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Database: UniProt
Entry: J4D906_THEOR
LinkDB: J4D906_THEOR
Original site: J4D906_THEOR 
ID   J4D906_THEOR            Unreviewed;      1119 AA.
AC   J4D906;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=NFACT RNA-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TOT_030000383 {ECO:0000313|EMBL:BAM41120.1};
OS   Theileria orientalis strain Shintoku.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM41120.1, ECO:0000313|Proteomes:UP000003786};
RN   [1] {ECO:0000313|EMBL:BAM41120.1, ECO:0000313|Proteomes:UP000003786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shintoku {ECO:0000313|EMBL:BAM41120.1,
RC   ECO:0000313|Proteomes:UP000003786};
RX   PubMed=22951932;
RA   Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA   Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA   Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA   Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA   Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT   "Comparative genome analysis of three eukaryotic parasites with differing
RT   abilities to transform leukocytes reveals key mediators of Theileria-
RT   induced leukocyte transformation.";
RL   MBio 3:e00204-e00212(2012).
CC   -!- SIMILARITY: Belongs to the NEMF family.
CC       {ECO:0000256|ARBA:ARBA00008318}.
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DR   EMBL; AP011948; BAM41120.1; -; Genomic_DNA.
DR   RefSeq; XP_009691421.1; XM_009693126.1.
DR   AlphaFoldDB; J4D906; -.
DR   STRING; 869250.J4D906; -.
DR   EnsemblProtists; BAM41120; BAM41120; TOT_030000383.
DR   GeneID; 20715563; -.
DR   KEGG; tot:TOT_030000383; -.
DR   VEuPathDB; PiroplasmaDB:TOT_030000383; -.
DR   eggNOG; KOG2030; Eukaryota.
DR   OrthoDB; 129892at2759; -.
DR   Proteomes; UP000003786; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0072344; P:rescue of stalled ribosome; IEA:UniProt.
DR   Gene3D; 2.30.310.10; ibrinogen binding protein from staphylococcus aureus domain; 1.
DR   InterPro; IPR021846; NFACT-C.
DR   InterPro; IPR008532; NFACT_RNA-bd.
DR   PANTHER; PTHR15239; NUCLEAR EXPORT MEDIATOR FACTOR NEMF; 1.
DR   PANTHER; PTHR15239:SF6; RIBOSOME QUALITY CONTROL COMPLEX SUBUNIT NEMF; 1.
DR   Pfam; PF11923; NFACT-C; 1.
DR   Pfam; PF05670; NFACT-R_1; 1.
DR   Pfam; PF05833; NFACT_N; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003786}.
FT   DOMAIN          484..620
FT                   /note="NFACT RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF05670"
FT   DOMAIN          1027..1092
FT                   /note="NFACT protein C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11923"
FT   REGION          661..779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          826..867
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          882..928
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..773
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        832..847
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..867
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        898..917
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1119 AA;  129007 MW;  DF633D992C3D8BDE CRC64;
     MVRERLNAID VAISVANLKK TLDNITLVNI YDITNRLFIL KFSRNENKIY VLIEIGCRIH
     TTQFLRSVDH LPSNFNAKLR KHLRNRRLRD VKQMSQDRII DFTFSSEEHA MHLIVQLFLP
     GNIYLTDHEY KVLAVLKPKN TGDNFFKVGT NYVCDMEYNS WFEPVKRTLV EELVMGNKLT
     DLVKTIFPSI HNGFILSVLK MNGNAEEDVK KLDRVYAMDE LDVVYEYVEA VRQCLVGLLT
     RKDIVPGYIY RNAKGVMDDF GPFELQNAEY HEDYNYALDA FFTKNELVKQ EKKTESKKPT
     KLTKIKADQD KRESKLMEEI MGYDKQIRVL EENIDIVDNC LNLTKALIAS GASWNDIYEQ
     LQIQRKQNHP LVCYIKEINI PNQTLVFVSN PEGNERDDEP ERKELVEEQV VVLDYRLTGY
     QNLKKFYINR KKAENKLERT KIGKEYALKK VAKSLSKQPE VKKGDRRTRE VKISSLRKRF
     WFEKFYWFIT SQGYLVLAGR DSLQNELLVK KYLTKGDLYF HADIHGASSV ILKTNSQELI
     KSSESAEVSE VEKAGGRGNE EEFIAKIRVS IEEAANFAVC HSNAWNDKFS VQSWWVYWHQ
     VSKTPPTGEY VPQGSFVIRG KKNYLQPQKL EMGITYLFQV HPFQTLDNQE EAELAAKEEA
     GNHGVNDERN EQEDEEDEQV GQGGEEVGEY SSTDDVEEDE EDYMEQENED YDDDEINQRE
     YDEEENYMED NYEGEEEDEE DMDGALDQEG ESVDSVDEED EEDTYEVDED INDNIDHEDK
     SVRMGNVVTI GECEANIVKR TRGRLATAYP LKAQLNKLKD RLEMLNLTKS SGDDEEEEEE
     EEEESSDEEA GRTVKIMEPE RVSHTEEAIR KIRQRKATCV SPNLSELRKL INSENNKMDS
     DEEEEVGEED EEDDDGSSAS MGGPKGAAVK VALKAEHELN VKKSSNRAMR LMSQKASKVK
     KKYAQDDEET QELRRMLTGS KKMKQRTGAA TKTSFQVGPV TTDRAKESRL KGRDKEIPTI
     SDRELETYMK QLSCLSRELK EDDDVLSVIP MCAPYSAIKH YRHVLKLVPG NAKKGTIATQ
     SLQHFVKNDA QNAHYLKLIT TDQLTLTLIG NCKFTNAKM
//
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