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Database: UniProt
Entry: A0A1G8T1M0_9ACTN
LinkDB: A0A1G8T1M0_9ACTN
Original site: A0A1G8T1M0_9ACTN 
ID   A0A1G8T1M0_9ACTN        Unreviewed;       523 AA.
AC   A0A1G8T1M0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=SAMN05421806_1013 {ECO:0000313|EMBL:SDJ35428.1};
OS   Streptomyces indicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=417292 {ECO:0000313|EMBL:SDJ35428.1, ECO:0000313|Proteomes:UP000199155};
RN   [1] {ECO:0000313|EMBL:SDJ35428.1, ECO:0000313|Proteomes:UP000199155}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5727 {ECO:0000313|EMBL:SDJ35428.1,
RC   ECO:0000313|Proteomes:UP000199155};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; FNFF01000001; SDJ35428.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8T1M0; -.
DR   STRING; 417292.SAMN05421806_1013; -.
DR   Proteomes; UP000199155; 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; cd00161; RICIN; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 2.80.10.50; -; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:SDJ35428.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000199155};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:SDJ35428.1};
KW   Transferase {ECO:0000313|EMBL:SDJ35428.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        310..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          17..274
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          336..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..414
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   523 AA;  54259 MW;  EDDE8A88FC4F5ED3 CRC64;
     MSWSGLRAGD PRRIGGWTLV GRLGAGGMGV VYLAHAADGA PVALKRLRED LADDAEFRAR
     FRREAAALLR VQGACTARVL AVDVDASRPF AVMEYVPGPT LAEHVAEYGP LRGDMAHGFA
     LGLAEALAAI HGAGVVHRDL KPGNVLLSDQ GPKVIDFGIA QAADATALTR TGVAVGTVGY
     MAPEQLSGQA GPPADVFAWA LTVAFATTGR PPFGTGPVAA LLHRIEHEEP DLDGVPAHLR
     ALLTSALSPS PEQRPSAEEL LAALAGSGGG GTRVDADEVS TVLATAWQMP EPSPSPSPSP
     PPLPRPRRPW IAAWTSLAVL LAAMVGLLWA VLPDRGHSSE SGGTASGSAP TATATSAPES
     PATPPSSPPE TSAQPTTQDA TPSSTTPAQA QPTPFSSTGA LRNSHSGLCV DTNGPQRPGL
     NLQLRSCGNF SGQQWSYDGT GQHFTNTPSD LCLDTDGKPA AGVRAVLNPC GHYSGQLWRH
     DSENGRFVNT ESGLCLDTNG PPAVYVDLVL RPCGHFTGQY WQM
//
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