ID A0A0M8SSS0_9ACTN Unreviewed; 508 AA.
AC A0A0M8SSS0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=ADK54_22080 {ECO:0000313|EMBL:KOU40573.1};
OS Streptomyces sp. WM6378.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU40573.1, ECO:0000313|Proteomes:UP000037774};
RN [1] {ECO:0000313|Proteomes:UP000037774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM6378 {ECO:0000313|Proteomes:UP000037774};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) 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:KOU40573.1}.
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DR EMBL; LGDD01000288; KOU40573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8SSS0; -.
DR PATRIC; fig|1415557.3.peg.4896; -.
DR Proteomes; UP000037774; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.40.1000.10; Mog1/PsbP, alpha/beta/alpha sandwich; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45832; SERINE/THREONINE-PROTEIN KINASE SAMKA-RELATED-RELATED; 1.
DR PANTHER; PTHR45832:SF25; SERINE_THREONINE-PROTEIN KINASE SAMKA-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 317..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..248
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 255..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..272
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..306
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 508 AA; 54132 MW; AA48E49B8ACB89D2 CRC64;
MGRVWRAADE ILDRQVAVKE MRINELDAED SRIRRERTLR EARATARIDH PNVVRVYDVV
AEESDRLWIV MELVESRSLE KLLLEDGPVA PREAARIGVG LAAALVEVHA VGVLHRDIKP
GNVLLGPGGR VVLTDFGIAA IQDAAALTVV GMLVGSPDYM APERVSGKPQ GPASDVWSLG
ATLCAAVAGC SPFARPSTLA TLHAVLYEEP ELPDSAGPLA PLLAQLLVKD PELRPGLDEI
AARLMPIAAP PTVLAAGPAP APHPPTLQVF GDPPPWPGNQ SVREEPPPPP RELTSAPQPV
PEEPKPPPRR PWARKRILLT AVVVVAAAVA AVLIATTANQ HGGSGAAGGS SSAAPPTVDG
TSRPPSATPP PGSIDETGFA WIPPKGWTRT AKSPSNIHYH APGGKQEIAA SYALVRGGDL
MTQWQEAEAG SHDVPGYQKI RLDRTTFHDQ PAIIWDYDFT QNGIPWKARQ IGFNEGGKSY
QINTWYEADT ESAALGTYDA VTSSFTPL
//
