ID   ENDA_HALMA              Reviewed;         335 AA.
AC   Q5UYF6;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 94.
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=rrnAC2964;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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; AY596297; AAV47697.1; -; Genomic_DNA.
DR   RefSeq; WP_004960627.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5UYF6; -.
DR   SMR; Q5UYF6; -.
DR   STRING; 272569.rrnAC2964; -.
DR   PaxDb; 272569-rrnAC2964; -.
DR   EnsemblBacteria; AAV47697; AAV47697; rrnAC2964.
DR   GeneID; 64823801; -.
DR   KEGG; hma:rrnAC2964; -.
DR   PATRIC; fig|272569.17.peg.3524; -.
DR   eggNOG; arCOG01701; Archaea.
DR   HOGENOM; CLU_791347_0_0_2; -.
DR   Proteomes; UP000001169; Chromosome I.
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; 2.
DR   Gene3D; 3.40.1350.10; -; 2.
DR   Gene3D; 3.40.1170.20; tRNA intron endonuclease, N-terminal domain; 2.
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; 2.
DR   SUPFAM; SSF53032; tRNA-intron endonuclease catalytic domain-like; 2.
DR   SUPFAM; SSF55267; tRNA-intron endonuclease N-terminal domain-like; 2.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome; tRNA processing.
FT   CHAIN           1..335
FT                   /note="tRNA-splicing endonuclease"
FT                   /id="PRO_0000309815"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT   ACT_SITE        311
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
SQ   SEQUENCE   335 AA;  36748 MW;  3D5E96FED66ABB76 CRC64;
     MELTLEGDVV RAGYEARERF YDSRGYGKVR NGDIDLAPVE AAHLLYRGDI ESIDGMDFRG
     FLGSAAVSEV DFAVYKDLRD RGFYLTPARE GWVDDAAGAD FVVYPRGKGP WDNEVAYRVR
     IIGERDTAVA TDLGGCVLAV VDEESEVTYL DTDRREVSGT SDAAVPATAG ELLGERVVCW
     EPPAELYEQA FYGQQLGDDG AVQLSLVEAA YLTQEGMLTV EGGADAVVER GREVEGDRFD
     RRLAVYTALR ASGVAPKTGF KFGADFRTYA DVESAENLGH SELLVRVLPA DHRFEPRDLA
     LDVRLAHGVR KTMVFALTTD GGDEIEWVAV ERLTP
//