ID M9YQG8_AZOVI Unreviewed; 438 AA.
AC M9YQG8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Protein kinase {ECO:0000313|EMBL:AGK20572.1};
GN ORFNames=AvCA6_23420 {ECO:0000313|EMBL:AGK20572.1};
OS Azotobacter vinelandii CA6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=1283331 {ECO:0000313|EMBL:AGK20572.1, ECO:0000313|Proteomes:UP000012988};
RN [1] {ECO:0000313|EMBL:AGK20572.1, ECO:0000313|Proteomes:UP000012988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CA6 {ECO:0000313|EMBL:AGK20572.1,
RC ECO:0000313|Proteomes:UP000012988};
RX PubMed=23792740; DOI=10.1128/genomeA.00313-13;
RA Noar J.D., Bruno-Barcena J.M.;
RT "Complete Genome Sequences of Azotobacter vinelandii Wild-Type Strain CA
RT and Tungsten-Tolerant Mutant Strain CA6.";
RL Genome Announc. 1:E00313-E00313(2013).
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DR EMBL; CP005095; AGK20572.1; -; Genomic_DNA.
DR RefSeq; WP_012700928.1; NC_021150.1.
DR AlphaFoldDB; M9YQG8; -.
DR KEGG; avd:AvCA6_23420; -.
DR PATRIC; fig|1283331.3.peg.2242; -.
DR HOGENOM; CLU_035565_0_0_6; -.
DR Proteomes; UP000012988; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF1; ZGC:77287; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00364; LRR_BAC; 5.
DR SMART; SM00369; LRR_TYP; 5.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51450; LRR; 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:AGK20572.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:AGK20572.1}.
FT DOMAIN 207..438
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 438 AA; 47486 MW; BFF1E0DBBAFB53EE CRC64;
MSTLEQLRRG ELAGSARLTL SADLDAFPEE IFALADSLEI LDLSGNRLTS LPADLPRLGK
LRILFCSDNP FSVLPEVLGD CPRLEMIGFK ANRIHHLPAA ALPPALRWLI LTDNRLEHLP
TELGERPRLQ KLMLAGNRLR TLPASLAGLE RLELLRIAAN RLAALPGWLA ELPRLSWLAF
AGNPFSDASE AEVLRRHPLP PIPRSDIALG EILGQGASGI IQRADWRSPG QPARPMAAKL
FKGSVTSDGL PRSEMAACLA AGEHANLIRV AGPLAERPGA PPGLLLELID PTFRVLAGPP
SLASCSRDCY APERRFVFDE ALRIARGVAA AVNHLHGRGI LHGDLYAHNL LVDEQGDCLL
GDFGAASFFE PGSAAGRALQ RIEARAFGCL LEELLERCPA DERNLRQRRL GQLREACMST
QAEQRPDFAS LSADLAAL
//
