ENDA_THEAC
ID ENDA_THEAC Reviewed; 289 AA.
AC Q9HIY5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=Ta1191;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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; AL445066; CAC12316.1; -; Genomic_DNA.
DR RefSeq; WP_010901598.1; NC_002578.1.
DR PDB; 2OHC; X-ray; 2.50 A; A/B=1-289.
DR PDB; 2OHE; X-ray; 2.70 A; A=1-289.
DR PDBsum; 2OHC; -.
DR PDBsum; 2OHE; -.
DR AlphaFoldDB; Q9HIY5; -.
DR SMR; Q9HIY5; -.
DR STRING; 273075.Ta1191; -.
DR EnsemblBacteria; CAC12316; CAC12316; CAC12316.
DR GeneID; 1456687; -.
DR KEGG; tac:Ta1191; -.
DR eggNOG; arCOG01701; Archaea.
DR HOGENOM; CLU_965070_0_0_2; -.
DR OMA; PYECLYL; -.
DR OrthoDB; 110254at2157; -.
DR BRENDA; 4.6.1.16; 6324.
DR EvolutionaryTrace; Q9HIY5; -.
DR Proteomes; UP000001024; 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_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; IPR036740; tRNA_intron_Endonuc_N_sf.
DR InterPro; IPR006676; tRNA_splic.
DR InterPro; IPR023516; tRNA_splic_arch_long.
DR Pfam; PF01974; tRNA_int_endo; 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..289
FT /note="tRNA-splicing endonuclease"
FT /id="PRO_0000109490"
FT ACT_SITE 229
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT ACT_SITE 236
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT ACT_SITE 265
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:2OHC"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2OHC"
FT HELIX 40..48
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:2OHC"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:2OHC"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2OHE"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:2OHC"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:2OHC"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:2OHC"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:2OHC"
FT HELIX 250..262
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:2OHC"
FT STRAND 276..284
FT /evidence="ECO:0007829|PDB:2OHC"
SQ SEQUENCE 289 AA; 33230 MW; B0DFA251D84DBEBF CRC64;
MEQGICGSHV FFIEDGKSKN YIIGKYKIGY LSGDNLILDP YECLYLYFKG RISFQNSDSF
RDLFDTVTFD RYVAYEILKN KGYRVKEDSG LIYFRKGTEK PLSLRVMREY DRIQFSDLVE
NPVDYYFTVD EEGDPTVYSS QEIFPAGRNL VSPVSAPVVR MGGRSFGAGD LEWWIGTAFH
GFRLLTENEA NYISGNHSAS QVDMVYSDLV GRGCIVKTGF KYGANFRVYL GRDSQHAEYL
VSVMPEEERW YSISRGVRVA SSVRKTMIYA SIYKNEVRYV ALKRVKDII
