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Database: UniProt
Entry: A0A1Q4W3K0_9ACTN
LinkDB: A0A1Q4W3K0_9ACTN
Original site: A0A1Q4W3K0_9ACTN 
ID   A0A1Q4W3K0_9ACTN        Unreviewed;      1021 AA.
AC   A0A1Q4W3K0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=A6A06_07575 {ECO:0000313|EMBL:OKI04614.1};
OS   Streptomyces sp. CB02923.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1718985 {ECO:0000313|EMBL:OKI04614.1, ECO:0000313|Proteomes:UP000185893};
RN   [1] {ECO:0000313|EMBL:OKI04614.1, ECO:0000313|Proteomes:UP000185893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB02923 {ECO:0000313|EMBL:OKI04614.1,
RC   ECO:0000313|Proteomes:UP000185893};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKI04614.1}.
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DR   EMBL; LWKZ01000012; OKI04614.1; -; Genomic_DNA.
DR   RefSeq; WP_073761369.1; NZ_LWKZ01000012.1.
DR   AlphaFoldDB; A0A1Q4W3K0; -.
DR   STRING; 1718985.A6A06_07575; -.
DR   OrthoDB; 137117at2; -.
DR   Proteomes; UP000185893; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR031634; PknG_rubred.
DR   InterPro; IPR031636; PknG_TPR.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR24363:SF0; SERINE/THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF16919; PknG_rubred; 1.
DR   Pfam; PF16918; PknG_TPR; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:OKI04614.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185893};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:OKI04614.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          282..563
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          89..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          949..972
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..608
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1021 AA;  104403 MW;  9247F83146B0DEE5 CRC64;
     MSEERTGGVA CQRRECPGTY EDVGGGELYC DTCGLAPVVS PEGMVGSPPT GVTAARRGGG
     GGALGGGVAG MAGAEGAGYG AGSVGLAGSG GSAGSAGSGG SGGSAGSGGS GGSGGSGGSG
     GSGGSGGSVG LEGAAGSGSA GGRGSASVTS AGGRTSSSGS RTSRRSVSGR LSRSVPGSST
     RSMSVSVRSA GRGTGSGPSR GRLGAGLVSV PEVPRPDPRT AVLENPEVPE RKRFCSRGDC
     GAPVGRARGD RTGRTEGFCT KCGHPYSFVP KLRPGDVVHG SYEVVGCLAH GGLGWIYLAI
     DRAVSDRWVV LKGLLDTGDE EALAVAASER RFLAEIEHSN IVRIYNFVEH LDRATGSLDG
     YIVMEYVGGK SLKDIANERR TANGRRDPLP VEQACAYGIE ALEALGHLHS RNLLYCDFKV
     DNAIQQHDQL KLIDMGAVRR MDDDESAIYG TVGYQAPEVA VAGPSVASDL YTVARTLAVL
     TFDFQGYTNI FADSLPDPDN IEVFRAYESF YRLLVRATDP DPARRFSSAE EMAEQLTGVL
     REVMALRTGE QRPALSTLFG PELRVVDTDV VAPAEGDTSL LGARAVAAGR TRTERKGRAG
     REGKARRAGR GAGNAVVGPA TGVGAPGGIG GSGGVGGSGV AVPAQVAYEV TSATGPQTMT
     GGAGAAAGTV TPAATGAGAA AVAAGGPPGA PALRPLDTGL AVLALPVPRV DPADPNAGFL
     AGLLAAAPAE LVSALRAAPA DTIETRLRKL RAQLERGDGA AALHELRGIE TEPGQGWAED
     WRVVWYRGLV ALTNGDRETA ALSFDAMYDA FPGESAPKLA LAVCAEVLGQ LDNAAEYYRL
     VWAADHSYVS AAFGLARVRL ADGDRTGAVA ALESVPESSI HYTAARIAAI RARLRQRPAH
     DALLDDLRAA AGQVGQLADS GLDAERREQL TTEVLGCALD WVLSGSRGAE QRGRTLPSGA
     LSPGSGGTAA RPGLLGSALD ERGLRFGLER SFRLLARLAQ RGEERIELVE RANRFRPRTW
     V
//
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