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Database: UniProt
Entry: A0A094ED19_9PEZI
LinkDB: A0A094ED19_9PEZI
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ID   A0A094ED19_9PEZI        Unreviewed;       646 AA.
AC   A0A094ED19;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE   Flags: Fragment;
GN   ORFNames=V498_09588 {ECO:0000313|EMBL:KFY76419.1};
OS   Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY76419.1, ECO:0000313|Proteomes:UP000029270};
RN   [1] {ECO:0000313|EMBL:KFY76419.1, ECO:0000313|Proteomes:UP000029270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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. STE Ser/Thr
CC       protein kinase family. COT1 subfamily. {ECO:0000256|ARBA:ARBA00038271}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFY76419.1}.
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DR   EMBL; JPKA01004158; KFY76419.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094ED19; -.
DR   HOGENOM; CLU_000288_67_4_1; -.
DR   Proteomes; UP000029270; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd21776; MobB_Sid2p-like; 1.
DR   CDD; cd05600; STKc_Sid2p_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR000961; AGC-kinase_C.
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; PTHR24356:SF417; CELL CYCLE PROTEIN KINASE DBF2-RELATED; 1.
DR   PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
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:0000256|ARBA:ARBA00022777};
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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          245..548
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          549..628
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          623..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         274
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFY76419.1"
SQ   SEQUENCE   646 AA;  72252 MW;  AC4BAA2C5D96D321 CRC64;
     ASFTTPTQTP QGSPSKNRNP PGAIDLPTAF DTALKLTPAA LDSPTKLSPG AGARPLSPGK
     GNAVVQGDES YFAQGGDESV LHKPAVMAGG GGGGREVPGS PTRRMGKENT SPVGRLGEFS
     AAGATLGQNP AAASRQEVYQ GRDQGGPTIR KYNTQRGLTA EELEILQKPN VKRLANVTQL
     YFLDYYFDLL TYVGTRQTRL NHFKAEYPAP PATAEETYDP LWHKYTGRER ANLRKRRVRL
     RQGDFQILTQ VGQGGYGQVF LAQKKDTREV CALKVMSKKL LFKLDEIRHV LTERDILTNA
     KSEWLVRLLY SFQDEQSIYL AMEYVPGGDF RTLLNNTGVL ANRHARFYIA EMFCSVDALH
     QLGYIHRDLK PENFLIDSTG HVKLTDFGLA AGFLAPGKIE SMRIKLEQVG ETSVPFGKPM
     EQRTVAERRE GYRSMRDKDV NYAKSIVGSP DYMAPEVLKG DEYEFSVDYW SLGCMLFEAL
     TGFPPFAGAT VDETWKNLKH WREVLKRPTW EDPNYFISNR TWNFITNLIA SKTKRFPNIQ
     SVYTHQYFAE VDWTTLRTQR APFVPELDSE TDAGYFDDFS NETDMAKYKE VHDKQAALES
     MADREGAMGK ALFVGFTFRH RKTPGEGGES PRKSILPDAG GFGTML
//
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