ID   CLP1_MALGO              Reviewed;         665 AA.
AC   A8PWG8;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 58.
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=MGL_1095;
OS   Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=425265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4612 / CBS 7966;
RX   PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA   Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA   Kronstad J.W., DeAngelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA   Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA   Chu L., Sears R., Yuan B., Dawson T.L. Jr.;
RT   "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT   virulence traits shared with plant and human fungal pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(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; AAYY01000003; EDP44613.1; -; Genomic_DNA.
DR   RefSeq; XP_001731827.1; XM_001731775.1.
DR   AlphaFoldDB; A8PWG8; -.
DR   SMR; A8PWG8; -.
DR   STRING; 425265.A8PWG8; -.
DR   EnsemblFungi; EDP44613; EDP44613; MGL_1095.
DR   GeneID; 5856132; -.
DR   KEGG; mgl:MGL_1095; -.
DR   VEuPathDB; FungiDB:MGL_1095; -.
DR   InParanoid; A8PWG8; -.
DR   OMA; DITGWWP; -.
DR   OrthoDB; 814241at2759; -.
DR   Proteomes; UP000008837; 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..665
FT                   /note="mRNA cleavage and polyadenylation factor CLP1"
FT                   /id="PRO_0000375210"
FT   REGION          218..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          593..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..243
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..615
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT   BINDING         195..200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
SQ   SEQUENCE   665 AA;  73010 MW;  F87B068A9EAE91B6 CRC64;
     MEDIVDDVRS STYQVVENDA CGTGKANLLS LSLLYLRSTL KWMIELDAGE AVAIRFVPDP
     ISGHYGDAEV FGAPLVAGSQ ERWYTFGNEA KFAISSWGGA EVEILGAAST EYMADEPSPT
     YTYCTNLHLN LERARIRARE QLRTDPSLQK ILEDMDVSER TIPASYEQHG AGASGSDLYR
     AAGQGPRVMI VGPESAGKTS LIKFLANYAL RSPALANVKE GDDASRRAKH RSEPEIHPGP
     DVAHDDDDDD DVENRKDDEE SGINDMKHPK NRKKHSSADS QAKKTLSDIT GWWPMIVALD
     PSEGAVPVPG CVSAIPLTPM PTNWLPSPSP ALPYGITTQT TGTLPPSVST VQSVMPISLW
     MGKENVRENE RHSRRVIDWL AYYIEKRLVK DWRARMSGLL LDMPGVITAD ARTRYGFIQY
     CVRAFKIDTI VVLGHEKLNL ELTRIYANDT SGHAPRIVKV PRSGGAVEVD EVYKQKLHDL
     QIRSYFYGMP PALTKEAAVT SMSMNDENTP ASIPAGLDEH LGAVPTLSPY STTIPLDLLS
     IYRVGQDRVA PSSALPIGAE RVLSEMQVVK LDPVNSSNDM SMLLHSVLAL VEPPPRNQSK
     DETSSPDDPG HHDYEDDELL GAAILGFVHV SDMDLHRKKL TVLSPKPGKL PSTTALIGNL
     QWQDM