ID   ENDA_METMP              Reviewed;         177 AA.
AC   Q6LY59;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=MMP1132;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(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. {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}.
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DR   EMBL; BX950229; CAF30688.1; -; Genomic_DNA.
DR   RefSeq; WP_011171076.1; NC_005791.1.
DR   AlphaFoldDB; Q6LY59; -.
DR   SMR; Q6LY59; -.
DR   STRING; 267377.MMP1132; -.
DR   EnsemblBacteria; CAF30688; CAF30688; MMP1132.
DR   GeneID; 41279717; -.
DR   KEGG; mmp:MMP1132; -.
DR   PATRIC; fig|267377.15.peg.1165; -.
DR   eggNOG; arCOG01701; Archaea.
DR   HOGENOM; CLU_114393_0_0_2; -.
DR   OMA; KGPGIDH; -.
DR   OrthoDB; 98477at2157; -.
DR   BioCyc; MMAR267377:MMP_RS05845-MON; -.
DR   Proteomes; UP000000590; 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..177
FT                   /note="tRNA-splicing endonuclease"
FT                   /id="PRO_0000109472"
FT   ACT_SITE        114
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
FT   ACT_SITE        123
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
FT   ACT_SITE        154
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
SQ   SEQUENCE   177 AA;  20731 MW;  BEE30B619690FD92 CRC64;
     MMAKPKKTIP AKLSDERIVI YDKDGISRLN EKRYGELHEN FLSLSFVEGL YLVSKNWISL
     RDKNKKLLSF EELFDVAQNI DRKLCIRYLA YKDLRNRGYT VRTGLKYGSD FRLYERSNID
     EIHSRYLVKV FSEEIPCEIS EITGFVRVAH SVRKELIIAI VDADGSVVYY NMGYLKL