ID ENDA_NANEQ Reviewed; 154 AA. AC Q74MP4; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 96. 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=NEQ205; OS Nanoarchaeum equitans (strain Kin4-M). OC Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales; OC Nanoarchaeaceae; Nanoarchaeum. OX NCBI_TaxID=228908; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Kin4-M; RX PubMed=14566062; DOI=10.1073/pnas.1735403100; RA Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M., RA Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E., RA Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D., RA Stetter K.O., Short J.M., Noorderwier M.; RT "The genome of Nanoarchaeum equitans: insights into early archaeal RT evolution and derived parasitism."; RL Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003). 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; AE017199; AAR39058.1; -; Genomic_DNA. DR PDB; 3IEY; X-ray; 2.11 A; A=1-154. DR PDBsum; 3IEY; -. DR AlphaFoldDB; Q74MP4; -. DR SMR; Q74MP4; -. DR STRING; 228908.NEQ205; -. DR EnsemblBacteria; AAR39058; AAR39058; NEQ205. DR KEGG; neq:NEQ205; -. DR HOGENOM; CLU_114393_0_0_2; -. DR BRENDA; 4.6.1.16; 8261. DR EvolutionaryTrace; Q74MP4; -. DR Proteomes; UP000000578; 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 1: Evidence at protein level; KW 3D-structure; Lyase; Reference proteome; tRNA processing. FT CHAIN 1..154 FT /note="tRNA-splicing endonuclease" FT /id="PRO_0000109474" FT ACT_SITE 86 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833" FT ACT_SITE 102 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833" FT ACT_SITE 133 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833" FT STRAND 4..6 FT /evidence="ECO:0007829|PDB:3IEY" FT STRAND 9..11 FT /evidence="ECO:0007829|PDB:3IEY" FT HELIX 19..28 FT /evidence="ECO:0007829|PDB:3IEY" FT HELIX 43..52 FT /evidence="ECO:0007829|PDB:3IEY" FT HELIX 56..68 FT /evidence="ECO:0007829|PDB:3IEY" FT STRAND 72..76 FT /evidence="ECO:0007829|PDB:3IEY" FT HELIX 77..79 FT /evidence="ECO:0007829|PDB:3IEY" FT STRAND 81..86 FT /evidence="ECO:0007829|PDB:3IEY" FT TURN 94..96 FT /evidence="ECO:0007829|PDB:3IEY" FT STRAND 99..102 FT /evidence="ECO:0007829|PDB:3IEY" FT STRAND 106..111 FT /evidence="ECO:0007829|PDB:3IEY" FT STRAND 115..117 FT /evidence="ECO:0007829|PDB:3IEY" FT HELIX 118..130 FT /evidence="ECO:0007829|PDB:3IEY" FT STRAND 135..152 FT /evidence="ECO:0007829|PDB:3IEY" SQ SEQUENCE 154 AA; 18254 MW; AFC04DE8E9F9061E CRC64; MIGYLFGNRV LVDDKELPLI EAYYLLDKGE LEVYEDDKKL SKEEFLKKCL TYDERFLIRY KAYKELRDKG YTLGTALKFG ADFRVYDIGV IPKKGKRSER EHSKWVLYPV SKDETFDFYE FASKNRVAHS TRKKLLLGIV SDKIEFIEVS WKKP //