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NCBP2_DROGR
ID   NCBP2_DROGR             Reviewed;         154 AA.
AC   B4JUT1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=GH15101;
OS   Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Hawaiian Drosophila.
OX   NCBI_TaxID=7222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15287-2541.00;
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; CH916374; EDV91251.1; -; Genomic_DNA.
DR   RefSeq; XP_001994622.1; XM_001994586.1.
DR   AlphaFoldDB; B4JUT1; -.
DR   SMR; B4JUT1; -.
DR   STRING; 7222.FBpp0149007; -.
DR   EnsemblMetazoa; FBtr0150515; FBpp0149007; FBgn0122576.
DR   GeneID; 6568059; -.
DR   KEGG; dgr:6568059; -.
DR   eggNOG; KOG0121; Eukaryota.
DR   HOGENOM; CLU_070952_2_0_1; -.
DR   InParanoid; B4JUT1; -.
DR   OMA; TKCASPE; -.
DR   OrthoDB; 1421503at2759; -.
DR   PhylomeDB; B4JUT1; -.
DR   Proteomes; UP000001070; 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_0000385265"
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;  17671 MW;  C5EBA1C23ADD9F32 CRC64;
     MTASVDLSSY RDQHFKGSRS EQERSLRDST TLYVGNLSFY TTEEQIHELF SRCGDVRIIV
     MGLDKYKKTP CGFCFVEYYT RAEAEAAMRF VNGTRLDDRL IRVDWDAGFI EGRQYGRGKT
     GGQVRDEYRT DYDAGRGGYG KLLSQKIAPN TDNR
 
 
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