ID   ARCH_PYRAB              Reviewed;         142 AA.
AC   Q9V105; G8ZJ91;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Protein archease;
DE   AltName: Full=tRNA m5C methyltransferase chaperone;
GN   OrderedLocusNames=PYRAB06240; ORFNames=PAB1946;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
RN   [3]
RP   FUNCTION AS A CHAPERONE, AND SUBUNIT.
RX   PubMed=17470432; DOI=10.1074/jbc.m607459200;
RA   Auxilien S., El Khadali F., Rasmussen A., Douthwaite S., Grosjean H.;
RT   "Archease from Pyrococcus abyssi improves substrate specificity and
RT   solubility of a tRNA m5C methyltransferase.";
RL   J. Biol. Chem. 282:18711-18721(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). Chaperone or modulator of proteins
CC       involved in DNA or RNA processing. Protects the tRNA (cytosine-5-)-
CC       methyltransferase PAB1947 against aggregation and increases its
CC       specificity. {ECO:0000250, ECO:0000269|PubMed:17470432}.
CC   -!- SUBUNIT: In solution, exists as a monomer, trimer and hexamer.
CC       Oligomeric states form a tripartite complex with tRNA and PAB1947
CC       methyltransferase. {ECO:0000269|PubMed:17470432}.
CC   -!- SIMILARITY: Belongs to the archease family. {ECO:0000305}.
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DR   EMBL; AJ248284; CAB49546.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70018.1; -; Genomic_DNA.
DR   PIR; C75183; C75183.
DR   RefSeq; WP_010867748.1; NC_000868.1.
DR   AlphaFoldDB; Q9V105; -.
DR   SMR; Q9V105; -.
DR   STRING; 272844.PAB1946; -.
DR   EnsemblBacteria; CAB49546; CAB49546; PAB1946.
DR   GeneID; 1495531; -.
DR   KEGG; pab:PAB1946; -.
DR   PATRIC; fig|272844.11.peg.664; -.
DR   eggNOG; arCOG04055; Archaea.
DR   HOGENOM; CLU_111362_3_0_2; -.
DR   OMA; WLSELLY; -.
DR   OrthoDB; 125788at2157; -.
DR   PhylomeDB; Q9V105; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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   1: Evidence at protein level;
KW   Calcium; Metal-binding; tRNA processing.
FT   CHAIN           1..142
FT                   /note="Protein archease"
FT                   /id="PRO_0000068847"
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;  16590 MW;  1616A3373FB62591 CRC64;
     MKRWEHYEHT ADIGIRGYGD SLEEAFEAVA IALFDVIVNV NKVEKKEVRE VEVEGEDLES
     LLYNFLEELL VIHDIEGLVF RDFEVKIEKT EKGYKLKAKA YGEKLDPEKH EPKEEVKAIT
     YHDMKIEKLP DGRWMAQLVP DI