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Database: UniProt
Entry: A0A0D2DSN0_9EURO
LinkDB: A0A0D2DSN0_9EURO
Original site: A0A0D2DSN0_9EURO 
ID   A0A0D2DSN0_9EURO        Unreviewed;      1478 AA.
AC   A0A0D2DSN0;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=PV06_09610 {ECO:0000313|EMBL:KIW38659.1};
OS   Exophiala oligosperma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW38659.1, ECO:0000313|Proteomes:UP000053342};
RN   [1] {ECO:0000313|EMBL:KIW38659.1, ECO:0000313|Proteomes:UP000053342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW38659.1,
RC   ECO:0000313|Proteomes:UP000053342};
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 oligosperma CBS72588.";
RL   Submitted (JAN-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. Ser/Thr protein
CC       kinase family. GCN2 subfamily. {ECO:0000256|ARBA:ARBA00037982}.
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DR   EMBL; KN847341; KIW38659.1; -; Genomic_DNA.
DR   RefSeq; XP_016258875.1; XM_016411068.1.
DR   STRING; 215243.A0A0D2DSN0; -.
DR   GeneID; 27361684; -.
DR   VEuPathDB; FungiDB:PV06_09610; -.
DR   HOGENOM; CLU_001222_2_0_1; -.
DR   OrthoDB; 8734at2759; -.
DR   Proteomes; UP000053342; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IEA:InterPro.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR016255; Gcn2.
DR   InterPro; IPR041715; HisRS-like_core.
DR   InterPro; IPR024435; HisRS-related_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR006575; RWD-domain.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR11042:SF136; EIF-2-ALPHA KINASE GCN2; 1.
DR   PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR   Pfam; PF12745; HGTP_anticodon2; 1.
DR   Pfam; PF00069; Pkinase; 3.
DR   Pfam; PF05773; RWD; 1.
DR   Pfam; PF13393; tRNA-synt_His; 1.
DR   PIRSF; PIRSF000660; Ser/Thr_PK_GCN2; 2.
DR   SMART; SM00591; RWD; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50908; RWD; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000660-
KW   2}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000660-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053342};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          47..156
FT                   /note="RWD"
FT                   /evidence="ECO:0000259|PROSITE:PS50908"
FT   DOMAIN          215..531
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          568..986
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          677..776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1353..1372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        707..733
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        744..776
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        831
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT   BINDING         574..582
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT   BINDING         597
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT   BINDING         598
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1478 AA;  167846 MW;  56DC18F04634F590 CRC64;
     MPTKKKTKPL AVQTPIPDPP TPNPPSFGRS HRGLEEEIAD YPEIQRNEFL TTRAIYPDEF
     ERVRGRKDAW QRYENLAFQV RIGPLESPDY FAKLIFEFPR EYPKVRPKIN ILDVQPKDPA
     IRKRIEQITA DYPRQHQGNE CVYEVTSAIM DFLTEINLDK AAKKNEFSLE EERAAKEART
     KKQQESVRRR QEEETEKQEL LFESKVENEK QRRLKTITRK ITGDENADFY DAPEEPIRFD
     QSMTSRDIVT STPFKFKAVT GRSVILKRPD KKVLIVAPRV DIDRVQAPRF LLKMIYLPET
     IAPKAKLQKC MEVVEQDLES SKEHRHPNVV DLINYKIELM DLGQDVGQWN LTILSEFAEQ
     GSLSDLLDIV GALSAARIRS WARQLADALL FFDQQGYVHP AVHAGNVMLF RSASGGVTVK
     LADGYGTQLR DLVRAAQSLS EPSEQDLPLW IPPELNSTPP RRSNKTCIWD LGIIIMQMAV
     EKNVKETYTS PYQVIAGCGF GTNATRLLTA MFQSETGKRP TAFELTRKAF FTEEREPIFR
     NTYPETPGTP SRRRRYSDRF VSRYHNDFEE VERIGKGGFG NVYRARLKLD GQFYAVKKIE
     STSERELEGI LAEVTLLARL NHPYVVRYYN SWVEREDAEY IEESPQPRVP DRSLQQAPAI
     STGHDFLEVS VYRNQGAEYS SSDDDGNMFG YQEPPSLDEQ EGYEDDNDPF KTDPESSRPD
     EAQAKEEEPE SDPFSVRIPT SPGFMGSYDN NPFENSTESP SNSIAPTRSR TPLRQKQKST
     LYIQMELCEG KTLWNRMKEG LSQDVPAVWR LFRRIVEGLA YIHAQSIVHR DLKPENIFLD
     AHDNPKIGDF GLATAGQTVS KPNVSKPGMT ITDSWGVGTK GYTAPELLER GKKYDARADM
     YSLGIMFFEM CYPIPTQYEK NILLQGLAKQ PPQLPAFFEE DIHQTQGEII SQLVNIDQQF
     RPTARELLDS GKIPEPLEEE KFQRFIDRLA EQNPEEYQDL IGKLFSKPND PVSSLAWEDR
     SGESMVPVDP MLWISVTDQL KVIFRRHGAI EAPRQGIIPK TGFTPNPAVF LDPSGLTVQL
     PEDLTLPFAR TLGQIPCNLA KTYCFGAVYR ATVPGNQPRQ VPEVDFDFVS QSARDLSLKE
     AEVIKVMDEI LHEFPALAAR EWTIYLTHAD LIDIVLDFCR IKSHDVPQVK QALSYLSTGD
     GKWEKVRERL RSTAINIAET SVTDLSKFNV VGDVERVRTK FSQLFGQGDH LNKALSLFAR
     LDELVHVLRQ MSIQTQVLVA PLRNNAEHLY RGSVLFQCME KSHRKLLAVG GRYDSLIQEF
     QTKSDKGSTR AVGFRLNILD LLAYVRGQSK AQQQQHHHKT GRYAGGGAGG GGGAETKTVP
     RYGDVLVTSF DPNTLKSVCV EVVSSLWAAG LSAELSEEFR SLEELERAYR VEGANYWLVI
     VRGGADRGMK VRSPTRAEHE VKLAELVGFL RLNMAKNK
//
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