ENDA_METJA
ID ENDA_METJA Reviewed; 179 AA.
AC Q58819;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=tRNA-splicing endonuclease;
DE EC=4.6.1.16;
DE AltName: Full=tRNA-intron endonuclease;
GN Name=endA; OrderedLocusNames=MJ1424;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF HIS-125.
RX PubMed=9321408; DOI=10.1093/emboj/16.20.6290;
RA Lykke-Andersen J., Garrett R.A.;
RT "RNA-protein interactions of an archaeal homotetrameric splicing
RT endoribonuclease with an exceptional evolutionary history.";
RL EMBO J. 16:6290-6300(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9535656; DOI=10.1126/science.280.5361.279;
RA Li H., Trotta C.R., Abelson J.;
RT "Crystal structure and evolution of a transfer RNA splicing enzyme.";
RL Science 280:279-284(1998).
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.
CC {ECO:0000269|PubMed:9321408}.
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 -!- 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:0000269|PubMed:9321408}.
CC -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family. Archaeal
CC short subfamily. {ECO:0000305}.
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DR EMBL; L77117; AAB99435.1; -; Genomic_DNA.
DR PIR; G64477; G64477.
DR PDB; 1A79; X-ray; 2.28 A; A/B/C/D=9-179.
DR PDBsum; 1A79; -.
DR AlphaFoldDB; Q58819; -.
DR SMR; Q58819; -.
DR STRING; 243232.MJ_1424; -.
DR EnsemblBacteria; AAB99435; AAB99435; MJ_1424.
DR KEGG; mja:MJ_1424; -.
DR eggNOG; arCOG01701; Archaea.
DR HOGENOM; CLU_114393_0_0_2; -.
DR InParanoid; Q58819; -.
DR OMA; KGPGIDH; -.
DR PhylomeDB; Q58819; -.
DR BRENDA; 4.6.1.16; 3260.
DR EvolutionaryTrace; Q58819; -.
DR Proteomes; UP000000805; 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_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 1: Evidence at protein level;
KW 3D-structure; Lyase; Reference proteome; tRNA processing.
FT CHAIN 1..179
FT /note="tRNA-splicing endonuclease"
FT /id="PRO_0000109470"
FT ACT_SITE 115
FT ACT_SITE 125
FT ACT_SITE 156
FT MUTAGEN 125
FT /note="H->A: Induces a strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:9321408"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:1A79"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:1A79"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:1A79"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1A79"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:1A79"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:1A79"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1A79"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1A79"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:1A79"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:1A79"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:1A79"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1A79"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:1A79"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:1A79"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:1A79"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1A79"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:1A79"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:1A79"
FT STRAND 169..177
FT /evidence="ECO:0007829|PDB:1A79"
SQ SEQUENCE 179 AA; 20664 MW; BCC4675E4AD21BE6 CRC64;
MVRDKMGKKI TGLLDGDRVI VFDKNGISKL SARHYGNVEG NFLSLSLVEA LYLINLGWLE
VKYKDNKPLS FEELYEYARN VEERLCLKYL VYKDLRTRGY IVKTGLKYGA DFRLYERGAN
IDKEHSVYLV KVFPEDSSFL LSELTGFVRV AHSVRKKLLI AIVDADGDIV YYNMTYVKP
