ID A0A177HF94_9ACTN Unreviewed; 665 AA.
AC A0A177HF94;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Serine/threonine-protein kinase AfsK {ECO:0000313|EMBL:OAH09269.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:OAH09269.1};
GN Name=afsK_9 {ECO:0000313|EMBL:OAH09269.1};
GN ORFNames=STSP_73530 {ECO:0000313|EMBL:OAH09269.1};
OS Streptomyces jeddahensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH09269.1, ECO:0000313|Proteomes:UP000077381};
RN [1] {ECO:0000313|EMBL:OAH09269.1, ECO:0000313|Proteomes:UP000077381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381};
RA Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J., Madkour M.H.,
RA Al-Ansari A.M., Almakishah N.H., Steinbuechel A., Daniel R.;
RT "Genome sequence of Streptomyces sp. G25.";
RL Submitted (DEC-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 -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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:OAH09269.1}.
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DR EMBL; LOHS01000206; OAH09269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177HF94; -.
DR STRING; 1716141.STSP_73530; -.
DR PATRIC; fig|1716141.3.peg.7794; -.
DR Proteomes; UP000077381; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 2.80.10.50; -; 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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:OAH09269.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000077381};
KW Transferase {ECO:0000313|EMBL:OAH09269.1}.
FT DOMAIN 70..329
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 36..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 665 AA; 68229 MW; 114A48000DC6970A CRC64;
MSCLVGFLMV PVADSVEHPL ERFSRRGFHF GGRAGSDVNG ETLSGEDGFD LSGSGARPLE
ADDPRRIGPI PLVGRLGSGG MGQVFLGVHE GRYAAVKQVL PSVISEDADF LRRFGHELDN
LSRLPVEATA PLLASDRTAR PPWFATAYVP GLTLREALDV HGGPLPADSL WLLLREAASG
LAAVHARKMV HRDLKPSNVM LTLDGLTLID FGIARADEQT TLTLTGMMVG TPAYMSPEQA
SGARPLTGAT DVFALGSLVA YAASGRPPFG DESRNGVLYR IVHEEPDLEP VRARDPELAE
VVAACLDKDP ESRPTAAELV ERAERHGPFA PPLWPPAVTE RLDERAAFAT TVPSADRLGI
PEPADTLEEP GAEGEADATA EPDAAAERDV AAKPDEPGDG KPAKAEPAPR PDRGERLRTR
ILFAVIPVVV VTGTTLAIQL LPYTFSSGDR AGSTPTASVS ASSLPMPSTT GASASKTAKP
AKSSSSPPDK GKGAGASPAA AGDAQDGSDG STGSGGSGGS GGSSGSGSSD GSGGTSTGAV
TNPASGTYRF KNGDTGKCLT QVYGAAGTGD CADSTAYWTV KSSSAGGFEL VNQQTGQCLS
ANMLGQATFV GDCDQASPRL WRTGSGSTLR SVSNGGCLDV GSGGGAGVHT PSCESGKASQ
RWTKV
//
