ENDA_PYRFU
ID ENDA_PYRFU Reviewed; 170 AA.
AC Q8U429;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=tRNA-splicing endonuclease {ECO:0000255|HAMAP-Rule:MF_01833};
DE EC=4.6.1.16 {ECO:0000255|HAMAP-Rule:MF_01833};
DE AltName: Full=tRNA-intron endonuclease {ECO:0000255|HAMAP-Rule:MF_01833};
GN Name=endA {ECO:0000255|HAMAP-Rule:MF_01833}; OrderedLocusNames=PF0266;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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. {ECO:0000255|HAMAP-
CC Rule:MF_01833}.
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_01833};
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:0000255|HAMAP-Rule:MF_01833}.
CC -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family. Archaeal
CC short subfamily. {ECO:0000255|HAMAP-Rule:MF_01833}.
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DR EMBL; AE009950; AAL80390.1; -; Genomic_DNA.
DR RefSeq; WP_011011381.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U429; -.
DR SMR; Q8U429; -.
DR STRING; 186497.PF0266; -.
DR EnsemblBacteria; AAL80390; AAL80390; PF0266.
DR GeneID; 41712056; -.
DR KEGG; pfu:PF0266; -.
DR PATRIC; fig|186497.12.peg.278; -.
DR eggNOG; arCOG01701; Archaea.
DR HOGENOM; CLU_114393_0_0_2; -.
DR OMA; KGPGIDH; -.
DR OrthoDB; 98477at2157; -.
DR PhylomeDB; Q8U429; -.
DR Proteomes; UP000001013; 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_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 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 3: Inferred from homology;
KW Lyase; Reference proteome; tRNA processing.
FT CHAIN 1..170
FT /note="tRNA-splicing endonuclease"
FT /id="PRO_0000109477"
FT ACT_SITE 110
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
FT ACT_SITE 116
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
FT ACT_SITE 147
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
SQ SEQUENCE 170 AA; 19921 MW; 1590EC40E1348E78 CRC64;
MKTVIEFYLS GDRVYSEREK AINQLHINRG YGELKGKRLF LSLIEAAYLL EKGWIKVLDG
ERELSFYDVV SLGKKKDEDF DVKYLVYKDL RDRGYIVKSA LKFGSHYRVY RKGAEHSDWL
VWVVRESQKL SPNDITARAR VAHGVRKTMV LAVVDEDGDV VYYKVEWTKF