ID   A0A183NDN3_9TREM        Unreviewed;       208 AA.
AC   A0A183NDN3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, 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};
GN   ORFNames=SMTD_LOCUS219 {ECO:0000313|EMBL:VDO68610.1};
OS   Schistosoma mattheei.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=31246 {ECO:0000313|WBParaSite:SMTD_0000021801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMTD_0000021801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO68610.1, ECO:0000313|Proteomes:UP000269396}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Denwood {ECO:0000313|EMBL:VDO68610.1}, and Denwood, Zambia
RC   {ECO:0000313|Proteomes:UP000269396};
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|ARBA:ARBA00009710, ECO:0000256|PIRNR:PIRNR017888}.
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DR   EMBL; UZAL01000165; VDO68610.1; -; Genomic_DNA.
DR   STRING; 31246.A0A183NDN3; -.
DR   WBParaSite; SMTD_0000021801-mRNA-1; SMTD_0000021801-mRNA-1; SMTD_0000021801.
DR   Proteomes; UP000269396; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000269396};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRNR:PIRNR017888}.
FT   DOMAIN          64..188
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   208 AA;  23923 MW;  FBAF99BF4286C09E CRC64;
     MVHMTGWPKG SAEKFLHSTP VAKTITLYPL KSYSFGTKEP NYERDRSVPA RFQRLQEDFE
     KYGMRRSVEG ILLVHEHNLP HVLLLQLGTF FKLPGGELHP GEEEIEGLKR LLSEMLGRTD
     GIPVDWIPED CIGNWWRPNF EPPRYPYIPA HVTKPKEQTR LFLIQLPEKT LFAVPSNYKL
     VAAPLFELFD NARAYGPIIS SLPQVLSR
//