ID A0A2T7TFH4_9ACTN Unreviewed; 709 AA.
AC A0A2T7TFH4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Protein kinase {ECO:0000313|EMBL:PVE13903.1};
GN ORFNames=Y717_03925 {ECO:0000313|EMBL:PVE13903.1};
OS Streptomyces scopuliridis RB72.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1440053 {ECO:0000313|EMBL:PVE13903.1, ECO:0000313|Proteomes:UP000245992};
RN [1] {ECO:0000313|EMBL:PVE13903.1, ECO:0000313|Proteomes:UP000245992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RB72 {ECO:0000313|EMBL:PVE13903.1,
RC ECO:0000313|Proteomes:UP000245992};
RA Olson J.B.;
RT "Annotated genome of Streptomyces scopuliridis.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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:PVE13903.1}.
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DR EMBL; AZSP01000013; PVE13903.1; -; Genomic_DNA.
DR RefSeq; WP_030349905.1; NZ_JOEI01000003.1.
DR AlphaFoldDB; A0A2T7TFH4; -.
DR STRING; 1440053.GCA_000718095_00694; -.
DR OrthoDB; 951193at2; -.
DR Proteomes; UP000245992; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR44129; WD REPEAT-CONTAINING PROTEIN POP1; 1.
DR PANTHER; PTHR44129:SF13; WD REPEAT-CONTAINING PROTEIN POP1; 1.
DR Pfam; PF07676; PD40; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:PVE13903.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000245992};
KW Transferase {ECO:0000313|EMBL:PVE13903.1};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 42..294
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 460..492
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 675..709
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 709 AA; 74498 MW; DA44A1F0853FAC25 CRC64;
MSQPGYVPPA VPPVRGERPG WPTTPPSHRP LGPGDPAEAG PYRLEAVLGA GGMGRVYLGR
TPAGSAVAVK VVHREYAGDR AFRTRFEHEV AAARRVQGLY TVPVVDADLR ADEPWLATAY
VPGPSLQDAV AEYGPLPVDA AVGLIARVAE ALQSIHAADV IHRDLKPSNI LLTAEGPKVI
DFGIARAADV TSVTGTGMLT GTPAYMAPEY IRGQTVTEAV DVFALGVVAC FAVTGRPAFG
VGSHHGVTYR ILEQAPDLDD CPEPVRTIAA GCLEKDPRRR PTPAEVIQLC LPRTRTVVSP
GTRTVVSPAP GLHDAVTTPA SPATRQEQGG GAAPGGPVAP SGSDTRPYPP SPDPHTTPAP
SLPVLLGGVG ILVLVVMLVA VLLPEHSADR DTPSSIKPVA TITEVLHPGN GVAVAFSPDG
KTIAAGGGGR VELRDVADRK LRATFTQRDK SGKAVLGTPS LAFSPNGKLL AVGTGSGVVG
LWDVAKRRQV GLTHGDRTKT IESVAFSPDG KLLATGGGDG VRLWDADSGK EQIGEVAVLD
DEASIDHVAF SPDGRTLASA GYNFFPPVPS EGYSVRLWDV SGRKARKTLY DSKQIWGVAF
SPDGKTLATT DEDYTVTLLN VASGRQEGSL VDETDAQLRT VAFSPDGKTL AVVMGDEVWL
WDMADHKRRT SLISDQENAD NVKSVVFRPD GQFLATMTYG GTARLWKMP
//
