CLP1_CRYNJ
ID CLP1_CRYNJ Reviewed; 548 AA.
AC P0CM76; Q55RV6; Q5KGA9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=mRNA cleavage and polyadenylation factor CLP1 {ECO:0000255|HAMAP-Rule:MF_03035};
GN Name=CLP1 {ECO:0000255|HAMAP-Rule:MF_03035}; OrderedLocusNames=CNE04260;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AE017345; AAW43773.1; -; Genomic_DNA.
DR RefSeq; XP_571080.1; XM_571080.1.
DR AlphaFoldDB; P0CM76; -.
DR SMR; P0CM76; -.
DR STRING; 5207.AAW43773; -.
DR PaxDb; P0CM76; -.
DR EnsemblFungi; AAW43773; AAW43773; CNE04260.
DR GeneID; 3257560; -.
DR KEGG; cne:CNE04260; -.
DR VEuPathDB; FungiDB:CNE04260; -.
DR eggNOG; KOG2749; Eukaryota.
DR HOGENOM; CLU_018195_3_1_1; -.
DR InParanoid; P0CM76; -.
DR OMA; VQYVNCH; -.
DR OrthoDB; 814241at2759; -.
DR Proteomes; UP000002149; Chromosome 5.
DR GO; GO:0005849; C:mRNA cleavage factor complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051731; F:polynucleotide 5'-hydroxyl-kinase activity; IBA:GO_Central.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IBA:GO_Central.
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; IPR003593; AAA+_ATPase.
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; 2.
DR Pfam; PF16573; CLP1_N; 1.
DR Pfam; PF16575; CLP1_P; 1.
DR SMART; SM00382; AAA; 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..548
FT /note="mRNA cleavage and polyadenylation factor CLP1"
FT /id="PRO_0000375203"
FT REGION 437..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..496
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT BINDING 123..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
SQ SEQUENCE 548 AA; 59903 MW; 0DB4477C6E5360E8 CRC64;
MAEQQTTELT NIDLEAGSEW RFELEADENI ALRTLSSDPV FINSQELTPS AWYPIYRHTK
SALYAPTSAR IQVTNLPASH YTSTSTVQPQ LLNLHLAMER QRILSKRGME QRGPRVMIMG
PQSSGKTTVM KNLVNLALGT GMGWTPGAIG LDPSSPPNLI PGSLSISTPS HPIPTHHLAH
PLGSPPASTA ANTISGDVET ASWWLGALEP TNKNAEVWRV LVEHMAEAWG MRCEKDKIAN
ISGLFLDTPA AFTVPTLGTK KDDPKARYTL VSHAIQAFDI DTIIVIGHEK LHIDLSRLPL
VQSRQLNVIR IPKSGGAVDL DDHDRETAHI FQVRTYFYGE PPLPPQISSL VGKMVSLDFE
LSPYSFQIPW SRLVVLRVGE ENSAPSSALP LGSSKILSPL RLTRVDPSGP GHVVRLLNRV
LALVDVKPED RIVPAKESEV KEEVKEEKNE KDGEIKQDGE GEKKGEGKGE GEGEGEGKDG
EEEGEAEGED DEEEVPFREE IGTREVMGFI VITAIDTFAR KYTVLSPTPG RLPTTVAIAG
AIEWVDSA
