ID A0A178E4V8_9PLEO Unreviewed; 1614 AA.
AC A0A178E4V8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=IQ07DRAFT_507713 {ECO:0000313|EMBL:OAL50998.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL50998.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL50998.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL50998.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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 ---------------------------------------------------------------------------
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; KV441643; OAL50998.1; -; Genomic_DNA.
DR STRING; 765867.A0A178E4V8; -.
DR InParanoid; A0A178E4V8; -.
DR OrthoDB; 8734at2759; -.
DR Proteomes; UP000077535; 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; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000660-
KW 2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OAL50998.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 49..157
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 278..532
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 579..951
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1460..1486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..675
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..720
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 807
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT BINDING 585..593
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 608
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 609
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1614 AA; 181640 MW; 060F67A12B1E5998 CRC64;
MAPHKTPRNK KHHQNVSKPN GNHAAGVPSP VEDSLPVGHS ETYEKAQEDE REVLKAVFMD
DYEEVEAKGA WSKTTDRVLR LKLRSFSNDD ISVTLCAKLT ATYPRTLPTL TLEDGSSLRK
STWDKLRKLL NTRPKELLGE VMIHEIATAI QDILEDEIAV RENDGAFENL DAERAGQEAE
AAELAKQQEE ELQKKRDEAK AEEERVLQQM VSDEMRRKDL MAKRKNRASG ITPTSYFPST
ANTNIVSFDR SIPLQQGDTI VDCSAVEGLL SFRTGPVTEE LLVKPVGSKI PITMVLKRAS
VGSGSFTAGP QLKKAIMDFE EEMEDIKRIR HLAIMAVYDF KIEHLADSGW EINILMEHAN
KGSLGEKLED DGHIAVTKVR SWTIELLEAL DFYHRNGIIH KRIHPGNILF KKSPSGSVTV
NLADAGFQES LHRLQDICKG EPAASTSRSA FWVAAELAQD SRRTRKTDVW DLGVVFLQML
FGLDAPQKYN SPKDLSDSVG CSDPLQEIMR KFFKPDPKKR PSAFDLIPCE FLRDDVPVYA
QPPTPLRSRH SSTSFGHYKL RRESSTGIGP SYSRYATDWV EQGRLGKGGY GEVVKARNKV
DGSIYAIKKI KQKSAAALTE VLSEVMLLSR LNHSCVVRYY TAWPEEDVFG SSGGEEDGST
TFDGDDSESS SEMTQEETDD VGFSKSTGGL DFISSSGYPK IEFGSDAESE EEDDGAVVFG
SDSEDETGTA SAGPHSPMIK RRKRSNSIPT RASRSILYIQ MEFCEKQTLR DLIRRDLYDD
PDEYWRLFRQ ILEGLAHIHG HGIIHRDLKP DNIFIDFAKI PKIGDFGLAT SGQYQRPDKK
VSAGIQDGDM TRSVGTALYV APELSSNVTG NYNDKVDMYS MGIIFFEMCF PLKTAMERDK
VVRSLRERKH DLPKDFETPE KSLQGSIITS LISHRPSERP SCTELLRSGK VPVQIEDEAV
KEALKALSDR NSPHYAKMMA ALFSQKPDTQ AKDHAWDMGV TSQTIKANDV LLQNLVKDRL
AMVFRSHGAV EVQRPLLLPW SDHYANSKAV KLFDPSGTLV QLPYDLTLPY ARSIGRGASF
LEKTFTIGQV YRDNYGGAPR SSGEADFDIL SYDTLDLALK EAEVIKVVDE IVDEFPCFGT
SSMCFHLNHS DLLEMIMEFC RVSAPQRPAV KTVLSRLNIA KNNWQTIRNE LRSSEIGISS
TSLDDLARFD WRDTPEKAFS KLRRIFEGTK YLDRTHAIFA HLTSVVHYMK LWNVKRKVYI
SVLSSFNEKF YAGGILFQCL FDVKQREVLA AGGRYDKLIE EYRPRRPGHN QINTGYHAVG
VNLGWDRLAN AMNRYLKKPE RSAFLKKHAE EDTSSISWMP RRCDCLVASF DSNVLRSTGV
KMVSELISHG YTAELAVDAH SVEDILRHYR DDRHSWVIVI KHGLAPDKPE LKVKSIAKKE
DTDLRTGDLL NYLRNELRDR EGREGSAAQR LMRSTTAPSA STATASKSNV DVLIAQHRSK
KSNKWAIVEA AQARSTELLS VFQFAPIAAI ESKEEVMNLI KETRLSDPDS WRHAIQKMPI
AERKYLQEVH DLLLKYKTRW ETMRNEEGKG SGDVGKAFVY NFRTGGCVLY DLES
//
