ID F0ZKW8_DICPU Unreviewed; 1255 AA.
AC F0ZKW8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=DICPUDRAFT_33484 {ECO:0000313|EMBL:EGC35386.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC35386.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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DR EMBL; GL871061; EGC35386.1; -; Genomic_DNA.
DR RefSeq; XP_003288062.1; XM_003288014.1.
DR AlphaFoldDB; F0ZKW8; -.
DR STRING; 5786.F0ZKW8; -.
DR EnsemblProtists; EGC35386; EGC35386; DICPUDRAFT_33484.
DR GeneID; 10501506; -.
DR KEGG; dpp:DICPUDRAFT_33484; -.
DR eggNOG; KOG0192; Eukaryota.
DR InParanoid; F0ZKW8; -.
DR OMA; PCIVTEY; -.
DR OrthoDB; 11310at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblProtists.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblProtists.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:EnsemblProtists.
DR GO; GO:2000146; P:negative regulation of cell motility; IEA:EnsemblProtists.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IEA:EnsemblProtists.
DR GO; GO:0051593; P:response to folic acid; IEA:EnsemblProtists.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd13999; STKc_MAP3K-like; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_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 PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR23257:SF779; SERINE_THREONINE-PROTEIN KINASE WNK4; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022527};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 818..1071
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 612..653
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1106..1150
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 845
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1255 AA; 143169 MW; FA76B886DF78B249 CRC64;
MEGPLRINNP KNNKSNNTSL DNNIINNSSN NSTTTDNINL NNSINNNNSN SENNSNIVNN
NNKNDNSSTK ENKINGNTEE DEDDIHSKRS QNTTGGGVYT MDTSLTGDSH YKKRKNIEDE
NEVAPYHPHK RASFSINISP TQLQNDSNLN IFNSNNAINN NNNNNYNNIL QTTTTSSSST
DSNIHSPTQQ LQQQLQQHEN QQQQPEEIEE INRERQERDK MLHEEVDLDS YNNYNNYKYG
DGEEGENYET LIHHHNRSAH SDETTNNESG SPNRNKMLAD EDLINQDDNN NTDGDEPYHQ
KEEEEEEDKN ANQDSDYHEH QSTDDDHMKS DGEKEPESAR NSGEQLKMGH KDESTVSTPQ
HAYNNEDDED DEEEYDVPLR IQQVSNNKLP KLSLSNCWLK VIPTDVWSLL EIRDLDLSAN
QLKKISKSIG QLVHLKRLRL NHNQLTALPK ELYSLPRLTT LYLNNNNFKV VPKEINRLTS
LKTLDLSFNQ ITDISPQSNI NLMTNLVELR LRYNQLSTLP SNMLEATHLQ VLWLEGNRLP
LNKAILKKSP SEILSFLREY KPPNKKANEK SIKGIHNVSA ALPPIDTAST IAVAQAFAQK
EMDIKKRKKE NFDDIKKQHI ETELKLKQLE EELQIANAKA TKFEEEASFL QQHFNNPAAP
QGGGNTQHLN LPQILLNQPH LGWDHQPNGG SPNIPTPPAS TSPVLTGQQV VNGISQISLL
SPTNNPPSPI SVFNQQPPLP TQTLQQQNQN GSNSPPPQQK QQQQHQLNNS QQHLPIVQIN
QNNNNNNNLK DNFPIPTPPT KVIEPEKPFE WEVPLSEIVI GARIGRGGYG QVFRGSWRGT
EVAVKMLFND NVNAKLISDL RKEVDLLCKL RHPNIVLFMG ACTEPVSPCI VTEYLSRGSL
ANILLDENIE MDWGLRLQLG FDCARGMTYL HSRNPIIIHR DLKTDNLLVD DSWQVKVADF
GLATVKSHTF AKTMCGTTGW VAPEVLAEEG YTEKADVYSY AIVLWELLTR LIPYAGKNTM
QVVRSIDRGE RLPMPSWCPP KYATLINRCW ETDPQNRPSF PEILPLMEEM ISEFQSEKRD
AISQGRPIPY VGPPEKNPAI LHHQQNKLLE QQLILQQQQA QQQQQQLQQL QQQLEQQQKI
QQQLQQQIVN PNNPNNFYFQ QQLQQQQHFQ NQLQQHQQHI LQQQQFQQLQ QQQQPYLYQQ
PSQIVNNNNS LSPAATNTNN NEDQMKISDK NLKKKIDGTT QDNSNNKNFY KSSIP
//
