ID E6ZL11_SPORE Unreviewed; 749 AA.
AC E6ZL11;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Probable SCH9-serine/threonine protein kinase involved in stress response and nutrient-sensing signaling pathway {ECO:0000313|EMBL:CBQ68014.1};
GN ORFNames=sr11880 {ECO:0000313|EMBL:CBQ68014.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ68014.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ68014.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
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DR EMBL; FQ311430; CBQ68014.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZL11; -.
DR EnsemblFungi; CBQ68014; CBQ68014; sr11880.
DR VEuPathDB; FungiDB:sr11880; -.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_52_3_1; -.
DR OrthoDB; 10768at2759; -.
DR Proteomes; UP000008867; Chromosome 1.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:1904828; P:positive regulation of hydrogen sulfide biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0060963; P:positive regulation of ribosomal protein gene transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IEA:EnsemblFungi.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IEA:EnsemblFungi.
DR GO; GO:1901494; P:regulation of cysteine metabolic process; IEA:EnsemblFungi.
DR GO; GO:0032880; P:regulation of protein localization; IEA:EnsemblFungi.
DR GO; GO:0047484; P:regulation of response to osmotic stress; IEA:EnsemblFungi.
DR GO; GO:0090153; P:regulation of sphingolipid biosynthetic process; IEA:EnsemblFungi.
DR CDD; cd11651; YPK1_N_like; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351:SF245; AGC_AKT PROTEIN KINASE SCK2; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 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:CBQ68014.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:CBQ68014.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 140..293
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 326..585
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 586..699
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 749 AA; 82078 MW; DDC757A38678EFF0 CRC64;
MASNMLRGLW PSGPADQTTP KASSSHSNGA AERNPFDNMH PPAMTKQSSR SSLTSSIISN
HLPGDVTPGL RTPGGIASQS AIPTTSISLS DPDFTMKLPP AKPKHDAANA APVQSTSNGV
PPGSAVAASA SSSNGAVASV SSGSSTSKTR NTNAPRGHLT VKIVSGRNLA VSSPAARPYA
VVQFDKNEFI GREPIDEFGE EAKGFAQPRS EAGEAGRSRA KTVTPADALA RTGHNHNPVW
KHEVTFDVTQ DSQPIYISVY DRHSEDEGFL GMREIKPRLV HKMMSDQWYP LSSRDDEEGM
DNHRGEIRVQ ISYERMPQKK LTPHDFEYLK LIGRGTFGRV FQVRKKDTKR IYAMKVLSKR
EIALKKEVTH TMGERKILEK SLDCPFLVGL KFSFQSATEL YFVTDYKSGG ELFWHLQREG
RFTEERARFY IAELVLALEH LHKYNIVYRD LKPENILLDA TGHVALCDFG LSKPDLGAGQ
LTNTFCGTTE YLAPEVLLDE SGYSKLVDFW SLGVLLFEMC CGWSPFYAED TQQMYRNICF
GKIKFPRGAI GDDGKQFVKG LLNRNPRHRL GAARDAQDLK EHPFFKDIDF DALAKKQLTP
PFKPLVESDE SVANFDPEFT ETDLKDVAVI PGFEGSSTDA ANALQNGDIL SEKDANGKGV
AIRKGRGGED EDDQLLTRSI QDKFRGFSYS GTYEGSLAGS FGGRRGSAGF GLAGASLGMS
RMGVTDDEAM DADVAALESL DADEVMQSR
//
