ID   A0A183GYU5_9BILA        Unreviewed;       433 AA.
AC   A0A183GYU5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   03-MAY-2023, entry version 25.
DE   RecName: Full=Protein CLP1 homolog {ECO:0000256|HAMAP-Rule:MF_03035};
GN   ORFNames=OFLC_LOCUS405 {ECO:0000313|EMBL:VDO25673.1};
OS   Onchocerca flexuosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=387005 {ECO:0000313|Proteomes:UP000050787, ECO:0000313|WBParaSite:OFLC_0000040401-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:OFLC_0000040401-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO25673.1, ECO:0000313|Proteomes:UP000267606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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; UZAJ01000129; VDO25673.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A183GYU5; -.
DR   STRING; 387005.A0A183GYU5; -.
DR   WBParaSite; OFLC_0000040401-mRNA-1; OFLC_0000040401-mRNA-1; OFLC_0000040401.
DR   Proteomes; UP000050787; Unplaced.
DR   Proteomes; UP000267606; 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   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          17..106
FT                   /note="Clp1 N-terminal beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF16573"
FT   DOMAIN          125..311
FT                   /note="Polyribonucleotide 5'-hydroxyl-kinase Clp1 P-loop"
FT                   /evidence="ECO:0000259|Pfam:PF16575"
FT   DOMAIN          317..428
FT                   /note="Pre-mRNA cleavage complex subunit Clp1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06807"
FT   BINDING         22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03035"
FT   BINDING         61
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03035"
FT   BINDING         128..133
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03035"
SQ   SEQUENCE   433 AA;  48243 MW;  D71BFA89326D13AF CRC64;
     MESTKTPPDQ DVQEFILKED NELRFEVANG DVMLELIDGR AEVFGTELIQ HKKYIFPPGS
     RVAVFTWKKA VVELVGKTES AYVAEQTPMI IYLNTHAALE QLREHAESVV MQQEQARGPS
     LMIVGPTDVG KTTVCRILCN YAVRVGRTPI FVDLDVGQGS ISVPGTVGAL YIEKTADVVE
     GFDKKAPLVY HFGNLSPGSN IPLYDLLVKQ LAEAVSKRRK ASQDATYGGV IINTCGWVKG
     EGYACLVNAA EEFEVDVVIV LDHERLYNEL QRDLPSFVKI LHQPKSGGVE NRSKEVRTSS
     RNAAVHKYFY GTRAVPLYPH TFELSFDEVQ FCKIGCERLP IECLPFGMKI DDHRTKVVPL
     EPTADLVHHL VSLSMCTTVD QSVLTTNVMG FIVITAVDME REKLTVLSPQ PYPLPSKILI
     LSEVTFIDDK ERT
//