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Database: UniProt
Entry: A0A3Q0CQI8_MESAU
LinkDB: A0A3Q0CQI8_MESAU
Original site: A0A3Q0CQI8_MESAU 
ID   A0A3Q0CQI8_MESAU        Unreviewed;       971 AA.
AC   A0A3Q0CQI8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=116 kDa U5 small nuclear ribonucleoprotein component {ECO:0000256|ARBA:ARBA00018774};
DE   AltName: Full=U5 snRNP-specific protein, 116 kDa {ECO:0000256|ARBA:ARBA00031432};
GN   Name=Eftud2 {ECO:0000313|RefSeq:XP_021082843.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021082843.1};
RN   [1] {ECO:0000313|RefSeq:XP_021082843.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_012968846.1; XM_013113392.1.
DR   RefSeq; XP_021082843.1; XM_021227184.1.
DR   AlphaFoldDB; A0A3Q0CQI8; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005681; C:spliceosomal 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; cd16264; snRNP_III; 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; IPR041095; EFG_II.
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; PF14492; EFG_III; 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   Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW   Ribonucleoprotein {ECO:0000313|RefSeq:XP_021082843.1};
KW   Spliceosome {ECO:0000256|ARBA:ARBA00022728}.
FT   DOMAIN          126..408
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..48
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   971 AA;  109335 MW;  1F8765CEED76C503 CRC64;
     MDTDLYDEFG NYIGPELDSD EDDDELGRET KDLDEDDDED EDDVGEHDDD HPGMEVVLHE
     DKKYYPTAEE VYGPEVETIV QEEDTQPLTE PIIKPVKTKK FTLMEQTLPV TVYEMDFLAD
     LMDNSELIRN VTLCGHLHHG KTCFVDCLIE QTHPEIRKRY DQDLCYTDIL FTEQERGVGI
     KSTPVTVVLP DTKGKSYLFN IMDTPGHVNF SDEVTAGLRI SDGVVLFIDA AEGVMLNTER
     LIKHAVQERL AVTVCINKID RLILELKLPP TDAYYKLRHI VDEVNGLISM YSTDENLTLS
     PLLGNVCFSS SQYSICFTLG SFAKIYADTF GDINYQEFAK RLWGDIYFNP KTRKFTKKAP
     TSSSQRSFVE FILEPLYKIL AQVVGDVDTS LPRTLDELGI HLTKEELKLN IRPLLRLVCK
     KFFGEFTGFV DMCVQHIPSP KVGAKPKIEH TYTGGVDSDL GEAMSDCDPD GPLMCHTTKM
     YSTDDGVQFH AFGRVLSGTI HAGQPVKVLG ENYTLEDEED SQICTVGRLW ISVARYHIEV
     NRVPAGNWVL IEGVDQPIVK TATITEPRGN EEAQIFRPLK FNTTSVIKIA VEPVNPSELP
     KMLDGLRKVN KSYPSLTTKV EESGEHVILG TGELYLDCVM HDLRKMYSEI DIKVADPVVT
     FCETVVETSS LKCFAETPNK KNKITMIAEP LEKGLAEDIE NEVVQITWNR KKLGEFFQTK
     YDWDLLAARS IWAFGPDATG PNILVDDTLP SEVDKALLGS VKDSIVQGFQ WGTREGPLCD
     ELIRNVKFKI LDAVVAQEPL HRGGGQIIPT ARRVVYSAFL MATPRLMEPY YFVEVQAPAD
     CVSAVYTVLA RRRGHVTQDA PIPGSPLYTI KAFIPAIDSF GFETDLRTHT QGQAFSLSVF
     HHWQIVPGDP LDKSIVIRPL EPQPAPHLAR EFMIKTRRRK GLSEDVSISK FFDDPMLLEL
     AKQDVVLNYP M
//
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