ID   ARCH_PYRFU              Reviewed;         142 AA.
AC   Q8U0N4;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Protein archease {ECO:0000255|HAMAP-Rule:MF_01222};
GN   OrderedLocusNames=PF1552;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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; AE009950; AAL81676.1; -; Genomic_DNA.
DR   RefSeq; WP_011012699.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U0N4; -.
DR   SMR; Q8U0N4; -.
DR   STRING; 186497.PF1552; -.
DR   EnsemblBacteria; AAL81676; AAL81676; PF1552.
DR   GeneID; 41713373; -.
DR   KEGG; pfu:PF1552; -.
DR   PATRIC; fig|186497.12.peg.1618; -.
DR   eggNOG; arCOG04055; Archaea.
DR   HOGENOM; CLU_111362_3_0_2; -.
DR   OMA; WLSELLY; -.
DR   OrthoDB; 125788at2157; -.
DR   PhylomeDB; Q8U0N4; -.
DR   Proteomes; UP000001013; 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; Reference proteome; tRNA processing.
FT   CHAIN           1..142
FT                   /note="Protein archease"
FT                   /id="PRO_0000068849"
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;  16628 MW;  C70427A1EF78CC7B CRC64;
     MRQWEHYEHT ADIGIRGYGD TLEEAFEAVA LALFDVIVNV RKIEKKVEID IEVEGEDLES
     LLYSFLEELL YLHDIEGLVF GDFKVKIEQK DGKYILRGKA YGEKFDPEKH EPKEEVKAIT
     YHDMKIERLP DGRWMAQLVP DI