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
//