ID ENDA_THEAC Reviewed; 289 AA. AC Q9HIY5; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 106. DE RecName: Full=tRNA-splicing endonuclease {ECO:0000255|HAMAP-Rule:MF_01834}; DE EC=4.6.1.16 {ECO:0000255|HAMAP-Rule:MF_01834}; DE AltName: Full=tRNA-intron endonuclease {ECO:0000255|HAMAP-Rule:MF_01834}; GN Name=endA {ECO:0000255|HAMAP-Rule:MF_01834}; OrderedLocusNames=Ta1191; OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC OS 15155 / AMRC-C165). OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales; OC Thermoplasmataceae; Thermoplasma. OX NCBI_TaxID=273075; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165; RX PubMed=11029001; DOI=10.1038/35035069; RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.; RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma RT acidophilum."; RL Nature 407:508-513(2000). 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 (By similarity). CC {ECO:0000250}. 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_01834}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01834}. CC -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family. Archaeal CC long subfamily. {ECO:0000255|HAMAP-Rule:MF_01834}. 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; AL445066; CAC12316.1; -; Genomic_DNA. DR RefSeq; WP_010901598.1; NC_002578.1. DR PDB; 2OHC; X-ray; 2.50 A; A/B=1-289. DR PDB; 2OHE; X-ray; 2.70 A; A=1-289. DR PDBsum; 2OHC; -. DR PDBsum; 2OHE; -. DR AlphaFoldDB; Q9HIY5; -. DR SMR; Q9HIY5; -. DR STRING; 273075.gene:9572414; -. DR PaxDb; 273075-Ta1191; -. DR EnsemblBacteria; CAC12316; CAC12316; CAC12316. DR GeneID; 1456687; -. DR KEGG; tac:Ta1191; -. DR eggNOG; arCOG01701; Archaea. DR HOGENOM; CLU_965070_0_0_2; -. DR InParanoid; Q9HIY5; -. DR OrthoDB; 46045at2157; -. DR BRENDA; 4.6.1.16; 6324. DR EvolutionaryTrace; Q9HIY5; -. DR Proteomes; UP000001024; 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; 3.40.1350.150; -; 1. DR HAMAP; MF_01834; EndA_long; 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; IPR036740; tRNA_intron_Endonuc_N_sf. DR InterPro; IPR006676; tRNA_splic. DR InterPro; IPR023516; tRNA_splic_arch_long. 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 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..289 FT /note="tRNA-splicing endonuclease" FT /id="PRO_0000109490" FT ACT_SITE 229 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834" FT ACT_SITE 236 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834" FT ACT_SITE 265 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834" FT STRAND 3..6 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 9..14 FT /evidence="ECO:0007829|PDB:2OHC" FT HELIX 19..26 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 30..32 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 35..37 FT /evidence="ECO:0007829|PDB:2OHC" FT HELIX 40..48 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 52..56 FT /evidence="ECO:0007829|PDB:2OHC" FT HELIX 59..66 FT /evidence="ECO:0007829|PDB:2OHC" FT HELIX 69..79 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 84..88 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 91..99 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 102..106 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:2OHE" FT HELIX 115..119 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 124..129 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 135..142 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 164..168 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 175..179 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 182..185 FT /evidence="ECO:0007829|PDB:2OHC" FT HELIX 187..193 FT /evidence="ECO:0007829|PDB:2OHC" FT HELIX 201..211 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 215..218 FT /evidence="ECO:0007829|PDB:2OHC" FT HELIX 220..222 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 224..231 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 238..243 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 246..249 FT /evidence="ECO:0007829|PDB:2OHC" FT HELIX 250..262 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 266..273 FT /evidence="ECO:0007829|PDB:2OHC" FT STRAND 276..284 FT /evidence="ECO:0007829|PDB:2OHC" SQ SEQUENCE 289 AA; 33230 MW; B0DFA251D84DBEBF CRC64; MEQGICGSHV FFIEDGKSKN YIIGKYKIGY LSGDNLILDP YECLYLYFKG RISFQNSDSF RDLFDTVTFD RYVAYEILKN KGYRVKEDSG LIYFRKGTEK PLSLRVMREY DRIQFSDLVE NPVDYYFTVD EEGDPTVYSS QEIFPAGRNL VSPVSAPVVR MGGRSFGAGD LEWWIGTAFH GFRLLTENEA NYISGNHSAS QVDMVYSDLV GRGCIVKTGF KYGANFRVYL GRDSQHAEYL VSVMPEEERW YSISRGVRVA SSVRKTMIYA SIYKNEVRYV ALKRVKDII //