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Database: UniProt
Entry: A0A3S9PEM1_STRLT
LinkDB: A0A3S9PEM1_STRLT
Original site: A0A3S9PEM1_STRLT 
ID   A0A3S9PEM1_STRLT        Unreviewed;       423 AA.
AC   A0A3S9PEM1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=EKH77_05830 {ECO:0000313|EMBL:AZQ70803.1};
OS   Streptomyces luteoverticillatus (Streptoverticillium luteoverticillatus).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=66425 {ECO:0000313|EMBL:AZQ70803.1, ECO:0000313|Proteomes:UP000267900};
RN   [1] {ECO:0000313|EMBL:AZQ70803.1, ECO:0000313|Proteomes:UP000267900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 15060 {ECO:0000313|EMBL:AZQ70803.1,
RC   ECO:0000313|Proteomes:UP000267900};
RA   Feng Z., Chen G., Zhang J., Zhu H., Yu X., Zhang W., Zhang X.;
RT   "The whole draft genome of Streptomyce luteoverticillatus CGMCC 15060.";
RL   Submitted (DEC-2018) 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; CP034587; AZQ70803.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S9PEM1; -.
DR   OrthoDB; 9762169at2; -.
DR   Proteomes; UP000267900; Chromosome.
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; 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; 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   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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}; Kinase {ECO:0000313|EMBL:AZQ70803.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000267900};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:AZQ70803.1};
KW   Transferase {ECO:0000313|EMBL:AZQ70803.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        372..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          17..268
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          272..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..334
FT                   /note="Basic and acidic 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   423 AA;  44947 MW;  E4C1B3AA945DCFFA CRC64;
     MTMMRLRRED PRVVGSFRLH RRLGAGGMGV VYLGSDRRGQ RVALKVIRPD LAEDQEFRSR
     FAREVSAARR IRGGCTARLV AADLEADRPW FATQYVPGPS LHDKVNEEGP LSAAQTASIG
     AALAEGLLAV HDAGVVHRDL KPSNILLSPK GPRIIDFGIA WATGASTLTH VGTAVGSPGF
     LAPEQVRGAA VTPATDVFAL GATLAYACTA DSPFGQGSSE VMLYRVVHEE PQLMGVPDAL
     APLIHACLAK DPEERPSTLQ LSLRLKEIAA REAHGISEGR PPAPRREPDR PSARSAAQYE
     RQRTERRPAG APTPRPQRPH TPERPAEGVR APERRPAPQR PAAAGRRSRP GARTGAGARR
     PGPDRKLLRQ RLIVFVVVTL LVALGIAAAQ GCQGPARSLG GVPSTPVTTM GAPGAVSPGD
     ARS
//
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