Y1197_DICDI
ID Y1197_DICDI Reviewed; 1347 AA.
AC Q54JC7;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0288147;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0288147;
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; AAFI02000109; EAL63361.1; -; Genomic_DNA.
DR RefSeq; XP_636866.1; XM_631774.1.
DR AlphaFoldDB; Q54JC7; -.
DR SMR; Q54JC7; -.
DR STRING; 44689.DDB0231197; -.
DR PaxDb; Q54JC7; -.
DR PRIDE; Q54JC7; -.
DR EnsemblProtists; EAL63361; EAL63361; DDB_G0288147.
DR GeneID; 8626477; -.
DR KEGG; ddi:DDB_G0288147; -.
DR dictyBase; DDB_G0288147; pkcA.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_257973_0_0_1; -.
DR InParanoid; Q54JC7; -.
DR OMA; NCGLASR; -.
DR PRO; PR:Q54JC7; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; 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: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:0140582; P:adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0110014; P:negative regulation of aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:1903669; P:positive regulation of chemorepellent activity; IMP:dictyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR GO; GO:1904007; P:positive regulation of phospholipase D activity; IMP:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009372; P:quorum sensing; IMP:dictyBase.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IMP:dictyBase.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; IMP:dictyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0048837; P:sorocarp sorus development; IGI:dictyBase.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
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 PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Metal-binding; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1347
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0288147"
FT /id="PRO_0000355155"
FT DOMAIN 599..854
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ZN_FING 12..67
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 262..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..399
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 724
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 605..613
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1347 AA; 152496 MW; 6ACB56C1A00BBBCB CRC64;
MQPNQLKRPS LNHRFEPYTL KHLTICKRCE KEIIGVSNSA QICYSCKNIY HTRCCKEIET
KKLELICLGP PKKIKTVWKI ALIPSLFKSL FSKSKVIVNY SQQLINEKTF TLEAIKIWVD
VMRVDNDRYI QITKYYDIFD EEVFNYIINM IIEKDINLPM VNIEFPVDLH SSVQQNQYIN
DQAVSQEQKQ QQQQLQQQLI LQQQQQQQLQ QQQLNESYDN STINNLNYSN DISNAFSPRS
VFSALELSSN AQVMNALELS VPFNEDDNND DSTLSASTYN RRNSNKNKNS NKNNTSSSSS
APASASSSKH SNLNESFSSS TTAAAIVNNI DNSNNSNNLA ALSPRSTAST TTTTTTTTTT
TSPKSNNHHH HQHHHQNSKS RKPSTIIINK KKIKSPKNKS SKRYMLTEQY KWSTQMIGLQ
ILYRILFNEK NMIHFLNDKF MAPLAVLYPI LINRLKAISL GSDNNNNNNN NNNNNNNNSN
NNNNNNNEDF KLLSINCKLL ISILNRMLDF ETLIPLFFTN KVIESIAKVN SDRESLRGKL
SKDEFEVMDR VVLLLGKYFH LEPYHSLIER RPEWIDMIIN YSVEHKVGIL HHEITRNEVK
INVEIYDSPL CTVYSGVYNG MDVAIKEFSQ DGMGFDWVSF YKEITIVSAS QHPKVIKCYG
AHTKNTNKPF IVTELCSRGT ISNALNQIRK TTGQPPAIPL IVHMAIDAAQ SLEFIHSKNI
IHRDVKGNNF LVNENWEVKL IDFGVSRFVE ARLGYTIVGT PNYMACELFN GQPYHQPADV
FSFGVVLWEM FTQDTPYKNL TRIEQALFVQ SGGRPTIPPT VPTTIANLIE SCWVQTPHLR
PTFTEILKVF YSLLTPPPDN EHLVPVVTRL FNSSIIQLKI LKYLDTNTLL NCGLASRQLR
YNLYNGISME KKTFSNFWIK LMNFSKSKFR YELLSPSERK NDSTGSSPII MCIQPFSPNS
QSKNNNNNKN HHSDDIIDDD DDDDDDKTYP SLVIPFSASS PTLNINSENK NNNNVNEDKT
SDTSSNSNNN NNNNNNNNNN NNNNNNNNNN NNNSNNNNNN NNLRQNQFLG NDLNKSQDNN
QLMDGSGGRR DRSRSKSRSR SASPSNNHLH DKSLMGLLSS SQTSEIGDNN TNNNSDNEVD
NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN IDNNNNNKDN NNILSSENNN
NTTVIEQQQQ QQNVTNNNSN EPKNSNNEPK NSNITNNIVN PNVFTTTTTT TTTTRTTTTT
VYDGTGTLNN LLFKINDGGI ISSDSSNSLS DPESEEYSMP IKRSSSIRSP GPVSAISPLF
KSLSPNLSPI VPNIINGYSF ENTSACD
