ID   CLP1_DEBHA              Reviewed;         497 AA.
AC   Q6BU98;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=mRNA cleavage and polyadenylation factor CLP1 {ECO:0000255|HAMAP-Rule:MF_03035};
GN   Name=CLP1 {ECO:0000255|HAMAP-Rule:MF_03035};
GN   OrderedLocusNames=DEHA2C12562g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Required for endonucleolytic cleavage during polyadenylation-
CC       dependent pre-mRNA 3'-end formation. {ECO:0000255|HAMAP-Rule:MF_03035}.
CC   -!- SUBUNIT: Component of a pre-mRNA cleavage factor complex. Interacts
CC       directly with PCF11. {ECO:0000255|HAMAP-Rule:MF_03035}.
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; CR382135; CAG86297.2; -; Genomic_DNA.
DR   RefSeq; XP_458221.2; XM_458221.1.
DR   AlphaFoldDB; Q6BU98; -.
DR   SMR; Q6BU98; -.
DR   STRING; 4959.XP_458221.2; -.
DR   EnsemblFungi; CAG86297; CAG86297; DEHA2C12562g.
DR   GeneID; 2900386; -.
DR   KEGG; dha:DEHA2C12562g; -.
DR   VEuPathDB; FungiDB:DEHA2C12562g; -.
DR   eggNOG; KOG2749; Eukaryota.
DR   HOGENOM; CLU_018195_3_0_1; -.
DR   InParanoid; Q6BU98; -.
DR   OMA; VQYVNCH; -.
DR   OrthoDB; 814241at2759; -.
DR   Proteomes; UP000000599; Chromosome C.
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.
PE   3: Inferred from homology;
KW   ATP-binding; mRNA processing; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..497
FT                   /note="mRNA cleavage and polyadenylation factor CLP1"
FT                   /id="PRO_0000375204"
FT   BINDING         34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT   BINDING         73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT   BINDING         157..162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
SQ   SEQUENCE   497 AA;  54844 MW;  1E2E736E7EA59E26 CRC64;
     MSAIPGFGGD LNSNIDEDSN LNKSSVVEIN GQSEWRFEVP FRTIMKLKVV NGIGEIFGTE
     LPLNVEISLT GVKYAIYAPL DEGCKVEYYC VSNKANSTST NEDDEISEYI SEETSMNHYM
     NLHFALESYR QSISEHNFVN SSSQKTGPRV LVVGNRHSGK TSLVKTLASY GCKMDRSPIL
     VNLNPRDGVF SVPGSLTATP ISDAFDLESV NGWGGSTTSG STFHNPKQPL VKNYGFTSHS
     DNLDLYKYQI SKLGVAVVSR MEEDIAVKNS GLLIDTPPLS IKDFTIIENI VSDFEVNIIV
     VIGNERLLID LKKKFKHKIA SSQLDFVKVP KSGGVIEVDD AYIRKSQEES IKEYFNGTIR
     SPLSPFKTEL DAKDFVIYKC VDSSEANSNL SFLPSGDSFT PEASEMSDGD KKEEFSLDTY
     YSQLQEPSSS NLDNSIVAIT QLPQNNKSAR DLMNTCVLGY AHVSKFDDTK SKMKVLLPFP
     GALPRNILIS TSVGYTE