ID   NCBP1_DROYA             Reviewed;         800 AA.
AC   B4Q034;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=GE16357;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01;
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; CM000162; EDX01186.1; -; Genomic_DNA.
DR   RefSeq; XP_002100078.1; XM_002100042.2.
DR   AlphaFoldDB; B4Q034; -.
DR   SMR; B4Q034; -.
DR   STRING; 7245.FBpp0261367; -.
DR   EnsemblMetazoa; FBtr0262875; FBpp0261367; FBgn0233887.
DR   GeneID; 6524215; -.
DR   KEGG; dya:Dyak_GE16357; -.
DR   eggNOG; KOG1104; Eukaryota.
DR   HOGENOM; CLU_013207_0_0_1; -.
DR   OMA; QPFKIPF; -.
DR   OrthoDB; 270650at2759; -.
DR   PhylomeDB; B4Q034; -.
DR   ChiTaRS; Cbp80; fly.
DR   Proteomes; UP000002282; Chromosome X.
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:0006406; P:mRNA export from nucleus; 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:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   GO; GO:0030422; P:siRNA processing; IEA:EnsemblMetazoa.
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   RNA-mediated gene silencing.
FT   CHAIN           1..800
FT                   /note="Nuclear cap-binding protein subunit 1"
FT                   /id="PRO_0000385242"
FT   DOMAIN          31..243
FT                   /note="MIF4G"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          669..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         9
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   800 AA;  93156 MW;  543D93E040718C49 CRC64;
     MSRRRAHDTE DEGYDHRRNK RRRVSENQEI EDRLESLILR VGERSTSSVE SNLEGLVSVL
     EADLGTFRLK ILRILSDCAV RMPEKCTVYT TLVGLLNAKN YKFGGEFVDH MVKTFKESLK
     LCRWDAARYS LRFLADLVNC HVISATSLLQ LLDTMIDVSN EDTVPQVRRD WFVFAVLSTL
     PWVGRDLYEK KESALESLLL RIEVYLNKRS KKHHNALRVW SSDAPHPQEE YLDCLWAQIR
     KLRQDNWAEK HIPRPYLVFD SILCEALQHN LPAIVPPPHH DNFEYPMPWV VYRMFDYTDC
     PDGPNLPGAH SIERFLIEEH LHHIIETYHH ERKDCAAQLL SFPFKHKIPL EYCIVEVIFA
     ELFHMPTPRY LDICYGSILI ELCKLQPATL PQVLAQATEI LFMRIDSMNT SCFDRFVNWF
     SYHLSNFKFT WSWDEWDSCL LLDGEHPRPK FIQEVLQKCL RLSYHQRITE MMPTTYAKLI
     PLTPVPNYKY ANEEAANLPG TTVAHQLVVA IRQKCTPEEV VNILKDIPSS GYSGEEMSDG
     SFNALKIDVF VQTLLNLGSK SFSHSFAAIS KFHSVFRALA ETEEAQICIL HNIYELWSSH
     QQMMVVLIDK LLKLQIVDCS AVATWIFSKE MTGEFTKMYL WEILHLTIKK MNKHVIKLNS
     ELSEAKDKLA KADSSSSDSE DDSSHKRKKP ITHADKPSEE VVERMEEKLE AANVNQKRLF
     LIVFQRFIMI LSEHLLRSDT DGRDPDTDWY RWTIGRLQQV FLMHHEQVQK YSSTLETLLF
     TSDLDTHILE VFQQFVALRA