ID   ARCH_THEGJ              Reviewed;         142 AA.
AC   C5A6Z1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Protein archease {ECO:0000255|HAMAP-Rule:MF_01222};
GN   OrderedLocusNames=TGAM_1501;
OS   Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=593117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX   PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA   Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA   Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT   "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT   the most radioresistant organism known amongst the Archaea.";
RL   Genome Biol. 10:R70.1-R70.23(2007).
CC   -!- FUNCTION: Activates the tRNA-splicing ligase complex by facilitating
CC       the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the
CC       guanylylation of RtcB, a key intermediate step in tRNA ligation. Can
CC       also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is
CC       used efficiently (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the archease family. {ECO:0000255|HAMAP-
CC       Rule:MF_01222}.
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DR   EMBL; CP001398; ACS34003.1; -; Genomic_DNA.
DR   RefSeq; WP_015859114.1; NC_012804.1.
DR   AlphaFoldDB; C5A6Z1; -.
DR   SMR; C5A6Z1; -.
DR   STRING; 593117.TGAM_1501; -.
DR   PaxDb; C5A6Z1; -.
DR   EnsemblBacteria; ACS34003; ACS34003; TGAM_1501.
DR   GeneID; 7987303; -.
DR   KEGG; tga:TGAM_1501; -.
DR   PATRIC; fig|593117.10.peg.1503; -.
DR   eggNOG; arCOG04055; Archaea.
DR   HOGENOM; CLU_111362_3_0_2; -.
DR   OMA; WLSELLY; -.
DR   OrthoDB; 125788at2157; -.
DR   Proteomes; UP000001488; Chromosome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.55.10.10; -; 1.
DR   HAMAP; MF_01222; Archease_arch; 1.
DR   InterPro; IPR002804; Archease.
DR   InterPro; IPR022952; Archease_arc.
DR   InterPro; IPR023572; Archease_dom.
DR   InterPro; IPR036820; Archease_dom_sf.
DR   PANTHER; PTHR12682; PTHR12682; 1.
DR   Pfam; PF01951; Archease; 1.
DR   SUPFAM; SSF69819; SSF69819; 1.
PE   3: Inferred from homology;
KW   Calcium; Metal-binding; tRNA processing.
FT   CHAIN           1..142
FT                   /note="Protein archease"
FT                   /id="PRO_1000213977"
FT   BINDING         12
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   142 AA;  16646 MW;  F2392BA881C21419 CRC64;
     MRRWEHYEHT ADIGVRGYGS TLEEAFEAVA LGLFDVMVDV RKVEPRECRE VEVEEEDLEA
     LLYSFLEELL VLHDMEGLVF GDVRVRIEKT ENGYRLKAKA CGEVLDYEKH EPKEEVKAIT
     YHDMRIEKLP DGRWMAQFVP DL