Y434_METJA
ID Y434_METJA Reviewed; 222 AA.
AC Q57876;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Gamma-glutamylcyclotransferase and putative RNase MJ0434;
DE Includes:
DE RecName: Full=Gamma-glutamylcyclotransferase family protein MJ0434;
DE Includes:
DE RecName: Full=Putative RNase MJ0434;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q8ECH6};
DE AltName: Full=Putative toxin MJ0434;
GN OrderedLocusNames=MJ0434;
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 MJ0435. Neutralization may be due to AMPylation by
CC MJ0435. {ECO:0000250|UniProtKB:Q8ECH6}.
CC -!- SUBUNIT: Homodimer, probably forms a complex with cognate antitoxin
CC MJ0435. {ECO:0000250|UniProtKB:Q8ECH6}.
CC -!- PTM: Modified by cognate antitoxin MJ0435; probably at least 2
CC successive AMPylation events occur on Tyr-82.
CC {ECO:0000250|UniProtKB:A0A0B0QJR1}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the HepT RNase toxin
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the gamma-
CC glutamylcyclotransferase family. {ECO:0000305}.
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DR EMBL; L77117; AAB98422.1; -; Genomic_DNA.
DR PIR; B64354; B64354.
DR AlphaFoldDB; Q57876; -.
DR SMR; Q57876; -.
DR STRING; 243232.MJ_0434; -.
DR EnsemblBacteria; AAB98422; AAB98422; MJ_0434.
DR KEGG; mja:MJ_0434; -.
DR eggNOG; arCOG05024; Archaea.
DR eggNOG; arCOG05099; Archaea.
DR HOGENOM; CLU_1243026_0_0_2; -.
DR InParanoid; Q57876; -.
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 CDD; cd06661; GGCT_like; 1.
DR InterPro; IPR009288; AIG2-like_dom.
DR InterPro; IPR013024; GGCT-like.
DR InterPro; IPR036568; GGCT-like_sf.
DR InterPro; IPR008201; HepT-like.
DR Pfam; PF01934; DUF86; 1.
DR Pfam; PF06094; GGACT; 1.
DR SUPFAM; SSF110857; SSF110857; 1.
PE 3: Inferred from homology;
KW Hydrolase; Nuclease; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Toxin-antitoxin system.
FT CHAIN 1..222
FT /note="Gamma-glutamylcyclotransferase and putative RNase
FT MJ0434"
FT /id="PRO_0000158262"
FT MOTIF 75..82
FT /note="RX(4)HXY motif"
FT /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT ACT_SITE 75
FT /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT MOD_RES 82
FT /note="O-di-AMP-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
SQ SEQUENCE 222 AA; 26742 MW; F0FA33F1634D1A11 CRC64;
MRKDVKIYLN HILESIELIE EYTKDKTEDD FFTSKFLQDA VIRRIEIIGE AIKNLPMEFR
EKYNHIPWKE FAEMRDILIR KYFGVDLGLT WEVVKKDIPK LKEEILKIME ELDKNKNNKY
NVFAYGELMK KERLLELINR VPKMIEGRVY GYEKFFDETI GYYGARKKEG SYIDGIILLD
ITDKELGIFD DYEDLDVYYI REKTTAVSED GRKYDVYIYL RK