ID A9GT80_SORC5 Unreviewed; 1187 AA.
AC A9GT80;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=sce6743 {ECO:0000313|EMBL:CAN96912.1};
OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS ce56)).
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN96912.1, ECO:0000313|Proteomes:UP000002139};
RN [1] {ECO:0000313|EMBL:CAN96912.1, ECO:0000313|Proteomes:UP000002139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139};
RX PubMed=17965706; DOI=10.1038/nbt1354;
RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA Puehler A., Mueller R.;
RT "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL Nat. Biotechnol. 25:1281-1289(2007).
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; AM746676; CAN96912.1; -; Genomic_DNA.
DR AlphaFoldDB; A9GT80; -.
DR STRING; 448385.sce6743; -.
DR KEGG; scl:sce6743; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_266262_0_0_7; -.
DR OrthoDB; 5488986at2; -.
DR BioCyc; SCEL448385:SCE_RS49645-MONOMER; -.
DR Proteomes; UP000002139; 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; IPR030616; Aur-like.
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 PANTHER; PTHR24350:SF35; AURORA KINASE; 1.
DR PANTHER; PTHR24350; SERINE/THREONINE-PROTEIN KINASE IAL-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; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAN96912.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002139};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAN96912.1}.
FT DOMAIN 15..287
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 301..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1187 AA; 123824 MW; C5254B99708229D1 CRC64;
MSAPVSLGDV VAGRYRVERL LGQGGMGVVM AARHLHLGNQ VALKLLRRDA LVDAAARERF
LREGRAAAAL RGEHVARVFD LGFLDTGDPF LVFELLEGCD LGALLRAQGP PPIEVAVGYV
LQACEGLAEA HARGIVHRDL KPGNLFLARR ADGSQLVKVI DFGIAKHTLA PAPAAAGEQL
TSTFAVLGTA LYMAPEQMRS ARTADARSDI WALGAVLYRL LSGAPPFPGE SLLDICAAIQ
RGPAPLAAAR PGTPPALEAA VLRCLRQDPA ERPADVAALA AALAPFAPHA GQAAERVART
LRGGGGPAAP PAPRGQPSGE PAAAPPEMAS APAAPPLAER SPDTASGSAA GAAPTLSRAN
APPARTVSRA EAPEIKAHPP LIARQAALAA LAGAADQIAG GARFVVITGP LGIGRTRVLQ
AGIEAAGLPA ERVLRGGCSP ERQSPLRPLR RALDTLPPGG RAALAQLSDA VDRALAPAAL
PSAGDADSAL EGVEAALLRA AAEPLLLALD DLQWADPTTL RLLSLLAEQA ASGDPARLLV
LAAARNEPSP SPKLRALLGA VRSRIRPGIK HLALERLDEA DSERLAHAIA PLSPELAQTV
ARGSGGVPFF AVHALLAWRE TGAITWQDGV LQAASGRALH EQVPGVAELV EDRLASHFEP
GSDAERAGLR ALAAIALYGG GLGFEVLYRV VASDELLESA VHAWVEAGML TVSAEPPEIG
FGQEMVRQAV LGVARKRPWF PRLHRALLDA IAAGPGAAAD AAFLAAGYEK LGAVEPARAW
LQRAMDAAFA AGLFEEAAGL GDRLAALAGD PGERAAIELD IVRVLLRGRA FEDARQRLER
PGASALAPAS AAGLRRRIYR LEVARGLHEA GSGDESLLAD ADALGDERLR CEARMALAGV
TRGPRAMALA GEAVELAVRC GPGLELPARV LRFELDYEAD RCDLELADAD LKRALELSAA
SASVWRQIEI DGDLAVVEAE LGRLAAAIER LYGLAARAER YGMRAQRRLL LQNLAAFLLR
AGRAAEAAEV AGRSAALATE AGDPALRGVA LSLRAEALRR CGDAGAALRC ADEAVALQEK
RGDAMLSLTL VRRAELLAGM GRSAEALADA RAARRVAEQH RERDRVLCAD LWEALHLARR
GAAPPEEVAR ALAEAQAADV TLRELTMKLM EEARAWLEQR PAPAASG
//
