ID   ARCH_METAC              Reviewed;         146 AA.
AC   Q8TU10;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Protein archease {ECO:0000255|HAMAP-Rule:MF_01222};
GN   OrderedLocusNames=MA_0265;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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; AE010299; AAM03718.1; -; Genomic_DNA.
DR   RefSeq; WP_011020323.1; NC_003552.1.
DR   AlphaFoldDB; Q8TU10; -.
DR   SMR; Q8TU10; -.
DR   STRING; 188937.MA_0265; -.
DR   EnsemblBacteria; AAM03718; AAM03718; MA_0265.
DR   GeneID; 1472157; -.
DR   KEGG; mac:MA_0265; -.
DR   HOGENOM; CLU_111362_3_0_2; -.
DR   InParanoid; Q8TU10; -.
DR   OMA; WLSELLY; -.
DR   OrthoDB; 125788at2157; -.
DR   PhylomeDB; Q8TU10; -.
DR   Proteomes; UP000002487; 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..146
FT                   /note="Protein archease"
FT                   /id="PRO_0000068842"
FT   BINDING         16
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
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"
SQ   SEQUENCE   146 AA;  16771 MW;  A9A94E3D21813BBE CRC64;
     MPSQGKKYEY LEHTADIKFL AYGNTLKEVF ENAALAMFNV IIDTGKVSGE TAREVCLTSP
     DLESLLVDWL SELLYLFEVD EIVFWKFRVE EIREEEGEYS IKAVASGEQY YPESHPFETE
     IKAVTYNQLE LEKTADGWKA QVVVDI