ID A0A1V9K9Z1_9ACTN Unreviewed; 850 AA.
AC A0A1V9K9Z1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=B0675_03800 {ECO:0000313|EMBL:OQQ16389.1};
OS Streptomyces sp. M41(2017).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1955065 {ECO:0000313|EMBL:OQQ16389.1, ECO:0000313|Proteomes:UP000192467};
RN [1] {ECO:0000313|EMBL:OQQ16389.1, ECO:0000313|Proteomes:UP000192467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M41 {ECO:0000313|EMBL:OQQ16389.1,
RC ECO:0000313|Proteomes:UP000192467};
RX PubMed=28326787; DOI=10.1021/acs.orglett.7b00545;
RA Wyche T.P., Ruzzini A.C., Beemelmanns C., Kim K.H., Klassen J.L., Cao S.,
RA Poulsen M., Bugni T.S., Currie C.R., Clardy J.;
RT "Linear Peptides Are the Major Products of a Biosynthetic Pathway That
RT Encodes for Cyclic Depsipeptides.";
RL Org. Lett. 19:1772-1775(2017).
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:OQQ16389.1}.
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DR EMBL; MWFK01000001; OQQ16389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9K9Z1; -.
DR STRING; 1955065.B0675_03800; -.
DR Proteomes; UP000192467; 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:OQQ16389.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192467};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:OQQ16389.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 202..491
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 40..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 850 AA; 90052 MW; 2F23C2566FB65330 CRC64;
MSEHAVGERQ GCQRPGCEGS YEDMGGGELY CDTCGLAPVV SAKGTVNSPP TGVTAGGGAA
RGSTSGSVRG SSRASSRTSS RSSQSRRSVS GRLSRSVSGG STGRSVSVRS SGSTAGSSGR
GRLGAGLVEV PGVPRPDPRE MVQENPEVPE RKRFCSRSDC GAPVGRSRGD LPGRTEGFCT
KCGHPYSFVP KLQSGDIVHG QYEVAGCLAH GGLGWVYLAV DRAVSDRWVV LKGLLDTGDQ
DAMAAAISER RFLAEIEHAN IVRIYNFVEH LDQRTGSLDG YIVMEYVGGK SLKEIANDRR
TADGRRDPLP VEQACAYGIE ALEALGHLHS RNLLYCDFKV DNAIQTEDQL KLIDMGAVRR
MDDDESAIYG TVGYQAPEVA EVGPSVASDL YTVARTLAVL TFDFQGYTNV FVDSLPDPGH
IEVFRQYESF YRLLVRATDP DPARRFASAQ EMAEQLTGVL REVVSLQTGR ARPSLSTLFG
PETKVTDTEL FGSVAGDVSR LGARVVPVRG RRAAPSLPAG GNGAAALPPP PDSPTLVKPV
PAAAAALALP VPRVDPGDPN AGFLAGLIAS APAELIAALH AAPAGSPELR LRELRARLEM
GEVAAAQHGV EALETDHPDD WRVVWYRGVT ALATGGNEIA ALSFDAVYDA FPGEPAPKLA
LGLCAEVLGQ LDNAAEYYRL VWTTDPSYVS AAFGLARVQL AAGDRRAAVS TLESVPESSI
HYTAARVAAV RARLRQRPVA DAAAPPFLDD LTAAAGQVEA LDGFGLDAVR REQLSTEVLG
CALDWVLSGS QGSAPASGGG HVLLGSALDE RGLRFGLERS YRTLARLARG GEERIDLVER
ANRYRPRTWV
//