ID ENDA_SULTO Reviewed; 180 AA. AC Q975R3; F9VMV1; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 123. 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}; GN OrderedLocusNames=STK_03580; OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) OS (Sulfolobus tokodaii). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfurisphaera. OX NCBI_TaxID=273063; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7; RX PubMed=11572479; DOI=10.1093/dnares/8.4.123; RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M., RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T., RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.; RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, RT Sulfolobus tokodaii strain7."; RL DNA Res. 8:123-140(2001). 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; BA000023; BAK54248.1; -; Genomic_DNA. DR RefSeq; WP_010978320.1; NC_003106.2. DR PDB; 2CV8; X-ray; 2.80 A; A/B=1-180. DR PDBsum; 2CV8; -. DR AlphaFoldDB; Q975R3; -. DR SMR; Q975R3; -. DR STRING; 273063.STK_03580; -. DR GeneID; 1458281; -. DR KEGG; sto:STK_03580; -. DR PATRIC; fig|273063.9.peg.416; -. DR eggNOG; arCOG01701; Archaea. DR OrthoDB; 46045at2157; -. DR BRENDA; 3.1.27.B1; 15396. DR BRENDA; 4.6.1.16; 15396. DR EvolutionaryTrace; Q975R3; -. DR Proteomes; UP000001015; 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..180 FT /note="tRNA-splicing endonuclease" FT /id="PRO_0000109482" FT ACT_SITE 117 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833" FT ACT_SITE 125 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833" FT ACT_SITE 156 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833" FT STRAND 2..6 FT /evidence="ECO:0007829|PDB:2CV8" FT STRAND 9..12 FT /evidence="ECO:0007829|PDB:2CV8" FT HELIX 15..25 FT /evidence="ECO:0007829|PDB:2CV8" FT STRAND 28..30 FT /evidence="ECO:0007829|PDB:2CV8" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:2CV8" FT STRAND 46..49 FT /evidence="ECO:0007829|PDB:2CV8" FT HELIX 50..58 FT /evidence="ECO:0007829|PDB:2CV8" FT STRAND 63..66 FT /evidence="ECO:0007829|PDB:2CV8" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:2CV8" FT HELIX 73..83 FT /evidence="ECO:0007829|PDB:2CV8" FT HELIX 87..99 FT /evidence="ECO:0007829|PDB:2CV8" FT STRAND 103..106 FT /evidence="ECO:0007829|PDB:2CV8" FT HELIX 108..110 FT /evidence="ECO:0007829|PDB:2CV8" FT STRAND 112..117 FT /evidence="ECO:0007829|PDB:2CV8" FT STRAND 128..134 FT /evidence="ECO:0007829|PDB:2CV8" FT STRAND 138..140 FT /evidence="ECO:0007829|PDB:2CV8" FT HELIX 141..144 FT /evidence="ECO:0007829|PDB:2CV8" FT STRAND 147..149 FT /evidence="ECO:0007829|PDB:2CV8" FT TURN 152..155 FT /evidence="ECO:0007829|PDB:2CV8" FT STRAND 157..163 FT /evidence="ECO:0007829|PDB:2CV8" FT TURN 165..167 FT /evidence="ECO:0007829|PDB:2CV8" FT STRAND 170..178 FT /evidence="ECO:0007829|PDB:2CV8" SQ SEQUENCE 180 AA; 20507 MW; 40615B98F1C05085 CRC64; MIGELVKDKI LIKNIEDARL IYKMGYYGKP IGISKPKSAE EINSELILSL IEGVYLVKKG KLEIVSNGER LDFERLYQIG VTQIPRFRIL YSVYEDLREK GYVVRSGIKY GADFAVYTIG PGIEHAPYLV IALDENSQIS SNEILGFGRV SHSTRKELIL GIVNLTNGKI RYIMFKWLKM //