ENDA_PYRAR
ID ENDA_PYRAR Reviewed; 183 AA.
AC A4WLV3;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Pars_1819;
OS Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=340102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700994 / DSM 13514 / JCM 11321 / PZ6;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000660; ABP51370.1; -; Genomic_DNA.
DR AlphaFoldDB; A4WLV3; -.
DR SMR; A4WLV3; -.
DR STRING; 340102.Pars_1819; -.
DR EnsemblBacteria; ABP51370; ABP51370; Pars_1819.
DR KEGG; pas:Pars_1819; -.
DR HOGENOM; CLU_114393_0_0_2; -.
DR OMA; KGPGIDH; -.
DR PhylomeDB; A4WLV3; -.
DR Proteomes; UP000001567; 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 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 3: Inferred from homology;
KW Lyase; tRNA processing.
FT CHAIN 1..183
FT /note="tRNA-splicing endonuclease"
FT /id="PRO_0000309821"
FT ACT_SITE 120
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
FT ACT_SITE 128
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
FT ACT_SITE 159
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01833"
SQ SEQUENCE 183 AA; 20687 MW; ECE01254337EBE4E CRC64;
MRGVLRGLAV VVEDVEFGRR LYKEGFYGRF LGYDKVKREE VDRINAPLVL ALYEALYLVE
RGVLEVVTDS GEKITQTRLV ELGREKLKNF DEIYKIYKYF RDLGYVVKSG LKFGALFSVY
EKGPGIDHAP MVVVFLEPDK GISATDITRG GRLGHSVKKT FTLATVLKNT GEVILLGFSW
ARL