ID A0A2U9CCG9_SCOMX Unreviewed; 283 AA.
AC A0A2U9CCG9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Translin-associated protein X {ECO:0000256|ARBA:ARBA00041076};
DE AltName: Full=Translin-associated factor X {ECO:0000256|ARBA:ARBA00042076};
GN ORFNames=SMAX5B_016808 {ECO:0000313|EMBL:AWP14265.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP14265.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP14265.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) 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}.
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DR EMBL; CP026257; AWP14265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CCG9; -.
DR STRING; 52904.ENSSMAP00000017418; -.
DR OMA; DTCMETC; -.
DR Proteomes; UP000246464; Chromosome 15.
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 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000246464}.
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 75..102
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR602848-1"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR602848-1"
SQ SEQUENCE 283 AA; 31698 MW; C801CC7BB73C324A CRC64;
MNTRGGDGCP RKKADAAQDR DAGDKPPTPV IAAFKVFQHE LDTKHDKYER LVKISRDVTI
ESKRTIFLLH RVTSVPNAEE ILNEAEVKLD GVRQKIGQIA EELRGEDIYQ FHRAFTPGIQ
EYVEAVSFLH YIRHRSLISL EEINASLVFM RTEEVGAQDA AETLLPGTHV LTFQVTPSDY
LLGVADLTGE LMRMCISSVG NGDIDTPFQL SQFLRQIHDG FSYIGNTGPY EVSKKLHTLR
QSLAKVEDAC YALRVRGSEI PKHMLADVFS SRTTLIDPEE GVV
//
