ID ENDA_PYRAE Reviewed; 183 AA. AC Q8ZVI1; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 109. 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=PAE2269; OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP OS 104966 / NBRC 100827 / IM2). OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae; OC Pyrobaculum. OX NCBI_TaxID=178306; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / RC IM2; RX PubMed=11792869; DOI=10.1073/pnas.241636498; RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I., RA Miller J.H.; RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum RT aerophilum."; RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE009441; AAL64075.1; -; Genomic_DNA. DR PDB; 2ZYZ; X-ray; 1.70 A; B/D=1-183. DR PDBsum; 2ZYZ; -. DR AlphaFoldDB; Q8ZVI1; -. DR SMR; Q8ZVI1; -. DR STRING; 178306.PAE2269; -. DR EnsemblBacteria; AAL64075; AAL64075; PAE2269. DR KEGG; pai:PAE2269; -. DR PATRIC; fig|178306.9.peg.1689; -. DR eggNOG; arCOG01701; Archaea. DR HOGENOM; CLU_114393_0_0_2; -. DR InParanoid; Q8ZVI1; -. DR BRENDA; 4.6.1.16; 5239. DR EvolutionaryTrace; Q8ZVI1; -. DR Proteomes; UP000002439; 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; IBA:GO_Central. DR GO; GO:0000379; P:tRNA-type intron splice site recognition and cleavage; IBA:GO_Central. 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 1: Evidence at protein level; KW 3D-structure; Lyase; Reference proteome; tRNA processing. FT CHAIN 1..183 FT /note="tRNA-splicing endonuclease" FT /id="PRO_0000109476" 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" FT STRAND 2..5 FT /evidence="ECO:0007829|PDB:2ZYZ" FT STRAND 7..12 FT /evidence="ECO:0007829|PDB:2ZYZ" FT HELIX 15..23 FT /evidence="ECO:0007829|PDB:2ZYZ" FT STRAND 28..30 FT /evidence="ECO:0007829|PDB:2ZYZ" FT HELIX 38..43 FT /evidence="ECO:0007829|PDB:2ZYZ" FT STRAND 48..51 FT /evidence="ECO:0007829|PDB:2ZYZ" FT HELIX 52..60 FT /evidence="ECO:0007829|PDB:2ZYZ" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:2ZYZ" FT HELIX 76..86 FT /evidence="ECO:0007829|PDB:2ZYZ" FT HELIX 90..102 FT /evidence="ECO:0007829|PDB:2ZYZ" FT STRAND 106..109 FT /evidence="ECO:0007829|PDB:2ZYZ" FT HELIX 111..113 FT /evidence="ECO:0007829|PDB:2ZYZ" FT STRAND 115..122 FT /evidence="ECO:0007829|PDB:2ZYZ" FT STRAND 124..128 FT /evidence="ECO:0007829|PDB:2ZYZ" FT STRAND 131..135 FT /evidence="ECO:0007829|PDB:2ZYZ" FT HELIX 144..153 FT /evidence="ECO:0007829|PDB:2ZYZ" FT STRAND 161..166 FT /evidence="ECO:0007829|PDB:2ZYZ" FT TURN 168..170 FT /evidence="ECO:0007829|PDB:2ZYZ" FT STRAND 173..180 FT /evidence="ECO:0007829|PDB:2ZYZ" SQ SEQUENCE 183 AA; 20775 MW; E59B9BAD7352AD33 CRC64; MIGYLRGLAV IVEDVEFARR LYKEGFYGRF LGYDKVKRDE VEKINAPLIL GLYEALYLAE KGRLKVMGED GREVAPEELA ALGRERMRNF DEIYKIYKYF RDLGYVVKSG LKFGALFSVY EKGPGIDHAP MVVVFLEPDK GISATDITRG GRLSHSVRKT WTLATVLRQT GEVVLLGFGW ARL //