ID A0A1I8ELC7_WUCBA Unreviewed; 229 AA.
AC A0A1I8ELC7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 5 {ECO:0000256|ARBA:ARBA00016266, ECO:0000256|PIRNR:PIRNR017888};
OS Wuchereria bancrofti.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Wuchereria.
OX NCBI_TaxID=6293 {ECO:0000313|WBParaSite:maker-PairedContig_2960-snap-gene-0.11-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-PairedContig_2960-snap-gene-0.11-mRNA-1}
RP IDENTIFICATION.
RC STRAIN=pt0022
RC {ECO:0000313|WBParaSite:maker-PairedContig_2960-snap-gene-0.11-mRNA-1};
RG WormBaseParasite;
RL Submitted (NOV-2016) 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|ARBA:ARBA00009710, ECO:0000256|PIRNR:PIRNR017888}.
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DR AlphaFoldDB; A0A1I8ELC7; -.
DR STRING; 6293.A0A1I8ELC7; -.
DR WBParaSite; maker-PairedContig_2960-snap-gene-0.11-mRNA-1; maker-PairedContig_2960-snap-gene-0.11-mRNA-1; maker-PairedContig_2960-snap-gene-0.11.
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; IPR015797; NUDIX_hydrolase-like_dom_sf.
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 SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR017888};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|PIRNR:PIRNR017888};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR017888};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRNR:PIRNR017888}.
FT DOMAIN 78..203
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 229 AA; 26176 MW; 304BF08428B566D1 CRC64;
MTGMSRTGWP VATRPQKIVT TPVTLKKPND TRNSIDRAIN LYPLTNYTFG TKDPQAERDH
SVQARFQRMR EEYEKIGMRR SVEGVLLVHE HSLPHVLLLQ IGTTFFKLPG GELNPGEDEV
EGLKRLLTET LGRQDGAKDL WTIEDVIGNW WRPNFDPPRY PYIPAHVTKP KEQTKLFLVQ
LPERALFAVP KNYKLVAAPL FELYDNSTGY GNLIASLPQI QFSVYAMKL
//