ID   CLP1_DICDI              Reviewed;         459 AA.
AC   Q54N48;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Protein CLP1 homolog {ECO:0000255|HAMAP-Rule:MF_03035};
GN   Name=clp1; ORFNames=DDB_G0285507;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Required for endonucleolytic cleavage during polyadenylation-
CC       dependent pre-mRNA 3'-end formation. {ECO:0000255|HAMAP-Rule:MF_03035}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Clp1 family. Clp1 subfamily.
CC       {ECO:0000255|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; AAFI02000079; EAL64591.1; -; Genomic_DNA.
DR   RefSeq; XP_638095.1; XM_633003.1.
DR   AlphaFoldDB; Q54N48; -.
DR   SMR; Q54N48; -.
DR   STRING; 44689.DDB0235305; -.
DR   PaxDb; Q54N48; -.
DR   EnsemblProtists; EAL64591; EAL64591; DDB_G0285507.
DR   GeneID; 8625143; -.
DR   KEGG; ddi:DDB_G0285507; -.
DR   dictyBase; DDB_G0285507; clp1.
DR   eggNOG; KOG2749; Eukaryota.
DR   HOGENOM; CLU_018195_1_0_1; -.
DR   InParanoid; Q54N48; -.
DR   OMA; VQYVNCH; -.
DR   PhylomeDB; Q54N48; -.
DR   Reactome; R-DDI-72163; mRNA Splicing - Major Pathway.
DR   PRO; PR:Q54N48; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005849; C:mRNA cleavage factor complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051731; F:polynucleotide 5'-hydroxyl-kinase activity; IBA:GO_Central.
DR   GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR   GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IBA:GO_Central.
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..459
FT                   /note="Protein CLP1 homolog"
FT                   /id="PRO_0000375189"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT   BINDING         94
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT   BINDING         156..161
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
SQ   SEQUENCE   459 AA;  50472 MW;  1E09BAC149CFB6FD CRC64;
     MSNDNSVNIN NFSSMNGGGG GSDIQFPLKP SQQQQQQQQN SINQSTIRTL EITQELRYEI
     DFDQNGWMKL IEGTAECFGT ELSLNKVYKL SGTKGAVFTW TGCKIEITNN CQPYIGEKTP
     MPQYAGVYQE LDAFRVSILD EPKKSGPRVI IVGPTDSGKS SLSKILLAYS ARSGYQPLFV
     DLDPGQGSIT IPGTISAAHI QNPLDIEEGL AGGIPLAHFY GHTSLDVNPD LFKALCKNLA
     SFIDKQLDSS NISRISGFIA NTCGWIDGLG YKILLQNIDV FKANLIIVMD NEKLYSDISS
     HYSQKDNSIK IIKLPKSGGV FIRPPVFRKK TRMNRIKEYF NGINDNLSPH YIVLDFKDVS
     IYRTGGGPAA PASALPIGTS SQIDPLQITE VYPSLDMCHS IFAISYAKQA SNIFHSNVAG
     FLYVSDIDME TKKITVISPA PGPLPSRFLL LGTLKWMEN