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Y1548_METJA
ID   Y1548_METJA             Reviewed;          87 AA.
AC   Q58943;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   07-APR-2021, sequence version 2.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Putative RNase MJ1548;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:Q8ECH6};
DE   AltName: Full=Putative toxin MJ1548;
GN   OrderedLocusNames=MJ1548;
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).
CC   -!- FUNCTION: Probable toxic component of a putative type VII toxin-
CC       antitoxin (TA) system, probably an RNase. Probably neutralized by
CC       cognate antitoxin MJ1547. Neutralization may be due to AMPylation by
CC       antitoxin MJ1547. {ECO:0000250|UniProtKB:Q8ECH6}.
CC   -!- SUBUNIT: Homodimer, probably forms a complex with cognate antitoxin
CC       MJ1547. {ECO:0000250|UniProtKB:Q8ECH6}.
CC   -!- PTM: Modified by cognate antitoxin MJ1547; probably at least 2
CC       successive AMPylation events occur on Tyr-72.
CC       {ECO:0000250|UniProtKB:A0A0B0QJR1}.
CC   -!- SIMILARITY: Belongs to the HepT RNase toxin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB99566.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; L77117; AAB99566.1; ALT_FRAME; Genomic_DNA.
DR   PIR; C64493; C64493.
DR   AlphaFoldDB; Q58943; -.
DR   SMR; Q58943; -.
DR   STRING; 243232.MJ_1548; -.
DR   EnsemblBacteria; AAB99566; AAB99566; MJ_1548.
DR   KEGG; mja:MJ_1548; -.
DR   eggNOG; arCOG02109; Archaea.
DR   HOGENOM; CLU_152343_0_0_2; -.
DR   PhylomeDB; Q58943; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0110001; C:toxin-antitoxin complex; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR   Gene3D; 1.20.120.580; -; 1.
DR   InterPro; IPR008201; HepT-like.
DR   InterPro; IPR037038; HepT-like_sf.
DR   Pfam; PF01934; DUF86; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Nuclease; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Toxin-antitoxin system.
FT   CHAIN           1..87
FT                   /note="Putative RNase MJ1548"
FT                   /id="PRO_0000158265"
FT   MOTIF           65..72
FT                   /note="RX(4)HXY motif"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT   ACT_SITE        65
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT   ACT_SITE        70
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT   MOD_RES         72
FT                   /note="O-di-AMP-tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
SQ   SEQUENCE   87 AA;  10328 MW;  685075019C11F980 CRC64;
     MRLQKGLYYI SLQVCVDITM DVVAMLVKDI GLNVEDDYTN IKKLLKHDVI TKDEATLLKQ
     YNRLRNAIVH KYDKIKLRSC KRRFKKN
 
 
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