ENDA_PICTO
ID ENDA_PICTO Reviewed; 284 AA.
AC Q6L1P9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=PTO0518;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; AE017261; AAT43103.1; -; Genomic_DNA.
DR RefSeq; WP_011177319.1; NC_005877.1.
DR AlphaFoldDB; Q6L1P9; -.
DR SMR; Q6L1P9; -.
DR STRING; 263820.PTO0518; -.
DR EnsemblBacteria; AAT43103; AAT43103; PTO0518.
DR GeneID; 25392590; -.
DR KEGG; pto:PTO0518; -.
DR eggNOG; arCOG01701; Archaea.
DR HOGENOM; CLU_965070_0_0_2; -.
DR OMA; PYECLYL; -.
DR OrthoDB; 110254at2157; -.
DR Proteomes; UP000000438; 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; Reference proteome; tRNA processing.
FT CHAIN 1..284
FT /note="tRNA-splicing endonuclease"
FT /id="PRO_0000109489"
FT ACT_SITE 222
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT ACT_SITE 229
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT ACT_SITE 257
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
SQ SEQUENCE 284 AA; 33533 MW; 000B863998A7D939 CRC64;
MDYIIEDGFH FDIKNGKSPS YLINKYRTGH VIGNVYLLNK YEAFYLYLKN KISIDDEFFN
GNIKFYMAYE NLIGSGLYVK ILNDCFMCRK SRNSRYKKVR FMPDDILLSF KDLYSDDSNI
YITVDEEYES VYYSMERIDI KGSRKDDFSA ASIDVSSGAY FGMNCPEWFG IDFHGKRLLN
DYEIRFLNND VKSNVDVIYK DLIKRGFIVK SGFKYGSNFR IYKNSMNEHS DYLVNYMDHD
LWYVIARAVR LASNVRKRLI ISGIIDNDPV YIKIERIKDI KTIL