Y9844_DICDI
ID Y9844_DICDI Reviewed; 1761 AA.
AC Q54RR9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0282963;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0282963;
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. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000049; EAL65925.1; -; Genomic_DNA.
DR RefSeq; XP_639282.1; XM_634190.1.
DR AlphaFoldDB; Q54RR9; -.
DR SMR; Q54RR9; -.
DR STRING; 44689.DDB0229844; -.
DR PaxDb; Q54RR9; -.
DR EnsemblProtists; EAL65925; EAL65925; DDB_G0282963.
DR GeneID; 8623851; -.
DR KEGG; ddi:DDB_G0282963; -.
DR dictyBase; DDB_G0282963; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_239097_0_0_1; -.
DR InParanoid; Q54RR9; -.
DR OMA; MVTEYCQ; -.
DR PRO; PR:Q54RR9; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
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; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1761
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0282963"
FT /id="PRO_0000355157"
FT DOMAIN 1476..1744
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 18..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..905
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1259..1274
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1597
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1482..1490
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1503
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1761 AA; 195076 MW; 6F5220EEE84D8F9E CRC64;
MKDNIPTGSI IIPLNHHPQQ QQIPQQQEQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ
QQQEQQNNNN NINDNINGNN NSNEIKNTKD ANITNNNGTS IIISLSPPPS PALNSSSSST
INSNNTTISG GDNENNNNNT NNTNNNINNS NNSNNNNSNN NSNNNNNNNN NNNNNNNNNN
NNNNNNNNNN NNNNNNTNEE GNKTNINTTN NNSQNININN GINKNTRNNN NNNNNNNKQM
TPPTFKNNLQ VKHQPQSSSG GSIGGSNKLS LSKRVKSTTS SRASIIDSID IDIVFNSLKN
SITSKNSFVL GVHRHRMSSI SSISNTTNET TTTTTTTTNT TIEDHQIGSI GNNNNNNNNN
NNNNNNYFNV NNGNSNNINN YNNSGNGNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNH
FNSYSNNNNN SNSNNNSNNN LHGLNNNNNG VMESSDFNSD TVGRGSIFTV SNSDVNSDSN
VGLNQPSFND LTITCDTLTE TDEEDLMEKF LEDSDPDIDE EDDDDDFNEE EFMKFQTQFL
HNKSQNSSLN INNNNNSSNN NNINNNNNNN NIMAGSTSSV IYKNSGKPPL NENNNNNINN
DNTVCNINNN NNSNNNKSNN SNNSNNSFKD DISSDEEPET DSDTEFKNNH HTNYHNSPKN
QKHVDRKPFV NSKNNTNTNT NTHNTYNNNK NNNNNNTFEQ QSNEDEESYS GSYKSSQNSV
IYKPNLVSSP NFKSSLSSSS LISVGTNSLK NSPFPPSSPI LSPQTDDPNN NNNNNNSNTT
ISQPLPIALN VSIESPRAFY NSGSNNNNNN NNNNNNNNNN NNNNTNSTSA TTPIIQAQTH
PTTQIPTSDI DTSNSDNNNN NNNNNTSDNN FNDYNNDYNN DYNNYETEFL PPKKTPPPPI
PTKMSSTPPS STSSFLSTSS VTSVNSNNSV TSSTSTNTSN SSSPKHSSSQ KSKSVFSKII
KEGKKRLATK FNSHHHHNSG NNSSNSNNNN NDDEVPTYIH IYRGNGDESW RVKVTSSTTV
RDLLSMSLTS TVKGEPPSLK LYLTSSLNSC TCVSSPNNLS SAPAVSSSSS SSTTLETTTI
ITSASPSSSS SSFTSPTTTN SLNSHLNHSN NINNNNNNNT NNNNNNNNNN NNNNNNNNTD
RTNSNCTCNV NKPEKELNED DKVLSVQKKW SGPSIFVLKN NCTKSSSSST SSSSSSNNTN
NNNNNNNTIN NNSNNTGTRY SVSSITSESS EQSSNSHNSL NNNNHNNNNN NHSHNHNNSN
NNNHHHHHHH HHNNNNNQNG QQEGVADSSS SSPWSSPALS SPSKQHSLQY FENIPTLALD
STNNNNNNNN DTDSTSSNMG TPTTSRRITT IFQKQHSRNN SSNNQNNNNI NNNNNNNNNN
NNNNNNEHLT PLSNSTSLSS ASSISFLNSS NGNNSPNSNN SNSNNNNNNN NNNNNNNNNK
KTTTTTTTTT MNSNGECWKN AERPRTGVRW ISSTDLFLIK KIGAGSFSKV YKAKYMGEIV
AIKVLKGEAT SEQIELFKKE YDILSLVSSQ NLIKFYGACK EKKLRMVTEY CQHGSLYHIM
SKRKMDISWP LVFKWMHQAV DGINSLHTMR PALVHRDIKS QNLLINSQFD LKVADFGLAK
PTELQTGSNS TIKGTMAYCA PELYNGISYS EKADVYSLGI VLWEITTRVI TGKYQRPYED
NTEISFDFQI VIMSSKQGIR PTMPPNVPPK LSYLIQKCWN QDPNERPSCQ QILLAITSLY
DDYIYNPSRY NDLILNNDLN N
