ID A0A0K1EGN6_CHOCO Unreviewed; 1690 AA.
AC A0A0K1EGN6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AKT40030.1};
GN ORFNames=CMC5_041830 {ECO:0000313|EMBL:AKT40030.1};
OS Chondromyces crocatus.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae;
OC Chondromyces.
OX NCBI_TaxID=52 {ECO:0000313|EMBL:AKT40030.1, ECO:0000313|Proteomes:UP000067626};
RN [1] {ECO:0000313|EMBL:AKT40030.1, ECO:0000313|Proteomes:UP000067626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cm c5 {ECO:0000313|EMBL:AKT40030.1,
RC ECO:0000313|Proteomes:UP000067626};
RA Zaburannyi N., Bunk B., Maier J., Overmann J., Mueller R.;
RT "Genome analysis of myxobacterium Chondromyces crocatus Cm c5 reveals a
RT high potential for natural compound synthesis and the genetic basis for the
RT loss of fruiting body formation.";
RL Submitted (JUL-2015) 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 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};
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DR EMBL; CP012159; AKT40030.1; -; Genomic_DNA.
DR STRING; 52.CMC5_041830; -.
DR KEGG; ccro:CMC5_041830; -.
DR PATRIC; fig|52.7.peg.4603; -.
DR OrthoDB; 5521237at2; -.
DR Proteomes; UP000067626; Chromosome.
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; cd07041; STAS_RsbR_RsbS_like; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.750.24; STAS domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF01740; STAS; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52091; SpoIIaa-like; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50801; STAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AKT40030.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000067626};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:AKT40030.1};
KW Transferase {ECO:0000313|EMBL:AKT40030.1}.
FT DOMAIN 7..266
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 528..600
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1564..1675
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT COILED 1524..1558
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1690 AA; 184151 MW; B1ED99212EC8613D CRC64;
MQQIAEFTLV EQIHESPEVF LCRGYRNEDR APVTLKLLKE EIQSPRAVAR LRHEYAILRD
LDIRGVVKSY GLVEHGQSCA LVLEDPGGEP LHHVLRRERL ELRTALELAS SLADTLAALH
ARKVIHKDLK PHNVLVSLST RTTKLIDFGI STRLSRETQS ARNPEALEGT LAYMSPEQTG
RTNRLLDQRS DLYSFGVMFY EMLTGSLPFP TTDALELVHS HIARKPTPPH EVVPKLPRVV
SDITMRLLAK AVEDRYQSAR GLHADLVECL ARLSPTGTIA PFPIAQHDRV GVLHLPQRLF
GREESLSTLE AAWRETISGT AGVALVRGPS GVGKSSLVAE LSQAVQRAGG VLVAGKFDQL
GSSTPYAPIA YALRELVRRV LAEPPATLAR WREALRAALG KNGRILTDRI PELELIIGPQ
EPVAALGPVE AQVRFQLLFQ SFLRLFTTRS RPLALFLDDL QWADAESLRL VEMMLSEPSG
RHLLLIGAYR DREVDADHPL NASLAALRRA GTRFVEITLQ PLDERRVGQL VGEALSCDPT
TVTSLVEVVW KRTEGNPFFV HRFLEALHEQ NLLTFDPRRG TWSCDAQHLQ DTIIVESVVA
LMAQKIQRLS PTSQQALKLA ACVGHEFDLH TLSVVYQRPV AETVADLGEA LCEGLIVPLG
DDYSLVDASR AGPSSRVVPT GVDVSYRFLH DRVQQAAYMM VPEGEKQQVH LSIGRLLLAA
SEGEPSQEGL FKIAEHLNRG LAHVTDPADR VMVARVNLDA GRRAKAAIVH QTATGYLRAG
IGLLDEARWE DEYELCYGLH AELAECGFLA GAQTEAEAAC EAAIEHARSI TDKAQLYSLR
TVLYTTVGKY EEALTAGWTA LSLFGVARPE GMAALGAEVQ GELIQVQALL SRRPIASLLD
APELTDPDRR LEMQILVDLM GASFFVDQLQ FTLVVAKMVS LSLRHGQMDL SAFAYMLYAV
VLGATGMLRE AYGFGKLGIE LCARWNSPRI EAKVLSSATT TTLTLFEPLQ LSLVRSARGL
QVALEAGDIL SYSYSAYMMV FNRAAMGEAL GAYRAGLADV QAFLVRVKNG PGADVVGLGR
QFAACLMGET KGRMSLSNDT FDEDALVATL DKPDAAVTAG WYHTLKVQLA VLYGDHELAL
AHAATAESLS AKATGCFFIT ELLFHANLAR AALARGGADV EALTGARAQL ATWAECCPDT
FLHKRLLVDA LVARASGDEL SAIDLFDQAV EAACKSGFVH HQALASELLA QLHLERGRKH
AAQVHLAAAH SAYLQWGATA KAQQLTERYG PSFAPWAGAP RPSSEAPATQ GRLSTSITIT
TTGDIRGTTL DMLTVFRAAQ AIAGEIELER VLERILRIVV ENTGAELGHL FLPHEDALVL
RTSMTVQADA VVQRASVPLE ATTDVPRSVV YYAVRTLEAV VLGDALKDAR FAADPHISAT
QPRSILCLPL LHQGKLSGVL HLAHHAATDV FTPARIELCQ VLCAQAAIAV ENALLVGRVQ
ASTVALQRLN SALETEIGQR TEELRASNAQ LVLELREREH AERERTRLQE EIIRAQGERL
SEMSTPLIPI TDRIMVMPLI GTLDRARVRQ VLEAALEGAQ ARAASVVILD ITGVRDVDTE
VANSLLKTAA ALRLLGAQVV LTGMRPEVAR TVVSLNIDLR GIVIRGTLQS AILHAIRLSG
EAAQVRRVLA
//