ID A0A1B8E3W7_9PEZI Unreviewed; 1601 AA.
AC A0A1B8E3W7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=VE03_03249 {ECO:0000313|EMBL:OBT66063.1};
OS Pseudogymnoascus sp. 23342-1-I1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1524831 {ECO:0000313|EMBL:OBT66063.1, ECO:0000313|Proteomes:UP000091879};
RN [1] {ECO:0000313|EMBL:OBT66063.1, ECO:0000313|Proteomes:UP000091879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=23342-1-I1 {ECO:0000313|EMBL:OBT66063.1,
RC ECO:0000313|Proteomes:UP000091879};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000091879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=23342-1-I1 {ECO:0000313|Proteomes:UP000091879};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV454998; OBT66063.1; -; Genomic_DNA.
DR STRING; 1524831.A0A1B8E3W7; -.
DR OrthoDB; 8734at2759; -.
DR Proteomes; UP000091879; 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 CDD; cd14012; PK_eIF2AK_GCN2_rpt1; 1.
DR CDD; cd14046; STKc_EIF2AK4_GCN2_rpt2; 1.
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_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
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; 1.
DR SMART; SM00591; RWD; 1.
DR SMART; SM00220; S_TKc; 2.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000660-
KW 2}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OBT66063.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000091879};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 46..157
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 272..545
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 593..962
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 176..207
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 308..335
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 674..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..735
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 821
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT BINDING 599..607
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 622
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 623
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1601 AA; 179344 MW; 9DEE8DC4A3667A11 CRC64;
MAPTYPWGGS KPKQTTKLND RSFPSLKDTE ANKPAPESEY NQVQEDELLV LGAIYGDDFE
REDTKPGAWK KLEPSFNIRI TSSTEGLSVS LHVVFTATYP KSAPLLTLKF GDSLREGTKF
KLQKVVETKA AQMAAERPME PMIHEIGEAL KETLDGAAEA EAAGREIPSL EEERAMHEAA
VALKVAKEEE EQAAREKAAQ IAEEERLTAD AQVLVARYEK NTKDSRRKSK APVAYEDQIV
DEDLEAMRAV VAFEEPIKLV DDFGNERTFQ AVTSYYRIRQ GPVSECFTAR PVLKGDPIQL
LVLKKTTIRS SENKKSEFRA QLAGLEREIS TLMKIDRDNI LRIYAYKLTK ESGTNAASDG
LWTVSILTEY GNKGSLEECL DISGSLMAER VKSWAMALLD ALTYLHSQGI THRNLHASNV
LLVRSPLGVV SPKIADVGFQ HRLHTLKNAT TVGKLELARS VYWVQPENVN SERPQYTDKT
DIWDFGIIFL QMIWGLGVMR EFSAPQRIPE EQVVSRPLED MIRKLFSSDP KKRPRASDLK
MSTFLTTTEG TDDEVSMPLP KSGSSAALNS FSARRSSKVD HRPLHFSRYH EDFIQEGRLG
KGGFGEVLKA RKKLDGQFYA VKKITQKSSS SLEEIIKEVQ FLSALRHPYI VQYHNSWTEI
IPDTGDADDD TELDSSTAGG TTGPSPPDNG LTIEFGTSTG GLDFISSSRY IEFDDDDDAD
TASDDDEEAI IDDEDESSSL SVPAIQHRNR RQLALTRTRS DSRPGGITVL YIQMEYCEGK
TLRDVIKRGS LLDNVDEIWR LFRQLLEALK YLHGNNVVHR DLKPENVFID GASNIRLGDF
GLATSGQYTI PETLSSTQGT HDMTTNIGTA SYVAPEVMLG ADYTSKVDLY SLGIILFEMC
YHPIVGMERA EVLKELRNPK TILPNDFQTD KKGHFGDIIL SLLNHDPEVR PSSSSLLDSG
KLPVQMGSEA IQLALASLQD PKSPYYPKMM AALYSRPTDQ AKDLAWDMSN KKPPAPADSI
MRTHVKEQLI SVFRLHGALE VPRPIMFPRS SYYASDAVQL LEPGGTLVQL RYDLTLPFAR
SIAKNPPRMQ NSYAFGDVFR DKSGGQPLSF GEVNFDIVSD SLDLALKEAE VIKVLDEIIA
SFPCMANVPM CFQLNHSDIL NLIFDHCGVD VGCRLSATET LSKLHVSQWT WSRIKTDLRS
NGLSAASIDE LSSFDFRDSP DRVFQKLKTL LDGTEAFNRA SPAIAHLKDV VKYINRFGVT
SKIFITPLGS IRERFYKGGM LFSCLYDRDK KEVFAAGGRY DSLVREFLPK TVRQPEVCHA
VGFNFAWENL AQSMFSYHQK SLKKQSKKPA IELRGIWTGK RCDVLVSSFD GQVLRSEGVS
LMNELWRNQI SAELAGDARS PEDLMSKYKD DDHFWIVTIK QDSMVKIKTM GRKDVEDVDM
AESQVVSWLR GQIRDRDHRE GQNLNKMARR TSHNDGPVGP HLKQQVHILT TGTKAKKAAL
KNTIQNQAQV AAAKLVEGFL EGQVLAIETT DDVLFKIKET PLSDPDKWKQ LAQSVGAGEK
RYIQQIEDHL RGLLANRRGE RRNAFLYNSR TSSIIYYDVS I
//
