ID   A0A044TPR4_ONCVO        Unreviewed;       242 AA.
AC   A0A044TPR4;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   29-SEP-2021, entry version 26.
DE   RecName: Full=Cleavage and polyadenylation specificity factor subunit 5 {ECO:0000256|PIRNR:PIRNR017888};
OS   Onchocerca volvulus.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=6282 {ECO:0000313|EnsemblMetazoa:OVOC5279, ECO:0000313|Proteomes:UP000024404};
RN   [1] {ECO:0000313|Proteomes:UP000024404}
RP   NUCLEOTIDE SEQUENCE.
RA   Cotton J., Tsai J., Stanley E., Tracey A., Holroyd N., Lustigman S.,
RA   Berriman M.;
RT   "Genome sequencing of Onchocerca volvulus.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:OVOC5279}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2014) to UniProtKB.
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; CMVM020000154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EnsemblMetazoa; OVOC5279; OVOC5279; WBGene00242088.
DR   OMA; DIYPLNH; -.
DR   Proteomes; UP000024404; 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   InterPro; IPR016706; Cleav_polyA_spec_factor_su5.
DR   PANTHER; PTHR13047; PTHR13047; 1.
DR   Pfam; PF13869; NUDIX_2; 1.
DR   PIRSF; PIRSF017888; CPSF-25; 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:UP000024404};
KW   RNA-binding {ECO:0000256|PIRNR:PIRNR017888}.
SQ   SEQUENCE   242 AA;  28061 MW;  AEFD48E8482C5B7A CRC64;
     MTTTMFYPGE SQLSCKREHQ SVSSVIRLYP LKNYCVRNND YKDPPRLSEY KQFLKLREEY
     ESNGMIRTVK AVLLCYQHSI IHVLLLKNGN GPMSSKLPGG RLKSDEDETA GMKRVMTQVQ
     LNLFATQALV RRSKYSIQLT YLIMESENDV DSICKIQHVA NWWRPNFEAP IYPYIPSHIT
     KPKEVIKIFS VELPKRAMIT IAKNNTLVAA PLFEIYRNVG QYGPIIAYLP HVLGRFNYFY
     NL
//