PKN3_MYXXA
ID PKN3_MYXXA Reviewed; 547 AA.
AC Q9XBQ0;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Serine/threonine-protein kinase pkn3;
DE EC=2.7.11.1;
GN Name=pkn3;
OS Myxococcus xanthus.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=34;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DZF1;
RA Inouye S., Jain R., Ueki T., Nariya H., Xu C., Hsu M., Munoz-Dorado J.,
RA Farez-Vidal E., Inouye M.;
RT "Sequence analysis of 13 eukaryotic-like protein Ser/Thr kinases of
RT Myxococcus xanthus, a developmental bacterium and significance of their
RT coexistence with protein His kinases.";
RL Submitted (MAY-1999) 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 -!- 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;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AF159689; AAD42851.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9XBQ0; -.
DR SMR; Q9XBQ0; -.
DR PRIDE; Q9XBQ0; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Kinase; Nucleotide-binding; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..547
FT /note="Serine/threonine-protein kinase pkn3"
FT /id="PRO_0000171229"
FT DOMAIN 18..288
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 290..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 24..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 547 AA; 59430 MW; 39452DBF3B228019 CRC64;
MRTPDTDEYV GKTIAYKYRV EALIGEGGMG KVFRARQLSL DKVVVLKVLR HTLLSDERTV
ARFQREAKAA SRLNHPNSIS VLDFGQAEDG ALFIAMEYVA GQDLHQILSR EWPLNEGRVV
RIVSQVLSAL SDAHGAGVIH RDLKPENIMV EPRRNEPDFV KVLDFGIAKI TDSTDDGPAL
TRAGFVCGTP EYMSPEQARG SQLDHRSDLY AVGVILYQLM TGLLPFESDS AVGFATKHLT
EEPPPPTRRR PDARISPAME RLILRALSKN PADRPASAEA FKAELQAVDK ERRRMDSAPR
RSANSSAVLA PLPRKSAASP QSDVRDATLP GWGNEVTMEA TVRALPGVLE PLPANADAMA
ATRETTDSLV HTQPGAGGSS GVAFFFKSLT ILLVVAALGF FAYYFFMGAG SGGAQDLPYA
LPTNAPVPAG ANNSAVGASP DVPLYDRAIV SGARNVERAL DVAREGDKAL QRADVGLAAT
KYREAFSRSG DPELALKLGE VYWHRQNPDK EEARGWWNRH LREQPASKAR ALIEQRLNGA
VAQPTSP