CDC7_DICDI
ID CDC7_DICDI Reviewed; 1061 AA.
AC Q54DK3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Probable serine/threonine-protein kinase cdc7;
DE EC=2.7.11.1;
DE AltName: Full=Cell division control protein 7;
GN Name=cdc7; ORFNames=DDB_G0292152;
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 -!- 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; Evidence={ECO:0000250};
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; AAFI02000187; EAL61432.1; -; Genomic_DNA.
DR RefSeq; XP_629869.1; XM_629867.1.
DR AlphaFoldDB; Q54DK3; -.
DR SMR; Q54DK3; -.
DR STRING; 44689.DDB0231210; -.
DR PaxDb; Q54DK3; -.
DR EnsemblProtists; EAL61432; EAL61432; DDB_G0292152.
DR GeneID; 8628551; -.
DR KEGG; ddi:DDB_G0292152; -.
DR dictyBase; DDB_G0292152; cdc7.
DR eggNOG; KOG1167; Eukaryota.
DR HOGENOM; CLU_289259_0_0_1; -.
DR InParanoid; Q54DK3; -.
DR OMA; IHFNDPP; -.
DR Reactome; R-DDI-68962; Activation of the pre-replicative complex.
DR PRO; PR:Q54DK3; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; 2.
DR SMART; SM00220; S_TKc; 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 3: Inferred from homology;
KW ATP-binding; Coiled coil; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1061
FT /note="Probable serine/threonine-protein kinase cdc7"
FT /id="PRO_0000362009"
FT DOMAIN 622..1048
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 315..393
FT /evidence="ECO:0000255"
FT COILED 558..588
FT /evidence="ECO:0000255"
FT COMPBIAS 115..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 741
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 628..636
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 654
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1061 AA; 120073 MW; 48F20DD2017EB179 CRC64;
MNWDSNNNNN KNSNNNNNNS SSSSYNINNN YSSFNNSNNN NINNNNINTN NNNNNNNNNN
NNNNNNNNNN NNNNNNNNNK NNSSNNYHLA HINVYQQYPI KPLPISFNSF NTNMFQQQQQ
QQQQQQQLPQ HLPPLGSSGS SNGGPNLMGY AQIPPNYFKP LSPPSFHPPT SPQSFFNNNT
NNNNNNNNNN NNNINININN NNNSNNYIND STNSNNLNTS NGAINTSSHL FINSPNHHSD
NRSFIESRSP ASMNASPIHF NDPTFKVPVH LPSLSITNSP SLNSSIDSSY RLNNNNNNNN
NNGSNNSSFN STPTKFEQLQ LQLQQQQLQQ QLQQQQQLQQ QQQQLQQQQQ LQQQQQQQLQ
QQQQQQLQQQ QQQQQQQLQQ QQQLQQQQQQ QSTSHIHFST APTPIVSHHY NLQQPLQQYP
QNIYSHTNIL NQNNNSKPIN TNSSSSNNNN NNNNNNNNNN NNNNNNNNCN YNNSNNSYNN
NTTNTNNNPN NKRSQTKNQQ QQQPQPQQQQ LQQQQPQQSV INVNKKTTKV SKTKTSNQKL
TVNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNTIQQQQQQ QSNDIKLLLK NSIYSSRNDL
KELLSQPTEY TDSEYPEIVG KYRILEKIGQ GTFSGVYKSV CIDGPNIGLI VALKRVAPTS
SPARILNEIH SLLRVGGHYN VSALFGALRY KDQVTLILPF FEHDSFKDYF FQMSNENIKH
YLYALFDSLR HIHQNNICHR DVKPTNFLYS IKNNSFLLID FGLAQEMPNS NSNSNSNSNS
NSNSNSNSNS NSNSNNNNNN NNNNTNNNFN GNNSNNDFNN FINMNNSNSN NNNNNNSNNN
NNNNNNNNNN NNNNSNNNNN SNNSQEEIIL PSTNENGTTT SNASSTSNTT SSSSSSSNKS
KNLRNDPKPQ PAPRAGTRGF RAPEVLLKYN KQTTAIDIWS VGVILLCMIS GRYPFFISPD
DMTSLAEIVS IIGTKKIVDI AHLLEKKISI SHSIPPTPWR DLSRRLRSES SCDKQDVPVE
LYDLLERCLD PNPLTRITAS EALLHPFLVV NNNSNNNNNN S
