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Y1380_METJA
ID   Y1380_METJA             Reviewed;         109 AA.
AC   Q58775;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   07-APR-2021, sequence version 2.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Putative RNase MJ1380;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:Q8ECH6};
DE   AltName: Full=Putative toxin MJ1380;
GN   OrderedLocusNames=MJ1380;
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 MJ1379. Neutralization may be due to AMPylation by
CC       antitoxin MJ1379. {ECO:0000250|UniProtKB:Q8ECH6}.
CC   -!- SUBUNIT: Homodimer, probably forms a complex with cognate antitoxin
CC       MJ1379. {ECO:0000250|UniProtKB:Q8ECH6}.
CC   -!- PTM: Modified by cognate antitoxin MJ1379; probably at least 2
CC       successive AMPylation events occur on Tyr-83.
CC       {ECO:0000250|UniProtKB:A0A0B0QJR1}.
CC   -!- SIMILARITY: Belongs to the HepT RNase toxin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB99390.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; L77117; AAB99390.1; ALT_FRAME; Genomic_DNA.
DR   PIR; C64472; C64472.
DR   AlphaFoldDB; Q58775; -.
DR   SMR; Q58775; -.
DR   STRING; 243232.MJ_1380; -.
DR   EnsemblBacteria; AAB99390; AAB99390; MJ_1380.
DR   KEGG; mja:MJ_1380; -.
DR   eggNOG; arCOG05024; Archaea.
DR   HOGENOM; CLU_142825_4_0_2; -.
DR   InParanoid; Q58775; -.
DR   PhylomeDB; Q58775; -.
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..109
FT                   /note="Putative RNase MJ1380"
FT                   /id="PRO_0000158264"
FT   MOTIF           76..83
FT                   /note="RX(4)HXY motif"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT   ACT_SITE        76
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT   MOD_RES         83
FT                   /note="O-di-AMP-tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
SQ   SEQUENCE   109 AA;  13058 MW;  CA967C92E5E41087 CRC64;
     MSKRDVKAFL YDILESANDV IEFTKDIDYN EFINNKMIRY AVIRALEIIG EASRYINNDF
     REKFPNVPWK EMVGLRNILI HKYFGIDYIL LWKIVKEDVP KIKKEVEIV
 
 
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