NCBP2_BOMMO
ID NCBP2_BOMMO Reviewed; 154 AA.
AC Q1HE01;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Nuclear cap-binding protein subunit 2;
DE AltName: Full=20 kDa nuclear cap-binding protein;
DE AltName: Full=NCBP 20 kDa subunit;
DE Short=CBP20;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang L.-L., Chen K.-P., Yao Q., Hu Z.-G., Gao G.-T.;
RT "RNA binding proteins in Bombyx mori.";
RL Submitted (APR-2006) 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 (By similarity). {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 RRM NCBP2 family. {ECO:0000305}.
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DR EMBL; DQ497196; ABF55961.1; -; mRNA.
DR RefSeq; NP_001037598.1; NM_001044133.1.
DR AlphaFoldDB; Q1HE01; -.
DR SMR; Q1HE01; -.
DR STRING; 7091.BGIBMGA007585-TA; -.
DR GeneID; 733050; -.
DR KEGG; bmor:733050; -.
DR CTD; 42166; -.
DR eggNOG; KOG0121; Eukaryota.
DR HOGENOM; CLU_070952_1_1_1; -.
DR OrthoDB; 1421503at2759; -.
DR Proteomes; UP000005204; 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:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
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; PTHR18847; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing.
FT CHAIN 1..154
FT /note="Nuclear cap-binding protein subunit 2"
FT /id="PRO_0000385260"
FT DOMAIN 30..108
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT BINDING 10
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 102..106
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 113..117
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 123..124
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
SQ SEQUENCE 154 AA; 17920 MW; 79A1022AC0BCB7AF CRC64;
MNSSIEISSY RDQHFKGSRS EQEKLLKASS TLYMGNLSFY TTEEQIYELY SRCGDIRRVI
MGLDKYKKTP CGFCFVEYYA REDAENCMRY INGTRLDDRI IRCDWDAGFI EGRQYGRGKT
GGQVRDEYRT DYDGGRGGYG KIIAQKINPN TLER