ID   CLP1_ASPNC              Reviewed;         477 AA.
AC   A2RAW3;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=mRNA cleavage and polyadenylation factor clp1 {ECO:0000255|HAMAP-Rule:MF_03035};
GN   Name=clp1; ORFNames=An18g04570;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(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}.
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DR   EMBL; AM270408; CAK43259.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2RAW3; -.
DR   SMR; A2RAW3; -.
DR   PaxDb; A2RAW3; -.
DR   EnsemblFungi; CAK43259; CAK43259; An18g04570.
DR   VEuPathDB; FungiDB:An18g04570; -.
DR   HOGENOM; CLU_018195_3_1_1; -.
DR   Proteomes; UP000006706; Chromosome 8L.
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..477
FT                   /note="mRNA cleavage and polyadenylation factor clp1"
FT                   /id="PRO_0000375195"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         32
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT   BINDING         71
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT   BINDING         127..132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
SQ   SEQUENCE   477 AA;  50698 MW;  2EC57336C64963C3 CRC64;
     MSLPGLDLTQ PSADREFAPA PPSQISLPKG SEWRFEVAFG TTVRVKLLAG TAELFGTELA
     PSQTYTFSGT KAAIYTWHGC TLESEYVAEE TPMVEYANVH FALETLRQEA KATGKDGPRV
     LILGPEDAGK TSLSKILTAY ATKVGRQPLV VNLDPTEGML SVPGTLTATA FRTMIDVEEG
     WGSSPMSGPS AVPVKLPLVY FYPMQNPLEA DGSVYKAIVS RLALSVTGRM AEDEDARETG
     IIVDTPGILS QSKAGNVEMI NHIVTEFAIT TILVIGSERL YSIMMKNFDN KPTASASAAA
     SDERISVVKL SKSGGCVDRD AAFMKAVSES QIRTYFFGNP IPSTASAALS LSASSTTNVT
     LSPHAQQLDF NALAVYNYTI ASAEEDEDEY DPSQLGTGDA FLPGGSNDVD LALANSLLAI
     THASSTASPA DVRDASIMGF LYVADVDAEK GKIRVLAPVG GRVPPRAIKK YIDSSKV