GenomeNet

Database: UniProt
Entry: F0ZBL5_DICPU
LinkDB: F0ZBL5_DICPU
Original site: F0ZBL5_DICPU 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system