CDC7_SCHPO
ID CDC7_SCHPO Reviewed; 1062 AA.
AC P41892;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Cell division control protein 7;
DE EC=2.7.11.1;
GN Name=cdc7; ORFNames=SPBC21.06c;
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8039497; DOI=10.1002/j.1460-2075.1994.tb06600.x;
RA Fankhauser C., Simanis V.;
RT "The cdc7 protein kinase is a dosage dependent regulator of septum
RT formation in fission yeast.";
RL EMBO J. 13:3011-3019(1994).
RN [2]
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 [3]
RP INTERACTION WITH SPG1.
RX PubMed=9203579; DOI=10.1101/gad.11.12.1519;
RA Schmidt S., Sohrmann M., Hofmann K., Woollard A., Simanis V.;
RT "The Spg1p GTPase is an essential, dosage-dependent inducer of septum
RT formation in Schizosaccharomyces pombe.";
RL Genes Dev. 11:1519-1534(1997).
CC -!- FUNCTION: Protein kinase essential for cell division. Plays a key role
CC in initiation of septum formation and cytokinesis.
CC {ECO:0000269|PubMed:8039497}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBUNIT: Interacts with spg1. Seems to interact with cdc11.
CC {ECO:0000269|PubMed:9203579}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC7 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; X78799; CAA55382.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB36886.1; -; Genomic_DNA.
DR PIR; S46367; S46367.
DR RefSeq; NP_596340.1; NM_001022261.2.
DR AlphaFoldDB; P41892; -.
DR SMR; P41892; -.
DR BioGRID; 277185; 47.
DR STRING; 4896.SPBC21.06c.1; -.
DR iPTMnet; P41892; -.
DR MaxQB; P41892; -.
DR PaxDb; P41892; -.
DR PRIDE; P41892; -.
DR EnsemblFungi; SPBC21.06c.1; SPBC21.06c.1:pep; SPBC21.06c.
DR GeneID; 2540660; -.
DR KEGG; spo:SPBC21.06c; -.
DR PomBase; SPBC21.06c; cdc7.
DR VEuPathDB; FungiDB:SPBC21.06c; -.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_001872_2_1_1; -.
DR InParanoid; P41892; -.
DR OMA; NIARDKY; -.
DR PhylomeDB; P41892; -.
DR BRENDA; 2.7.11.24; 5613.
DR BRENDA; 2.7.12.2; 5613.
DR PRO; PR:P41892; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0071958; C:new mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0071957; C:old mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0140281; P:positive regulation of mitotic division septum assembly; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:1902542; P:regulation of protein localization to mitotic spindle pole body; IMP:PomBase.
DR GO; GO:0031028; P:septation initiation signaling; IMP:PomBase.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1062
FT /note="Cell division control protein 7"
FT /id="PRO_0000085765"
FT DOMAIN 9..259
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 296..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1062
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 15..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1062 AA; 119291 MW; 04459AD60C0E2EDD CRC64;
MHNIQASSIT LGDCLGKGAF GAVYRGLNIK NGETVAVKKV KLSKMLKSDL SVIKMEIDLL
KNLDHPNIVK YRGSYQTNDS LCIILEYCEN GSLRSICKNF GKIPENLVAL YTFQVLQGLL
YLHNQGVIHR DIKGANILTT KDGTIKLADF GVATKINALE DHSVVGSPYW MAPEVIELVG
ATTASDIWSV GCTVIELLDG NPPYYDLDPT SALFRMVKDE HPPLPSNISS AAKSFLMQCF
QKDPNLRIKT RKLLKHPWVI MNQTSSKFSD AIDEVQKYNE RVKESTLTAI IEPTSNRINP
TLHSGRQSSY HMPESPKTPI AESPDHDNWD NEFQGTLKIS DDVLKKSEHF MDFCSNFKGK
NNSSSITSSP SKSRHAFNSD QISESNNFNA SPLSTPLKAQ FDPSKPALNR SIDHQKTPQH
KRYLSTEFKE NIPDGIEKFV ETPRDSEFTD IFPTSSIKVQ GLRKETGLGT LVLNKCYGSW
NNEENEDGEE SDIFDSIETN LENLDIENNI ALDKRTHLAS LLSSLLGSLR DKNIGSKDTT
VSQIASILSE DLSLKREIIQ AHGILPLLET LREIKTPDVQ LLLLKLINTV AFDDHTTLQK
VCFAGGLPLM LSFSNREHSF EFRYESAIFI QQMYRTSALT LQMFLSSNGL NSLLLFIKED
YGTNRDFVFV GVEGIWKLLR QQDYIPKNDI CTMVVNDSLE PLTKAMLKAL ATDDDSSRMS
LTRICEILLA LSQADNYVKE SLLCESALRR ILRILLYLPH SDMAITLQFF KQLSMVPSSL
SLLRKVHIIP LLTHILGDSK IEKGRKEIRS EALAALFNVC KLDKKSQEEA VISGAIPLLQ
EVIIKDRLFK EFALPILLAL PQAGPVSRIY LWQNKCLDFF LSLLSDLNWQ SAVFDTIASW
LQFELREVQR VLAEKRNVQL VLKVFCISQS ASSNRMLDTL GRVCQISPRL AASYGQPIIF
QKFKEKLTHK GTKPIVVLNI FQIMKSMCEA SSQSVAYIAH CGLPDVVANL NQTSDSVLVK
ELAKDLLKYL KVPQGPINEH KSPISKPHMP PPRWQPKQPL TQ
