ID A0A0Q8NHQ0_9ACTN Unreviewed; 489 AA.
AC A0A0Q8NHQ0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:KRB60675.1};
GN ORFNames=ASE03_09790 {ECO:0000313|EMBL:KRB60675.1};
OS Kitasatospora sp. Root187.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=1736486 {ECO:0000313|EMBL:KRB60675.1, ECO:0000313|Proteomes:UP000051829};
RN [1] {ECO:0000313|EMBL:KRB60675.1, ECO:0000313|Proteomes:UP000051829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root187 {ECO:0000313|EMBL:KRB60675.1,
RC ECO:0000313|Proteomes:UP000051829};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB60675.1, ECO:0000313|Proteomes:UP000051829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root187 {ECO:0000313|EMBL:KRB60675.1,
RC ECO:0000313|Proteomes:UP000051829};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRB60675.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMHX01000051; KRB60675.1; -; Genomic_DNA.
DR RefSeq; WP_057234589.1; NZ_LMHX01000051.1.
DR AlphaFoldDB; A0A0Q8NHQ0; -.
DR STRING; 1736486.ASE03_09790; -.
DR Proteomes; UP000051829; 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; 1.10.530.10; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1.
DR PANTHER; PTHR44329:SF214; ZINC FINGER CONTAINING PROTEIN KINASE-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:KRB60675.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000051829};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:KRB60675.1};
KW Transferase {ECO:0000313|EMBL:KRB60675.1}.
FT DOMAIN 15..290
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 489 AA; 52223 MW; 90B32F9ACDA87B39 CRC64;
MEPTDVPTGY LVAGYRITGL IGAGAWGRVY AGRSEADGSP VAVKFLPAGR LAPGQRRTLA
ELTRREIRFS RRADHPQLIR TLAVVTVRDP DRQALDGAVA LVMERAERSL QQLLQDAEPG
RPLPRAGPLL TELCTGLAHM HGKGWVHGDL KPGNVLLMAD GSVRLADFGL TTELEGTHAY
IPPLGSLDHV PPEWWSQRSG PRGVQLRPGA DVWAFGVLAH QVLSGGLHPF LGATARARGL
AAQAYARGVT PLRLDDRLPA GWRALIADCL AVDQAVRPNA GRLTARLRAL HTPPPRRRNR
IGRLTALALL AAAPATGWAG LISGPGQAPL PPPPPAVGAL PPDADVPATL REPIERAARA
CPEPEISPAL IAAMLKAESG FDPAATRPAT QEYGIAMWTP SVFKAWAQDG DGDGRKDYMS
APDAIITMGN YVCWLDQQLK RRGTGGDLRE LVAAGYRTSD KTVADAGGVP ERVRPHVDLV
LRYLAQYGG
//