YJU2_DICDI
ID YJU2_DICDI Reviewed; 324 AA.
AC Q54WR5;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Splicing factor YJU2 {ECO:0000255|HAMAP-Rule:MF_03226};
DE AltName: Full=Coiled-coil domain-containing protein 94 homolog {ECO:0000305};
GN Name=yju2; Synonyms=ccdc94; ORFNames=DDB_G0279481;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Part of the spliceosome which catalyzes two sequential
CC transesterification reactions, first the excision of the non-coding
CC intron from pre-mRNA and then the ligation of the coding exons to form
CC the mature mRNA. Plays a role in stabilizing the structure of the
CC spliceosome catalytic core and docking of the branch helix into the
CC active site, producing 5'-exon and lariat intron-3'-intermediates.
CC {ECO:0000255|HAMAP-Rule:MF_03226}.
CC -!- SUBUNIT: Component of the spliceosome. Present in the activated B
CC complex, the catalytically activated B* complex which catalyzes the
CC branching, the catalytic step 1 C complex catalyzing the exon ligation,
CC and the postcatalytic P complex containing the ligated exons (mRNA) and
CC the excised lariat intron. {ECO:0000255|HAMAP-Rule:MF_03226}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BW85,
CC ECO:0000255|HAMAP-Rule:MF_03226}.
CC -!- SIMILARITY: Belongs to the CWC16 family. YJU2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03226}.
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DR EMBL; AAFI02000031; EAL67679.1; -; Genomic_DNA.
DR RefSeq; XP_641652.1; XM_636560.1.
DR AlphaFoldDB; Q54WR5; -.
DR SMR; Q54WR5; -.
DR STRING; 44689.DDB0233745; -.
DR PaxDb; Q54WR5; -.
DR EnsemblProtists; EAL67679; EAL67679; DDB_G0279481.
DR GeneID; 8622059; -.
DR KEGG; ddi:DDB_G0279481; -.
DR dictyBase; DDB_G0279481; ccdc94.
DR eggNOG; KOG2989; Eukaryota.
DR HOGENOM; CLU_053603_0_0_1; -.
DR InParanoid; Q54WR5; -.
DR OMA; PLETHYK; -.
DR PhylomeDB; Q54WR5; -.
DR PRO; PR:Q54WR5; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IEA:UniProtKB-UniRule.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR HAMAP; MF_03226; YJU2; 1.
DR InterPro; IPR007590; Saf4/Yju2.
DR InterPro; IPR043701; Yju2.
DR PANTHER; PTHR12111; PTHR12111; 1.
DR Pfam; PF04502; Saf4_Yju2; 1.
PE 3: Inferred from homology;
KW Metal-binding; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Spliceosome; Zinc.
FT CHAIN 1..324
FT /note="Splicing factor YJU2"
FT /id="PRO_0000389020"
FT REGION 294..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226"
SQ SEQUENCE 324 AA; 37472 MW; 2F5C927AA72BD139 CRC64;
MGERKVISKY YPPDFDPSKV AKIKVKRPTF TKVTTMLPMS IRCNTCGEYI GRGTKFNAKK
ETVQNEDYLG IKIYRFFLRC KKCAAELTIK TDPKNSEYVC ESGATRNYEP WKETDEEKSN
RMTKEQEEEQ DAMIALENRT LESKREMEML DALEEIKSLN SRNSEIDTEQ LLEYNLQKQE
LEEKLQDEED DLLVKSIFNN KNKLELNQIN DNNSINNNID SNKIKRIEND DDDGDKFNSL
FSNNNKNNKN IINNNNNNNN NINTTSISNT IETTPTTNQK TSILGNKVKV VINKQEEPIP
KNNNNSEPNS FSSFMSAYSD DEED
