ID   CLP1_PICST              Reviewed;         453 AA.
AC   A3LNJ3;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 3.
DT   03-AUG-2022, entry version 71.
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=PICST_55332;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABN64342.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000496; ABN64342.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001382371.2; XM_001382334.1.
DR   AlphaFoldDB; A3LNJ3; -.
DR   SMR; A3LNJ3; -.
DR   STRING; 4924.XP_001382371.2; -.
DR   EnsemblFungi; ABN64342; ABN64342; PICST_55332.
DR   GeneID; 4837068; -.
DR   KEGG; pic:PICST_55332; -.
DR   eggNOG; KOG2749; Eukaryota.
DR   HOGENOM; CLU_018195_3_0_1; -.
DR   InParanoid; A3LNJ3; -.
DR   OrthoDB; 814241at2759; -.
DR   Proteomes; UP000002258; Chromosome 2.
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;
KW   Reference proteome.
FT   CHAIN           1..453
FT                   /note="mRNA cleavage and polyadenylation factor CLP1"
FT                   /id="PRO_0000375215"
FT   BINDING         31
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT   BINDING         70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT   BINDING         146..151
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
SQ   SEQUENCE   453 AA;  49783 MW;  E52C3B51B1FBB12D CRC64;
     MSIPGFGAEA QVYSETGSKG LVEVAIPEGS EWRIEVPHKT ILKFKVTEGV AEIFGTELPI
     NVELQISGTK TMVYAPIIYE TFKNKTVMSN ESEEIVEYLS NDSVMANYIN LHLVVEAMRQ
     QVSDNNILNP TELQSGPRVL IVGNGNSGKT SLAKLLSAYA IKSDSTPVLV NLNPRDGVFS
     LPGSLTATPI SDSLDVESAN GWGFTTTSGS LFHNPKQPIV KNYGFVDVNE NLDLYKYQVS
     KLGVTVLSRL EEDIACRNGG VIIDTPALGI KDFTVIENIV SDFEVNLIVV LGNERLMIDL
     KKRFKHKSAL QIVKVPKSEG LVEVDEAFIR RTQEESIKEY FNGNYKTRLS PFKTDIDVND
     HTIYKCVLSS DVNSALSFLP AEPSSSNLDN SILAITQLPS THKSGRELLN TSILGYVHVS
     KFDDAKGKIK VLLPFPGGFP RNMLISTNIG FNE