ID   ENDA_METAC              Reviewed;         350 AA.
AC   Q8TGX1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 102.
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}; OrderedLocusNames=MA_3624;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(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; AE010299; AAM06979.1; -; Genomic_DNA.
DR   RefSeq; WP_011023532.1; NC_003552.1.
DR   AlphaFoldDB; Q8TGX1; -.
DR   SMR; Q8TGX1; -.
DR   STRING; 188937.MA_3624; -.
DR   EnsemblBacteria; AAM06979; AAM06979; MA_3624.
DR   GeneID; 1475517; -.
DR   KEGG; mac:MA_3624; -.
DR   HOGENOM; CLU_791347_0_0_2; -.
DR   InParanoid; Q8TGX1; -.
DR   OMA; GADFRTY; -.
DR   OrthoDB; 110254at2157; -.
DR   PhylomeDB; Q8TGX1; -.
DR   Proteomes; UP000002487; 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; IBA:GO_Central.
DR   GO; GO:0000379; P:tRNA-type intron splice site recognition and cleavage; IBA:GO_Central.
DR   Gene3D; 3.40.1350.10; -; 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   PANTHER; PTHR21227; PTHR21227; 2.
DR   Pfam; PF01974; tRNA_int_endo; 2.
DR   Pfam; PF02778; tRNA_int_endo_N; 2.
DR   SUPFAM; SSF53032; SSF53032; 2.
DR   SUPFAM; SSF55267; SSF55267; 2.
DR   TIGRFAMs; TIGR00324; endA; 2.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome; tRNA processing.
FT   CHAIN           1..350
FT                   /note="tRNA-splicing endonuclease"
FT                   /id="PRO_0000109487"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT   ACT_SITE        297
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT   ACT_SITE        328
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
SQ   SEQUENCE   350 AA;  40133 MW;  472FF8999A2C4C44 CRC64;
     MKTQLEGDRV LAGKEAVAEL YKTGYFGRPR EDGLELSLVE AAYLQFRGKI EIELEGRKLD
     FRALFEQASL RQPNFELKYI VYKDLKERGY YVQPSAADFR VYPRGSHPGK SAAKIFVHVL
     SERQPLPVKL LQDSVISAEN VHKQFILAVV DEESDLTFYE IKTASPQGEM PEPYPEVKTD
     ATFLEDRVIA WDAEASGALY AGGFYGKMLD PERLQLSLVE SLYLFSRGII VVRDRKDRIF
     SFDEFVEKAS EIESSFLRKY GAYKALRDSG HVVKTGFKFG THFRVYRKVE SIEKIPHSEY
     LVNVIPSDYE FRLPVMSGAV RLANSVRKRM LFAVEKEEGV EYLDISRVKM