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Database: UniProt
Entry: A0A0N4UE91_DRAME
LinkDB: A0A0N4UE91_DRAME
Original site: A0A0N4UE91_DRAME 
ID   A0A0N4UE91_DRAME        Unreviewed;       188 AA.
AC   A0A0N4UE91;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Translin {ECO:0000256|ARBA:ARBA00022196};
DE   AltName: Full=Component 3 of promoter of RISC {ECO:0000256|ARBA:ARBA00030513};
GN   ORFNames=DME_LOCUS726 {ECO:0000313|EMBL:VDN50753.1};
OS   Dracunculus medinensis (Guinea worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX   NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000568101-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:DME_0000568101-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN50753.1, ECO:0000313|Proteomes:UP000274756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-binding protein that specifically recognizes consensus
CC       sequences at the breakpoint junctions in chromosomal translocations,
CC       mostly involving immunoglobulin (Ig)/T-cell receptor gene segments.
CC       Seems to recognize single-stranded DNA ends generated by staggered
CC       breaks occurring at recombination hot spots.
CC       {ECO:0000256|ARBA:ARBA00025374}.
CC   -!- FUNCTION: Exhibits both single-stranded and double-stranded
CC       endoribonuclease activity. May act as an activator of RNA-induced
CC       silencing complex (RISC) by facilitating endonucleolytic cleavage of
CC       the siRNA passenger strand. {ECO:0000256|ARBA:ARBA00025410}.
CC   -!- SUBUNIT: Ring-shaped heterooctamer of six TSN and two TSNAX subunits,
CC       DNA/RNA binding occurs inside the ring.
CC       {ECO:0000256|ARBA:ARBA00011685}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the translin family.
CC       {ECO:0000256|ARBA:ARBA00005902}.
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DR   EMBL; UYYG01000007; VDN50753.1; -; Genomic_DNA.
DR   STRING; 318479.A0A0N4UE91; -.
DR   WBParaSite; DME_0000568101-mRNA-1; DME_0000568101-mRNA-1; DME_0000568101.
DR   Proteomes; UP000038040; Unplaced.
DR   Proteomes; UP000274756; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR   GO; GO:0016070; P:RNA metabolic process; IEA:InterPro.
DR   CDD; cd14819; Translin; 1.
DR   InterPro; IPR033956; Translin.
DR   InterPro; IPR016069; Translin_C.
DR   InterPro; IPR002848; Translin_fam.
DR   InterPro; IPR016068; Translin_N.
DR   InterPro; IPR036081; Translin_sf.
DR   PANTHER; PTHR10741:SF2; TRANSLIN; 1.
DR   PANTHER; PTHR10741; TRANSLIN AND TRANSLIN ASSOCIATED PROTEIN X; 1.
DR   Pfam; PF01997; Translin; 1.
DR   SUPFAM; SSF74784; Translin; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR602848-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR602848-1};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000274756};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   BINDING         118
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602848-1"
SQ   SEQUENCE   188 AA;  22025 MW;  EF39912504EE55F0 CRC64;
     MQFGIRLLNE RRLRINKQDL TLLYKILHAY VIDNALITIT DAINARLQWQ IEIKYHDAFR
     FTTQRIVFVV AFAYFLEHHS LISRNIIANL IGLETDPLKG AHLDLEDYLQ GILNLASELV
     RYAVNAFVAG DNKKPFQIAD FVTLIDTNFR LLNLKNDVLR RRYDVLKYDV QKAEQMVFDL
     TVRGFKRP
//
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