NCBP1_DROSE
ID NCBP1_DROSE Reviewed; 800 AA.
AC B4I0W6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 57.
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=GM12358;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25;
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; CH480819; EDW53147.1; -; Genomic_DNA.
DR RefSeq; XP_002036988.1; XM_002036952.1.
DR AlphaFoldDB; B4I0W6; -.
DR SMR; B4I0W6; -.
DR STRING; 7238.B4I0W6; -.
DR EnsemblMetazoa; FBtr0195343; FBpp0193835; FBgn0167295.
DR GeneID; 6612480; -.
DR KEGG; dse:6612480; -.
DR HOGENOM; CLU_013207_0_0_1; -.
DR OMA; QPFKIPF; -.
DR PhylomeDB; B4I0W6; -.
DR ChiTaRS; Cbp80; fly.
DR Proteomes; UP000001292; 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: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 Reference proteome; RNA-mediated gene silencing.
FT CHAIN 1..800
FT /note="Nuclear cap-binding protein subunit 1"
FT /id="PRO_0000385239"
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; 93255 MW; FFB940377339C486 CRC64;
MSRRRAHDTE DEGYDHRRNK RRRVSENQEI EDRLESLILR VGERSTSSVE SNLEGLVSVL
EADLGTFRLK ILRILSDCAV RMPEKCTVYT TLVGLLNAKN YKFGGEFVDH MVKTFKESLK
MCRWDAARYS LRFLADLVNC HVISATSLLQ LLDTMIDVSN EDTVPQVRRD WFVFAVLSTL
PWVGRDLYEK KESALESLLL RIEVYLNKRS KKHHNALRVW SSDAPHPQEE YLDCLWAQIR
KLRQDNWAEK HIPRPYLVFD SILCEALQHN LPTIVPPPHH DNFEYPMPWV VYRMFDYTDC
PDGPNLPGAH SIERFLIEEH LHHIIETYHH ERKDCAAQLL SFPYKHKIPL EYCIVEVVFA
ELFHMPTPRY LDICYGSILI ELCKLQPATL PQVLAQATEI LFMRIDSMNT SCFDRFVNWF
SYHLSNFKFT WSWDEWDSWL LLDGEHPRPK FIQEVLQKCL RLSYHQRITE MMPTTYAKLI
PLTPVPNYKY ANEEAASLPG TTVAHQLVVA IRQKCTPEEV VNILKDIPNS GYSGEEMSDG
SFNALKIDVF VQTLLNLGSK SFSHSFAAIS KFHSVFRALA ETEEAQICIL HNIFELWSSH
QQMMVVLIDK LLKLQIVDCS AVATWIFSKE MTGEFTKLYL WEILHLTIKK MNKHVIKLNS
ELSEAKDKLA KADSSSSDSE DDSSHKRKKP ITHADKPSEE VVERMEEKLE AANVNQKRLF
LIVFQRFIMI LSEHLLRSDT DGRDPDTDWY RWTIGRLQQV FLMHHEQVQK YSSTLETLLF
TSDLDTHILE VFQQFVALRA