ID   ARCH_DICDI              Reviewed;         151 AA.
AC   Q54BU9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Protein archease-like;
GN   ORFNames=DDB_G0293404;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Component of the tRNA-splicing ligase complex required to
CC       facilitate the enzymatic turnover of catalytic subunit RtcB.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the archease family. {ECO:0000305}.
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DR   EMBL; AAFI02000207; EAL60736.1; -; Genomic_DNA.
DR   RefSeq; XP_629152.1; XM_629150.1.
DR   AlphaFoldDB; Q54BU9; -.
DR   SMR; Q54BU9; -.
DR   STRING; 44689.DDB0305182; -.
DR   PaxDb; Q54BU9; -.
DR   EnsemblProtists; EAL60736; EAL60736; DDB_G0293404.
DR   GeneID; 8629209; -.
DR   KEGG; ddi:DDB_G0293404; -.
DR   dictyBase; DDB_G0293404; -.
DR   eggNOG; KOG4528; Eukaryota.
DR   HOGENOM; CLU_111362_0_1_1; -.
DR   InParanoid; Q54BU9; -.
DR   OMA; WLSELLY; -.
DR   PhylomeDB; Q54BU9; -.
DR   PRO; PR:Q54BU9; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0072669; C:tRNA-splicing ligase complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IBA:GO_Central.
DR   Gene3D; 3.55.10.10; -; 1.
DR   InterPro; IPR002804; Archease.
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..151
FT                   /note="Protein archease-like"
FT                   /id="PRO_0000327513"
FT   BINDING         20
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   151 AA;  17311 MW;  B0B05D42691A8B7A CRC64;
     MESYGLGQLK NFEYLDHTAD IMFHTWGKDL KEALEQMVLI MNNYMVELDS VELDDSATEQ
     TISVNGHDMD SLLFALLDEF LFVFSTEFII FKQVQIISFD RENFSIKAIG KGVELDKSKH
     TTGTEIKAIT YSCMKIEENP DKSDIHVIVD I