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Database: UniProt
Entry: A0A1E7KJF7_9ACTN
LinkDB: A0A1E7KJF7_9ACTN
Original site: A0A1E7KJF7_9ACTN 
ID   A0A1E7KJF7_9ACTN        Unreviewed;       488 AA.
AC   A0A1E7KJF7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=AN216_09610 {ECO:0000313|EMBL:OEV03974.1};
OS   Streptomyces oceani.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1075402 {ECO:0000313|EMBL:OEV03974.1, ECO:0000313|Proteomes:UP000176101};
RN   [1] {ECO:0000313|EMBL:OEV03974.1, ECO:0000313|Proteomes:UP000176101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO 02100 {ECO:0000313|EMBL:OEV03974.1,
RC   ECO:0000313|Proteomes:UP000176101};
RX   PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA   Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA   Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT   "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT   Adaptation to the Marine Environment and Their Diversity at the Genomic
RT   Level.";
RL   Front. Microbiol. 7:998-998(2016).
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   -!- 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:OEV03974.1}.
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DR   EMBL; LJGU01000115; OEV03974.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E7KJF7; -.
DR   STRING; 1075402.AN216_09610; -.
DR   PATRIC; fig|1075402.3.peg.5317; -.
DR   Proteomes; UP000176101; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 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   InterPro; IPR011990; TPR-like_helical_dom_sf.
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; PF13374; TPR_10; 3.
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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000176101}.
FT   DOMAIN          1..249
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          280..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         27
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   488 AA;  51568 MW;  0E2841C067DE144E CRC64;
     MRGRLGAGGM GEVFLGRSPG GRSVAVKVVY PHLAGQREFR ARFAAEVAAA EAVGGAFTAP
     VVASGPEDDP PWIATAYIPG PNLAEAVAEA GPLPERSVWG LAAGLVEALQ AIHARGLLHR
     DLKPANVMLA ADGPRVIDFG IARTLEVTSV TRTGMVVGTA GFMPPEQAQG GQVGPAADVF
     SLGVVLAFAA SGSEPFGQGQ PLAILHRVVN DDPRLDALDG PLRDLVAACL AKSPDERPTL
     PQLLDRITVH WDPPDGASGT SPWPVGVTTL IEHRVDAPTA SYTQASDSTH DAPTATADTT
     EKELSRRFED ALHGASRPAD AVELFEQAVA NHAHVLGPDH PATLLRRHEE AQNLGLVGVR
     AEAAELFAGV AADRARVLGP DHPDTLCSRH HHALYLSGGT KNLKAARLMA GVAADQARVL
     GPDHPDTLCS RRNRALYLGQ GGRFLKAARL MAGVAADQAR VLGPDHPDTW RSHHDHARFL
     SRSRRLRW
//
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