ID F0ZBL5_DICPU Unreviewed; 2578 AA.
AC F0ZBL5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=roco5 {ECO:0000313|EMBL:EGC38713.1};
GN ORFNames=DICPUDRAFT_148631 {ECO:0000313|EMBL:EGC38713.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC38713.1, 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).
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 Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. ROCO subfamily. {ECO:0000256|ARBA:ARBA00008171}.
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DR EMBL; GL870971; EGC38713.1; -; Genomic_DNA.
DR RefSeq; XP_003284809.1; XM_003284761.1.
DR STRING; 5786.F0ZBL5; -.
DR EnsemblProtists; EGC38713; EGC38713; DICPUDRAFT_148631.
DR GeneID; 10506815; -.
DR KEGG; dpp:DICPUDRAFT_148631; -.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; F0ZBL5; -.
DR OMA; EREMNTP; -.
DR OrthoDB; 10797at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13999; STKc_MAP3K-like; 1.
DR Gene3D; 3.30.310.200; -; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR Gene3D; 3.30.70.1390; ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR032171; COR.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48005; LEUCINE RICH REPEAT KINASE 2; 1.
DR PANTHER; PTHR48005:SF13; SERINE/THREONINE-PROTEIN KINASE DDB_G0278509-RELATED; 1.
DR Pfam; PF16095; COR; 2.
DR Pfam; PF13516; LRR_6; 2.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF16652; PH_13; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF08477; Roc; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00364; LRR_BAC; 5.
DR SMART; SM00368; LRR_RI; 3.
DR SMART; SM00365; LRR_SD22; 6.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS51450; LRR; 4.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS51424; ROC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
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:ARBA00022679}.
FT DOMAIN 199..462
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 494..603
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1180..1400
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT DOMAIN 1981..2245
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1819..1842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2333..2487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2521..2578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2333..2441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2442..2456
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2460..2487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2521..2563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2008
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2578 AA; 284704 MW; 2F91BF8A5895F515 CRC64;
MDLNKKDKEK EKKDKDKELK KEKKEKKKEK KDKEKKKDKD KDDKGGLFSI VGGLIGGLTD
