ID A0A1G9KHK8_9ACTN Unreviewed; 817 AA.
AC A0A1G9KHK8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN05216298_4048 {ECO:0000313|EMBL:SDL48863.1};
OS Glycomyces sambucus.
OC Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC Glycomyces.
OX NCBI_TaxID=380244 {ECO:0000313|EMBL:SDL48863.1, ECO:0000313|Proteomes:UP000198662};
RN [1] {ECO:0000313|EMBL:SDL48863.1, ECO:0000313|Proteomes:UP000198662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3147 {ECO:0000313|EMBL:SDL48863.1,
RC ECO:0000313|Proteomes:UP000198662};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNGF01000006; SDL48863.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9KHK8; -.
DR STRING; 380244.SAMN05216298_4048; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000198662; 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 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:SDL48863.1};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 219..486
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..60
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 817 AA; 89554 MW; 2A69D3226AC546EC CRC64;
MSDQQPPPEH TQRYQPGQYQ QPQIEESDTL AVRRRMSTPP AVPPQPGFAP APPAPAAGQP
VAALPPGTAA LSPPSMTTPV GPPQAYAGSP APIVPPNGQS QQVLPANAVV SAPPAPYRAP
AAPMPQPITG PVTRSTTSST RQRGGLSDMP PVPPRDPAEA VMADPKVPEH KRFCSSCGKP
VGRPQAGRGG RVEGFCPHCR ARYWFTPSLS PGDLLSDRYE VLGAIAHGGL GWIYLANDRN
FADDLTQRWV VIKGLINTSD EDAIEAAINE RRFLVGVDHP NVVDIHDFVT SVDPRSGQLQ
SFIVMEYIAG KSLRDIRDAV DEDGERRPLP LEQVLTYTAE LLPAFSYLHD RNLLFCDFKP
DNIIHVETWL KLIDLGAVRH AEDMESAIYG TPGYSVPNDE ILSVGPSVTS DLYTIGRSMA
VLALDFKGFT STYRDRLPPA SEAPQFAEYG SFHRLLLRAC HIEPRSRFQD ADDMRTQVRG
VLHEVQSVQR GEPRFEPSTL FSGEQSVFGE PDVEYDLHAV GDPFDVAHAL PSPMVDLADP
MAAFLATQQA TDVNGILAEL NSAPQQSPEV QLRRVRTLVN AGELHQAAAV LDQFAQREGN
TWQVTWLRGI ISLLAADFAT AAAHFDAVYS HLPGELSPRL ALAACAELAG RPDLALPHYT
RIWACDHRFV SAAYGRARLL DLEGNSTDAI TTLHQVPKTS AQYGIAQTAA IQTALHSRTA
PPSLLDLHHM AGRLDELKLE PRRRHLVSTR ILHLALETVE RTGPAGEPPV FGARPEEREL
RLALERAYRD LAHACTRRED QVYYFDLANR HRPRTML
//