ID A0A087QTX0_APTFO Unreviewed; 176 AA.
AC A0A087QTX0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Translin {ECO:0000256|ARBA:ARBA00022196};
DE AltName: Full=Component 3 of promoter of RISC {ECO:0000256|ARBA:ARBA00030513};
DE Flags: Fragment;
GN ORFNames=AS27_06791 {ECO:0000313|EMBL:KFM04674.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM04674.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM04674.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM04674.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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; KL225902; KFM04674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087QTX0; -.
DR STRING; 9233.A0A087QTX0; -.
DR Proteomes; UP000053286; 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:UP000053286};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR602848-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM04674.1"
FT NON_TER 176
FT /evidence="ECO:0000313|EMBL:KFM04674.1"
SQ SEQUENCE 176 AA; 20154 MW; 40FAFA9FE026D251 CRC64;
VPKKCQKARE HFGTVRTQLE SLKTKFPADQ YYRFHEHWRF VLQRLVFLAA FVVYLESETL
VTREAVAEIL GIEADRERGF HLDIEDYLSG VLILASELAR LAVNSVTAGD YSRPLRISTF
INELDSGFRL LNLKNDSLRK RYDGLKYDVK KIEEVVYDLS IRGLNKEAAV GAGGEK
//
