ENDA_SULIA
ID ENDA_SULIA Reviewed; 182 AA.
AC C3N6N2;
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=tRNA-splicing endonuclease {ECO:0000255|HAMAP-Rule:MF_01833};
DE EC=4.6.1.16 {ECO:0000255|HAMAP-Rule:MF_01833};
DE AltName: Full=tRNA-intron endonuclease {ECO:0000255|HAMAP-Rule:MF_01833};
GN Name=endA {ECO:0000255|HAMAP-Rule:MF_01833}; OrderedLocusNames=M1627_1782;
OS Sulfolobus islandicus (strain M.16.27).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=427318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M.16.27;
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: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at
CC the 5'- and 3'-splice sites to release the intron. The products are an
CC intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and
CC 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged
CC loops of 3 bases are separated by a stem of 4 bp. {ECO:0000255|HAMAP-
CC Rule:MF_01833}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-
CC half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with
CC a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.; EC=4.6.1.16;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01833};
CC -!- SUBUNIT: Homotetramer; although the tetramer contains four active
CC sites, only two participate in the cleavage. Therefore, it should be
CC considered as a dimer of dimers. {ECO:0000255|HAMAP-Rule:MF_01833}.
CC -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family. Archaeal
CC short subfamily. {ECO:0000255|HAMAP-Rule:MF_01833}.
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DR EMBL; CP001401; ACP55657.1; -; Genomic_DNA.
DR RefSeq; WP_012718943.1; NC_012632.1.
DR AlphaFoldDB; C3N6N2; -.
DR SMR; C3N6N2; -.
DR EnsemblBacteria; ACP55657; ACP55657; M1627_1782.
DR GeneID; 7812446; -.
DR GeneID; 7940345; -.
DR KEGG; sim:M1627_1782; -.
DR HOGENOM; CLU_114393_0_0_2; -.
DR OMA; KGPGIDH; -.
DR Proteomes; UP000002307; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0000213; F:tRNA-intron endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1350.10; -; 1.
DR HAMAP; MF_01833; EndA_short; 1.
DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR InterPro; IPR036167; tRNA_intron_Endo_cat-like_sf.
DR InterPro; IPR006677; tRNA_intron_Endonuc_cat-like.
DR InterPro; IPR006678; tRNA_intron_Endonuc_N.
DR InterPro; IPR036740; tRNA_intron_Endonuc_N_sf.
DR InterPro; IPR006676; tRNA_splic.
DR InterPro; IPR016442; tRNA_splic_arch_short.
DR PANTHER; PTHR21227; PTHR21227; 1.
DR Pfam; PF01974; tRNA_int_endo; 1.
DR Pfam; PF02778; tRNA_int_endo_N; 1.
DR PIRSF; PIRSF005285; tRNA_splic_archaea; 1.
DR SUPFAM; SSF53032; SSF53032; 1.
DR SUPFAM; SSF55267; SSF55267; 1.
DR TIGRFAMs; TIGR00324; endA; 1.
PE 3: Inferred from homology;
KW Lyase; tRNA processing.
FT CHAIN 1..182
FT /note="tRNA-splicing endonuclease"
FT /id="PRO_1000216079"
FT ACT_SITE 119
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
FT ACT_SITE 127
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
FT ACT_SITE 158
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
SQ SEQUENCE 182 AA; 20798 MW; A155C4FA4C666054 CRC64;
MVKALLVGSK VLIPNVDESR YIYSNGFYGK AIGISKPKGP KDIIRPLELS LIESVYLAKK
GLIKVIDKNG EVLEYEKLYE YSSKIINKFD IMYRVYEDLR EKGFIVRSGV KYGADFAVYT
LGPGLEHAPY VVIAVDIDEE ITPHELLSFG RVSHSTRKRL VLALVDRKSE SVRYIMFKWV
KM