CLP1_CRYNB
ID CLP1_CRYNB Reviewed; 548 AA.
AC P0CM77; Q55RV6; Q5KGA9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 48.
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=CNBE4250;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAEY01000028; EAL20505.1; -; Genomic_DNA.
DR RefSeq; XP_775152.1; XM_770059.1.
DR AlphaFoldDB; P0CM77; -.
DR SMR; P0CM77; -.
DR EnsemblFungi; EAL20505; EAL20505; CNBE4250.
DR GeneID; 4936436; -.
DR KEGG; cnb:CNBE4250; -.
DR VEuPathDB; FungiDB:CNBE4250; -.
DR HOGENOM; CLU_018195_3_1_1; -.
DR Proteomes; UP000001435; Chromosome 5.
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; 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.
FT CHAIN 1..548
FT /note="mRNA cleavage and polyadenylation factor CLP1"
FT /id="PRO_0000410041"
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; 59951 MW; 17876E7C6E428118 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 GEGEGEGKYG
EEEGEAEGED DEEEVPFREE IGTREVMGFI VITAIDTFAR KYTVLSPTPG RLPTTVAIAG
AIEWVDSA
