ID T1DPN7_ANOAQ Unreviewed; 163 AA.
AC T1DPN7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Nuclear cap-binding protein subunit 2 {ECO:0000256|RuleBase:RU364036};
DE AltName: Full=20 kDa nuclear cap-binding protein {ECO:0000256|RuleBase:RU364036};
OS Anopheles aquasalis (Malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=42839 {ECO:0000313|EMBL:JAA98401.1};
RN [1] {ECO:0000313|EMBL:JAA98401.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole body {ECO:0000313|EMBL:JAA98401.1};
RG Brazilian Malaria Network (MCT/CNPq/MS/SCTIE/DECIT/PRONEX 555648/2009-5) and Research Network on Bioactive Molecules from Arthropod Vectors (NAP-MOBIARVE;
RG University of Sao Paulo);
RA Marinotti O., Ribeiro J.M.C., Costa-da-Silva A.L., Silva M.C.P.,
RA Lopes A.R., Barros M.S., Sa-Nunes A., Konjin B.B., Carvalho E., Suesdek L.,
RA Silva-Neto M.A.C., Capurro M.L.;
RT "Transcriptome sequencing and developmental regulation of gene expression
RT in Anopheles aquasalis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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 and is required for primary microRNAs (miRNAs) processing. Also
CC involved in innate immunity via the short interfering RNAs (siRNAs)
CC processing machinery by restricting the viral RNA production. In the
CC CBC complex, Cbp20 recognizes and binds capped RNAs (m7GpppG-capped
CC RNA) but requires Cbp80 to stabilize the movement of its N-terminal
CC loop and lock the CBC into a high affinity cap-binding state with the
CC cap structure. {ECO:0000256|RuleBase:RU364036}.
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:0000256|RuleBase:RU364036}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU364036}.
CC -!- SIMILARITY: Belongs to the RRM NCBP2 family.
CC {ECO:0000256|ARBA:ARBA00010725, ECO:0000256|RuleBase:RU364036}.
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DR EMBL; GAMD01003189; JAA98401.1; -; mRNA.
DR AlphaFoldDB; T1DPN7; -.
DR VEuPathDB; VectorBase:AAQUA_006913; -.
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:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
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; 20 KD NUCLEAR CAP BINDING PROTEIN; 1.
DR PANTHER; PTHR18847:SF0; NUCLEAR CAP-BINDING PROTEIN SUBUNIT 2; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU364036};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|RuleBase:RU364036};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364036};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176};
KW RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158}.
FT DOMAIN 38..116
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
SQ SEQUENCE 163 AA; 18640 MW; D8E69FD992153FD5 CRC64;
MSSPISSVHT PSVALSKYRD QHFKGSRHEQ EKLLRLSATL YVGNLSFYTT EEQIHELFSR
CGDVRRIIMG LDKFKKTPCG FCFVEYYSRI DAESAMRYIN GTRLDDRIVR VDWDAGFVEG
RQYGRGKTGG QVRDEYRQDH DLGRGGYGKM VQVGQLGAPS MRD
//