CWC2_DICDI
ID CWC2_DICDI Reviewed; 528 AA.
AC Q54PH5;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Pre-mRNA-splicing factor cwc2;
GN Name=cwc2; ORFNames=DDB_G0284563;
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: Involved in pre-mRNA splicing. Binds RNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Associated with the spliceosome. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The C-terminal RRM domain and the zinc finger motif are
CC necessary for RNA-binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRM CWC2 family. {ECO:0000305}.
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DR EMBL; AAFI02000066; EAL65208.1; -; Genomic_DNA.
DR RefSeq; XP_638557.1; XM_633465.1.
DR AlphaFoldDB; Q54PH5; -.
DR SMR; Q54PH5; -.
DR STRING; 44689.DDB0267176; -.
DR PaxDb; Q54PH5; -.
DR EnsemblProtists; EAL65208; EAL65208; DDB_G0284563.
DR GeneID; 8624650; -.
DR KEGG; ddi:DDB_G0284563; -.
DR dictyBase; DDB_G0284563; cwc2.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_516251_0_0_1; -.
DR InParanoid; Q54PH5; -.
DR OMA; NSRYEDH; -.
DR PRO; PR:Q54PH5; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
DR GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; ISS:dictyBase.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IBA:GO_Central.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036002; F:pre-mRNA binding; ISS:UniProtKB.
DR GO; GO:0017070; F:U6 snRNA binding; ISS:UniProtKB.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0045787; P:positive regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0033120; P:positive regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR CDD; cd12360; RRM_cwf2; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR039173; Cwc2.
DR InterPro; IPR039171; Cwc2/Slt11.
DR InterPro; IPR034181; Cwc2_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR032297; Torus.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR14089; PTHR14089; 1.
DR PANTHER; PTHR14089:SF2; PTHR14089:SF2; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF16131; Torus; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 3: Inferred from homology;
KW Metal-binding; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW RNA-binding; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1..528
FT /note="Pre-mRNA-splicing factor cwc2"
FT /id="PRO_0000356958"
FT DOMAIN 187..263
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 122..149
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..473
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 61401 MW; E76768792458FBAD CRC64;
MTSKKQKSSI DTITPTPPNT TTTTTTTSTT ATTKDKKKSK KPKSSGLTKV GADIIELQAS
LLNRPARKQA THVNSRYEDH DTDTTEYNIW YHKKLGNRNW KDRDVSETRC NVLKDCGKTR
ANKDANFCCY FARGKCINGA DCTSLHRIPT PEDDKRLRLT HDIFGRERHK TDRDDMNGVG
SFSRDNRTLY IGGIKTNVSG SLEDMVRKNF EEWGRIEYVR VITNRSISFV RYLTRSSAEF
AKEAMTDQTL DNGELLNIRW ATEDSNPYAK KVDERNLHRV ATEVINKRIR EMTPDDQSAL
KYQMTGQYPN TDQQYDQNGQ PINASPSTPY QLQYRGSTKY EAHPYARQYN NDLQKRVQSG
ETVDVAPLNG VGNYYSHSVG TMNQELQKQQ YDNYMQQYYQ AYGYDYSKLS DDQKLQLQQY
FQSYYYGNQQ EQQQQETQQI QNNNENNNDN EEEDDDDEDD DDDNEDDDND NEETKDNKND
KVENKEEENK EVQEKINTES KEDTKNEEQE KKEEKEKTDS DNIVNKED
