ID A0A2L0F6P4_SORCE Unreviewed; 1347 AA.
AC A0A2L0F6P4;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Protein kinase {ECO:0000313|EMBL:AUX47202.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:AUX47202.1};
GN ORFNames=SOCE26_087140 {ECO:0000313|EMBL:AUX47202.1};
OS Sorangium cellulosum (Polyangium cellulosum).
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=56 {ECO:0000313|EMBL:AUX47202.1, ECO:0000313|Proteomes:UP000238348};
RN [1] {ECO:0000313|EMBL:AUX47202.1, ECO:0000313|Proteomes:UP000238348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce26 {ECO:0000313|EMBL:AUX47202.1,
RC ECO:0000313|Proteomes:UP000238348};
RA Zaburannyi N., Bunk B., Overmann J., Mueller R.;
RT "Sorangium comparison.";
RL Submitted (SEP-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};
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; CP012673; AUX47202.1; -; Genomic_DNA.
DR OrthoDB; 5497887at2; -.
DR Proteomes; UP000238348; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
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 PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF17874; TPR_MalT; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 2.
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:AUX47202.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transferase {ECO:0000313|EMBL:AUX47202.1}.
FT DOMAIN 47..309
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 310..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1347 AA; 143719 MW; 1EE6AD17F0D010C7 CRC64;
MPRCPVCHRR VTGTTPCPRD AWLPSPSRTF DAAHAALEPA PPSLPGLTLV RPVGAGGFAT
VWEAARAEGG DAVALKVARW TSPLTTERFR RDAEALAHVG PPHVPRLHES GTLGDGRPYI
AMELVRGRTL AEELAELEEP PSAADVVATS EAILEALAAA HAKSVIHRDL KPENLLITEG
ERRVVLLDFG LTKHARAPEE EGITPRGTVA GTPEYMAPEQ LRGDPVQDER TDIYAFGVIL
YELMTLRLPF SGDRSAVEHG HLALRPPRPH EFAAVPEELE RLALACLAKE PERRPPDVDA
LRRALRRALA RSCPSDAPPT PPASPPRGAL LTEGRQPAIV LVAEAKSASA AVMSAVVARK
GFVARQRGTR LVCVFSGVDA DDPVSAAIAV AREVEERYAG RAALHLAGLI VRRKGQGPPA
VYGAPVEQPD AWMPPDGWGG VVLTVDLVRA LPQGELRGAT RDPALSRSAG RAFYRLAAAP
PALSDPSRAA RGAPLVGRGE VLGALAVSMD ASMSGACPGL FTLIGEGGLG KSRLADEAAA
LVRRMQGRAQ LIALRAAQPL AGERASIELL ARVLDATPGA PPEDPRAFCA ARLGEELAEE
TWRAVAAALG WTPAEEIPAS PWSLRQSTMR AIAGGLRRRA REAPVAVILD DAHWADDAAL
DALEYATLDA PGCALWVLVA AHPRFEEMRR GWGARAERHD RAVLGRLSEQ DTMRLAAELL
RPAEYPPEAA LRQLAGWAGH NPSSLAELVR ALKRAGAVQQ HPTGAFYVAT AALDQLPTLP
VWQWLAARRL DALSPELAAC VRLCSVLGPD VTREEVEEIQ DAIEQAGGAS TPIDAGVGLS
ALASIGLLVR SERGIYAFEN ATFRDAVYDG LAPAQRQTIH AHAFAWWRAR VDPLAPDRRG
LVHLARHAAA CGERAQAAAA HLALGDRATA SHDNVEADQR YTAALALLDA GDARPRALAL
AGRAKARYSL HRISEALADL ELARGLAGEL GDDRLAAELL LEEATALDHA TDFAGSARRA
DDARAIIERL GDPRLEDRLL MALGRSRWRQ QQVAEAIGLL DRASAGAAAG GDRETRVIAL
LLLSIALVIS GRLSDAEARF CEVIALSKEM NDRLHLCSAY ANRAYLWAAL SAPERGLEDL
SRAVELAREI GNPGPEHVAT HNLAELLHWC GRADEALALA RRSRVLEERF GGRDAPDDAL
LLARVQAARG DLGEAGRLVA WIDARCRPDP SSPAVYALFR TMKLVLAAAG IRSAAAVGAE
EDSWEALTEL AERTLPVEEL LEVLYFRARV AASAGRHAEA RAALDRARPA LAGCRMWQPR
FGAVAALLPS PNEPAGGAHP CAPGEPE
//
