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Database: UniProt
Entry: A0A0M8SK97_9ACTN
LinkDB: A0A0M8SK97_9ACTN
Original site: A0A0M8SK97_9ACTN 
ID   A0A0M8SK97_9ACTN        Unreviewed;       547 AA.
AC   A0A0M8SK97;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Protein kinase {ECO:0000313|EMBL:KOU35345.1};
GN   ORFNames=ADK54_37870 {ECO:0000313|EMBL:KOU35345.1};
OS   Streptomyces sp. WM6378.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU35345.1, ECO:0000313|Proteomes:UP000037774};
RN   [1] {ECO:0000313|Proteomes:UP000037774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM6378 {ECO:0000313|Proteomes:UP000037774};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-2015) 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};
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:KOU35345.1}.
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DR   EMBL; LGDD01000337; KOU35345.1; -; Genomic_DNA.
DR   RefSeq; WP_053730349.1; NZ_LGDD01000337.1.
DR   AlphaFoldDB; A0A0M8SK97; -.
DR   PATRIC; fig|1415557.3.peg.8336; -.
DR   OrthoDB; 9762169at2; -.
DR   Proteomes; UP000037774; 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   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; 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; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:KOU35345.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Transferase {ECO:0000313|EMBL:KOU35345.1}.
FT   DOMAIN          58..316
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..30
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   547 AA;  58549 MW;  AC9B7B650A3B11F8 CRC64;
     MRDDGGRANE PTSYGLRPPE PAPVPQQTAY EPKPYEPTQQ QPADGAGDGT GRLLGGRYRL
     VGRLGHGGMG TVWRARDEVV DRDVAVKEPR VPDHLGERER ANVYLRMQRE ARAAARIDHP
     SVVTVHDVVM EDGKPWIVME LVRGQSLADR LQEGTLDVRE AARIGLAVLG ALSAAHEAGV
     LHRDVKPDNV LLGRGDRVVL TDFGIAQVEG EQGLTETGAF VGSPEFIAPE RVLGQRPGPE
     SDLWSLGVVL YAAVEGVSPY RRSNTPATLQ AVLSAEPQVP ARGSGAFGTL VMQLLRKDPA
     ARPSTTEIRA TLEPAANPAP APLAATRLYA GDGAPTGGSR WVPPVFVGNR GAQLGLGGVV
     LVVVGALVLL LVNPFGGGGL PAGWQVRPEN EVLHADVAVP DDYARTQGTE GDNVTYKDPS
     AVFQIYADRL DPATDKAHNT LPGDAGAWKT YYEKGGRNGT EFTNGKVTTT TVKHQGKQAY
     DIVTDYTPNS ASSDPNPTRY RYHELLVPGK GTAYWRLRVS MPAAGKAEQD GERLFAQVAD
     GLKIHDL
//
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