ID   ENDA_METMA              Reviewed;         353 AA.
AC   Q8PZI1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 122.
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=MM_0512;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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}.
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DR   EMBL; AE008384; AAM30208.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8PZI1; -.
DR   SMR; Q8PZI1; -.
DR   KEGG; mma:MM_0512; -.
DR   PATRIC; fig|192952.21.peg.610; -.
DR   eggNOG; arCOG01701; Archaea.
DR   HOGENOM; CLU_791347_0_0_2; -.
DR   Proteomes; UP000000595; 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; 2.
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; 2.
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; 2.
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; tRNA processing.
FT   CHAIN           1..353
FT                   /note="tRNA-splicing endonuclease"
FT                   /id="PRO_0000109488"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT   ACT_SITE        300
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT   ACT_SITE        331
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
SQ   SEQUENCE   353 AA;  40191 MW;  15D5DBAD60D3F7CF CRC64;
     MNLLKTQLKG DRVLAGKEAV AELYKTGYFG RPKDDGLELS LVEAAYLQSR GKLDIELEGK
     LLGFRAFFEQ ASLRQQNFEL KYIVYKDLKE RGYYVQPSAA DFRVYPRGSH PGKSAAKIFV
     HVLSERQPLS VKLLQESVAS AENVHKQFIL AVVDEESDLT FYEIKSASPK GEMPEPFPAV
     KADATFLEDR VIAWDAEASG ALYSRGFYGK MLDPERLQLS LVESLYLFSR GVIVVRDRKG
     KIFSFDEFVE KASEIEGSFL RKYSAYKALR DSGHVVKTGF KFGTHFRVYR KVESIEKIPH
     SEYLVNVIPE DYEFRLPVMS GAVRLANSVR KRMLFAVEKG EEVEYLDIGR VKM
//