ID   CLP1_LODEL              Reviewed;         555 AA.
AC   A5DY33;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=LELG_02270;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH981525; EDK44091.1; -; Genomic_DNA.
DR   RefSeq; XP_001527441.1; XM_001527391.1.
DR   AlphaFoldDB; A5DY33; -.
DR   SMR; A5DY33; -.
DR   STRING; 379508.A5DY33; -.
DR   EnsemblFungi; EDK44091; EDK44091; LELG_02270.
DR   GeneID; 5233835; -.
DR   KEGG; lel:LELG_02270; -.
DR   VEuPathDB; FungiDB:LELG_02270; -.
DR   eggNOG; KOG2749; Eukaryota.
DR   HOGENOM; CLU_018195_3_0_1; -.
DR   InParanoid; A5DY33; -.
DR   OMA; DITGWWP; -.
DR   OrthoDB; 814241at2759; -.
DR   Proteomes; UP000001996; 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.
PE   3: Inferred from homology;
KW   ATP-binding; mRNA processing; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..555
FT                   /note="mRNA cleavage and polyadenylation factor CLP1"
FT                   /id="PRO_0000375208"
FT   REGION          431..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..451
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT   BINDING         69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT   BINDING         156..161
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
SQ   SEQUENCE   555 AA;  60292 MW;  39D04E4EF1FC38FE CRC64;
     MSIPGFGGTN GSLASDSSEF TQISIPPANE WRIEVPFKKL LKLKVTLGTL EINGSELPNN
     VELQLSGVKL PIYAPPSINK EHAKVEYKLV TNPDQSVLLS SEDEEFTQYL SDETNMDLVV
     NLAMYIESKR QIAKDLKTNE GDHALGPRVL ILGGKYLGKT SLAKTLVSYA VKMGSSPVLV
     NLDPKHGVFA LPGSLSATVI NDSLDIECAN GYGFTMTTTG SLSKSMKQPV VKNFGFSDVD
     ENVKLYTRQI DQLGIAVLSK LEGIEDGSGS EVDGNHNKVR SSGVIVDTPP FTMKSFDIIS
     SIVSDLKIDL IVVLGNEKMK IDLTKKLKHK IEQGSLNIIK LSKSPGVVDD VNDRFIRMTQ
     EQTIREYFNG NHRIRLSPFK TEIDLPSSSS SASASASVSS SSSTSSSGLV IYKSVLTKEY
     ESSMAFLPSG DDFEHITNED ENGGDGNDGD GRGIVEDIKE YYQILEDPNS SNLDNSIVAI
     THLPLESGSS SVTNGASGSL NMSSKRKREL LNTSVMGYIH VSKVDDEKKK MKILLPFPGV
     FPRNVLIATS IGYNE