T1SG_MYCPN
ID T1SG_MYCPN Reviewed; 306 AA.
AC P75492;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Putative type I specificity subunit S.MpnORF285P {ECO:0000303|PubMed:12654995};
DE Short=S protein;
DE Short=S.MpnORF285P {ECO:0000303|PubMed:12654995};
DE AltName: Full=Putative type-1 specificity subunit MPN_285;
DE AltName: Full=S.MpnORFGP;
GN OrderedLocusNames=MPN_285; ORFNames=A65_orf306, MP550;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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: The specificity (S) subunit of a type I methyltransferase
CC (MTase); this subunit dictates DNA sequence specificity. The single R
CC subunit has multiple frameshifts and is probably not expressed.
CC {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:8948633}.
CC -!- SUBUNIT: The methyltransferase is composed of M and S polypeptides.
CC {ECO:0000250|UniProtKB:P05719}.
CC -!- DOMAIN: Contains two DNA recognition domains, each specifying
CC recognition of one of the two defined components of the target
CC sequence. {ECO:0000250|UniProtKB:P05719}.
CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase
CC family. {ECO:0000305}.
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DR EMBL; U00089; AAB96198.1; -; Genomic_DNA.
DR PIR; S73876; S73876.
DR AlphaFoldDB; P75492; -.
DR REBASE; 6701; S.MpnORF285P.
DR EnsemblBacteria; AAB96198; AAB96198; MPN_285.
DR KEGG; mpn:MPN_285; -.
DR HOGENOM; CLU_021095_6_2_14; -.
DR OMA; THYGTWA; -.
DR PRO; PR:P75492; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.90.220.20; -; 2.
DR InterPro; IPR000055; Restrct_endonuc_typeI_TRD.
DR InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR Pfam; PF01420; Methylase_S; 2.
PE 3: Inferred from homology;
KW DNA-binding; Reference proteome; Restriction system.
FT CHAIN 1..306
FT /note="Putative type I specificity subunit S.MpnORF285P"
FT /id="PRO_0000198051"
SQ SEQUENCE 306 AA; 34693 MW; DC16E8CD9A79A9F7 CRC64;
MAEIPIDFPP LKIQEKIATI LDTFTELSAE LSAELSAELS AELSAELSAE LSAELSAELS
AELSAELSAE LSAELSAELS AELSAELRER RKQYAFYRDY LLNQENIRKI YGANIPFETF
QIRDICEINR GREINEKYLR ENPGEFPVYS SATTNGGLIG KINDYDFHGE YVTWTTGGAH
AGNVFYRNEK FSCSQNCGLL EVKNKNKFSS KFLCFALKLQ SKKFVNYASA IPVLTIKRIA
EIELSFPPLE IQEKIADILF AFEKLCNDLT EGIPAEIELR KKQLDYYQNF LFNWVQNKKL
ESLKSL