ENDA_THEVO
ID ENDA_THEVO Reviewed; 292 AA.
AC Q97BQ3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=TV0402;
GN ORFNames=TVG0390826;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(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; BA000011; BAB59544.1; -; Genomic_DNA.
DR RefSeq; WP_010916658.1; NC_002689.2.
DR AlphaFoldDB; Q97BQ3; -.
DR SMR; Q97BQ3; -.
DR STRING; 273116.14324617; -.
DR EnsemblBacteria; BAB59544; BAB59544; BAB59544.
DR GeneID; 1440916; -.
DR KEGG; tvo:TVG0390826; -.
DR eggNOG; arCOG01701; Archaea.
DR HOGENOM; CLU_965070_0_0_2; -.
DR OMA; PYECLYL; -.
DR OrthoDB; 110254at2157; -.
DR PhylomeDB; Q97BQ3; -.
DR Proteomes; UP000001017; 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; IPR006676; tRNA_splic.
DR InterPro; IPR023516; tRNA_splic_arch_long.
DR Pfam; PF01974; tRNA_int_endo; 1.
DR SUPFAM; SSF53032; SSF53032; 1.
DR TIGRFAMs; TIGR00324; endA; 1.
PE 3: Inferred from homology;
KW Lyase; tRNA processing.
FT CHAIN 1..292
FT /note="tRNA-splicing endonuclease"
FT /id="PRO_0000109491"
FT ACT_SITE 231
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT ACT_SITE 238
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT ACT_SITE 267
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
SQ SEQUENCE 292 AA; 33923 MW; CC93607C8E2966E1 CRC64;
MSDGLCNGIS FNVSEGHGPN YIVGRYKLGF VQQGILFLDP YECLYLYFKG RITFEDSEES
ALKKLFSITS VERYTAYTLL KNKGYRVHED NGTIFFRKST EIPRSVVVVR EYDEIDVGKF
FTERPDFYFT VDEEGDATIY RIDEIDIKGT ENNKIGKCSV TDFGDRHFTK DDLPHWMGTK
FHEYRMLTDF EANLIEGKEP KGMAEEVYRD LLSRGCIVKT GFKYGTNFRV YEGEKSEHAE
YLVSVVENKL IWYYISRAVR VASSVRKKMI FTTIIDGKIK YIMISRSKDI VI