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Database: UniProt
Entry: A0A165NS88_9AGAM
LinkDB: A0A165NS88_9AGAM
Original site: A0A165NS88_9AGAM 
ID   A0A165NS88_9AGAM        Unreviewed;       204 AA.
AC   A0A165NS88;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-JUN-2023, entry version 13.
DE   RecName: Full=Cleavage and polyadenylation specificity factor subunit 5 {ECO:0000256|PIRNR:PIRNR017888};
GN   ORFNames=NEOLEDRAFT_1141232 {ECO:0000313|EMBL:KZT20033.1};
OS   Neolentinus lepideus HHB14362 ss-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX   NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT20033.1, ECO:0000313|Proteomes:UP000076761};
RN   [1] {ECO:0000313|EMBL:KZT20033.1, ECO:0000313|Proteomes:UP000076761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT20033.1,
RC   ECO:0000313|Proteomes:UP000076761};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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; KV425627; KZT20033.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165NS88; -.
DR   STRING; 1314782.A0A165NS88; -.
DR   InParanoid; A0A165NS88; -.
DR   OrthoDB; 142507at2759; -.
DR   Proteomes; UP000076761; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000076761};
KW   RNA-binding {ECO:0000256|PIRNR:PIRNR017888}.
SQ   SEQUENCE   204 AA;  23643 MW;  F93DFB91A1CA5396 CRC64;
     MSNTIPLYPL SNFTFSTKEA QPEEDPSVSA RLQRLQNNYE DFGMRRTVEG ILVVHDHGHP
     HILMLQIANA FFKLPGDYLK PGEDEIEGLK RLLDVRLAPP KDSHQFNASH GIDNDWEIGD
     CLAQWWRPNF ETFMYPFIPA HITKPKECKK LFLVHMPERK VLAVPKNMKL LAIPLFELYD
     NAARYGPQLS AIPHLLSRYN FIYQ
//
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