ID A0A0V0SKM6_9BILA Unreviewed; 244 AA.
AC A0A0V0SKM6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Translin-associated protein X {ECO:0000256|ARBA:ARBA00041076};
DE AltName: Full=Translin-associated factor X {ECO:0000256|ARBA:ARBA00042076};
DE Flags: Fragment;
GN Name=Tsnax {ECO:0000313|EMBL:KRX27206.1};
GN ORFNames=T07_8589 {ECO:0000313|EMBL:KRX27206.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX27206.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX27206.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX27206.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the translin family.
CC {ECO:0000256|ARBA:ARBA00005902}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX27206.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDL01000004; KRX27206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0SKM6; -.
DR STRING; 6336.A0A0V0SKM6; -.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IPR016069; Translin_C.
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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000054630}.
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR602848-1"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR602848-1"
FT NON_TER 244
FT /evidence="ECO:0000313|EMBL:KRX27206.1"
SQ SEQUENCE 244 AA; 28487 MW; 1DDB0FDC57294C5F CRC64;
MPVAVKPEKE AEEEGSLISL FTSYANEMDA VYDKRERILK ASQEITVSSK RVICLLHRCV
NENEESGWKI FEQAVEKLKS LANDQFKTVA FELKDEYCDR YEKYYSSGLQ EYIEAWSFLN
FLQYKKLITL FEIRQLLQYE FCDDGNVCLR QIHISYFDYV MGIADLAGEL MRYAVVSSNS
DIVSVNNIYN FMAAVYRCIK LLNLKRKRGF VRKEKEFLDS IMKVENIFYN RMLLAADSQS
AVAV
//
