ID   CLP1_ASPTN              Reviewed;         556 AA.
AC   Q0CEZ9;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=mRNA cleavage and polyadenylation factor clp1 {ECO:0000255|HAMAP-Rule:MF_03035};
GN   Name=clp1; ORFNames=ATEG_07735;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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=EAU31997.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CH476604; EAU31997.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001216356.1; XM_001216356.1.
DR   AlphaFoldDB; Q0CEZ9; -.
DR   SMR; Q0CEZ9; -.
DR   STRING; 341663.Q0CEZ9; -.
DR   EnsemblFungi; EAU31997; EAU31997; ATEG_07735.
DR   GeneID; 4322871; -.
DR   eggNOG; KOG2749; Eukaryota.
DR   OrthoDB; 814241at2759; -.
DR   Proteomes; UP000007963; 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;
KW   Reference proteome.
FT   CHAIN           1..556
FT                   /note="mRNA cleavage and polyadenylation factor clp1"
FT                   /id="PRO_0000375197"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          414..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..458
FT                   /note="Polar residues"
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         157..162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
SQ   SEQUENCE   556 AA;  58635 MW;  095887FC9820E754 CRC64;
     MSLPGLDLTQ PSAEREFAPA PPSQITLSAG SEWRFEVAFG TTVRVKLISG TAELFGTELA
     PSQTYTFCGT KSAIYTWHGC ELEVGAGDAI SALEATGMNG AATAQGFGAG GCQSEYTAEE
     TPMVEYANVH FALETMRQEA KATGKDGPRV LILGPEDAGK TSLSKILTAY ATKIGRQPIV
     VNLDPAEGML SVPGTLTATA FRTMMDIEEG WGSSPMSGPS AVPVKLPLVY FYPMQNPLEG
     DGSVYRSIVS RLALSVMGRM AEDEDSRETG IIVDTPGVLS QSKAGSLEMI NHIVTEFSIT
     TILVIGSERL YSTMMKNYDN KPTSSASAVA SDERISVVKL SKSGGCVDRD AAFMKHVRES
     QIRTYFFGNP IPSTASAALS VSASSTTNVT LSPHAQQLDF NSLGLYNYNI TSTEEDEDEY
     DPAQFGASDA FLPGGANDAE QGASQQDENP SATPLPGIVS SIESAVPSGA SNVPLKKLLP
     PAPSALANSL LAITHVPPTA TPSEIRDSSI MGFLYVADVD SEKGKIRVLA PVGGRVPPRA
     IVWGKRWPGE VVGLVG