ID   ENDA_METTH              Reviewed;         170 AA.
AC   O07165;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=MTH_250;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9200602; DOI=10.1016/s0092-8674(00)80269-x;
RA   Kleman-Leyer K., Armbruster D.W., Daniels C.J.;
RT   "Properties of H. volcanii tRNA intron endonuclease reveal a relationship
RT   between the archaeal and eucaryal tRNA intron processing systems.";
RL   Cell 89:839-847(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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; AF001577; AAC45445.1; -; Genomic_DNA.
DR   EMBL; AE000666; AAB84756.1; -; Genomic_DNA.
DR   PIR; D69131; D69131.
DR   AlphaFoldDB; O07165; -.
DR   SMR; O07165; -.
DR   IntAct; O07165; 1.
DR   STRING; 187420.MTH_250; -.
DR   EnsemblBacteria; AAB84756; AAB84756; MTH_250.
DR   KEGG; mth:MTH_250; -.
DR   PATRIC; fig|187420.15.peg.219; -.
DR   HOGENOM; CLU_114393_0_0_2; -.
DR   OMA; KGPGIDH; -.
DR   Proteomes; UP000005223; 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   Gene3D; 3.40.1350.10; -; 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   PANTHER; PTHR21227; PTHR21227; 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; SSF53032; 1.
DR   SUPFAM; SSF55267; SSF55267; 1.
DR   TIGRFAMs; TIGR00324; endA; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome; tRNA processing.
FT   CHAIN           1..170
FT                   /note="tRNA-splicing endonuclease"
FT                   /id="PRO_0000109473"
FT   ACT_SITE        106
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
FT   ACT_SITE        116
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
FT   ACT_SITE        147
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
SQ   SEQUENCE   170 AA;  19693 MW;  41FA9B6959447E0A CRC64;
     MRVEGQLGDE VVTIKATSIA RRLHGKSHYG KMYEDRLQLS LIEAAYLMER GKLKLMKDDD
     EVSPEEFISL LGERGLYSKY LVYRDLRNRG YIVKTGFKYG AEFRLYERGG APGRTHSAYL
     VRVISENDTI HALDFSSYVR VAHGVNKKLL MAFLDDEEDI TYYLVDWIRP