ID A0A0R3PPV0_ANGCS Unreviewed; 207 AA.
AC A0A0R3PPV0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 5 {ECO:0000256|PIRNR:PIRNR017888};
GN ORFNames=ACOC_LOCUS7280 {ECO:0000313|EMBL:VDM58865.1};
OS Angiostrongylus costaricensis (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0000727901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ACOC_0000727901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM58865.1, ECO:0000313|Proteomes:UP000267027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Costa Rica {ECO:0000313|EMBL:VDM58865.1,
RC ECO:0000313|Proteomes:UP000267027};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the cleavage factor Im (CFIm) complex that
CC functions as an activator of the pre-mRNA 3'-end cleavage and
CC polyadenylation processing required for the maturation of pre-mRNA into
CC functional mRNAs. CFIm contributes to the recruitment of multiprotein
CC complexes on specific sequences on the pre-mRNA 3'-end, so called
CC cleavage and polyadenylation signals (pA signals). Most pre-mRNAs
CC contain multiple pA signals, resulting in alternative cleavage and
CC polyadenylation (APA) producing mRNAs with variable 3'-end formation.
CC The CFIm complex acts as a key regulator of cleavage and
CC polyadenylation site choice during APA through its binding to 5'-UGUA-
CC 3' elements localized in the 3'-untranslated region (UTR) for a huge
CC number of pre-mRNAs. {ECO:0000256|PIRNR:PIRNR017888}.
CC -!- SUBUNIT: Homodimer (via N- and C-terminus); binds RNA as homodimer.
CC Component of the cleavage factor Im (CFIm) complex.
CC {ECO:0000256|PIRNR:PIRNR017888}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR017888}.
CC Cytoplasm {ECO:0000256|PIRNR:PIRNR017888}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. CPSF5 subfamily.
CC {ECO:0000256|PIRNR:PIRNR017888}.
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DR EMBL; UYYA01004023; VDM58865.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3PPV0; -.
DR STRING; 334426.A0A0R3PPV0; -.
DR WBParaSite; ACOC_0000727901-mRNA-1; ACOC_0000727901-mRNA-1; ACOC_0000727901.
DR OMA; NDEWEIG; -.
DR Proteomes; UP000050601; Unplaced.
DR Proteomes; UP000267027; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005849; C:mRNA cleavage factor complex; IEA:UniProtKB-UniRule.
DR GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR016706; Cleav_polyA_spec_factor_su5.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR13047:SF0; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 5; 1.
DR PANTHER; PTHR13047; PRE-MRNA CLEAVAGE FACTOR IM, 25KD SUBUNIT; 1.
DR Pfam; PF13869; NUDIX_2; 1.
DR PIRSF; PIRSF017888; CPSF-25; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR017888};
KW mRNA processing {ECO:0000256|PIRNR:PIRNR017888};
KW Nucleus {ECO:0000256|PIRNR:PIRNR017888};
KW Reference proteome {ECO:0000313|Proteomes:UP000267027};
KW RNA-binding {ECO:0000256|PIRNR:PIRNR017888}.
FT DOMAIN 49..174
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 207 AA; 23990 MW; 1143D4C2BCC31D8C CRC64;
MDIMSIYRNV NRFPLSNYTF GTKDAQSERD HSVQARFQRM REEYEKVGMR RSVDAVLIVH
EHSLPHILLL QIGTTFFKLP GGELEVGEEE TDGMRRLLDL TLGRSDGVKN EWKIEDEVGN
WWRPNFDPPR YPYIPAHVTK PKEHTKLLLV QMPEKAMFAV PKNYKLVAAP LFELYDNAAA
YGPLIASLPM ALSRWAFAFY TNYIILL
//
