ID A0A182RB20_ANOFN Unreviewed; 423 AA.
AC A0A182RB20;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE RecName: Full=Protein CLP1 homolog {ECO:0000256|HAMAP-Rule:MF_03035};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN003384-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN003384-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN003384-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- FUNCTION: Required for endonucleolytic cleavage during polyadenylation-
CC dependent pre-mRNA 3'-end formation. {ECO:0000256|HAMAP-Rule:MF_03035}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|HAMAP-Rule:MF_03035}.
CC -!- SIMILARITY: Belongs to the Clp1 family. Clp1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03035}.
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DR AlphaFoldDB; A0A182RB20; -.
DR STRING; 62324.A0A182RB20; -.
DR EnsemblMetazoa; AFUN003384-RA; AFUN003384-PA; AFUN003384.
DR VEuPathDB; VectorBase:AFUN003384; -.
DR VEuPathDB; VectorBase:AFUN2_011512; -.
DR OrthoDB; 56092at2759; -.
DR Proteomes; UP000075900; Unassembled WGS sequence.
DR GO; GO:0005849; C:mRNA cleavage factor complex; IEA:InterPro.
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 CDD; cd01983; SIMIBI; 1.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03035};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664, ECO:0000256|HAMAP-
KW Rule:MF_03035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03035};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03035}.
FT DOMAIN 13..105
FT /note="Clp1 N-terminal beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF16573"
FT DOMAIN 119..305
FT /note="Polyribonucleotide 5'-hydroxyl-kinase Clp1 P-loop"
FT /evidence="ECO:0000259|Pfam:PF16575"
FT DOMAIN 311..421
FT /note="Pre-mRNA cleavage complex subunit Clp1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06807"
FT BINDING 19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03035"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03035"
FT BINDING 122..127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03035"
SQ SEQUENCE 423 AA; 47031 MW; BD9869E3C008FDCD CRC64;
MSDDKAIPKT DYKLEADSEL RFEIENKNEK VAVVLLNGQA ELFGTELVVK KPYEFFTGAK
VAIFTYHGCT IELRGKPDVA YVAKETPMVM YLNANSALEH LRNKAEQEDA QGPIAMVVGP
TDVGKTTLCR IFLNYAVRLG RRPIFVDLDV GQGGIAIPGT IGALLVERPA PVAEGFSQQA
PLVYHYGHSS PSSNSTFYDV LISKLAETTL ERLQANKRAK SSGMIINTCG WVKKSGYSHI
LHTVKAFEVS AIFVLDQERL YNELLRDTKE TVQVIFLPKS GGVVERTKSQ RTEARDQRIR
EYFYGSKMPF FPHSFDVKFS DIKIFKVGSP PLPDSCLPLG MKAEDNYTKL VAVMPGPQLL
HHILAVSFAE STEENVIQTN VAGFICVTNV NMEKQVLTVL SPQPRPLPQT ILLVSDLQFM
DSH
//
