ID A0A0M0J550_9EUKA Unreviewed; 999 AA.
AC A0A0M0J550;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=U5 small nuclear ribonucleoprotein component {ECO:0000313|EMBL:KOO21605.1};
GN ORFNames=Ctob_001269 {ECO:0000313|EMBL:KOO21605.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO21605.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOO21605.1}.
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DR EMBL; JWZX01003349; KOO21605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0J550; -.
DR OrthoDB; 166721at2759; -.
DR Proteomes; UP000037460; 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; cd04096; eEF2_snRNP_like_C; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000037460};
KW Ribonucleoprotein {ECO:0000313|EMBL:KOO21605.1}.
FT DOMAIN 138..361
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 999 AA; 110376 MW; 47A9DA3143C3321D CRC64;
MDAEEDLYDE FGNYIGPEID SDEDEDGAPE IDDFGDDDED GDDEVVDVGG AGYAMDDDEV
AGEDDTRVTL HEDKKYYPTA MEVYGEEVET TVQEEDTQPI TQPIVAPMKA KEYDLVEKKI
PRSVYSHEFL TSLLPHPHLV RNVAIVGHMQ HGKTTLVDNL IATTHVPDPS AAAKNGKKAA
GGGAQTSRGR RYTDTRADEQ KRGLSIKAMP ITLLLQSPSE KHYVFNLIDT PGHVNFSDEV
SAALRLADGA LLVVDAVEGV SSTTEQLIRH LVTERVPVVL CVNKLDRLIL ELKLPPQDAY
FKLRQVIEEV NSALRAASGG AHKRLSPEEG SVIFASAEQD WCFTLESFAT IYADFYPSIP
AATLARRLWG DVYYQPVSRT FRRKPPDGGG PRTFVQFVLD PLYKLVSATI SSPEPELRDV
LADLGIGLKK AEFALDPKPM LKLTMARFFG GSYAGLVAAL VAHLPSPAQG AALKVEHTYS
GERSDSCVAP MLACDPSGLL MANVTKMYHK PDCESFDAFG RVFSGTLRVG DEVQVLGEAY
SLDDQEDSAQ KTISRLWIYM ARYRVEVTEV PAGCWALIEG VEGSLVKTGT ITSLGAEDVR
IFRPLAFDTM SVMKLATEPL HPSELPRMLE GLRKLNKAYP LLSTKVEESG EHVIIGTGEL
YLDCVMHDLR HVYAEIEVKV SDPVVTFCET VLETSSLKCF AESPNGRSKL AMIAEPLEKG
LAEDIERGAV DIRWDRKRLG EFFQTKYSWD LLAARSVWGF APDARGPNVL VDDTLPSEVD
KKLLGSIREY ILQGFGWASR EGPLCDEPMR NVKFKVLDAT IAAEPIQRGG GQIIPTARRV
AYSAFLMATP RLMEPVYAVE IMAPVDCVPA IYTVLGRRRG HVTSEGPRPG TPLHMLTAFV
PVIDSFGFET DLRSHTQGRA FALCTFHHYA IVPGDPLDKT ITLRPLEPQP VPHLAREFMV
KTRRRKGLSE DVSISKFFDD PMLLELAKQD AETNQTAYF
//
