CLP1_CHAGB
ID CLP1_CHAGB Reviewed; 497 AA.
AC Q2H1L0;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 57.
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=CHGG_04336;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408032; EAQ87717.1; -; Genomic_DNA.
DR RefSeq; XP_001223550.1; XM_001223549.1.
DR AlphaFoldDB; Q2H1L0; -.
DR SMR; Q2H1L0; -.
DR STRING; 38033.XP_001223550.1; -.
DR EnsemblFungi; EAQ87717; EAQ87717; CHGG_04336.
DR GeneID; 4391675; -.
DR eggNOG; KOG2749; Eukaryota.
DR HOGENOM; CLU_018195_3_1_1; -.
DR InParanoid; Q2H1L0; -.
DR OMA; VQYVNCH; -.
DR OrthoDB; 814241at2759; -.
DR Proteomes; UP000001056; 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..497
FT /note="mRNA cleavage and polyadenylation factor CLP1"
FT /id="PRO_0000375201"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT BINDING 168..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
SQ SEQUENCE 497 AA; 52711 MW; D1EF7ACCF7699A7E CRC64;
MSIPGLGQIA PQQPTTSTTR TITLRPFWEW RFEVPRSSIP TTNAAISAIG LGGAGAGGGG
ATVRLTSGTA ERDGTELALN RTYTFPRNTQ SKLLTYTGAT LEVSGAFVDS VAQYPAPEAS
PQLPVLNLHF ALQELRAAAA AGGSNHNNNN TNGGGAPGPR VMICGEKDSG KTTVARTLAA
LATRAGGQPL VGSVDPREGM LALPGTVSAA VFGTVMDVED PAAGFGVSGT PSSGPSAVPV
KLPMVYYVGR ERVDEDVPLW RDLVGKLGSA VRDKFAADEV VREAGLLLDT PAASVAKGDL
EVLTHVVNEF AGGLLGAGRT AGWQLTVTVN IVVVLGSVDL HAELQRRFEN QRTVHGEAIT
LILLDKSDGV AERDKDFMKF TREAAIKEYF FGDAKRTLSP FTQSVSFDDV AVFRTPDALE
RAEVSAEMSH WTLAVMNASV NDPPEVIRQA PVMGFVAIAD VDEDRRRLKV LSPVSGRLGN
RPMIWGRWPE PYINLLG