ID   ENDA_HYPBU              Reviewed;         181 AA.
AC   A2BIW2;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
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};
GN   OrderedLocusNames=Hbut_0045;
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Hyperthermus.
OX   NCBI_TaxID=415426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX   PubMed=17350933; DOI=10.1155/2007/745987;
RA   Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA   She Q., Garrett R.A., Klenk H.-P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
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; CP000493; ABM79923.1; -; Genomic_DNA.
DR   RefSeq; WP_011821240.1; NC_008818.1.
DR   AlphaFoldDB; A2BIW2; -.
DR   SMR; A2BIW2; -.
DR   STRING; 415426.Hbut_0045; -.
DR   EnsemblBacteria; ABM79923; ABM79923; Hbut_0045.
DR   GeneID; 4782745; -.
DR   KEGG; hbu:Hbut_0045; -.
DR   eggNOG; arCOG01701; Archaea.
DR   HOGENOM; CLU_114393_0_0_2; -.
DR   OrthoDB; 46045at2157; -.
DR   Proteomes; UP000002593; 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   CDD; cd22363; tRNA-intron_lyase_C; 1.
DR   Gene3D; 3.40.1350.10; -; 1.
DR   Gene3D; 3.40.1170.20; tRNA intron endonuclease, N-terminal domain; 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   NCBIfam; TIGR00324; endA; 1.
DR   PANTHER; PTHR21227; TRNA-SPLICING ENDONUCLEASE SUBUNIT SEN2; 1.
DR   PANTHER; PTHR21227:SF0; TRNA-SPLICING ENDONUCLEASE SUBUNIT SEN2; 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; tRNA-intron endonuclease catalytic domain-like; 1.
DR   SUPFAM; SSF55267; tRNA-intron endonuclease N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome; tRNA processing.
FT   CHAIN           1..181
FT                   /note="tRNA-splicing endonuclease"
FT                   /id="PRO_0000309816"
FT   ACT_SITE        118
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
FT   ACT_SITE        157
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
SQ   SEQUENCE   181 AA;  20892 MW;  A1C361B1456F3696 CRC64;
     MIRAVLLGLR AVVFDREAAR RLYASGYYGK PLGIPKPRGS NFDAPLELGL LETLHLLERG
     MLEVYDEEGH RVSVEEVRRR AERFIPKFEL LYKVYRDLRD RGYVVRSGLK YGSDFAVYER
     GPGLEHAPYL VHVMRVDEEI DPLEIVRAGR LSHSVRKAFI LALTGPRDTP IRYLLLKWSK
     P
//