MTX2_XANOR
ID MTX2_XANOR Reviewed; 424 AA.
AC P52311; Q5H5A9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Type II methyltransferase M.XorII {ECO:0000303|PubMed:12654995};
DE Short=M.XorII {ECO:0000303|PubMed:8078464};
DE EC=2.1.1.37;
DE AltName: Full=Cytosine-specific methyltransferase XorII;
DE AltName: Full=Modification methylase XorII;
GN Name=xorIIM; OrderedLocusNames=XOO0607;
OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=291331;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=JW89011;
RX PubMed=8078464; DOI=10.1007/bf00286690;
RA Choi S.H., Leach J.E.;
RT "Identification of the XorII methyltransferase gene and a vsr homolog from
RT Xanthomonas oryzae pv. oryzae.";
RL Mol. Gen. Genet. 244:383-390(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC10331 / KXO85;
RX PubMed=15673718; DOI=10.1093/nar/gki206;
RA Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA Go S.-J.;
RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT bacterial blight pathogen of rice.";
RL Nucleic Acids Res. 33:577-586(2005).
RN [3]
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 CGATCG-3', methylates C-? on both strands and protects the DNA from
CC cleavage by the XorII endonuclease. {ECO:0000303|PubMed:12654995,
CC ECO:0000305|PubMed:8078464}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW73861.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U06424; AAA50432.1; -; Genomic_DNA.
DR EMBL; AE013598; AAW73861.1; ALT_INIT; Genomic_DNA.
DR PIR; S46293; S46293.
DR RefSeq; WP_041181951.1; NC_006834.1.
DR AlphaFoldDB; P52311; -.
DR SMR; P52311; -.
DR STRING; 291331.XOO0607; -.
DR REBASE; 10811; M.XorKI.
DR REBASE; 203186; M.Bam1267ORF544P.
DR REBASE; 3534; M.XorII.
DR PRIDE; P52311; -.
DR EnsemblBacteria; AAW73861; AAW73861; XOO0607.
DR KEGG; xoo:XOO0607; -.
DR HOGENOM; CLU_006958_2_4_6; -.
DR PRO; PR:P52311; -.
DR Proteomes; UP000006735; Chromosome.
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; Reference proteome; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..424
FT /note="Type II methyltransferase M.XorII"
FT /id="PRO_0000087910"
FT DOMAIN 4..367
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT REGION 404..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018"
FT CONFLICT 60..61
FT /note="GD -> RS (in Ref. 1; AAA50432)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 46900 MW; EBC3FD08DBACADEC CRC64;
MTRPIGIDLF AGAGGLSLGF EQAGFDLVAA VDIDPIHCAA HKFNFPKCAT VCKSVVDVTG
DELRRIAGIG KRDIDIVIGG APCQGFSLIG KRALDDSRNQ LVHHYVRVVM ELKPKYFVFE
NVKGLTVGKH RQFLKEVIEA FQNGGYDVVT DYRVLNAADY GVPQDRRRLI LMGARKGLPL
PAYPEPTGRT TVGDAIGDIP DAESFPELWE RDWVKAKYGK PSTYAAYLRG KKDDPTDFGY
RRQFDPMLLT GSLLTDHTEL SRQRFAAIAP DDVEPVSRFK KLALNGICNT LRAGTASDRG
AFTSPRPIHP TVPRVITVRE AARLHSYPDW FRFHATKWHG FRQIGNSVPP LLARAVGGQI
MKALRKKPEK PSEMLALGDQ SLIGISMTDA AAMFGVSSTV IARRSRPVDR PAPRRHEERE
LVTA
