ENDA_HALS3
ID ENDA_HALS3 Reviewed; 343 AA.
AC B0R7C0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=OE_4102R;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
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_01834}.
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; AM774415; CAP14639.1; -; Genomic_DNA.
DR RefSeq; WP_010903640.1; NC_010364.1.
DR AlphaFoldDB; B0R7C0; -.
DR SMR; B0R7C0; -.
DR EnsemblBacteria; CAP14639; CAP14639; OE_4102R.
DR GeneID; 5954436; -.
DR KEGG; hsl:OE_4102R; -.
DR HOGENOM; CLU_791347_0_0_2; -.
DR OMA; GADFRTY; -.
DR PhylomeDB; B0R7C0; -.
DR Proteomes; UP000001321; 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; -; 2.
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; IPR006678; tRNA_intron_Endonuc_N.
DR InterPro; IPR036740; tRNA_intron_Endonuc_N_sf.
DR InterPro; IPR006676; tRNA_splic.
DR InterPro; IPR023516; tRNA_splic_arch_long.
DR PANTHER; PTHR21227; PTHR21227; 1.
DR Pfam; PF01974; tRNA_int_endo; 1.
DR Pfam; PF02778; tRNA_int_endo_N; 2.
DR SUPFAM; SSF53032; SSF53032; 2.
DR SUPFAM; SSF55267; SSF55267; 2.
DR TIGRFAMs; TIGR00324; endA; 1.
PE 3: Inferred from homology;
KW Lyase; tRNA processing.
FT CHAIN 1..343
FT /note="tRNA-splicing endonuclease"
FT /id="PRO_1000188344"
FT ACT_SITE 277
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT ACT_SITE 288
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT ACT_SITE 319
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
SQ SEQUENCE 343 AA; 37872 MW; E84404AC0C317CA8 CRC64;
MDGDLRGDTV HIGGDARQRF HDARGYGYPL GGNDIAVSLV EAAHLLFRGD LDSVDGMGFR
AFLTDREAGF AARFLVYVDL RDRGFYLVPD RDPWWRDPGD GDFVVFPRGN TRRDGVVKHR
VRVVDERTTL PVDGLSESVL AVVDEESEIT YLDIAPETPT GETTLDRPTD VPGVLLDDRV
LVWEPPQRLH NAGFYGQPLG GRAADHDALQ LSLVEAAYLI DAGVLRLTDA TIDDVRARGR
LGEGEHFDCR LAVYRALRDA GAVPKTGFKF GADFRVYSAV SSVDDLGHSE LLVRVITDTH
VFSPGDLSLD VRLAHGVRKR MVFAATDDTD DTIRWLSVSR LTP