NCBP2_DROAN
ID NCBP2_DROAN Reviewed; 154 AA.
AC B3LYP1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=GF16759;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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 via its interaction with Ars2 and is required for primary microRNAs
CC (miRNAs) processing. Also involved in innate immunity via the short
CC interfering RNAs (siRNAs) processing machinery by restricting the viral
CC RNA production. In the CBC complex, Cbp20 recognizes and binds capped
CC RNAs (m7GpppG-capped RNA) but requires Cbp80 to stabilize the movement
CC of its N-terminal loop and lock the CBC into a high affinity cap-
CC binding state with the 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. Interacts with Ars2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRM NCBP2 family. {ECO:0000305}.
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DR EMBL; CH902617; EDV42956.1; -; Genomic_DNA.
DR RefSeq; XP_001954395.1; XM_001954359.2.
DR AlphaFoldDB; B3LYP1; -.
DR SMR; B3LYP1; -.
DR STRING; 7217.FBpp0119951; -.
DR EnsemblMetazoa; FBtr0121459; FBpp0119951; FBgn0093780.
DR GeneID; 6499553; -.
DR KEGG; dan:6499553; -.
DR eggNOG; KOG0121; Eukaryota.
DR HOGENOM; CLU_070952_2_0_1; -.
DR InParanoid; B3LYP1; -.
DR OMA; TKCASPE; -.
DR OrthoDB; 1421503at2759; -.
DR PhylomeDB; B3LYP1; -.
DR Proteomes; UP000007801; Unassembled 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:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IEA:EnsemblMetazoa.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IEA:EnsemblMetazoa.
DR GO; GO:0031053; P:primary miRNA processing; IEA:EnsemblMetazoa.
DR GO; GO:0030422; P:siRNA processing; IEA:EnsemblMetazoa.
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..154
FT /note="Nuclear cap-binding protein subunit 2"
FT /id="PRO_0000385263"
FT DOMAIN 30..108
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 102..106
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 113..117
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 123..124
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
SQ SEQUENCE 154 AA; 17673 MW; E7FB365F764A6298 CRC64;
MSTSVDLSSY RDQHFKGSRS EQERSLRDST TLYVGNLSFY TTEEQIHELF SRCGDVRVIV
MGLDKYKKTP CGFCFVEYYT RAEAEAAMRF VNGTRLDDRL IRVDWDAGFI EGRQYGRGKT
GGQVRDEYRT DYDAGRGGYG KLLSQKIAPN TDNR
