ID A0A0M8SCY1_9ACTN Unreviewed; 777 AA.
AC A0A0M8SCY1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=ADK54_42265 {ECO:0000313|EMBL:KOU33313.1};
OS Streptomyces sp. WM6378.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU33313.1, 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 -!- 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:KOU33313.1}.
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DR EMBL; LGDD01000359; KOU33313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8SCY1; -.
DR PATRIC; fig|1415557.3.peg.9326; -.
DR Proteomes; UP000037774; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 2.40.10.480; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR22983; PROTEIN KINASE RELATED; 1.
DR PANTHER; PTHR22983:SF6; SERINE_THREONINE-PROTEIN KINASE 36; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 2.
DR SMART; SM00564; PQQ; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 2.
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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KOU33313.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:KOU33313.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..267
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 291..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..401
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 777 AA; 81842 MW; EA2AB6A02FBE4FBF CRC64;
MTQHDPRRIG PFEVLGRLGA GGMGLVYLAR SASGRRVAIK TVRTELAEDQ LFRVRFTREV
EAARAVSGFY TAAVVDADPR APVPWLATAY VPAPSLEEIV NECGPLPAQA VRWLAAGIAE
ALQSIHGAGL VHRDLKPSNV LVVEDGPRVI DFGIASGVSN TRLTMTNVAV GTPAYMSPEQ
AKDSRSVTGA SDVFSLGSTL VFAATGHAPF HGANPVETVF MLLREGPDVT GLPDELRPLI
ESCMQMEHPN RPSPEDLQAQ LAPHLFASGS DDSGTASAWL PPRSVAMIEQ RRGGGRMQVA
KAADPSPSSV LHSGRQAPPR PADPPYPGRH GGSAVTYPPV HADDPVHLPG AKVPIGPGPR
ASDASRVAID AGPATGWVRR PGANGAQASP VPPPTHPPET PGRWRPWRFR MSNDVWGTPA
VAGDLLYVTS FEVHALDVGT GRRQFKTRDV AWAMAVEAGR IHASDGPTLY ALDAADGGEL
WRLPADAWVY SLKADRGTVV TGTRGGGVQA WEAANGEKLW ETAGAQTDFE TPEAGPTIHD
GTVYVWQDAR LRALDARTGV ERWSYPVGDA ASCGGVPVRV APAQDGYVYV SAGTRVLAID
VASGHVRWHF EAPAVFLCPP TFAPGPAVAG GGVYLADYLG TVYALDASTG KDRWRIATES
RQSVEPVLVA DGNVHVGSGN ALYTLDAVTS TPKWRFAAGG EVVGTPVVAD GRIHFGSADH
CLYTLDAAGG QLRWKLATGG EITGSPVVRG GVVYACSKDR CVYALDAVKG TATSGSR
//
