ID F3ZJF6_9ACTN Unreviewed; 778 AA.
AC F3ZJF6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Putative serine/threonine protein kinase {ECO:0000313|EMBL:EGJ73041.1};
GN ORFNames=STTU_0252 {ECO:0000313|EMBL:EGJ73041.1};
OS Streptomyces sp. Tu6071.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=355249 {ECO:0000313|EMBL:EGJ73041.1};
RN [1] {ECO:0000313|EMBL:EGJ73041.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tu6071 {ECO:0000313|EMBL:EGJ73041.1};
RA Erxleben A., Wunsch-Palasis J., Gruening B.A., Luzhetska M., Bechthold A.,
RA Gunther S.;
RT "Genome sequence of Streptomyces sp. Tu6071.";
RL Submitted (APR-2011) 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}.
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DR EMBL; CM001165; EGJ73041.1; -; Genomic_DNA.
DR RefSeq; WP_007818953.1; NZ_CM001165.1.
DR AlphaFoldDB; F3ZJF6; -.
DR HOGENOM; CLU_000288_135_1_11; -.
DR Proteomes; UP000003955; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 1.10.510.10; 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; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR SMART; SM00564; PQQ; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:EGJ73041.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:EGJ73041.1};
KW Transferase {ECO:0000313|EMBL:EGJ73041.1}.
FT DOMAIN 14..266
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 274..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 778 AA; 80749 MW; C66924FFC0268236 CRC64;
MSLRVGDPAE IGGYVLEARL GSGGMGTVFL ARTGSGRPVA IKLIHQQFAA DEEFRTRFRQ
EVAAARRVSG AFTAAVVDAA PDAEQPWMAT SYIEGDTLSQ HIAAKGPLGG AELRRLAIGL
AEALRDIHRV GVVHRDLKPS NVVLSPEGPR VIDFGISRAA DQQTLTMTGR IIGTPPFMSP
EQLQAPRGVG PRSDVFSLGT LLVYSVTGHG PFDADSPYMT AYQVVHEEPA LDAVPQPLRA
LVELCLDKEP DRRPSADELL VLLRDLPSDL GTVGGDGLGA SRTRDVTTRH DEVTSRTAGA
ILPAGAPPSP EVPRTADAHA DAPEAARAPV VPDAARAPVV PDVPGDHADP GDTTLNGRRP
RRRWRSVLAA VVAVSAVGGG VAVVTAAGSG EGKNSGVAAP APPDGFAPWR QTVLGGRADI
PDELRCVARG EAVFCGGGGV IASRFDVKDG SRAWTVKSQG VPVQGLYFVG ATQDTVLGYR
FAPEDAPQEP RREVVALDAK TGHELWSVPT DTQSQAVTGR SQEALVAGTA VVSVDATGSQ
LEARDAHSGD VTWKTPFPAG TRCAPVLAGT RLLAMCAREG EIDALDVRHP TLHTVDRASG
RLGSALAVKG PVVPVGATGG RLALLQVHKE GPASTGYDGV ALADPATRKV TYAPFARTYD
GTPGMAGGTV YVSGQTGRVT AIDPESGRAK WSRQTAVEGA SGPASGERAL YFSSATGRVV
ALSPSTGEIL WTTDPRVDGL TGEQGSGPRV TVAGGALVVA ADKNTLFAFD ARKPPKSG
//
