ID A4SM26_AERS4 Unreviewed; 457 AA.
AC A4SM26;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABO89948.1};
GN OrderedLocusNames=ASA_1873 {ECO:0000313|EMBL:ABO89948.1};
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245 {ECO:0000313|EMBL:ABO89948.1, ECO:0000313|Proteomes:UP000000225};
RN [1] {ECO:0000313|Proteomes:UP000000225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449 {ECO:0000313|Proteomes:UP000000225};
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(2008).
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DR EMBL; CP000644; ABO89948.1; -; Genomic_DNA.
DR RefSeq; WP_005315340.1; NC_009348.1.
DR AlphaFoldDB; A4SM26; -.
DR STRING; 29491.GCA_000820065_02725; -.
DR KEGG; asa:ASA_1873; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG4886; Bacteria.
DR HOGENOM; CLU_035565_0_0_6; -.
DR Proteomes; UP000000225; 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 Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
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; 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:ABO89948.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABO89948.1};
KW Transferase {ECO:0000313|EMBL:ABO89948.1}.
FT DOMAIN 210..457
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 457 AA; 49071 MW; C7EA91548EDA9335 CRC64;
MYTLEQLRAG ELCGARHLKL CENLTEFPPE ILSLKETLEV LDLTGNQLSA LPDELAGFSK
LRIIFCSENR FTELPEVLGR CPALTMVGFK ANRIDTVPAA SLPAGLRWLI LTDNAIAQLP
DELGQCSRLQ KLMLAGNRLR ELPASLANCR NLELLRIAAN RIERFPDWLL SLPRLAWLAY
SGNPFSEGEE ARTIDDAHVA HIATVPWRAL ELGELLGQGA SGVIHSATRI TCDGLQGDGP
RSVAVKLFKG AVTSDGLPHC EMAASLAAGT HPNLIRVLGK VADHPSGMPA LVMALIDPTF
ANLAGPPSLD SCTRDVYPAG LSFPPAAVLA MAQGIAAAAG HLHERGIMHG DLYGHNILHS
FQGKGQVLLG DFGAASCYDR TECVLAEGLE RIEVRAFGCL LDELLARCQP QSESLQDLIL
LARACLCEQV SQRPSFAQIS ARITAVAAMM VAEPVCA
//
