ID   A0A0N4ZH32_PARTI        Unreviewed;       230 AA.
AC   A0A0N4ZH32;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   RecName: Full=Cleavage and polyadenylation specificity factor subunit 5 {ECO:0000256|PIRNR:PIRNR017888};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000719600.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0000719600.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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   AlphaFoldDB; A0A0N4ZH32; -.
DR   STRING; 131310.A0A0N4ZH32; -.
DR   WBParaSite; PTRK_0000719600.1; PTRK_0000719600.1; PTRK_0000719600.
DR   Proteomes; UP000038045; Unplaced.
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   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.
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   RNA-binding {ECO:0000256|PIRNR:PIRNR017888}.
SQ   SEQUENCE   230 AA;  26360 MW;  85BA0A2A314AACAD CRC64;
     MDVTIKLEES SGTVKNEVPN ISQESFICNR NPDNSDYIVG LYPLSNYTFA IKDAQSEKDS
     SVQARFQRMR NEYQTIGMRR SVEAVMIVNE HNTPHILLLQ IGTTFFKLPG GELMPEENDI
     DGLKRILNET LSSPDKPPTN WNVTDMLAKW WRSNFEPPRY PYVPSHVTRP KECCKLYLVQ
     LPSSAYFAVP RNFKLVAAPL FELYDNATGY GPVISTLPQL LSRFEMKFLK
//