ENDA_HALVD
ID ENDA_HALVD Reviewed; 339 AA.
AC O07118; D4GY02;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 109.
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=HVO_2952;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 68-76; 90-107;
RP 203-220 AND 273-283, FUNCTION, AND SUBUNIT.
RC STRAIN=DS2 / DSM 5716 / WFD11;
RX PubMed=9200602; DOI=10.1016/s0092-8674(00)80269-x;
RA Kleman-Leyer K., Armbruster D.W., Daniels C.J.;
RT "Properties of H. volcanii tRNA intron endonuclease reveal a relationship
RT between the archaeal and eucaryal tRNA intron processing systems.";
RL Cell 89:839-847(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBSTRATE RECOGNITION.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=3192521; DOI=10.1016/s0021-9258(19)81308-x;
RA Thompson L.D., Daniels C.J.;
RT "A tRNA(Trp) intron endonuclease from Halobacterium volcanii. Unique
RT substrate recognition properties.";
RL J. Biol. Chem. 263:17951-17959(1988).
RN [4]
RP FUNCTION, AND SUBSTRATE RECOGNITION.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=1698785; DOI=10.1016/s0021-9258(17)44723-5;
RA Thompson L.D., Daniels C.J.;
RT "Recognition of exon-intron boundaries by the Halobacterium volcanii tRNA
RT intron endonuclease.";
RL J. Biol. Chem. 265:18104-18111(1990).
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.
CC {ECO:0000269|PubMed:1698785, ECO:0000269|PubMed:3192521,
CC ECO:0000269|PubMed:9200602}.
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 ECO:0000269|PubMed:3192521};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:3192521};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:3192521};
CC Note=Divalent cations; Ca(2+) better than Mg(2+).
CC {ECO:0000269|PubMed:3192521};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5-8.5. {ECO:0000269|PubMed:3192521};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01834,
CC ECO:0000269|PubMed:9200602}.
CC -!- PTM: The N-terminus is blocked.
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; AF001578; AAC45446.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE04265.1; -; Genomic_DNA.
DR PIR; T44993; T44993.
DR RefSeq; WP_004044805.1; NZ_AOHU01000104.1.
DR AlphaFoldDB; O07118; -.
DR SMR; O07118; -.
DR STRING; 309800.C498_17920; -.
DR EnsemblBacteria; ADE04265; ADE04265; HVO_2952.
DR GeneID; 8926183; -.
DR KEGG; hvo:HVO_2952; -.
DR eggNOG; arCOG01701; Archaea.
DR HOGENOM; CLU_791347_0_0_2; -.
DR OMA; GADFRTY; -.
DR OrthoDB; 110254at2157; -.
DR Proteomes; UP000008243; 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; 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 1: Evidence at protein level;
KW Direct protein sequencing; Lyase; Reference proteome; tRNA processing.
FT CHAIN 1..339
FT /note="tRNA-splicing endonuclease"
FT /id="PRO_0000109486"
FT ACT_SITE 274
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT ACT_SITE 285
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT ACT_SITE 316
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01834"
FT CONFLICT 151
FT /note="Y -> I (in Ref. 1; AAC45446)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 37418 MW; 40825AEC6EB798E0 CRC64;
MQGRLEDGVV HLPGDARQRF HDSRGYGRPT GGDDLEVAPV EAAHLLSRDD IDGVDGMGLR
ELLARTGTTL DFVVYKDLRD RGFYLSPARE GWPGVADAAD ADFLVYPRGK GPWDGEVEHR
VRVVGERESI PVSSLGEVVL AIVDEDGDLT YFDTEGDDPE GTAAEDLPAD LDAELLSDRA
LVWDGVDRLY QRGFFGQRLY GRNADSGPLQ LSLLEAAYLA RADALAIDEA DVVSRGRDVE
GDRFDRRLAV YAALREAKTV PKSGFKFGSD FRVYTEFESV DDLSHSEFLV RVVAPDHTFV
PRDLSLDVRL AGGVRKRMVF ALTDDNGEID WLSVSRLTP
