ID   A0A452RF58_URSAM        Unreviewed;       168 AA.
AC   A0A452RF58;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Translin-associated protein X {ECO:0000256|ARBA:ARBA00041076};
DE   AltName: Full=Translin-associated factor X {ECO:0000256|ARBA:ARBA00042076};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000017386.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000017386.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Acts in combination with TSN as an endonuclease involved in
CC       the activation of the RNA-induced silencing complex (RISC). Possible
CC       role in spermatogenesis. {ECO:0000256|ARBA:ARBA00037653}.
CC   -!- SUBUNIT: Ring-shaped heterooctamer of six TSN and two TSNAX subunits.
CC       Interacts with GOLGA3, TSNAXIP1, SUN1 and AKAP9. Interacts with the
CC       homodimeric form of C1D following gamma-radiation. Interacts with TSN
CC       and C1D in a mutually exclusive manner.
CC       {ECO:0000256|ARBA:ARBA00038594}.
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DR   AlphaFoldDB; A0A452RF58; -.
DR   STRING; 9643.ENSUAMP00000017386; -.
DR   Ensembl; ENSUAMT00000019453.1; ENSUAMP00000017386.1; ENSUAMG00000013798.1.
DR   GeneTree; ENSGT00940000153568; -.
DR   OMA; VPDMEEM; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   InterPro; IPR002848; Translin_fam.
DR   InterPro; IPR016068; Translin_N.
DR   InterPro; IPR036081; Translin_sf.
DR   PANTHER; PTHR10741; TRANSLIN AND TRANSLIN ASSOCIATED PROTEIN X; 1.
DR   PANTHER; PTHR10741:SF5; TRANSLIN-ASSOCIATED PROTEIN X; 1.
DR   Pfam; PF01997; Translin; 1.
DR   SUPFAM; SSF74784; Translin; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR602848-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR602848-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291022}.
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         129
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602848-1"
SQ   SEQUENCE   168 AA;  19568 MW;  A339216686C9F5AE CRC64;
     MSSKEGSGGF RKRKHDNFPH NQRREGKDVN SSSPVMLAFK SFQQELDARH DKYERLVKLS
     RDITVESKRT IFLLHRITSA PDMEEILTES EIKLDGVRQK ILQVAQELSG EDMHQFHRAI
     TTGLQEYVEA VSFQHFIKTR SLISMDEINK QLIFTTEEYG KENKTVRI
//