ID S4XMV5_SORCE Unreviewed; 1271 AA.
AC S4XMV5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=SCE1572_04985 {ECO:0000313|EMBL:AGP33904.1};
OS Sorangium cellulosum So0157-2.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP33904.1, ECO:0000313|Proteomes:UP000014803};
RN [1] {ECO:0000313|EMBL:AGP33904.1, ECO:0000313|Proteomes:UP000014803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So0157-2 {ECO:0000313|EMBL:AGP33904.1,
RC ECO:0000313|Proteomes:UP000014803};
RX PubMed=23812535; DOI=10.1038/srep02101;
RA Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G.,
RA Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.;
RT "Extraordinary expansion of a Sorangium cellulosum genome from an alkaline
RT milieu.";
RL Sci. Rep. 3:2101-2101(2013).
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; CP003969; AGP33904.1; -; Genomic_DNA.
DR AlphaFoldDB; S4XMV5; -.
DR STRING; 1254432.SCE1572_04985; -.
DR KEGG; scu:SCE1572_04985; -.
DR PATRIC; fig|1254432.3.peg.1113; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2114; Bacteria.
DR eggNOG; COG2909; Bacteria.
DR HOGENOM; CLU_006367_0_0_7; -.
DR OrthoDB; 9758570at2; -.
DR Proteomes; UP000014803; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR045269; Atg1-like.
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; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
FT DOMAIN 1..249
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 1271 AA; 137347 MW; 03B09672350715B0 CRC64;
MGEVWKAHDQ ETREAVAVKL SPQRDAEEAA RFEREAQILA GMSHPHVVRY VAHGACADGM
PYLVMEWLEG EDLAARLARG PLEIDESVAL ATTVADILGF AHERGVVHRD LKPSNLFLPG
RRLDGVKVLD FGIARLGQAA RMTRPGVLIG TPGYMAPEQA RGEASIDARA DVFSLGCVLF
ECLTGRPAFG GQHVAAILTK VLFEETPRLQ TLRTGVPEAL DDLLRSMLSK RREERPLGGH
AAAAALRALE DASRSPAVSS VRSPSLTISE QRAVAVIVVS AAADAEVRAF GGDTTLIISP
GDEAVLREAE AHGGRSERLL DGSVVVMLAG TETATDLCAQ AARCALALRR CAAGRRVALA
MGRGERTARS MGPAIDRAAR LASTTARHVA PEGAVIVDEV VAGLLDARFE VREGEGVITL
RGERPLAEGT RLLLGRVTPC VGRELELGML RALVLESVEE STAQAALVTA PPGVGKSRLA
QEFLQEIRGQ GAGVSVWAVR GDALRAGSPL GMLGQALRSA CGIHEGEPVE VRRRKLSAEI
EARVPPGHRR RVEEFLGEIV GAAFPDEDSL PLRAARRDAQ RMADQVRAAF LDYLAAIVAG
GPLIVVLEDL HWGDRPTVSL LDAALRDLSD RPLFVLALAR PEVRELFPRL WEGRRLHELR
LNELSRRAGE RLARHVLGER ADADAIARIV RLSEGNAFYL EELIRWTAEG RGPDVPGTVV
AMVESRLGAL DDEARRLLRA ASVFGDVCWA GGVAALVGGE ARRSHVTAGL DALVALEILV
RRRESRFPAE EELSFRHALL REGAYAMLTE GDRVLGHRLA GEWLERAGEP DPVVLAEHLQ
RGRALDQAAC HYLRAGRQSC DRGDFASALA RAQRGVDCGV HGETLGNLMA LRAMAHCWRS
EFDAAQQASA AALPLTGRGS RWACIALFHR AWASLVLDAE DDFMETADRF VQFQPDAEAG
REYMLWAPLA ASLLQTYGRR ELCKALLDRA DALAAALPAL DLDLRGALAI GRSDYVRAFE
RDPWRQLQLT RQAVEAFQAI EDLRNQITAL NRLGQAEAEL GDPEAGEATL RRAVALAQRI
AIPFAQRQSA LHLAALLSRG SDPSKWGEAS DMARSLLGAA GVSVGYRGWA HGICAEVLLQ
RGSYEDAVRQ AREADALCAR IPLRRLWVTA LLVRGLIQLG DRDEAARVAS RIEPGLACLG
GGGYVEIDAR VALAEAYWTG GRQDEARAAL DEAIRGIAAR VEAIPDAAWR ARYTACVPEI
ARARRLASAW A
//