ID A0A0D1ZKJ3_EXOME Unreviewed; 894 AA.
AC A0A0D1ZKJ3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Serine/threonine-protein kinase SCH9 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV10_02826 {ECO:0000313|EMBL:KIV95142.1};
OS Exophiala mesophila (Black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV95142.1, ECO:0000313|Proteomes:UP000054302};
RN [1] {ECO:0000313|EMBL:KIV95142.1, ECO:0000313|Proteomes:UP000054302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV95142.1,
RC ECO:0000313|Proteomes:UP000054302};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala mesophila CBS40295.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847521; KIV95142.1; -; Genomic_DNA.
DR RefSeq; XP_016226716.1; XM_016367198.1.
DR AlphaFoldDB; A0A0D1ZKJ3; -.
DR STRING; 212818.A0A0D1ZKJ3; -.
DR GeneID; 27320671; -.
DR VEuPathDB; FungiDB:PV10_02826; -.
DR OMA; SFVMMER; -.
DR OrthoDB; 10768at2759; -.
DR Proteomes; UP000054302; Unassembled WGS sequence.
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 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054302};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 311..472
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 507..768
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 769..853
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 536
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 894 AA; 98998 MW; B8E5F87A629CEF41 CRC64;
MAQTGVNSHH AADLLRQAMA QNSARQDARD DLHEQIGSGS PTPSGVETPR PDFHDKRLPG
IMSYFGQVGR DPSQNTPSRS SQVATYPEKD QETSFVSVES ERGIPASRSS SASSGSMVMV
EREPAAVPTP PPEDSLGEAV RSGSGTDASR LPPTPISSAA SVVHRDGEAA ENGSSVAEGG
IASITQALRN FVLPKTSAIG RKDRRHQSLP VSSVTKSTVS AAHISNPTST HSSQPHSPQI
SSENSAKRPP SQSEQESSVL TLGVADVPRD KSTPPQTPRA LSQEDRRDQN RSPLSSTSIP
AENPPVELES DQTRSRRSSL PSTTLPRGKL SIKIAEGRNI RPSIDPYVVC QFEWNEYVSK
GPKLDRMEVD GDNQKGPVAS LQSVPIRRTD SDMGKPMAIP MRSRQSSSTG EERPFEKVTD
PQWDHEATFD VVSPRSELDV TVYDRGSADA FLGHVRLCLN LTEQHPTLEG FFRLEPRVEE
DQDITGEIHI RMQFSKVDKR QFGPNDFSIL KLIGKGTFGQ VYQVRKKDTQ RIYAMKVLSK
KVIIQKKEIQ HTIGERNILV RTAMTDSPFI VGLKFSFQTP TDLYLVTDFM SGGELFWHLQ
KEGRFKEDRA KFYIAELIVA LKHLHDHDIV YRDLKPENIL LDANGHIALC DFGLSKANLS
QDDTTNTFCG TTEYLAPEVL LDEQGYTKMV DFWSLGVLVF EMCCGWSPFY AEDTQQMYKN
IAFGKVRFPR DALSTEGRNF VKGLLNRNPK HRLGATRDAQ ELIEHPFFAD IDWDALGKKN
LVPPFKPKLT SMADTSNFDP EFTNALNTSS SLNARAAALA AGAAPASTPL SPTMQNAFQG
FTFVDESTME ERFGGSREPD DDRFDEVNLT RSRTQEHRMS GVQRTGDDGF YFEE
//
