ID A0A1G9HS81_9ACTN Unreviewed; 899 AA.
AC A0A1G9HS81;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Serine/threonine-protein kinase PknG {ECO:0000313|EMBL:SDL15676.1};
DE Flags: Fragment;
GN ORFNames=SAMN05421806_1201 {ECO:0000313|EMBL:SDL15676.1};
OS Streptomyces indicus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=417292 {ECO:0000313|EMBL:SDL15676.1, ECO:0000313|Proteomes:UP000199155};
RN [1] {ECO:0000313|EMBL:SDL15676.1, ECO:0000313|Proteomes:UP000199155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5727 {ECO:0000313|EMBL:SDL15676.1,
RC ECO:0000313|Proteomes:UP000199155};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNFF01000020; SDL15676.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9HS81; -.
DR STRING; 417292.SAMN05421806_1201; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000199155; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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; 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; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:SDL15676.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199155};
KW Transferase {ECO:0000313|EMBL:SDL15676.1}.
FT DOMAIN 218..475
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 189..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:SDL15676.1"
SQ SEQUENCE 899 AA; 99171 MW; BE7BF4D76CD8FD14 CRC64;
QLPHPTPHHP DDEALLARIA ADCPGMTAAF VLPEACASSP EAVLALLRAA RARRRARLLL
AFRDPRAPLL RLLHEELLGP EWPAAVGDRI AERLTELHRV QRRLSERGGA ARADGAEELL
VRLERLRRTV RGDPLGAAHE LFLLELDVEN LLLAARAREA RLAAPLEISI EAAGDGLEDL
PWVQVQGPEL TEPAPQDAPP RPPAAEGGSR FAEAEQQYHV VGKLASGSYG QVYLAHDRAL
LNRLVALKRH NPRDPGAAEQ AARERLRLVE INHPFIVKVH NAILDKDGAG PLLVMEFADG
LTLEEIRQRI LRREPPFEGA RVLEFIAVYG VRILDALHYL HTRKEQELVY GDLSLNNVLH
CGDTIKLIDV AAVRGFDEPG PTTVTPPEAG PDGRMGPAGD LYCLGHVLTS LLDAAPAVGT
LGERSLRLTL ARATRPDPAG RFATAEEMAG QLHAVLRELR SLRLNEETFA PSLHFGPVAD
TLDGGLGSAP PLEQWAGGGS YKRLLGPQRP PAPGDAAADL PPPHPDRKDP NWKRLQRTSY
HDPKGLLDRT ASWEHTPELL FLRCRLHIQE ARAARHALTQ PRPEPVAFEG DGPAERPRTP
LDELARQLAA AGAAARKAGQ LIGEERARHD WRVPWHQGLI ELAHQRVEQA RAAFTQVYED
IPGEYAPKLA LGYCHEHLGA SEQAKEFYRS VWCRNHAQGS AAFGLARMHL AEGLPQDAVD
ALEGVPPDSR HRTAARTALV RIRAGLHEAR PEPSLAQFTL AYQALLRLVE HEGLTDPAAE
ERLRADLLEL QVLVVESARR TGIDPWSELA DRLPVDLDHD LPVRLRVPRT EEQLLLRLSD
SYRRLAHQVP RSGRAKDDAL IEALLDNAHH IRPTRLRHRP PGTAPRLPRW LSGGREPEG
//