ID Q1CWM8_MYXXD Unreviewed; 1021 AA.
AC Q1CWM8;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABF92937.1};
GN OrderedLocusNames=MXAN_7082 {ECO:0000313|EMBL:ABF92937.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF92937.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF92937.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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}.
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DR EMBL; CP000113; ABF92937.1; -; Genomic_DNA.
DR RefSeq; WP_011557001.1; NC_008095.1.
DR AlphaFoldDB; Q1CWM8; -.
DR STRING; 246197.MXAN_7082; -.
DR EnsemblBacteria; ABF92937; ABF92937; MXAN_7082.
DR GeneID; 41364257; -.
DR KEGG; mxa:MXAN_7082; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_009368_0_0_7; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000002402; 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 CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.10.10.1320; Anti-sigma factor, zinc-finger domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041916; Anti_sigma_zinc_sf.
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 InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR027383; Znf_put.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13424; TPR_12; 1.
DR Pfam; PF13181; TPR_8; 1.
DR Pfam; PF13490; zf-HC2; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 4.
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:ABF92937.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABF92937.1};
KW Transferase {ECO:0000313|EMBL:ABF92937.1}.
FT DOMAIN 66..338
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1021 AA; 111366 MW; 1BD3350E389545CC CRC64;
MSCPDENDLA RHLEGQLSSE RAQQVRAHVA GCAECRSVLA ALSSNEARTS FAGVGPLAPG
TRVGRYVVLG LLGEGGMGRV HVAYDPELDR KVALKLLKPE RFHEDSLALA RQRLEREART
MAKLSHPHIA SLHDVGEYQG QLFLVMEFLE GGTLRRWLTE QPRPLREVLE RFRQAADGLA
ASHALGIVHR DFKPDNVLLT KGGLVRITDF GLANATLVPG TAAPGTVSPA SLTVTGTLLG
TLAYGAPEQL RGEHGDARSD QFSFCVALYE ALNGQRPFEG KTREALLEQV ARKAVRPERA
GVPAWLRAVV RRGLSADPAE RFSSMEVLRA RLSRDPGARW RTVALVMLGA VLTGLAVFGL
LSRQAPQALC QGSERHFAGV WDAETREATR RAFLATGALD AEASFSAVAA ALERWKLDWT
RAHQEACEAT RVWGEQPEQV LGLRMACLDE RLEEVTRVVA ALQGADARTV ARGFGLGGSL
ASLRRCSDAR TLLEAVAPPE DPAVLLEVTA VRAELARANA GLFAGHTPEA LKVALAARER
AVRTRYRPLE AEAHLLCATL QEDASAFEDA RASLVQAGLA AEAGRHHAVL ARVLYAQAWL
SGHDLERTQE AWAYLNRAQA VAEPLRDPEF DALLNYVRAE LFEQEGRFSE AEPLLREALD
RVTAKGVSHA AARAELNGRL GLLARHQGRL LEAKRWQEEA LRLQEDLHGP DHRDTARALV
NLGGTLAHAG ELARAEAVVQ RALANLRRSL GEEHLVVART LSNLAVIYFE WGRGPEALRA
AEQSLAVARK SVPPEGADAV LMGMTSNRTG VLGELGAREA ELEQARRSLA HRERVYGATH
PEVALDLHEV GRLLRLLGRA KEARGFHARG VALQESLVAR GELEGEGLRW LADALLFLGR
VEEARGHAER ALARLERDWG PVAPERIKAL VLMGDIHLAR RAPAEAVAPL RTALAALASE
QVASARVPLA RRRLAQALRQ SGASDEACQE ARRAWLEWEP WRKAYPGEVA EARAEKDRCP
R
//
