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Database: UniProt
Entry: A0A0N1HL91_9EURO
LinkDB: A0A0N1HL91_9EURO
Original site: A0A0N1HL91_9EURO 
ID   A0A0N1HL91_9EURO        Unreviewed;       648 AA.
AC   A0A0N1HL91;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=AB675_134 {ECO:0000313|EMBL:KPI37714.1};
OS   Phialophora attinorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI37714.1, ECO:0000313|Proteomes:UP000038010};
RN   [1] {ECO:0000313|EMBL:KPI37714.1, ECO:0000313|Proteomes:UP000038010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI37714.1,
RC   ECO:0000313|Proteomes:UP000038010};
RA   Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA   de Vries M., Cruz L.M., Souza E.M.;
RT   "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT   131958.";
RL   Submitted (JUN-2015) 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:KPI37714.1}.
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DR   EMBL; LFJN01000022; KPI37714.1; -; Genomic_DNA.
DR   RefSeq; XP_017997677.1; XM_018141231.1.
DR   AlphaFoldDB; A0A0N1HL91; -.
DR   STRING; 1664694.A0A0N1HL91; -.
DR   GeneID; 28733100; -.
DR   OrthoDB; 10768at2759; -.
DR   Proteomes; UP000038010; 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; cd05600; STKc_Sid2p_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KPI37714.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000038010};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          244..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..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          623..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         273
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   648 AA;  73883 MW;  6AFDF017D5D9C4B1 CRC64;
     MAVTPLSPRS QQAQNMAMPM PPPLLHTRSG NEAYDRPSTP NSNAFVSPSQ TPVGSPSKKQ
     LPPGSTDLPN VFDNALKLAP SSPTKGPISP NKLALADDSM LRQDYNDPFG RSESPTRQSN
     KENTPAGDGK AVQSHAAMSR RGQYETVDSR RNIPTRGLTP EELQKLQNPK MKRLANVTQL
     YFLDHYYDLL TYVHNRQVRD DLFREAYPAD STTPQEREAA FSKHLGKERA GLRKRRTRLR
     HGDFQILTQV GQGGYGQVYL AQKKDTREVC ALKVMRKKLL FKLDEIRHIL TERDILTAAK
     SEWLVKLLYS FQDDEQIYLA MEYVPGGDFR TLLNNTGVLH NRHARFYIAE MFECVDALHT
     LGYIHRDLKP ENFLIDATGH VKLTDFGLAA GMLSPIKIES MRVKLEEVGN TPVPFGLPPP
     EERTAEQRRE GYRSLRRKDM NYAKSIVGSP DYMAPEVLKG EQYDSTVDYW SLGCMLFEAL
     AGYPPFAGAT VDETWQNLKR WQRVLRKPVY DDPNYFLSKR TWDLITRLVA GKENRFKNIG
     EIHKHEYFAE VDWAGLREQK APFVPELDSD TDAGYFDDFS NEADMAKYKE VHDKQRALED
     MAERDEKMNK NLFVGFTFRH RKPNVDGEGK PESPRKAIAT DGTFGTMF
//
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