ID E3FJV0_STIAD Unreviewed; 671 AA.
AC E3FJV0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN OrderedLocusNames=STAUR_5190 {ECO:0000313|EMBL:ADO72962.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:ADO72962.1, ECO:0000313|Proteomes:UP000001351};
RN [1] {ECO:0000313|EMBL:ADO72962.1, ECO:0000313|Proteomes:UP000001351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO72962.1,
RC ECO:0000313|Proteomes:UP000001351};
RX PubMed=21037205; DOI=10.1093/molbev/msq292;
RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA Sogaard-Andersen L.;
RT "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL Mol. Biol. Evol. 28:1083-1097(2011).
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DR EMBL; CP002271; ADO72962.1; -; Genomic_DNA.
DR AlphaFoldDB; E3FJV0; -.
DR STRING; 378806.STAUR_5190; -.
DR KEGG; sur:STAUR_5190; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_000288_151_1_7; -.
DR OMA; PHLAEND; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000001351; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR013229; PEGA.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR PANTHER; PTHR43671:SF13; SERINE/THREONINE-PROTEIN KINASE NEK2; 1.
DR Pfam; PF08308; PEGA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ADO72962.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ADO72962.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 446..469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..284
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 328..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 671 AA; 73529 MW; 1DAB21C0CE99879B CRC64;
MSLEIYGNYH LVKRLALGGM AQIYLARRKG QDASAPLVVV KRILPHLAEN LEFVRMFLDE
ARIAARLAHP NIVQLYDLGA QDDSFFLAME YIHGDDVRRI CKRAESLNHP LPVALACRVI
IDACAGLDYA HKKLDPLGKP LGIVHRDVSP QNILVSFEGE VKVVDFGIAK AADQATVTRS
GVLKGKYSYM SPEQAAGKRV DCRSDVFALG VVLYELLTGT RLFKRSTDMQ TLSAVAECQV
TPPSEVSPRV PADLDAIVLK ALARDPDTRY AEALQLQVAL EEWLRAHPSA SSQADLAAFM
QEVYAERLAR EARTGQVVVE EEAPALVQRS AGEGARRSGS GPSPSSKDVT RADRGEVVEA
VALEATARSP MRPSRPNRVA EVVPDPDETD RQRPERRTLT PRPVDVRRPE PTVSVQTRTD
QDAPSLSITD TTQPPSRSRP GLVSRWGWLM GLAAFLLVAG GTALLWVWLA PGLLPMPETA
QAAPVPTPAK PPPPQAVPQT PPPVWVQLTL ETKPSDATVF VDGQERQGPR PMVIQAMKDQ
ELEVKVMAPD YETAVRRVKV TASPSQLERF VLTRPLRTAP SAPVPAPIKT SRGGPLKPGE
PPATGRVRFN VTPWARVSCN ERPLGTTPML NEVTLPEGVY QCKFHNPELD RTESRSIEVK
ALTLNEVEVR F
//