ID Q4UAD2_THEAN Unreviewed; 1269 AA.
AC Q4UAD2;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 97.
DE SubName: Full=U5 snRNP subunit, putative {ECO:0000313|EMBL:CAI76219.1};
GN ORFNames=TA09375 {ECO:0000313|EMBL:CAI76219.1};
OS Theileria annulata.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5874 {ECO:0000313|EMBL:CAI76219.1, ECO:0000313|Proteomes:UP000001950};
RN [1] {ECO:0000313|EMBL:CAI76219.1, ECO:0000313|Proteomes:UP000001950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ankara {ECO:0000313|Proteomes:UP000001950};
RX PubMed=15994557; DOI=10.1126/science.1110418;
RA Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA Shiels B., Tait A., Barrell B.G., Hall N.;
RT "Genome of the host-cell transforming parasite Theileria annulata compared
RT with T. parva.";
RL Science 309:131-133(2005).
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DR EMBL; CR940353; CAI76219.1; -; Genomic_DNA.
DR RefSeq; XP_952844.1; XM_947751.1.
DR AlphaFoldDB; Q4UAD2; -.
DR STRING; 5874.Q4UAD2; -.
DR GeneID; 3863287; -.
DR KEGG; tan:TA09375; -.
DR VEuPathDB; PiroplasmaDB:TA09375; -.
DR eggNOG; KOG0468; Eukaryota.
DR InParanoid; Q4UAD2; -.
DR OMA; YIFRPIR; -.
DR OrthoDB; 166721at2759; -.
DR Proteomes; UP000001950; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd04098; eEF2_C_snRNP; 1.
DR CDD; cd04090; EF2_II_snRNP; 1.
DR CDD; cd01683; EF2_IV_snRNP; 1.
DR CDD; cd04167; Snu114p; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR031950; EFTUD2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR044121; Snu114_GTP-bd.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR035655; U5-116kDa_C.
DR PANTHER; PTHR42908:SF6; 116 KDA U5 SMALL NUCLEAR RIBONUCLEOPROTEIN COMPONENT; 1.
DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF16004; EFTUD2; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR SMART; SM00838; EFG_C; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
PE 4: Predicted;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001950}.
FT DOMAIN 1126..1215
FT /note="Elongation factor EFG"
FT /evidence="ECO:0000259|SMART:SM00838"
FT REGION 193..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1269 AA; 143047 MW; 61D2E365A0E0572E CRC64;
MDQNLYDEFG NYIGPGFEDD YDNGFNSDIS DTESNYNSNH NNKIQDSIDN SIDNLKVDSV
VDSLKDSINS LKDSVDSINS LKDTVNEEEV YKGVEVYIRE EDIQTIEIPI IKSNEINKRK
KYKLDSDITL KNFHILEENL PENKFNFQFL SSITKNPQFI RNICIAGNFH DGKTTFIDRL
IEFTRQHTHT HTFHTNSHYN TNNSNSPNNS TNSHKSTVKY NKYSNRNGDM EYNRYMDNRM
DEQLRELSIK STPISIILEN RLYEKINEES NYPKYKSYLF NIFDTPGHVN FMDEFVYSLA
ICDGCVLIVD VLIGLTKVTE QIIIQCLQTG VHMCLILNCI DRLILELKLP PADAYLKIQH
TIIEINQFIY SSSTVLGHTG TTSTKVSSSN TNTKETHFGD KETPFGGTLG PSTVTELFDP
KNNNVGFGSS KFGIFFTLKS FATLYTNDNV TQFSKLLYGN YYYDPIHNII TTNNTTTNST
RTNGVGVNGM SDGLDGTSDR VNGMEEGNNE IELERTFVVF ILEPLYKLIS HIASDEKEDL
DLILSDLSNS LFNTKLTHTK NTNFNTEDLD TEDYDMEDVD MEDEEDEENS SIENSFKNNK
KKIILRKLDY KLTTNKIIRK VFNQIFTDAS AFVDLILTTI PSSLENNLNK FICHYSGTLY
KNLLNSVGNC DPSGPLIIFI TKNYYFDDGF SLFGRIFSGT IFKGQKVKLL GPSYTLDDDE
DVIIRNISNI WIYEGRYRIE VTNMTAGNWV MLSGIDLSHY KITTIVNSSS TVLGPTDTNG
PNTITNGPNT NTNGVYNNKE APFGAVDTGA VGASPVTEEL ELMKIITNIK CIRPIFKIGL
EPLNPNELPK MINGLRSIEK SYPGSLVKVE ESGEHIILGT GELYLDCILH DLRLFGNLEI
KVSDPVVKFS ETITESTSLI TFTHTNNLKN KLYMISQPLE SNISTLLDST IGVNSIRLDS
GLNGMGLNGG LDSMGLNGVN RGVYRGVGMS SMGMSGLDME LNKEWDILDI KNVWSFGNGI
PDVLINDTIP NEVDINLLNH IKSSIIQGFQ WAIKEGPLIE EHIRYCVTVL ATAAPISPLT
STVTPNVKFR LINCELSNEY INITPGQIIP ATRRLCYSSF LLSTPRLMEP ILFSEIFCPA
DCVSEAYKIL SKRRGHVLKD MPKPGTPFYI VHAYLPAIES FGFETDLRVD TSGQAFCLSM
FDHWNIVPGD PLDKSIILRT LEPAPIPHLA REFLVKTRRR KGLTEDVSIN TFFDEEMITS
LAENLQEFY
//
