ID   ARCH_PYRIL              Reviewed;         147 AA.
AC   A1RV54;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Protein archease {ECO:0000255|HAMAP-Rule:MF_01222};
GN   OrderedLocusNames=Pisl_1685;
OS   Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=384616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT   "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000504; ABL88836.1; -; Genomic_DNA.
DR   RefSeq; WP_011763411.1; NC_008701.1.
DR   AlphaFoldDB; A1RV54; -.
DR   SMR; A1RV54; -.
DR   STRING; 384616.Pisl_1685; -.
DR   EnsemblBacteria; ABL88836; ABL88836; Pisl_1685.
DR   GeneID; 4617781; -.
DR   KEGG; pis:Pisl_1685; -.
DR   eggNOG; arCOG04055; Archaea.
DR   HOGENOM; CLU_111362_3_0_2; -.
DR   OMA; WLSELLY; -.
DR   OrthoDB; 125788at2157; -.
DR   Proteomes; UP000002595; 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..147
FT                   /note="Protein archease"
FT                   /id="PRO_1000066783"
FT   BINDING         17
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   147 AA;  17239 MW;  69BAC6337146C791 CRC64;
     MKCGKPVDYR YGEHTADVLI QAYGCTLEEA FKNAAIALAE LTYHTEKVEP RYAKEITIDY
     NDLEGLLFRW IDELLFLFDT EKFAISREIV LNLGKNDVYY IKAVLYGEPY DIEKHGFTGL
     IVKAMTFHMM EIRQIDDYWM LQYVVDV