ID F1KTY9_ASCSU Unreviewed; 979 AA.
AC F1KTY9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=116 kDa U5 small nuclear ribonucleoprotein component {ECO:0000313|EMBL:ADY41343.1};
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY41343.1};
RN [1] {ECO:0000313|EMBL:ADY41343.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21685128; DOI=10.1101/gr.121426.111;
RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA Davis R.E.;
RT "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT functional diversification, and novel developmental profiles.";
RL Genome Res. 21:1462-1477(2011).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JI165828; ADY41343.1; -; mRNA.
DR AlphaFoldDB; F1KTY9; -.
DR EnsemblMetazoa; AgR031_g016_t01; AgR031_g016_t01; AgR031_g016.
DR EnsemblMetazoa; AgR031_g016_t03; AgR031_g016_t03; AgR031_g016.
DR EnsemblMetazoa; AgR031_g016_t04; AgR031_g016_t04; AgR031_g016.
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; 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; 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 2: Evidence at transcript level;
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:ADY41343.1}.
FT DOMAIN 132..415
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..53
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 979 AA; 111220 MW; 469E764B65D9F678 CRC64;
MDADLYDEFG NYIGPELDSD DSDDEDASFV QTRNVEEEEE KEAEEEEETV EEEPERAPAN
QIVLHEDKKY YATAMEIYGE DVETIVQEED AQPLTEPIIK PIKQRKFQAL EQSLPETTYN
KEYLADLMDC PHVMRNVAIA GHLHHGKTTF IDCLMEQTHP DFMRGEDTDT RFTDTLFIEQ
QRGCSVKAMP VTLMLQDSRH KSYLLNIIDT PGHVNFSDEM TAAYRLSDGV VIVVDAHEGV
MLQTERAIRH AVQERLPVTV CINKIDRLIL ELKLPPTDAY YKLRFVLDQV NGLLQTFSDD
AESAQVSPLL HNVIFASSRY NICFSLESFA NLYADHYGSF NGMEFARRLW GEQYFDKKTR
KFVKKPPHSG APRSFVEFIL EPLYKIFSQV VGDVDTCLPL MMSELGIKLS KEEQRMNVRP
LIALICRRFF GDFTAFVDLV TRNIKSPTEN ARIKTEHIYL GPMDSKMAEA LFKCDAEGPL
MVHTTKNYAT VDATSFHVFG RVMSGTLSAG QDVRVLGENY SIQDEEDCRV MTVGRLWVSE
ARYTVEVSRV PAGNWVLIEG IDQPIVKTST ITQLDFDEDV YIFRPLKFNT KSVVKMAVEP
INPSELPKML DGLRKVNKSY PLLTTRVEES GEHVMLGTGE LYMDCVMHDM RKVFSEIDIK
VADPVVSFCE TVVETSSLKC FAETPNKKNK LTMIAEPLEK GLAEDIESEV VQIGWNRKRL
GEFFQTKYDW DLLAARSIWA FGPDTTGPNV LLDDTLPSEV DKQLLGSVRE SLVQGFQWAT
REGPLCEEPI RNVKFKMLDA VIAQEPLYRG GGQIIPTARR CAYSAFLMAT PRLMEPYYFV
EVTAPADCVS SVYTVLAKRR GHVTTDAPIP GSPLYTIKAY IPVIDSFGFE TDLRTHTQGQ
AFCLSVFSHW QIVPGDPLDK SIVIRPLELQ PAPHLAREFM VKTRRRKGLS EDVSVNKFFD
DPMLLELAKQ QDVFSYANF
//