SQQPSQPPNH STTVSAQSTT QAKEELSKPV IQENHKKAMD FWINNTATST STITTSASSH
PTIVTTTPTP VNNNSNNSKT TNSNSGSNVK LNTSLENGGN NDSKKDLSNE HSPKNRKEDN
KDNSSNKDNN IVETPADENR KKLVESLMKS LCSFSESIKI ILDLFYTPLK KSELLSHEEL
KGIFSVIEMI GGFKQAILED FKKYLSNWNS ANQAALYSTF SQFVGYLKLY QVYALQYNYS
LSSLSLLMFD NQKFETFIKN AESKLANLQY TLAPIVTVSS SSATVKPVSL AEILGPQYDQ
SAAQNNNNGT QPAFTQVSLR RTGNSTFLTS TGGSNSASGK FTQEYNYSNL ASLLILPIHF
LARFHHFFKT IMDSLPVLHP DYKPYNLLYK KITAVVKDIV TESVNINKVI SISKSIKSPT
IGLFNSTDIV QNRKFLKEGI LIEQFNNQRV SYYTFLFSDL ILFTEKIEDG STITSTTLMP
YEGSFYLLKK LERISNIQVD DPELGFEYRK GFQIKTKDSS IFYMTASEKE KSNWFQILSQ
ATLNSNKSKS NNSNPYSNIG LSRQSISNIE IDLNNDDSKD DDDDPKDIAS FCKMITSGQR
PRVELNASLL KLSDPKPLFA ALASTHFVNH LVFSPSTMSD KYMQMTLSMM SLNKSITHLT
LSQNSINDSC AIALGDMLRY NHSLIQMDLS ENQIGDKGLA ALIDGILSHP SITVVILSQN
QITDVGAKHI PKLLKFNQTL NALFLEDNNI SNQMASEILD QWISNHTTVL TRIILPSIPN
DYNEKIKTKA ISIANRLDKK KKQINTSSTS SSNIKSQATS NINNSLIAPG KGILDIGSFD
YSEISLQLLN KINMMMTDSR RLSDLKELFL DHNCISNIPV TILRELKNLQ LLDLSNNQLS
SLPAEICELK ELVKLNVSHN NLASLPLEIG QLIKLTHLDI SFNFIEAINV NSLSQLVNLK
VLMMQRNYFN RLPISIFQKL NLLESFSING SPCFHPIKQR IYESIAIRST RLDLSDSGLS
YLPIEIGSIQ TLTELDLSNN RIKDLPPQIG KLSNLSILNL TNNQLEYLPW QLSQLTKLKL
LNITGNQISF DNSGKITIPD VLSGEGLTGL LKYLKLSSTK EKPCMRMKLM LVGQENVGKT
SIAKCLKKEI IPVSKKLRQT IGLGTKKNKT PTLMEQSSSI DFNAPQNINP LNTSLNISTD
GINMDDWRPP SEDQSPAVTF SIWDFAGQEV YYSTHQFFIS SRSVFIVVFD MSVYNPDEVS
RVPYWLQCIE AFGGDSSVIL VGTHLDELPN GVDINQITQE IHNKYFTKFP NLKLFLPVSC
KSGKNINKLQ NHIVKLGKLE KKLGEVYNRS FFQLESLILS EREMNTPPII TFDEFSDMAQ
SCGIPATAVN KAADFLKELG IIVYFDDVKS GLDQFIFIDP PWLTRLMATI ITSKPNFVQS
GVLDQSNLHQ IWKPPDFPQH LHHVLLAILQ KFEIVHPLPD KNNNSSNIKS NVPSKSSAVT
EAKKAFNNKS TNQSSTTLLN GVSRFGNGSI SKGSSLNLVK KLNEAGLNVS TVSSSTATTT
TNSLSISNEN NLVPKASTKH LVPILLSEER PNSIEKVMDH IINKEQNFLE RIYQFEFLPV
GFFSKLMIRT MHFTTVKEYW KNGLLVERDG STCLIESIHS YSQINLKAWG TNPSNVLRFI
IETAELLISG WYKLQFHFLV PCNCLNCISI LGFSTGNSSG VVNGMMGGGP TLNTSNSSNS
LSSNSSTLSL NSNISNTSSV SSASSTPSVL SPPLTNSLDS AEASGDSLDL DFSDYYEGDV
SPGGTLKSKR KKNQNKFLTL YRNNKTNSSG SKQNQQQPID LTKVSNMINQ QLTFGPVFKS
HDLRTMFLYE DIERTFLSKK FEMICKSNIT GEETIVRLDS LVPELLMSDI GPNFTLEYKD
LEIIEQVGEG GFGIVHKGKL RGELVAIKQI AMNGNNQAAA EEIYREFRRE VWLSNILTHP
SIVSLKGYCL DPCCIVMEYI PNGTLYSYLH KASAEKPIGW PLKLKISINI ADAIKHMHNF
TPKICHRDLK SPNILMLSDM NANVVCKVSD FGETRAVVTS ALGRDKLSNP IWLSPEIMRG
EEYTEKADVY SFGIVLWEIL TGQLPFDEYP VAHSSFMYQL EDEIMNGLRP SIPAGSNADY
VQLIKDCWQN DPLLRPTFPD IHLRLCQMAG ITPTITTTPP PTNSPQLTNN NNNANIIQNG
TGSFKRTNSI VQRPSVSSIF NNTSSNVNPV TAPVTPHPPL VRKISRNISS SQIVSSPVSS
TLNNSSTTTA SSSPSVSVTP VNSTISSNIT PTPSAKPPLR HNLSQASITP KPAPVSSFTK
PPSHSSLSLS TPQSSNSGNT ATSPSSTSTT TSPSSTSPTS TPQHPISPPI LKPSRALPPK
PANITSNPSS SSTTSSPIPS PSSSIIKPST AKALPALPTQ SSSATTPGST LKFNSVANKT
IGQSSTLPAS TFKSTGSSTS PSGSTSVPNS TTTSPSSSFL LRPTGGNFKK LPALPNQK
//