ID A0A0M9YPL3_9ACTN Unreviewed; 695 AA.
AC A0A0M9YPL3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:KOU55566.1};
GN ORFNames=ADK57_44160 {ECO:0000313|EMBL:KOU55566.1};
OS Streptomyces sp. MMG1533.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415546 {ECO:0000313|EMBL:KOU55566.1, ECO:0000313|Proteomes:UP000037741};
RN [1] {ECO:0000313|Proteomes:UP000037741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1533 {ECO:0000313|Proteomes:UP000037741};
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 -!- 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:KOU55566.1}.
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DR EMBL; LGDG01000282; KOU55566.1; -; Genomic_DNA.
DR RefSeq; WP_053755405.1; NZ_LGDG01000282.1.
DR AlphaFoldDB; A0A0M9YPL3; -.
DR STRING; 1415546.ADK57_44160; -.
DR PATRIC; fig|1415546.3.peg.9506; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000037741; 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-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; 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; 2.
DR SMART; SM00564; PQQ; 6.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 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:KOU55566.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000037741};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:KOU55566.1};
KW Transferase {ECO:0000313|EMBL:KOU55566.1}.
FT DOMAIN 22..284
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 284..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 695 AA; 73454 MW; 05C3B06381FC0B3A CRC64;
MAPQRNTGAG AEAELPEYAG HYRLESCLGS GGMGIVHLAR STSGMKLAVK VVHAEFAKDP
EFRGRFRQEV AAARKVSGAF TASVVDADSE AERPWMATLF IPGPTLSDHV KRNGAMSPGE
LRRLMAGLAE ALRDIHRVGV VHRDLKPSNV LLAEDGPKVI DFGISRPKDS ELRTETGKLI
GTPPFMAPEQ FRRPREVGPA ADIFALGSVM VHAATGRGPF DSDSPYVVAY QVVHDEPDLT
GVPENLAPLV LRCLAKEPED RPTPDELMRE LRSVAASYDT QAFIPAQRAE PLGPEPRAEK
PEPQPVKRRG RWAALGAGAL GLAAVVALTS VQLLDGGSAV PRSSSTPRTT SAGFGSWKAT
APSGKDTPQC AYGNGKLLCG QTGLVFALDP SDGRLLWRHA DARVRAGQPV VSGGLVQPTL
DLNLRLEALD PASGKARWQR SMSSYSGLGH TSRMLLLTTA DGTVTGLDSA SGDTTWSHRI
PGHKAPFFVS FAGDPLAYAT STSDDGTSTR VTAVDPDTGD LRWDKQLKGS LEPVGTGDGS
VFFAATDAVY DDTRAVVRYN PDDGTSRRVT LAVPLQQAQG TVRGNVVYLM GTGGSLVAVD
MAAGKQRWSL ETAVTRGSAP VADGRHVYIT APDGRLLAVD AAGGRLLGQT PPRLDTNSDQ
IAGALSSPVL AHDHVYATAP DGTVFAVPAK DPSAW
//
