NDRD_DICDI
ID NDRD_DICDI Reviewed; 2112 AA.
AC Q54HD2;
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 ndrD;
DE EC=2.7.11.1;
DE AltName: Full=Nuclear DBF2-related kinase D;
GN Name=ndrD; ORFNames=DDB_G0289543;
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}.
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DR EMBL; AAFI02000142; EAL62667.1; -; Genomic_DNA.
DR RefSeq; XP_636170.1; XM_631078.1.
DR AlphaFoldDB; Q54HD2; -.
DR SMR; Q54HD2; -.
DR STRING; 44689.DDB0229453; -.
DR PaxDb; Q54HD2; -.
DR EnsemblProtists; EAL62667; EAL62667; DDB_G0289543.
DR GeneID; 8627193; -.
DR KEGG; ddi:DDB_G0289543; -.
DR dictyBase; DDB_G0289543; ndrD.
DR eggNOG; KOG0605; Eukaryota.
DR HOGENOM; CLU_232232_0_0_1; -.
DR InParanoid; Q54HD2; -.
DR OMA; SECHIRE; -.
DR PRO; PR:Q54HD2; -.
DR Proteomes; UP000002195; Chromosome 5.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
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 InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 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; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2112
FT /note="Probable serine/threonine-protein kinase ndrD"
FT /id="PRO_0000362025"
FT DOMAIN 1555..1872
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1873..1958
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 59..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1722..1750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1986..2027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2055..2093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1349..1386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2055..2088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1683
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1561..1569
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1584
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 2112 AA; 233800 MW; 189C4F63B139A8D9 CRC64;
MNQSTQNIFK MEEEEEDDVD GEIIENNHCI NTIIPLHIHS NGLNSIEPIL EEVDQNQISN
DNRFNNNNNN NNNNNNNRNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN RKSWIGHLFV
KNKKEKKHIQ PITIENNNNS SSDDSYLSEN ISSGSSNGMD NSSSGSSSSG SSSGSSSSSS
STNTSAYTSP NTNSTTNTPT SSNNNTPLST PSNSTRKKFI QNFLSIFSKS DDNRNHSTNG
NSNQSQNIHH LSLNNGNLTN INNNNNNGNN NNNNNSECHI RERHKTLSKF WKKRTPFVHS
PSNYHIVDNK HHRNHKRSSS SSQLANSVSC DQLNIKYIST KHERSSKSSS MALRKMMYND
LFENLIHQQQ LQLQQQQQQQ PQQQIDNIPE NNINININTN VNLNVNNNNN NNNNNNNNNN
NNINGDDFLR NNIIHNSNDS EQQFELNHNS IINNVNKSIS TNNIKNSNEN LIINSPNNSN
SSDMLIIPNN IIEDSSMTPQ IIIDRNHNRQ NSNDLKNSGD LILNDQNQNN NNNSNNNNNN
NNNNNNNNNN NNNNNNNNNN NNNNNNNQTI PISSTIVTTC NIMKKSTNST NDEFDPSLTP
IVKGYSNPIP IITCNNNNNN NNNNNNNNLN YNFPTATASN TPSTPTQSHI LNNLQVSSNT
VPNNNNTTTL STTTTTTTTT TTISTINKPT ASNSVGDEKK YIHSWSPSKG KGQQFPRTSA
PSALRAISDS NGSSNSISNS TNNSTDDLYN PDSMLNNNNN NASCNNLSME IQLQHSQSFY
NNSLDRSDTQ RLLSSPPRIG SAHHMLGLKP LVKKEGILNN SVGGTSTLSG GSSSSSSSSN
GGNGLIPDEL LINRPLVEHR QSDDHLRAKN KLLHDELFPI QRASSSISKW VTAAPSSPPP
SHGCNSPDAS PDCLSPVSSM IRIYYVPLEN SNNNTTNNNP IITTTTLANN NNNNNNTNNN
TNNTNNSIIN NNNNNNNNNN NNNNNNTNPN DFPFSKISDD NNNNNNNNTT TTTTTTTTTT
TTTTANTNIN NNNNNIAPLP NLPFSHNHRY SISSSITKGN PQTFANYWTQ IIGTTTLAKE
IVDSIANKMD KDPQYLKLCC SVNPYDYLED DKPVNLVRIK KFYLLEIAEE VIIHEDIVNP
PIQCMQNYVF GSNTFSSSGS LSGNLLTSSQ NNSNGSGGSN NNNNNNTNNN NNNNNNNNNN
NNNNNNNNNN NNNNNNNNFN NSTGNLANIQ SGGHVNGNGL TSALHSHHIG GGIGYTSLSG
NALISASWSP NCKFLSVSPA YGFGMKSNLN NHNNHNNINS GNNINNSINN SNNNNNNNNI
NNNNNKIYTT GLSVEGDFMS SQKFEDHDFN FSTSPINEGL SPTTSSSRSS ITDDTYGGGV
GNESPSSPSS PPLPFSLSTS LNGNGMSGNN GRSSNNNNNN NNNNNNYNNN NNNNSNFHNN
HINNLKNGKK IRGSTFCSTG AEGGGISIGG IEQPKISAQL KEKIKILDNY FQHYYRELEN
YLSQRKKRMD TLEQVLTESG IKPNSIAWSR CWKEHTQKES GYLRSKRSKL GPSDFQKLTA
IGKGGFGKVY LARKKDSNEI VTLKVIRKST YHRANQMTSV TKEKEVMMIP HSSKDQSQWI
TRLLYSFHDS QYLYLAMEYH CGGDFKTLLN NLQRLEDDIA PFYMAEMILA VESLHRLGYI
HRDLKPSNFV VDKLGHLKLI DFGLSKEGFI SRNSKYHTTW KNLREDNTPS NNNNNPNNNS
LKSSTSLKNS SDCVGNIHGN NFKQPLNKKV TFSKVGSPEY MAPEMLAGKG YDISYDYWSL
GVVFFEMLIG DTPFNGDTPE EVFMNILDWK NILDWDLYSD YISEYAVDLL QKLICEPDKR
IGIDEMKVHP YFVNIDWENI RSVTPPFVPQ VQNEVDTSYF EGAENINEDE EHVDDFVETA
QEANQTSNVE SELEDTTIRL MPFGGFNFQR FPTIVEGARA KGLLKSFYVE EKSVSRAPSV
SSFNIQTSTI NNNNNNNNNN NNSNNNNNNN NNNNNNNNNN NNNNNLTVTT TATSVSASNS
PTILSANNSN LNISSNNSNL GSSGGIPSSN SSLTPNNKST SPSSGPVSTL FKGPLLRVSS
KNCVQSTNSS KK
