ENDA_THEON
ID ENDA_THEON Reviewed; 171 AA.
AC B6YXU4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=TON_1417;
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1;
RX PubMed=18790866; DOI=10.1128/jb.00746-08;
RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA Colwell R.R., Kim S.-J., Lee J.-H.;
RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT mixed heterotrophic and carboxydotrophic metabolism.";
RL J. Bacteriol. 190:7491-7499(2008).
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; CP000855; ACJ16907.1; -; Genomic_DNA.
DR RefSeq; WP_012572379.1; NC_011529.1.
DR AlphaFoldDB; B6YXU4; -.
DR SMR; B6YXU4; -.
DR STRING; 523850.TON_1417; -.
DR EnsemblBacteria; ACJ16907; ACJ16907; TON_1417.
DR GeneID; 7018451; -.
DR KEGG; ton:TON_1417; -.
DR PATRIC; fig|523850.10.peg.1428; -.
DR eggNOG; arCOG01701; Archaea.
DR HOGENOM; CLU_114393_0_0_2; -.
DR OMA; KGPGIDH; -.
DR OrthoDB; 98477at2157; -.
DR Proteomes; UP000002727; 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..171
FT /note="tRNA-splicing endonuclease"
FT /id="PRO_1000188343"
FT ACT_SITE 110
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
FT ACT_SITE 117
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
FT ACT_SITE 148
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
SQ SEQUENCE 171 AA; 20286 MW; BEFA08021C7A99D9 CRC64;
MKEPIEFKLS GDRAFSEREK AINQLYNRRY FGEVVNGKLF LSLIEAAYLM ERGKIKVLDG
GKELSFEELF ELGRKKDDQF DIKYLVYKDL RDRGYIVKSA LKFGSHFRVY RRGMDEHSQW
LIWVVPENLR FSANDITARV RVAHGVRKNM VMAVVDEDND VVYYKIEWVK F