ID ENDA_METJA Reviewed; 179 AA. AC Q58819; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 138. DE RecName: Full=tRNA-splicing endonuclease; DE EC=4.6.1.16; DE AltName: Full=tRNA-intron endonuclease; GN Name=endA; OrderedLocusNames=MJ1424; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM OS 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L., RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF HIS-125. RX PubMed=9321408; DOI=10.1093/emboj/16.20.6290; RA Lykke-Andersen J., Garrett R.A.; RT "RNA-protein interactions of an archaeal homotetrameric splicing RT endoribonuclease with an exceptional evolutionary history."; RL EMBO J. 16:6290-6300(1997). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=9535656; DOI=10.1126/science.280.5361.279; RA Li H., Trotta C.R., Abelson J.; RT "Crystal structure and evolution of a transfer RNA splicing enzyme."; RL Science 280:279-284(1998). 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. CC {ECO:0000269|PubMed:9321408}. 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 -!- 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:0000269|PubMed:9321408}. CC -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family. Archaeal CC short subfamily. {ECO:0000305}. 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; L77117; AAB99435.1; -; Genomic_DNA. DR PIR; G64477; G64477. DR PDB; 1A79; X-ray; 2.28 A; A/B/C/D=9-179. DR PDBsum; 1A79; -. DR AlphaFoldDB; Q58819; -. DR SMR; Q58819; -. DR STRING; 243232.MJ_1424; -. DR PaxDb; 243232-MJ_1424; -. DR EnsemblBacteria; AAB99435; AAB99435; MJ_1424. DR KEGG; mja:MJ_1424; -. DR eggNOG; arCOG01701; Archaea. DR HOGENOM; CLU_114393_0_0_2; -. DR InParanoid; Q58819; -. DR PhylomeDB; Q58819; -. DR BRENDA; 4.6.1.16; 3260. DR EvolutionaryTrace; Q58819; -. DR Proteomes; UP000000805; 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..179 FT /note="tRNA-splicing endonuclease" FT /id="PRO_0000109470" FT ACT_SITE 115 FT ACT_SITE 125 FT ACT_SITE 156 FT MUTAGEN 125 FT /note="H->A: Induces a strong decrease in activity." FT /evidence="ECO:0000269|PubMed:9321408" FT STRAND 10..15 FT /evidence="ECO:0007829|PDB:1A79" FT STRAND 18..21 FT /evidence="ECO:0007829|PDB:1A79" FT HELIX 24..32 FT /evidence="ECO:0007829|PDB:1A79" FT STRAND 36..38 FT /evidence="ECO:0007829|PDB:1A79" FT STRAND 43..46 FT /evidence="ECO:0007829|PDB:1A79" FT HELIX 47..55 FT /evidence="ECO:0007829|PDB:1A79" FT STRAND 59..62 FT /evidence="ECO:0007829|PDB:1A79" FT STRAND 64..67 FT /evidence="ECO:0007829|PDB:1A79" FT HELIX 71..81 FT /evidence="ECO:0007829|PDB:1A79" FT HELIX 85..97 FT /evidence="ECO:0007829|PDB:1A79" FT STRAND 101..104 FT /evidence="ECO:0007829|PDB:1A79" FT HELIX 106..108 FT /evidence="ECO:0007829|PDB:1A79" FT STRAND 110..115 FT /evidence="ECO:0007829|PDB:1A79" FT TURN 121..123 FT /evidence="ECO:0007829|PDB:1A79" FT STRAND 127..134 FT /evidence="ECO:0007829|PDB:1A79" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:1A79" FT HELIX 142..153 FT /evidence="ECO:0007829|PDB:1A79" FT STRAND 157..163 FT /evidence="ECO:0007829|PDB:1A79" FT STRAND 169..177 FT /evidence="ECO:0007829|PDB:1A79" SQ SEQUENCE 179 AA; 20664 MW; BCC4675E4AD21BE6 CRC64; MVRDKMGKKI TGLLDGDRVI VFDKNGISKL SARHYGNVEG NFLSLSLVEA LYLINLGWLE VKYKDNKPLS FEELYEYARN VEERLCLKYL VYKDLRTRGY IVKTGLKYGA DFRLYERGAN IDKEHSVYLV KVFPEDSSFL LSELTGFVRV AHSVRKKLLI AIVDADGDIV YYNMTYVKP //