NCBP2_CULQU
ID NCBP2_CULQU Reviewed; 160 AA.
AC B0W939;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Nuclear cap-binding protein subunit 2;
DE AltName: Full=20 kDa nuclear cap-binding protein;
DE AltName: Full=NCBP 20 kDa subunit;
DE Short=CBP20;
GN Name=Cbp20; ORFNames=CPIJ003555;
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB;
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the cap-binding complex (CBC), which binds co-
CC transcriptionally to the 5' cap of pre-mRNAs and is involved in various
CC processes such as pre-mRNA splicing and RNA-mediated gene silencing
CC (RNAi). The CBC complex is involved in miRNA-mediated RNA interference
CC and is required for primary microRNAs (miRNAs) processing. Also
CC involved in innate immunity via the short interfering RNAs (siRNAs)
CC processing machinery by restricting the viral RNA production. In the
CC CBC complex, Cbp20 recognizes and binds capped RNAs (m7GpppG-capped
CC RNA) but requires Cbp80 to stabilize the movement of its N-terminal
CC loop and lock the CBC into a high affinity cap-binding state with the
CC cap structure (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the nuclear cap-binding complex (CBC), a
CC heterodimer composed of Cbp80 and Cbp20 that interacts with m7GpppG-
CC capped RNA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRM NCBP2 family. {ECO:0000305}.
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DR EMBL; DS231862; EDS39736.1; -; Genomic_DNA.
DR RefSeq; XP_001845223.1; XM_001845171.1.
DR AlphaFoldDB; B0W939; -.
DR SMR; B0W939; -.
DR STRING; 7176.CPIJ003555-PA; -.
DR EnsemblMetazoa; XM_001845171.2; XP_001845223.1; LOC6034967.
DR GeneID; 6034967; -.
DR KEGG; cqu:CpipJ_CPIJ003555; -.
DR VEuPathDB; VectorBase:CPIJ003555; -.
DR VEuPathDB; VectorBase:CQUJHB013442; -.
DR eggNOG; KOG0121; Eukaryota.
DR HOGENOM; CLU_070952_2_0_1; -.
DR InParanoid; B0W939; -.
DR OMA; AENCMRY; -.
DR OrthoDB; 1421503at2759; -.
DR PhylomeDB; B0W939; -.
DR Proteomes; UP000002320; Partially assembled WGS sequence.
DR GO; GO:0005846; C:nuclear cap binding complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000339; F:RNA cap binding; IEA:InterPro.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR CDD; cd12240; RRM_NCBP2; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR027157; NCBP2.
DR InterPro; IPR034148; NCBP2_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR18847; PTHR18847; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing.
FT CHAIN 1..160
FT /note="Nuclear cap-binding protein subunit 2"
FT /id="PRO_0000385261"
FT DOMAIN 34..112
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT BINDING 14
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 106..110
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 117..121
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 127..128
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
SQ SEQUENCE 160 AA; 18508 MW; E3104C595E3E555A CRC64;
MTSVHTPSVA LSKYRDQHFK GSRHEQERLL RNSSTLYIGN LSFYTTEEQI HELFSRCGDI
RRIVMGLDKF KKTPCGFCFV EYYARIDSEY AMRYINGTRL DDRIVRVDWD AGFVEGRQYG
RGKTGGQVRD EYRQDHDLGR GGYGKMVAMG QLGAPNMRES
