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Database: UniProt
Entry: A0A2C9JER1_BIOGL
LinkDB: A0A2C9JER1_BIOGL
Original site: A0A2C9JER1_BIOGL 
ID   A0A2C9JER1_BIOGL        Unreviewed;       216 AA.
AC   A0A2C9JER1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Translin-associated protein X {ECO:0000256|ARBA:ARBA00041076};
DE   AltName: Full=Translin-associated factor X {ECO:0000256|ARBA:ARBA00042076};
GN   Name=106055338 {ECO:0000313|EnsemblMetazoa:BGLB001507-PB};
OS   Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Planorbidae; Biomphalaria.
OX   NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB001507-PB, ECO:0000313|Proteomes:UP000076420};
RN   [1] {ECO:0000313|EnsemblMetazoa:BGLB001507-PB}
RP   IDENTIFICATION.
RC   STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB001507-PB};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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   RefSeq; XP_013067009.1; XM_013211555.1.
DR   AlphaFoldDB; A0A2C9JER1; -.
DR   STRING; 6526.A0A2C9JER1; -.
DR   EnsemblMetazoa; BGLB001507-RB; BGLB001507-PB; BGLB001507.
DR   GeneID; 106055338; -.
DR   KEGG; bgt:106055338; -.
DR   VEuPathDB; VectorBase:BGLB001507; -.
DR   OrthoDB; 10121at2759; -.
DR   Proteomes; UP000076420; 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   CDD; cd14820; TRAX; 1.
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}.
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         155
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602848-1"
SQ   SEQUENCE   216 AA;  24663 MW;  EAAE6944259FFCB4 CRC64;
     MDSSGTGASR SRFKKSHNDN PSIIINDHDG NRGREDRNTS SSNRKRLKVN DSSLSKDSPI
     FKAFNIFREE LDNRNNRHER IVKISRDITI ESKRIIFLLQ RVTGSEESEK VFAEAKDKIL
     DLNRTKFLEL AHELHGQDPY QFVRAYSPGL QEYIEAVTFY HYLHSEELIG LERIQADLIY
     LVKAQDAPGL SSELTLGTNS SECLSVKTLA IESNTF
//
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