ARCH_SULIM
ID ARCH_SULIM Reviewed; 139 AA.
AC C3MVY1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Protein archease {ECO:0000255|HAMAP-Rule:MF_01222};
GN OrderedLocusNames=M1425_1450;
OS Sulfolobus islandicus (strain M.14.25 / Kamchatka #1).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=427317;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M.14.25 / Kamchatka #1;
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001400; ACP38203.1; -; Genomic_DNA.
DR RefSeq; WP_012711448.1; NC_012588.1.
DR AlphaFoldDB; C3MVY1; -.
DR SMR; C3MVY1; -.
DR EnsemblBacteria; ACP38203; ACP38203; M1425_1450.
DR GeneID; 7814266; -.
DR GeneID; 7939560; -.
DR KEGG; sia:M1425_1450; -.
DR HOGENOM; CLU_111362_3_0_2; -.
DR OMA; WLSELLY; -.
DR Proteomes; UP000001350; 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; tRNA processing.
FT CHAIN 1..139
FT /note="Protein archease"
FT /id="PRO_1000213974"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
SQ SEQUENCE 139 AA; 16328 MW; 145A33E478E7F8C8 CRC64;
MRSFEFFEHT ADVGIRAYGK SLEEAFSNAA LGVFEVITDT SKVKPIEYRE IYLNGYDLEN
LLYKWIEELL YYYDSELMVF SKFDLMIDQD SMTLEGKAWG EKFNGKIHER RTVVKAMTYH
QLSIEKTENG YVITFVVDI