ID   NCBP1_DROVI             Reviewed;         783 AA.
AC   B4M7T6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Nuclear cap-binding protein subunit 1;
DE   AltName: Full=80 kDa nuclear cap-binding protein;
DE            Short=CBP80;
DE            Short=NCBP 80 kDa subunit;
GN   Name=Cbp80; ORFNames=GJ17049;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87;
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
CC       cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in
CC       various processes such as pre-mRNA splicing and RNA-mediated gene
CC       silencing (RNAi). The CBC complex is involved in miRNA-mediated RNA
CC       interference via its interaction with Ars2 and is required for primary
CC       microRNAs (miRNAs) processing. Also involved in innate immunity via the
CC       short interfering RNAs (siRNAs) processing machinery by restricting the
CC       viral RNA production. In the CBC complex, Cbp80 does not bind directly
CC       capped RNAs (m7GpppG-capped RNA) but is required to stabilize the
CC       movement of the N-terminal loop of Cbp20 and lock the CBC into a high
CC       affinity cap-binding state with the cap structure (By similarity).
CC       {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 NCBP1 family. {ECO:0000305}.
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DR   EMBL; CH940653; EDW62853.1; -; Genomic_DNA.
DR   RefSeq; XP_002057367.2; XM_002057331.2.
DR   AlphaFoldDB; B4M7T6; -.
DR   SMR; B4M7T6; -.
DR   STRING; 7244.FBpp0231466; -.
DR   GeneID; 6633562; -.
DR   KEGG; dvi:6633562; -.
DR   eggNOG; KOG1104; Eukaryota.
DR   HOGENOM; CLU_013207_0_0_1; -.
DR   InParanoid; B4M7T6; -.
DR   OMA; QPFKIPF; -.
DR   PhylomeDB; B4M7T6; -.
DR   ChiTaRS; Cbp80; fly.
DR   Proteomes; UP000008792; 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:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0006406; P:mRNA export from nucleus; IEA:InterPro.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR027159; CBP80.
DR   InterPro; IPR015172; MIF4G-like_typ-1.
DR   InterPro; IPR015174; MIF4G-like_typ-2.
DR   InterPro; IPR003890; MIF4G-like_typ-3.
DR   PANTHER; PTHR12412; PTHR12412; 1.
DR   Pfam; PF02854; MIF4G; 1.
DR   Pfam; PF09088; MIF4G_like; 1.
DR   Pfam; PF09090; MIF4G_like_2; 1.
DR   SMART; SM00543; MIF4G; 1.
DR   SUPFAM; SSF48371; SSF48371; 3.
PE   3: Inferred from homology;
KW   mRNA capping; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; RNA-mediated gene silencing.
FT   CHAIN           1..783
FT                   /note="Nuclear cap-binding protein subunit 1"
FT                   /id="PRO_0000385240"
FT   DOMAIN          31..243
FT                   /note="MIF4G"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          652..683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         9
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   783 AA;  91393 MW;  05C5722311ECF1D5 CRC64;
     MSRRRAHDTE DESYDHRRNK RRRVSENQEI EDRLESLILR VGERSTSSVE SNLEGLVSVL
     EADLGTFRLK ILRILSDCAV RMPEKCTVYT TLVGLLNAKN YKFGGEFVDY MVKTFKESLK
     LCRWDAARYS LRFLADLVNC HVISATSLLQ LLDTIIDVSN EDTVPQVRRD WFVFAVLSTL
     PWVGRDLYEK KESALESLLL RIEVYLNKRS KKHHNALRVW SSDAPHPQEE YLDCLWAQIR
     KLRQDNWAEK HIPRPYLVFD AILCEALQHN LPQITPPPHH DAIEYPMPWV VYRMFDYTDC
     PDGPNLPGAH SIERFLIEEH LHHIIETHHH ERKDCAAQLL NFPFKHKIPL EYCIVEVIFA
     ELFHMPTPRY LDICYGSILI ELCKLQPGTL PQVLAQATEI LFMRIDSMNT SCFDRFVNWF
     SYHLSNFKFT WSWDEWDSCL LLDAEHPRPK FIQEVLQKCL RLSYHQRITE MMPTTYAKLI
     PVMPVPNYKY TSEEAANLPG TTVALQLVGA IRQKCTPEEV VNILKEIPSS GYSGEEMSDG
     SFNALKIDFC GQSKFHVVFR ALAETEEAQI CILHNIFELW SSHQQMMVVL IDKLLKLQIV
     DCSAVATWIF SKEMTGEFTK MYLWEILHLT IKKMNKHVIK LDTELDNAKE KLSKADSSSS
     DTDEDTPHKR KKPITHADKP SEEVVERMEE KLEAANVNQK RLFLIVFQRF IMILSEHLLR
     SDTDGRDPDT DWYRWTIGRL QQVFLMHHEQ VQKYSSTLET LLFTSDLDSH ILEVFQQFVA
     LRA