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ENDA_PYRIL
ID   ENDA_PYRIL              Reviewed;         183 AA.
AC   A1RSY7;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Pisl_0893;
OS   Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=384616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT   "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000504; ABL88069.1; -; Genomic_DNA.
DR   RefSeq; WP_011762644.1; NC_008701.1.
DR   AlphaFoldDB; A1RSY7; -.
DR   SMR; A1RSY7; -.
DR   STRING; 384616.Pisl_0893; -.
DR   EnsemblBacteria; ABL88069; ABL88069; Pisl_0893.
DR   GeneID; 4617308; -.
DR   KEGG; pis:Pisl_0893; -.
DR   eggNOG; arCOG01701; Archaea.
DR   HOGENOM; CLU_114393_0_0_2; -.
DR   OMA; KGPGIDH; -.
DR   OrthoDB; 98477at2157; -.
DR   Proteomes; UP000002595; 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..183
FT                   /note="tRNA-splicing endonuclease"
FT                   /id="PRO_0000309822"
FT   ACT_SITE        120
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
FT   ACT_SITE        159
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
SQ   SEQUENCE   183 AA;  20602 MW;  9299BC77A55D828A CRC64;
     MKGVLKGLAV VVEDVEFARK LYKEGFYGRF LGYDKVRREE VDKISAPLIL ALYEALYLAE
     RGKLKVVSKN GTEVLPEKLI ELGREKIKNF DDIYKIYKYF RDLGYVVKSG LKFGALFSVY
     ERGPGIDHAP MVVVFLEPDR GISATDITRG GRLSHSVKKT FTLATVSKQT GEVVLLGFSW
     AKL
 
 
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