NDRC_DICDI
ID NDRC_DICDI Reviewed; 1335 AA.
AC Q54P47;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Probable serine/threonine-protein kinase ndrC;
DE EC=2.7.11.1;
DE AltName: Full=Nuclear DBF2-related kinase C;
GN Name=ndrC; ORFNames=DDB_G0284839;
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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; AAFI02000071; EAL65072.1; -; Genomic_DNA.
DR RefSeq; XP_638411.1; XM_633319.1.
DR AlphaFoldDB; Q54P47; -.
DR SMR; Q54P47; -.
DR STRING; 44689.DDB0219984; -.
DR PaxDb; Q54P47; -.
DR PRIDE; Q54P47; -.
DR EnsemblProtists; EAL65072; EAL65072; DDB_G0284839.
DR GeneID; 8624781; -.
DR KEGG; ddi:DDB_G0284839; -.
DR dictyBase; DDB_G0284839; ndrC.
DR eggNOG; KOG0605; Eukaryota.
DR HOGENOM; CLU_258804_0_0_1; -.
DR InParanoid; Q54P47; -.
DR OMA; AYRRPIA; -.
DR PRO; PR:Q54P47; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005813; C:centrosome; IDA:dictyBase.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
DR GO; GO:0005524; F:ATP 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:0007098; P:centrosome cycle; IMP:dictyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IMP:dictyBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1335
FT /note="Probable serine/threonine-protein kinase ndrC"
FT /id="PRO_0000362024"
FT DOMAIN 718..1019
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1020..1106
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 586..613
FT /evidence="ECO:0000255"
FT COILED 1289..1325
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 840
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 724..732
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 747
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1335 AA; 149360 MW; C559C21F4C68FB52 CRC64;
MSRKENLNRS SSSNSIEFNR DRDRDSSNIS NSSNINCNNS SQTPPIPQHN SLSGRSKHSS
PIHSLKKKGS LVRQGIEDLF SSLSVDTHSS SNSNNNSSSN NNNNNNNHNI NSSSESSTPT
TPRSSFTPQV TMNSNQSSGN NSPQLSSRSS SQSTLIPSNE PTKSLAKFFL LAQQVDYVGD
SSSTLLPVEN LGLLSIQWKT YFTIGLNSTT TGYDVLKYIS IKTNRDLKSL TLADSDGKII
DNDYILTQQR CKKFVVVEDL NIDDLKMKQL NHLQQLPPPS QQQLPPPQSH QQQLLQQQLQ
QRLQNQNQNQ NNNSNSNSNS SSSSSCSTPQ SIVSQQQKLH QMLLNQQQIQ SSQSTTPTNS
SQKSSPNKVT DHQHVENCNF TSPSPSSPSS PSSPSSGMIL DGFNLDGNGG RPTPLIITPS
SPSSMRKNPP AIPPRSPSSF SGGSPLNNIL LNNTELISEP VTTTTTTTTT TSSSSSLSVT
TTISNPNYTQ NLPTTPLSNS SSNNNNNGSF ITLQDTTNNK SIINNNRESP PESPMGSRKS
SGSSNTTSST TNTTTPSSSS LTTSSGKESR DRDSKDKEKD LIGSGNNNNN NNNNNNNNNN
NNKVEKEKEN YCKFLDAVNS FNMVGNNGVL FNGEANRNMK LTNAQEEKCK ILDNYFNHYY
QELFKYLHQR HRRIKTIEDF TVESRMDRQG AEQWMKKQFE KETNFLRNKR AGMKLKEFKI
LTQIGKGGFG QVFLAQKKDT GDIVTLKRLK KQTVEWANQR NQVSQEKSVM LVDNKWITKL
LYSFQDANYL YLAMEYHCGG DFRALLNNLG TLSEDEARFY MIEMIEAISS LHEMGIVHRD
CKPSNFVLDK LGHIKLIDFG LSKEGIEKRN GWNKATMNEL RKSCLSASFT SNTMKAASAY
LSGGTNVMAY RRPIAHSAVG SPEYMSPEIV NDQGYDMTCD YWSLGCVFVE MLCGFNPFCA
DTPNDVFINI LRWKETLDWP LFTQELSVEA ADLLKNMLME QPHRLGGKGK QDFKNHPFFK
NHNWDEIVNG QVKPPFVPKV ESDIDTSYFE DAVNNDSSTW DIDDNDCGGY GSGGYGGGGP
QARDPFNNLK IPFFTYRKSS ALSLSMSSEI AQSLNYNNGN TYSNYTSNNN NNNLHNNQIH
EKNGNSGYNH FHFDSIEQQN QYQLSLLSPN SSDKSIGMIQ YIKKFRYQQL QQQLQQHFQQ
QNHLQQLKSN HRKSPTRQLI SSLLYKGDDK TSILQNYSSQ SQPSLANQLQ SSSSSPSPSL
QSQSQSPSLQ SSSKSTPNLS SSLLENPVKE ELEYKNQTEN EVEIKKENES EEIQSLRDQL
KEIIIYEDYD QEYSI
