ID ENDA_ARCFU Reviewed; 305 AA. AC O29362; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 135. 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}; GN OrderedLocusNames=AF_0900; OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC OS 100126 / VC-16). OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae; OC Archaeoglobus. OX NCBI_TaxID=224325; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16; RX PubMed=9389475; DOI=10.1038/37052; RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F., RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., RA Smith H.O., Woese C.R., Venter J.C.; RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing RT archaeon Archaeoglobus fulgidus."; RL Nature 390:364-370(1997). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=10986124; DOI=10.1006/jmbi.2000.3941; RA Li H., Abelson J.; RT "Crystal structure of a dimeric archaeal splicing endonuclease."; RL J. Mol. Biol. 302:639-648(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. 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. 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; AE000782; AAB90338.1; -; Genomic_DNA. DR PIR; D69362; D69362. DR PDB; 1R0V; X-ray; 2.00 A; A/B/C/D=1-305. DR PDB; 1R11; X-ray; 2.70 A; A/B=1-305. DR PDB; 1RLV; X-ray; 3.00 A; A/B=1-305. DR PDB; 2GJW; X-ray; 2.85 A; A/B/C/D=2-305. DR PDB; 3P1Y; X-ray; 2.05 A; A/B/C/D=1-305. DR PDBsum; 1R0V; -. DR PDBsum; 1R11; -. DR PDBsum; 1RLV; -. DR PDBsum; 2GJW; -. DR PDBsum; 3P1Y; -. DR AlphaFoldDB; O29362; -. DR SMR; O29362; -. DR STRING; 224325.AF_0900; -. DR PaxDb; 224325-AF_0900; -. DR EnsemblBacteria; AAB90338; AAB90338; AF_0900. DR KEGG; afu:AF_0900; -. DR eggNOG; arCOG01701; Archaea. DR HOGENOM; CLU_791347_0_0_2; -. DR PhylomeDB; O29362; -. DR BRENDA; 4.6.1.16; 414. DR EvolutionaryTrace; O29362; -. DR Proteomes; UP000002199; 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 Gene3D; 3.40.1170.20; tRNA intron endonuclease, N-terminal domain; 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; IPR006678; tRNA_intron_Endonuc_N. 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 Pfam; PF02778; tRNA_int_endo_N; 1. DR SUPFAM; SSF53032; tRNA-intron endonuclease catalytic domain-like; 2. DR SUPFAM; SSF55267; tRNA-intron endonuclease N-terminal domain-like; 2. PE 1: Evidence at protein level; KW 3D-structure; Lyase; Reference proteome; tRNA processing. FT CHAIN 1..305 FT /note="tRNA-splicing endonuclease" FT /id="PRO_0000109484" FT ACT_SITE 246 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834" FT ACT_SITE 257 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834" FT ACT_SITE 287 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834" FT STRAND 4..10 FT /evidence="ECO:0007829|PDB:3P1Y" FT HELIX 13..18 FT /evidence="ECO:0007829|PDB:3P1Y" FT STRAND 21..24 FT /evidence="ECO:0007829|PDB:3P1Y" FT STRAND 27..30 FT /evidence="ECO:0007829|PDB:3P1Y" FT HELIX 32..40 FT /evidence="ECO:0007829|PDB:3P1Y" FT HELIX 49..59 FT /evidence="ECO:0007829|PDB:3P1Y" FT STRAND 60..62 FT /evidence="ECO:0007829|PDB:2GJW" FT HELIX 63..75 FT /evidence="ECO:0007829|PDB:1R0V" FT STRAND 81..83 FT /evidence="ECO:0007829|PDB:1R0V" FT STRAND 86..97 FT /evidence="ECO:0007829|PDB:1R0V" FT HELIX 104..110 FT /evidence="ECO:0007829|PDB:1R0V" FT TURN 111..113 FT /evidence="ECO:0007829|PDB:1R0V" FT STRAND 118..122 FT /evidence="ECO:0007829|PDB:1R0V" FT STRAND 128..134 FT /evidence="ECO:0007829|PDB:1R0V" FT STRAND 149..154 FT /evidence="ECO:0007829|PDB:1R0V" FT STRAND 157..161 FT /evidence="ECO:0007829|PDB:1R0V" FT HELIX 164..167 FT /evidence="ECO:0007829|PDB:1R0V" FT STRAND 172..175 FT /evidence="ECO:0007829|PDB:1R0V" FT STRAND 178..181 FT /evidence="ECO:0007829|PDB:1R0V" FT HELIX 183..191 FT /evidence="ECO:0007829|PDB:1R0V" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:1R0V" FT HELIX 202..212 FT /evidence="ECO:0007829|PDB:1R0V" FT HELIX 216..228 FT /evidence="ECO:0007829|PDB:1R0V" FT STRAND 232..235 FT /evidence="ECO:0007829|PDB:1R0V" FT HELIX 237..239 FT /evidence="ECO:0007829|PDB:1R0V" FT STRAND 241..247 FT /evidence="ECO:0007829|PDB:1R0V" FT HELIX 252..257 FT /evidence="ECO:0007829|PDB:1R0V" FT STRAND 259..264 FT /evidence="ECO:0007829|PDB:1R0V" FT HELIX 272..284 FT /evidence="ECO:0007829|PDB:1R0V" FT STRAND 288..293 FT /evidence="ECO:0007829|PDB:1R0V" FT STRAND 296..303 FT /evidence="ECO:0007829|PDB:1R0V" SQ SEQUENCE 305 AA; 35959 MW; DC0B5A5DEBD99E35 CRC64; MIGGDFAVVK AKKSLERRGF GVKRGDKIYL HPLEVVYLQI KGIESFGELE DVLSWAESRM EDFSTYYFVY EDLRDRGNKV KIQGEFLLTK KPYLPISERK TIRMEEIAEK ARNFDELRLA VVDEESEITY FRVYEPDMMG EQKEELPEIA GILSDEYVIT KQTEIFSRYF YGSEKGDLVT LSLIESLYLL DLGKLNLLNA DREELVKRAR EVERNFDRRY EVYRNLKERG FVVKTGFKFG SEFRVYRKVE SVDDLPHSEY LVDIADSREI RLIDLARAVR LAQNVRKRMV FAYGKNYLCF ERVKV //