(data stored in ACNUC27637 zone)

HOGENOM: ANOGA_10_PE1736

ID   ANOGA_10_PE1736                      STANDARD;      PRT;   163 AA.
AC   ANOGA_10_PE1736; Q7QCB6;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Nuclear cap-binding protein subunit 2;AltName: Full=20 kDa
DE   nuclear cap-binding protein;AltName: Full=NCBP 20 kDa subunit;
DE   Short=CBP20; (ANOGA_10.PE1736).
GN   Name=Cbp20; ORFNames=AGAP002547;
OS   ANOPHELES GAMBIAE.
OC   Anophelinae; Pyretophorus; Pterygota; Protostomia; Pancrustacea;
OC   Panarthropoda; Neoptera; Nematocera; Metazoa; Mandibulata; Insecta;
OC   Hexapoda; Eumetazoa; Eukaryota; Endopterygota; Diptera; Dicondylia;
OC   Culicoidea; Culicimorpha; Culicidae; Coelomata; Bilateria; Arthropoda;
OC   Anopheles.
OX   NCBI_TaxID=7165;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ANOGA_10.PE1736.
CC       Anopheles gambiae chromosome 2R AgamP3  sequence 1..61545105
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:NCBP2_ANOGA
CC   -!- FUNCTION: Component of the cap-binding complex (CBC), which binds
CC       co-transcriptionally 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
CC       RNA interference and is required for primary microRNAs (miRNAs)
CC       processing. Also involved in innate immunity via the short
CC       interfering RNAs (siRNAs) processing machinery by restricting the
CC       viral RNA production. In the CBC complex, Cbp20 recognizes and
CC       binds capped RNAs (m7GpppG-capped RNA) but requires Cbp80 to
CC       stabilize the movement of its N-terminal loop and lock the CBC
CC       into a high affinity cap-binding state with the cap structure (By
CC       similarity).
CC   -!- SUBUNIT: Component of the nuclear cap-binding complex (CBC), a
CC       heterodimer composed of Cbp80 and Cbp20 that interacts with
CC       m7GpppG-capped RNA (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the RRM NCBP2 family.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -!- GENE_FAMILY: HOG000217589 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Anopheles_gambiae;AGAP002547;AGAP002547-RA;AGAP002547-PA.
DR   EMBL; AAAB01008859; - ;
DR   UniProtKB/Swiss-Prot; Q7QCB6; -.
DR   EMBL; AAAB01008859; EAA07524.3; -; Genomic_DNA.
DR   RefSeq; XP_312392.3; XM_312392.3.
DR   HSSP; P52298; 1H6K.
DR   ProteinModelPortal; Q7QCB6; -.
DR   SMR; Q7QCB6; 13-150.
DR   STRING; Q7QCB6; -.
DR   EnsemblMetazoa; AGAP002547-RA; AGAP002547-PA; AGAP002547.
DR   GeneID; 3290635; -.
DR   KEGG; aga:AgaP_AGAP002547; -.
DR   VectorBase; AGAP002547; Anopheles gambiae.
DR   eggNOG; inNOG09627; -.
DR   GeneTree; EMGT00050000003375; -.
DR   OMA; RTDYDAG; -.
DR   OrthoDB; EOG4K0P4N; -.
DR   PhylomeDB; Q7QCB6; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0006370; P:mRNA capping; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   HOGENOMDNA; ANOGA_10.PE1736; -.
KW   AGAP00254700017784; AGAP002547-PA17508; Q7QCB6; AAAB01008859;
KW   Complete proteome; mRNA capping; mRNA processing; mRNA splicing;
KW   Nucleus; Reference proteome; RNA-binding; RNA-mediated gene silencing.
SQ   SEQUENCE   163 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSSQIQSVHT PSVSLSKYRD QHFKGSRHEQ EKLLRVSSTL YVGNLSFYTT EEQIHELFSR
     CGDVRRIIMG LDKFKKTPCG FCFVEYYSRL DAESAMRYIN GTRLDDRIVR VDWDAGFIEG
     RQYGRGKTGG QVRDEYRQDH DLGRGGYGKM VQMGQLGAPS MRE
//

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