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U5S1_CHICK
ID   U5S1_CHICK              Reviewed;         972 AA.
AC   Q5F3X4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=116 kDa U5 small nuclear ribonucleoprotein component;
DE   AltName: Full=Elongation factor Tu GTP-binding domain protein 2;
DE   AltName: Full=U5 snRNP-specific protein, 116 kDa;
DE            Short=U5-116 kDa;
GN   Name=EFTUD2; Synonyms=SNRP116; ORFNames=RCJMB04_4m11;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC       spliceosome, including pre-catalytic, catalytic and post-catalytic
CC       spliceosomal complexes (By similarity). Component of the U5 snRNP and
CC       the U4/U6-U5 tri-snRNP complex, a building block of the spliceosome (By
CC       similarity). {ECO:0000250|UniProtKB:Q15029}.
CC   -!- SUBUNIT: Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex,
CC       a building block of the spliceosome (By similarity). Component of the
CC       pre-catalytic, catalytic and post-catalytic spliceosome complexes (By
CC       similarity). {ECO:0000250|UniProtKB:Q15029}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15029}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR   EMBL; AJ851526; CAH65160.1; -; mRNA.
DR   RefSeq; NP_001026672.1; NM_001031501.1.
DR   AlphaFoldDB; Q5F3X4; -.
DR   SMR; Q5F3X4; -.
DR   STRING; 9031.ENSGALP00000001456; -.
DR   PaxDb; Q5F3X4; -.
DR   Ensembl; ENSGALT00000001458; ENSGALP00000001456; ENSGALG00000000988.
DR   GeneID; 428281; -.
DR   KEGG; gga:428281; -.
DR   CTD; 9343; -.
DR   VEuPathDB; HostDB:geneid_428281; -.
DR   eggNOG; KOG0468; Eukaryota.
DR   GeneTree; ENSGT00940000155685; -.
DR   HOGENOM; CLU_002794_11_2_1; -.
DR   InParanoid; Q5F3X4; -.
DR   OMA; GPDEMGP; -.
DR   OrthoDB; 140796at2759; -.
DR   PhylomeDB; Q5F3X4; -.
DR   Reactome; R-GGA-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-GGA-72165; mRNA Splicing - Minor Pathway.
DR   PRO; PR:Q5F3X4; -.
DR   Proteomes; UP000000539; Chromosome 27.
DR   Bgee; ENSGALG00000000988; Expressed in testis and 13 other tissues.
DR   ExpressionAtlas; Q5F3X4; baseline and differential.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; ISS:UniProtKB.
DR   GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0030623; F:U5 snRNA binding; IBA:GO_Central.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   CDD; cd04098; eEF2_C_snRNP; 1.
DR   CDD; cd04167; Snu114p; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 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_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_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   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; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF54980; SSF54980; 2.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   2: Evidence at transcript level;
KW   GTP-binding; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW   Reference proteome; Spliceosome.
FT   CHAIN           1..972
FT                   /note="116 kDa U5 small nuclear ribonucleoprotein
FT                   component"
FT                   /id="PRO_0000315998"
FT   DOMAIN          127..409
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..49
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         136..143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         204..208
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         258..261
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   972 AA;  109478 MW;  8AC26F2335616FE0 CRC64;
     MDTDLYDEFG NYIGPELDSD DEDDELGRES KELDELEDDD DDDDMGDHDE DHPGMEVVLH
     EDKKYYPTAE EVYGPEVETI VQEEDTQPLT EPIIKPVKTK KFSLMEQTLP VTVYEMDFLA
     DLMDNSELIR NVTLCGHLHH GKTCFVDCLI EQTHPEIRKR YDQDLCYTDI LFTEQERGVG
     IKSTPVTIVL PDTKGKSFLF NIIDTPGHVN FSDEVTAGLR ISDGVVLFID AAEGVMLNTE
     RLIKHAVQER LAVTVCINKI DRLILELKLP PTDAYYKLRH IVDEVNGLIS MYSTDENLVL
     SPLLGNVCFS SSQYSICFTL GSFAKIYADT YGDINYQEFA KRLWGDIYFN PKTRKFTKKA
     PTSSSQRSFV EFILEPLYKI LAQVVGDVDT TLPRTLDELG IHLTKEELKL NIRPLLRLVC
     KKFFGEFTGF VDMCVQHIPS PKVGAKTKIE HTYTGGVDSD LGEAMSECDP DGPLMCHTTK
     MYSTDDGVQF HAFGRVLSGT IHAGQPVKVL GENYTLEDEE DSQICTVGRL WISVARYHIE
     VNRVPAGNWV LIEGVDQPIV KTATVTEPRG NEEAQIFRPL KFNTTSVIKI AVEPVNPSEL
     PKMLDGLRKV NKSYPSLTTK VEESGEHVIL GTGELYLDCV MHDLRKMYSE IDIKVADPVV
     TFCETVVETS SLKCFAETPN KKNKITMIAE PLEKGLAEDI ENEVVQITWN RKKLGEFFQT
     KYDWDLLAAR SIWAFGPDAT GPNILVDDTL PSEVDKALLG SVKDSIVQGF QWGTREGPLC
     DELIRNVKFK ILDAVIAQEP LHRGGGQIIP TARRVVYSAF LMATPRLMEP YYFVEVQAPA
     DCVSAVYTVL ARRRGHVTQD APIPGSPLYT IKAFIPAIDS FGFETDLRTH TQGQAFSLSV
     FHHWQIVPGD PLDKSIVIRP LEPQPAPHLA REFMIKTRRR KGLSEDVSIS KFFDDPMLLE
     LAKQDVVLNY PM
 
 
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