonucleases.";
RL Patent number WO9911821, 11-MAR-1999.
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 beta subtype methylase that recognizes the double-stranded
CC sequence 5'-GTAC-3', methylates C-4 on both strands, and protects the
CC DNA from cleavage by the MjaV endonuclease.
CC {ECO:0000303|PubMed:12654995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC subfamily. {ECO:0000305}.
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DR EMBL; L77117; AAB99509.1; -; Genomic_DNA.
DR PIR; A64487; A64487.
DR RefSeq; WP_010871021.1; NC_000909.1.
DR AlphaFoldDB; Q58893; -.
DR SMR; Q58893; -.
DR STRING; 243232.MJ_1498; -.
DR REBASE; 3897; M.MjaV.
DR PRIDE; Q58893; -.
DR EnsemblBacteria; AAB99509; AAB99509; MJ_1498.
DR GeneID; 1452405; -.
DR KEGG; mja:MJ_1498; -.
DR eggNOG; arCOG00115; Archaea.
DR HOGENOM; CLU_024927_2_3_2; -.
DR InParanoid; Q58893; -.
DR OMA; YFRDARK; -.
DR OrthoDB; 63009at2157; -.
DR PhylomeDB; Q58893; -.
DR PRO; PR:Q58893; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IBA:GO_Central.
DR GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-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; IPR002941; DNA_methylase_N4/N6.
DR InterPro; IPR017985; MeTrfase_CN4_CS.
DR InterPro; IPR001091; RM_Methyltransferase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR PRINTS; PR00508; S21N4MTFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00093; N4_MTASE; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Methyltransferase; Reference proteome; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..292
FT /note="Type II methyltransferase M.MjaV"
FT /id="PRO_0000087938"
SQ SEQUENCE 292 AA; 33877 MW; A5A46D7C8FBD3FE3 CRC64;
MEINKIYCMD CLEGMKQLKD KTVDVVVTSP PYNIGIKYNK YSDNLSREDY LNWIEEVVKE
IKRVLKDDGS FFINVGYTAK DPWIAFDVAN VIRKHFKLQN TIHWVKSIAI QKEDVGNYPN
IIGDIAVGHY KPINSDRFLS IMHEYIFHFT KNGNVKLDKL AIGVPYQDKS NIKRFNRKGD
LRDRGNTWFI PYETIQSKEK ERPHPATFPP KLPEMCIKLH GVKKTNLVLD PFMGIGSTAI
ACIRLGIDYI GFEIDEYYCR VAEERIKKEL LKTDGKFDNV KNKNIITLDA FI
