ID CLP1_BOTFB Reviewed; 461 AA.
AC A6S936;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-MAY-2023, entry version 84.
DE RecName: Full=mRNA cleavage and polyadenylation factor clp1 {ECO:0000255|HAMAP-Rule:MF_03035};
GN Name=clp1; ORFNames=BC1G_08728;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476899; EDN29714.1; -; Genomic_DNA.
DR RefSeq; XP_001552250.1; XM_001552200.1.
DR AlphaFoldDB; A6S936; -.
DR SMR; A6S936; -.
DR EnsemblFungi; Bcin12g03610.1; Bcin12p03610.1; Bcin12g03610.
DR GeneID; 5432770; -.
DR KEGG; bfu:BCIN_12g03610; -.
DR VEuPathDB; FungiDB:Bcin12g03610; -.
DR OMA; VQYVNCH; -.
DR OrthoDB; 56092at2759; -.
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; 2.60.120.1030; Clp1, DNA binding domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.330; Pre-mRNA cleavage complex subunit Clp1, C-terminal domain; 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; CLEAVAGE/POLYADENYLATION FACTOR IA SUBUNIT CLP1P; 1.
DR PANTHER; PTHR12755:SF6; POLYRIBONUCLEOTIDE 5'-HYDROXYL-KINASE CLP1; 1.
DR Pfam; PF06807; Clp1; 1.
DR Pfam; PF16573; CLP1_N; 1.
DR Pfam; PF16575; CLP1_P; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW ATP-binding; mRNA processing; Nucleotide-binding; Nucleus.
FT CHAIN 1..461
FT /note="mRNA cleavage and polyadenylation factor clp1"
FT /id="PRO_0000375198"
FT BINDING 34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT BINDING 134..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
SQ SEQUENCE 461 AA; 50489 MW; 60F55B90C6F61F02 CRC64;
MSIPGLGQAV HAARTAAPAA VAHTNIHELQ ANSEWRFEVA IGSSIEVKVL SGTAEIFGTE
LAVNHTYTFH GTKSSIYTWH GCRLEVNGPC EEYTAEETPM ISYINTHFAL ENLRSDAKKA
GQDGPRVLIV GPNNTGKTSL AKLLTAYAVR MGRQPIVVNT DSREGMLSIP GSLTAAAFKS
IVDVEEGWGS SSTSGPSPVP VKLPLCYYYG LPSPEDNVKL FKPVVTRLAL AATSRLQDDA
VCRETGMIID TPGVISQGKG GYDLISHIVS EFAVNIILVL GSERLHSEML RRFSTHKTDN
GEAITLVRLD KSGGCVDRDD AFMQQMREAT IKEYFFGDAK RTLSPHTQVV NFDELSIYKV
KEAHSMQSAF LPGGEEEVEP TQYEKVEPTP SMLHCIFAVM HASTRDSQDT IRDASVMGFV
YVAEVDEKKK RMKILAPLNT RVTDRPLIWG SWPEAPVNLM G
//
