ARCH_THEVO
ID ARCH_THEVO Reviewed; 133 AA.
AC Q97A49;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Protein archease {ECO:0000255|HAMAP-Rule:MF_01222};
GN OrderedLocusNames=TV0961; ORFNames=TVG0986240;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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; BA000011; BAB60103.1; -; Genomic_DNA.
DR RefSeq; WP_010917191.1; NC_002689.2.
DR AlphaFoldDB; Q97A49; -.
DR SMR; Q97A49; -.
DR STRING; 273116.14325178; -.
DR EnsemblBacteria; BAB60103; BAB60103; BAB60103.
DR GeneID; 1442039; -.
DR KEGG; tvo:TVG0986240; -.
DR eggNOG; arCOG04055; Archaea.
DR HOGENOM; CLU_111362_3_0_2; -.
DR OMA; DIEYEYI; -.
DR OrthoDB; 125788at2157; -.
DR PhylomeDB; Q97A49; -.
DR Proteomes; UP000001017; 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; IPR022952; Archease_arc.
DR InterPro; IPR023572; Archease_dom.
DR InterPro; IPR036820; Archease_dom_sf.
DR Pfam; PF01951; Archease; 1.
DR SUPFAM; SSF69819; SSF69819; 1.
PE 3: Inferred from homology;
KW Calcium; Metal-binding; tRNA processing.
FT CHAIN 1..133
FT /note="Protein archease"
FT /id="PRO_0000068856"
FT BINDING 11
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
SQ SEQUENCE 133 AA; 15514 MW; B23C4A1B4413A7F9 CRC64;
MTYEILDHES DIGIMVYGTT YEELFSNAVY AMADLILDVG KLKEKRKMHE IIRGNTPEDI
MVNLLSRVLF YVDTYYTLYF RATCKYEDST LDVYLYGSEI PEEVEYRNVI KAVTYSEIAV
KPEDGFARVI FDL