ENDA_PYRAE
ID ENDA_PYRAE Reviewed; 183 AA.
AC Q8ZVI1;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=PAE2269;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL64075.1; -; Genomic_DNA.
DR PDB; 2ZYZ; X-ray; 1.70 A; B/D=1-183.
DR PDBsum; 2ZYZ; -.
DR AlphaFoldDB; Q8ZVI1; -.
DR SMR; Q8ZVI1; -.
DR STRING; 178306.PAE2269; -.
DR EnsemblBacteria; AAL64075; AAL64075; PAE2269.
DR KEGG; pai:PAE2269; -.
DR PATRIC; fig|178306.9.peg.1689; -.
DR eggNOG; arCOG01701; Archaea.
DR HOGENOM; CLU_114393_0_0_2; -.
DR InParanoid; Q8ZVI1; -.
DR OMA; KGPGIDH; -.
DR BRENDA; 4.6.1.16; 5239.
DR EvolutionaryTrace; Q8ZVI1; -.
DR Proteomes; UP000002439; 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; IBA:GO_Central.
DR GO; GO:0000379; P:tRNA-type intron splice site recognition and cleavage; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Lyase; Reference proteome; tRNA processing.
FT CHAIN 1..183
FT /note="tRNA-splicing endonuclease"
FT /id="PRO_0000109476"
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"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:2ZYZ"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:2ZYZ"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:2ZYZ"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2ZYZ"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:2ZYZ"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:2ZYZ"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:2ZYZ"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2ZYZ"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:2ZYZ"
FT HELIX 90..102
FT /evidence="ECO:0007829|PDB:2ZYZ"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:2ZYZ"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2ZYZ"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:2ZYZ"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:2ZYZ"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:2ZYZ"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:2ZYZ"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:2ZYZ"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:2ZYZ"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:2ZYZ"
SQ SEQUENCE 183 AA; 20775 MW; E59B9BAD7352AD33 CRC64;
MIGYLRGLAV IVEDVEFARR LYKEGFYGRF LGYDKVKRDE VEKINAPLIL GLYEALYLAE
KGRLKVMGED GREVAPEELA ALGRERMRNF DEIYKIYKYF RDLGYVVKSG LKFGALFSVY
EKGPGIDHAP MVVVFLEPDK GISATDITRG GRLSHSVRKT WTLATVLRQT GEVVLLGFGW
ARL
