CLP1_CANGA
ID CLP1_CANGA Reviewed; 451 AA.
AC Q6FMC8;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=mRNA cleavage and polyadenylation factor CLP1 {ECO:0000255|HAMAP-Rule:MF_03035};
GN Name=CLP1 {ECO:0000255|HAMAP-Rule:MF_03035};
GN OrderedLocusNames=CAGL0K09086g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380957; CAG61579.1; -; Genomic_DNA.
DR RefSeq; XP_448616.1; XM_448616.1.
DR AlphaFoldDB; Q6FMC8; -.
DR SMR; Q6FMC8; -.
DR STRING; 5478.XP_448616.1; -.
DR EnsemblFungi; CAG61579; CAG61579; CAGL0K09086g.
DR GeneID; 2890247; -.
DR KEGG; cgr:CAGL0K09086g; -.
DR CGD; CAL0134843; CAGL0K09086g.
DR VEuPathDB; FungiDB:CAGL0K09086g; -.
DR eggNOG; KOG2749; Eukaryota.
DR HOGENOM; CLU_018195_3_0_1; -.
DR InParanoid; Q6FMC8; -.
DR OMA; VQYVNCH; -.
DR Proteomes; UP000002428; Chromosome K.
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:0003723; F:RNA binding; IEA:EnsemblFungi.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:EnsemblFungi.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IEA:EnsemblFungi.
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.
PE 3: Inferred from homology;
KW ATP-binding; mRNA processing; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..451
FT /note="mRNA cleavage and polyadenylation factor CLP1"
FT /id="PRO_0000375200"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT BINDING 136..141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
SQ SEQUENCE 451 AA; 50654 MW; F868E5D563CC6A69 CRC64;
MAEVEALPGL KQPVDDAGLL EDANQVHTLV IPSGHIWRVE LSSDEKLSLK VTAGIGEIFG
TELANNVEYT FWDWKFGIYA VEELEIEWKC PQLHDRELSI VENTTAHNVY NLHFALEKMR
SSTFDGPRIM VVGEKNTGKT ALCRTLCSYA IKNKPYQPMF VNLNPVEPIF SPPGCVTAVP
ISSTLDAQLP RWGETMTSGA TRLHGKQPII KNFGFETIAE NRSLYKLVTK KLFETVSERL
QNDSLVHRSG CIVDSPPLEN CDDEYSELVE AIVGLRINYL IILCNDNDKG REIYTKVSKI
VNTYVGERLL RVPTMAGVFE KDDVYIRAQQ RAAIREYFYG DTRTVLSPYN LGCDTSDITV
WRPKSVLQGE NTNLDTLEVA PVDSSTLQYA LVAITYASRK SDSEEVLQAP ILGFGLITEL
NEKRNKLKIL LPVPGRLPPN AMILTSFRYL E