ID   CLP1_SCHPO              Reviewed;         456 AA.
AC   Q10299;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 133.
DE   RecName: Full=mRNA cleavage and polyadenylation factor clp1 {ECO:0000255|HAMAP-Rule:MF_03035};
GN   Name=clp1; ORFNames=SPAC22H10.05c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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       ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}.
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; CU329670; CAA93606.1; -; Genomic_DNA.
DR   PIR; T38207; T38207.
DR   RefSeq; NP_593741.1; NM_001019172.2.
DR   AlphaFoldDB; Q10299; -.
DR   SMR; Q10299; -.
DR   BioGRID; 278397; 1.
DR   STRING; 284812.Q10299; -.
DR   iPTMnet; Q10299; -.
DR   MaxQB; Q10299; -.
DR   PaxDb; 4896-SPAC22H10-05c-1; -.
DR   EnsemblFungi; SPAC22H10.05c.1; SPAC22H10.05c.1:pep; SPAC22H10.05c.
DR   GeneID; 2541907; -.
DR   KEGG; spo:SPAC22H10.05c; -.
DR   PomBase; SPAC22H10.05c; -.
DR   VEuPathDB; FungiDB:SPAC22H10.05c; -.
DR   eggNOG; KOG2749; Eukaryota.
DR   HOGENOM; CLU_018195_3_1_1; -.
DR   InParanoid; Q10299; -.
DR   OMA; VQYVNCH; -.
DR   PhylomeDB; Q10299; -.
DR   PRO; PR:Q10299; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005848; C:mRNA cleavage stimulating factor complex; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051736; F:ATP-dependent polyribonucleotide 5'-hydroxyl-kinase activity; ISS:PomBase.
DR   GO; GO:0051731; F:polynucleotide 5'-hydroxyl-kinase activity; IBA:GO_Central.
DR   GO; GO:0180010; P:co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway; IC:PomBase.
DR   GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IBA:GO_Central.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; mRNA processing; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..456
FT                   /note="mRNA cleavage and polyadenylation factor clp1"
FT                   /id="PRO_0000116579"
FT   BINDING         11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT   BINDING         49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
FT   BINDING         116..121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03035"
SQ   SEQUENCE   456 AA;  50449 MW;  BBBCDD62EA48E9DF CRC64;
     MKEIFIPKEC EWRFEVDEPA IQIRLVSGNA EYFGTELALG PPYHFTRVKG AIYTWQGCTL
     EVEGEPSVEY VAEETPMSTY LNLHFALEGL RLQAENAAAN DESSYGPCVC LIGPRSCGKT
     SVLKILESYA LKQSRHPICV NLDPTQPMLA LPGSISAFHN ATILDIQDAD GFGASTSTGP
     THVLAKVPLV YNFGLDSPLD NPKLYKLSLS RLALAVHSRM SQSKDARVSG CLVDTSSIQE
     NAEKYQDILH SIITDFRINI IIVLGSERLY SSMKRKYADA TWLSVVKVSS SGGCIDREEE
     WIQQFQARCI KQYFYGDDRM PLSPLSMIVD STQLVVYRVL EASESGPKSS VLPLGFEEEN
     TQSEKQDGNT SLRLHGKGEF LERISTEAMT ILQNSILAVS SVGEDEDEAT VVDSCIIGYV
     FVSDVDDVKN RMTLLSPVPE QLPSNALIMG TCKWQE
//