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Database: UniProt
Entry: E1IIB0_9CHLR
LinkDB: E1IIB0_9CHLR
Original site: E1IIB0_9CHLR 
ID   E1IIB0_9CHLR            Unreviewed;       591 AA.
AC   E1IIB0;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:EFO79060.1};
GN   ORFNames=OSCT_3061 {ECO:0000313|EMBL:EFO79060.1};
OS   Oscillochloris trichoides DG-6.
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Oscillochloridaceae; Oscillochloris.
OX   NCBI_TaxID=765420 {ECO:0000313|EMBL:EFO79060.1, ECO:0000313|Proteomes:UP000054010};
RN   [1] {ECO:0000313|EMBL:EFO79060.1, ECO:0000313|Proteomes:UP000054010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG-6 {ECO:0000313|EMBL:EFO79060.1,
RC   ECO:0000313|Proteomes:UP000054010};
RX   PubMed=21037015; DOI=10.1128/JB.00931-10;
RA   Kuznetsov B.B., Ivanovsky R.N., Keppen O.I., Sukhacheva M.V.,
RA   Bumazhkin B.K., Patutina E.O., Beletsky A.V., Mardanov A.V., Baslerov R.V.,
RA   Panteleeva A.N., Kolganova T.V., Ravin N.V., Skryabin K.G.;
RT   "Draft genome sequence of the anoxygenic filamentous phototrophic bacterium
RT   Oscillochloris trichoides subsp. DG-6.";
RL   J. Bacteriol. 193:321-322(2011).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFO79060.1}.
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DR   EMBL; ADVR01000131; EFO79060.1; -; Genomic_DNA.
DR   RefSeq; WP_006563627.1; NZ_GL501404.1.
DR   AlphaFoldDB; E1IIB0; -.
DR   STRING; 765420.OSCT_3061; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_461413_0_0_0; -.
DR   OrthoDB; 9814968at2; -.
DR   Proteomes; UP000054010; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   PANTHER; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Kinase {ECO:0000313|EMBL:EFO79060.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054010};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:EFO79060.1};
KW   Transferase {ECO:0000313|EMBL:EFO79060.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        342..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          19..277
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          371..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   591 AA;  62146 MW;  E0FA8C450834FB97 CRC64;
     MQTQNPAEFP ANTLINQRYL ITRTIGRGGM GAVYEAVDQR LGATVALKQM TVTGANVATA
     FEREARILAS LRHPALPKVS DFFADAQGQF LVMEYIPGND LGHLLTKRGQ PFPVEEVVRW
     ADQCLAVLEY LHSQNPPIIH RDIKPQNLKL TPAGEIVLLD FGLAKGYANV QSPNTASIFA
     YTPNYAPLEQ VQGSGTGPLS DLYALAATIY HLLAGAPPPD VLQRLGATAS GQPDPLQMLS
     LVNPQVPQPL AAWVAHGMQL DQRNRPPSAA AMRRDLTQIM RAGPVANVGP TVVQPRGYDP
     TVVQASPAAP PPLPRAAPPP PPPAFALPLD ASAPVKRRGC SVLPIIVGLV VLLAAGGGVF
     WFVTRDGGPG TAPTSVAVGA TRTPRPSATP TDDRAPTAGA VQAGATSSPT GPSSGASGTT
     GTTPSGIQYG PVEQLFPYDI MASDAAPDGI DAAGNPISYS PWNVVDGYAD TAWRVPGDGI
     GQGLQLELGA PMLISEVQVI PGYAKVDPTD GTNRFWQNRR VVTVSLEFSD GSSIAATFAD
     DPSLQSIRLP KPVLSSYVRL VILETTAVPP EGGRDFTPIS EIVIMGQMPL P
//
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