ID   ARCH_THEMA              Reviewed;         124 AA.
AC   Q9X0H1;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Protein archease;
GN   OrderedLocusNames=TM_1083;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
RN   [2]
RP   PRELIMINARY FUNCTION.
RX   PubMed=15162483; DOI=10.1002/prot.20141;
RA   Canaves J.M.;
RT   "Predicted role for the archease protein family based on structural and
RT   sequence analysis of TM1083 and MTH1598, two proteins structurally
RT   characterized through structural genomics efforts.";
RL   Proteins 56:19-27(2004).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH CALCIUM.
RG   Joint Center for Structural Genomics (JCSG);
RT   "Crystal structure of archease, possible chaperone (TM1083) from Thermotoga
RT   maritima at 2.0 A resolution.";
RL   Submitted (JUL-2002) to the PDB data bank.
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). May also act as a chaperone or
CC       modulator of proteins involved in DNA or RNA processing. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the archease family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000512; AAD36160.1; -; Genomic_DNA.
DR   PIR; C72297; C72297.
DR   RefSeq; NP_228889.1; NC_000853.1.
DR   RefSeq; WP_004080400.1; NZ_CP011107.1.
DR   PDB; 1J5U; X-ray; 2.00 A; A=1-124.
DR   PDBsum; 1J5U; -.
DR   AlphaFoldDB; Q9X0H1; -.
DR   SMR; Q9X0H1; -.
DR   STRING; 243274.THEMA_08940; -.
DR   EnsemblBacteria; AAD36160; AAD36160; TM_1083.
DR   KEGG; tma:TM1083; -.
DR   eggNOG; COG1371; Bacteria.
DR   InParanoid; Q9X0H1; -.
DR   OMA; WILEISK; -.
DR   OrthoDB; 1786857at2; -.
DR   EvolutionaryTrace; Q9X0H1; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.55.10.10; -; 1.
DR   InterPro; IPR023572; Archease_dom.
DR   InterPro; IPR036820; Archease_dom_sf.
DR   Pfam; PF01951; Archease; 1.
DR   SUPFAM; SSF69819; SSF69819; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Metal-binding; Reference proteome; tRNA processing.
FT   CHAIN           1..124
FT                   /note="Protein archease"
FT                   /id="PRO_0000407063"
FT   BINDING         7
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|Ref.3"
FT   BINDING         10
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|Ref.3"
FT   BINDING         123
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|Ref.3"
FT   BINDING         124
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|Ref.3"
FT   STRAND          11..19
FT                   /evidence="ECO:0007829|PDB:1J5U"
FT   HELIX           20..35
FT                   /evidence="ECO:0007829|PDB:1J5U"
FT   STRAND          38..49
FT                   /evidence="ECO:0007829|PDB:1J5U"
FT   HELIX           54..69
FT                   /evidence="ECO:0007829|PDB:1J5U"
FT   STRAND          72..80
FT                   /evidence="ECO:0007829|PDB:1J5U"
FT   STRAND          83..93
FT                   /evidence="ECO:0007829|PDB:1J5U"
FT   STRAND          110..112
FT                   /evidence="ECO:0007829|PDB:1J5U"
FT   STRAND          115..123
FT                   /evidence="ECO:0007829|PDB:1J5U"
SQ   SEQUENCE   124 AA;  14666 MW;  637DF1E707B61AC1 CRC64;
     MRKPIEHTAD IAYEISGNSY EELLEEARNI LLEEEGIVLD TEEKEKMYPL EETEDAFFDT
     VNDWILEISK GWAPWRIKRE GNELKVTFRK IRKKEGTEIK ALTYHLLKFE RDGDVLKTKV
     VFDT