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Database: UniProt
Entry: R0KX46_ANAPL
LinkDB: R0KX46_ANAPL
Original site: R0KX46_ANAPL 
ID   R0KX46_ANAPL            Unreviewed;       285 AA.
AC   R0KX46;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
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   ORFNames=Anapl_11752 {ECO:0000313|EMBL:EOA97853.1};
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839 {ECO:0000313|EMBL:EOA97853.1, ECO:0000313|Proteomes:UP000296049};
RN   [1] {ECO:0000313|Proteomes:UP000296049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23749191; DOI=10.1038/ng.2657;
RA   Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA   Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA   Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA   Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA   Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA   Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA   Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA   Rao M., Pitel F., Wang J., Li N.;
RT   "The duck genome and transcriptome provide insight into an avian influenza
RT   virus reservoir species.";
RL   Nat. Genet. 45:776-783(2013).
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; KB743594; EOA97853.1; -; Genomic_DNA.
DR   AlphaFoldDB; R0KX46; -.
DR   Proteomes; UP000296049; 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   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:UP000296049}.
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         125
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602848-1"
FT   BINDING         192
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602848-1"
FT   CROSSLNK        274
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602848-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EOA97853.1"
FT   NON_TER         285
FT                   /evidence="ECO:0000313|EMBL:EOA97853.1"
SQ   SEQUENCE   285 AA;  32495 MW;  A4165A7B84FF2F5B CRC64;
     GSGGFRKRKH DNFPQGQKKE EKENVNPSSP LMTSFKSFQL ELDTRHDKYE RLVKLSRDIT
     IESKRTIFLL HRFTSAPNGE EILNESEVKL DAVRRKIKQV AQELIGEDMY QFHRAISPGL
     QEYVEAASFQ YFIKTRSLIS VEEINKQLVF TAEDREETTN TTSSSQDKQP NTWSLKVTPV
     DYLLGVADLT GELMRLCISS VGNGDIDTPF ELSQFLRQIY DGFTFIGNTG PYEVSKKLYT
     LKQSLAKVEN ACYTLKVRGS EIPKHMLADV FSSKTELIDQ EEGLS
//
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