ID   A0A3B3ZWX7_9GOBI        Unreviewed;       902 AA.
AC   A0A3B3ZWX7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
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};
OS   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000009238.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000009238.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   AlphaFoldDB; A0A3B3ZWX7; -.
DR   STRING; 409849.ENSPMGP00000009238; -.
DR   Ensembl; ENSPMGT00000009849.1; ENSPMGP00000009238.1; ENSPMGG00000007281.1.
DR   Proteomes; UP000261520; 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   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; 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   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   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.
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   Spliceosome {ECO:0000256|ARBA:ARBA00022728}.
FT   DOMAIN          636..755
FT                   /note="Translation elongation factor EFG/EF2"
FT                   /evidence="ECO:0000259|SMART:SM00889"
FT   DOMAIN          757..845
FT                   /note="Elongation factor EFG"
FT                   /evidence="ECO:0000259|SMART:SM00838"
FT   REGION          1..51
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   902 AA;  101307 MW;  5F83F58E6BD43C5D CRC64;
     MEADLYDEFG NYIGPELDSD DDDDDLDAED RDMDEDDEDD EPADADEEVP GMEVVLHEDK
     KYYPTAEEVY GPEVETIVQE EDTQPLTPII KPVKHRKFTL MEQELPATVY DMFLADLMDS
     PELIRNVTLC GHLHHGKTCF VDCLIEQTHP EIRKRDDLDL RYTDILFTEQ ERGVGIKSTP
     VTMVLPDSRG KSYLFNIMDT PVNFSDEVTS SIRLSDGIVL FIDAAEGTYS TDENVVVSPL
     LGNVCFASSQ YSICFTLGSF AKIYSDTYDI NYTEFAQRLW GDIYFNPKRK FTKKAPTSNS
     QRSFVEFVLE PLYKILSQVV GDVDTSLPRV LDELGIHLSK EELKLNIRPL LRLVCNRFFG
     EFTGLVDMCV QHIPSPQDGA KTKIEHTYTG GLDSDLGETM SECDPDGPLM CHTTKMYSTE
     DGVQFHAFGR VLSGTIQAGQ PVKVLGENYT LDDEEDSQVC TVGRLWISVA YQIEVNRVPA
     GNWVLIEGCD QSIVKTSTIT EPRGNEDAQI FRPLKFNTAS VIKIAVEPVN PSELPKMLDG
     LRKVNKSYPS LTTKVEESGE HVILGTGELY LDCVMHDLRK MYSEIDIKVA DPVVTFCETV
     VETSSLKCFA ETPNKNKITM IAEPLEKGLA EDIESEVVQI TWNKKLGEFF QTKYDWDLLA
     ARSIWAFGPD TTGPNILVDD TLPSEVDKAL LGSVKDSIVQ GFQWGTREGP LCDEIRNVKF
     KILDAVIAQE PLHRGGGQVI PTARRVVYSA FLMATPRLME PYYFVEVQAP ADCVSAVYTV
     LARRGHVTQD APIPGSPLYT IKAFIPAIDS FGFETDLRTH TQGQAFALSV FHHWQIVPGD
     PLDKSIVIRP LEPQPAPHLA REFMIKTRRR KGLSEDVSIS KFFDDPMLLE LAKQDVVLNY
     PM
//