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Database: UniProt
Entry: M7XI91_RHOT1
LinkDB: M7XI91_RHOT1
Original site: M7XI91_RHOT1 
ID   M7XI91_RHOT1            Unreviewed;       980 AA.
AC   M7XI91;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=116 kDa u5 small nuclear ribonucleoprotein component {ECO:0000313|EMBL:EMS19863.1};
GN   ORFNames=RHTO_03906 {ECO:0000313|EMBL:EMS19863.1};
OS   Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS19863.1, ECO:0000313|Proteomes:UP000016926};
RN   [1] {ECO:0000313|EMBL:EMS19863.1, ECO:0000313|Proteomes:UP000016926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NP11 {ECO:0000313|EMBL:EMS19863.1,
RC   ECO:0000313|Proteomes:UP000016926};
RX   PubMed=23047670; DOI=10.1038/ncomms2112;
RA   Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA   Ye M., Zou H., Zou H., Zhao Z.K.;
RT   "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL   Nat. Commun. 3:1112-1112(2012).
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DR   EMBL; KB722665; EMS19863.1; -; Genomic_DNA.
DR   RefSeq; XP_016270982.1; XM_016417575.1.
DR   AlphaFoldDB; M7XI91; -.
DR   GeneID; 27367919; -.
DR   eggNOG; KOG0468; Eukaryota.
DR   HOGENOM; CLU_002794_11_2_1; -.
DR   OrthoDB; 166721at2759; -.
DR   Proteomes; UP000016926; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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   Gene3D; 3.90.1430.10; Yeast translation eEF2 (G' domain); 1.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR004161; EFTu-like_2.
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; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR044121; Snu114_GTP-bd.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   InterPro; IPR035655; U5-116kDa_C.
DR   NCBIfam; TIGR00231; small_GTP; 1.
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; PF03764; EFG_IV; 1.
DR   Pfam; PF16004; EFTUD2; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 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.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
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   Ribonucleoprotein {ECO:0000313|EMBL:EMS19863.1}.
FT   DOMAIN          138..345
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   980 AA;  109089 MW;  D9407D91FCA94A02 CRC64;
     MDLYDEFGNY IGPEDDLESD YSDDEAGEQR QQDGAASPTP APLRAYDEDE VEPLEGMEVD
     DVPSSNAIVL HEDKTYYASA SATYGPGVET MVQEEDAQPL SVPIIEPVKT RKFRLGATTG
     PERRWDDQFM MGLASNPETV RNVAIVGHLH HGKTSLVDML VAETHKIDID TDKQLRFTDT
     HSLSQSRKIS IKSSPMSLVL SNTKGKSYLV NLVDTPGHSN FVDEIASAVR VADGAVVVVD
     AVEGVMLTTT QTIQHLVKNR IPIVLVVNKV DRLILELRLP PGDAYFKLKQ TIEEVNTVIS
     ELDPDPALRV SPERGNVAFA STQMGWCFTL KSFAKMYADT YGPMDLDQFA VRLWGNIYYH
     PETRKFSRQS APGAKRGFEH FIMEPLYKLY SQVIGEDTDS LRKTLHQLGI HFKPSVYKMD
     VRPLLRLVLA HFFGPPTGFV DMIVQHVPNP QQGARVKVES TYTGALDSPL GQALLNCDPE
     GPLAIQIVKL YPTPDASEFR AFGRVLSGTA QVGQEVKVLG EGYSPEDEED MVVQQIGGIY
     VGEARYDIET DAMPAGNFVQ LSGVDNSISK TATLIAADYD ASELRIFRPI AHFTQSVLKV
     SVEPLMPSEL PKMLDGLRKV NKTYPLIETR VEESGEHVLL GTGELYLDCA MHDLRVMFAE
     IEIKISDPVV RFCETVVETS ALKCYADTPN KKNKITMIAE PLERGIAEDI ETGKISIRLP
     PKQLGQHFQN KYGWDLLASR SIWAFGPDDQ GPNLLMDDTL PSDVDKKLLY TVKESIKQGF
     QWGCREGPLC DEPIRNVKFR LLGADLAHEP IYRGGGQIIP TARRVCYSSF LMATPRLQEP
     VYFVEIQAPQ DCVPAIYEIL ARRRGHVTKD IPKPGSPLFT VQAYIPVVDA NGFETDLRTH
     TLGQAFCVQT FDHWSICPGD PLDKTIQLRP LEPAPAQALA RDFVLKTRRR KGLNDQVNVA
     KFLEAEMVTL LASTEHLDLL
//
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