ID   CLP1_YEAS7              Reviewed;         445 AA.
AC   A6ZP88;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=mRNA cleavage and polyadenylation factor CLP1 {ECO:0000255|HAMAP-Rule:MF_03035};
GN   Name=CLP1 {ECO:0000255|HAMAP-Rule:MF_03035}; ORFNames=SCY_5303;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Component of the cleavage factor IA (CF IA) complex, which is
CC       involved in the endonucleolytic cleavage during polyadenylation-
CC       dependent pre-mRNA 3'-end formation. Associates with HRB1/CF IB to form
CC       the cleavage factor I (CF I) complex. CF I is required for correct
CC       positioning of a larger protein complex, the cleavage and
CC       polyadenylation factor (CPF) complex, which contains the catalytic
CC       subunits executing mRNA cleavage and polyadenylation. CLP1 mediates
CC       interactions between CF IA and CPF factors. CLP1 is also involved in
CC       maintaining the CF IA interaction with the C-terminal domain of RNA Pol
CC       II largest subunit via PCF11, which links pre-mRNA 3'-end processing to
CC       transcription termination. {ECO:0000255|HAMAP-Rule:MF_03035}.
CC   -!- SUBUNIT: Component of the cleavage factor IA (CF IA) complex, which is
CC       a heterohexameric complex with 2:2:1:1 stoichiometry of RNA14, RNA15,
CC       PCF11 and CLP1. It contains 2 copies of an RNA14-RNA15 dimer and 1 copy
CC       of CLP1-PCF11. The complex interacts with the cleavage factor HRB1/CF
CC       IB to form the cleavage factor I (CF I) complex, and binds to RNA.
CC       Interacts directly with PCF11. Interacts with the CPF components CFT1,
CC       PTA1, PFS2, YSH1 and SSU72 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03035}.
CC   -!- SIMILARITY: Belongs to the Clp1 family. Clp1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03035}.
CC   -!- CAUTION: May lack the polyribonucleotide 5'-hydroxyl-kinase and
CC       polynucleotide 5'-hydroxyl-kinase activities that are characteristic of
CC       the human ortholog. {ECO:0000305}.
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DR   EMBL; AAFW02000032; EDN63578.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZP88; -.
DR   SMR; A6ZP88; -.
DR   EnsemblFungi; EDN63578; EDN63578; SCY_5303.
DR   HOGENOM; CLU_018195_3_1_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005849; C:mRNA cleavage factor complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051731; F:polynucleotide 5'-hydroxyl-kinase activity; IEA:InterPro.
DR   GO; GO:0031124; P:mRNA 3'-end processing; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.30.330; -; 1.
DR   Gene3D; 2.60.120.1030; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_03035; Clp1; 1.
DR   InterPro; IPR028606; Clp1.
DR   InterPro; IPR045116; Clp1/Grc3.
DR   InterPro; IPR010655; Clp1_C.
DR   InterPro; IPR038238; Clp1_C_sf.
DR   InterPro; IPR032324; Clp1_N.
DR   InterPro; IPR038239; Clp1_N_sf.
DR   InterPro; IPR032319; CLP1_P.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12755; PTHR12755; 1.
DR   Pfam; PF06807; Clp1; 1.
DR   Pfam; PF16573; CLP1_N; 1.
DR   Pfam; PF16575; CLP1_P; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; mRNA processing; Nucleotide-binding; Nucleus.
FT   CHAIN           1..445
FT                   /note="mRNA cleavage and polyadenylation factor CLP1"
FT                   /id="PRO_0000375219"
FT   BINDING         33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT   BINDING         72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT   BINDING         133..138
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
SQ   SEQUENCE   445 AA;  50226 MW;  B00F7659E83090DA CRC64;
     MASLPGIDEH TTSEELITGD NEWHKLVIPK GSDWQIDLKA EGKLIVKVNS GIVEIFGTEL
     AVDDEYTFQN WKFPIYAVEE TELLWKCPDL TTNTITVKPN HTMKYIYNLH FMLEKIRMSN
     FEGPRVVIVG GSQTGKTSLS RTLCSYALKF NAYQPLYINL DPQQPIFTVP GCISATPISD
     ILDAQLPTWG QSLTSGATLL HNKQPMVKNF GLERINENKD LYLECISQLG QVVGQRLHLD
     PQVRRSGCIV DTPSISQLDE NLAELHHIIE KLNVNIMLVL CSETDPLWEK VKKTFGPELG
     NNNIFFIPKL DGVSAVDDVY KRSLQRTSIR EYFYGSLDTA LSPYAIGVDY EDLTIWKPSN
     VFDNEVGRVE LFPVTITPSN LQHAIIAITF AERRADQATV IKSPILGFAL ITEVNEKRRK
     LRVLLPVPGR LPSKAMILTS YRYLE