ID ENDA_METKA Reviewed; 179 AA. AC Q8TGZ7; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 105. 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=MK0341; OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938). OC Archaea; Euryarchaeota; Methanomada group; Methanopyri; Methanopyrales; OC Methanopyraceae; Methanopyrus. OX NCBI_TaxID=190192; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938; RX PubMed=11930014; DOI=10.1073/pnas.032671499; RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., RA Koonin E.V., Kozyavkin S.A.; RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and RT monophyly of archaeal methanogens."; RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(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; AE009439; AAM01556.1; -; Genomic_DNA. DR PDB; 5X89; X-ray; 1.53 A; A=2-179. DR PDBsum; 5X89; -. DR AlphaFoldDB; Q8TGZ7; -. DR SMR; Q8TGZ7; -. DR STRING; 190192.MK0341; -. DR PaxDb; 190192-MK0341; -. DR EnsemblBacteria; AAM01556; AAM01556; MK0341. DR KEGG; mka:MK0341; -. DR HOGENOM; CLU_114393_0_0_2; -. DR InParanoid; Q8TGZ7; -. DR Proteomes; UP000001826; 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; PTHR13070:SF0; TRNA-SPLICING ENDONUCLEASE SUBUNIT SEN34; 1. DR PANTHER; PTHR13070; TRNA-SPLICING ENDONUCLEASE SUBUNIT SEN34-RELATED; 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..179 FT /note="tRNA-splicing endonuclease" FT /id="PRO_0000109471" FT ACT_SITE 115 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833" FT ACT_SITE 123 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833" FT ACT_SITE 154 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833" FT STRAND 13..17 FT /evidence="ECO:0007829|PDB:5X89" FT STRAND 20..23 FT /evidence="ECO:0007829|PDB:5X89" FT HELIX 28..32 FT /evidence="ECO:0007829|PDB:5X89" FT STRAND 36..39 FT /evidence="ECO:0007829|PDB:5X89" FT STRAND 42..45 FT /evidence="ECO:0007829|PDB:5X89" FT HELIX 47..55 FT /evidence="ECO:0007829|PDB:5X89" FT STRAND 60..62 FT /evidence="ECO:0007829|PDB:5X89" FT HELIX 71..79 FT /evidence="ECO:0007829|PDB:5X89" FT HELIX 85..97 FT /evidence="ECO:0007829|PDB:5X89" FT STRAND 101..104 FT /evidence="ECO:0007829|PDB:5X89" FT HELIX 106..108 FT /evidence="ECO:0007829|PDB:5X89" FT STRAND 110..117 FT /evidence="ECO:0007829|PDB:5X89" FT TURN 119..121 FT /evidence="ECO:0007829|PDB:5X89" FT STRAND 126..131 FT /evidence="ECO:0007829|PDB:5X89" FT HELIX 139..151 FT /evidence="ECO:0007829|PDB:5X89" FT STRAND 155..163 FT /evidence="ECO:0007829|PDB:5X89" FT TURN 164..167 FT /evidence="ECO:0007829|PDB:5X89" FT STRAND 168..177 FT /evidence="ECO:0007829|PDB:5X89" SQ SEQUENCE 179 AA; 20939 MW; AC84893E8167E5D5 CRC64; MLCAGNGGKE LPRAKVFEGG SLVSKDYEDL KRRYFGTEHG NVLFLDPFET VYLTEKGEID PETPEGEPMS VEELLSFFER RRPGFRAGYV VYRDLTERGY VVKSGFKYGG RFRVYEEDPD REHSKYVVRV VEPDTELSTR DVLRATRLAH SVRKDFVLAV VEDVEEPRIE YVMWRWKRL //