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Database: UniProt
Entry: A0A1Z1WCV1_9ACTN
LinkDB: A0A1Z1WCV1_9ACTN
Original site: A0A1Z1WCV1_9ACTN 
ID   A0A1Z1WCV1_9ACTN        Unreviewed;       776 AA.
AC   A0A1Z1WCV1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ARX84182.1};
GN   Name=pknG {ECO:0000313|EMBL:ARX84182.1};
GN   ORFNames=SMD44_03620 {ECO:0000313|EMBL:ARX84182.1};
OS   Streptomyces alboflavus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67267 {ECO:0000313|EMBL:ARX84182.1, ECO:0000313|Proteomes:UP000195880};
RN   [1] {ECO:0000313|EMBL:ARX84182.1, ECO:0000313|Proteomes:UP000195880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MDJK44 {ECO:0000313|EMBL:ARX84182.1,
RC   ECO:0000313|Proteomes:UP000195880};
RA   Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Wang C., Yao L.;
RT   "Streptomyces alboflavus Genome sequencing and assembly.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP021748; ARX84182.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z1WCV1; -.
DR   STRING; 67267.GCA_000716675_06445; -.
DR   KEGG; salf:SMD44_03620; -.
DR   eggNOG; COG0515; Bacteria.
DR   OrthoDB; 137117at2; -.
DR   Proteomes; UP000195880; Chromosome.
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   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; IPR031636; PknG_TPR.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
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; 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; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Kinase {ECO:0000313|EMBL:ARX84182.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195880};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ARX84182.1};
KW   Transferase {ECO:0000313|EMBL:ARX84182.1}.
FT   DOMAIN          102..408
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..66
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..336
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..465
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   776 AA;  83687 MW;  4367DFE0EE174A43 CRC64;
     MEGDGTDSGP NSTRNESGWG DESRPEPSGP SGPPEPPESS LPPLFVAGPP PRAARVELPP
     ESPDPTVLPE ITLLDRAVSR GDDPDALDGL PLPPDRLLAR QYRVVRPLGY GGMGEVYLAL
     DTKVGGREVA IKILRPDNAG RECGAPQPAP DSPDHPLARE RQELVELNHE DIIRVFNYGH
     HPDVGDFLVL QYVDGPTLEE VRARAQLYPE EFGGSRFYEF VLAYGVRFLA GLGYLHAPER
     GKVYGDLKPS NVMHDGSAVK FVDVGSVRRA GAPGLTSADY RAPTVGPCGE STGADDLYSL
     GETLRHLCGL GDLDDLAGLP PLPRPEGPPA PPGPPQDRAT QLMTVPLPPD GLGLGLLSLA
     RALRRATRPD RADRFATARE MDEQLRGVFR ELRSLRLGVE TFEPSPLFLQ SAFALDGGLG
     VPPPLSRWVG PHPAPARYEA PRPGDLAKEL PVPRPDPDDA RHAELSRLGD DDPAALLQHT
     AEWPGSPEVQ LLRCRLLLRI ALRPGAQVPP RLDDAAVALV RAERAIGPGA APYDWRLAWH
     RGLLALAADD VPLARGHFDR VYAAIPGEYA PKLALGHCAE RLGRWREALT FHEAVRVRNP
     SLGGAAFGAA RARLALGGPR ALAYAVEALD AVAQHSRYRT AARVGAVRVC ADHARGAEDL
     AEVVRRLGRL FYAHGLTDEQ ARLRMRAQVW EVARALLSGG AVSAAGLRDV ARGADVRLGF
     PVSERQVRVD LSRFCVGLAQ QAARDPAGSD TSLAELLLDR AYAIRPFGLR HHRGTR
//
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