ID W7LVF6_GIBM7 Unreviewed; 1504 AA.
AC W7LVF6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=FVEG_04803 {ECO:0000313|EMBL:EWG43248.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG43248.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG43248.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
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};
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DR EMBL; DS022246; EWG43248.1; -; Genomic_DNA.
DR RefSeq; XP_018749439.1; XM_018892704.1.
DR GeneID; 30062840; -.
DR VEuPathDB; FungiDB:FVEG_04803; -.
DR OrthoDB; 8734at2759; -.
DR Proteomes; UP000009096; Chromosome 4.
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 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 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; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF000660; Ser/Thr_PK_GCN2; 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 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:EWG43248.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000009096};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..60
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 170..446
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 495..863
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 66..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..632
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 717
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT BINDING 501..509
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 525
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1504 AA; 169516 MW; 2D703FFEA3A5A2F0 CRC64;
MTATYPKSPP IITMKNYDLK EVTTFKIQKY LETKPKLFAQ DAQEMIDQIV EGVRDILEDA
AQAKANGKHL PSLEEERERH EASLAKLAEE EKEGAARKRR EEKQEEERAM ALTLQQHIYQ
NKQQAMESNR RPSNTPQQSS TSSEAEEIIE FEQLCNATDQ SGNTLFFKSV TSKRHLRQGP
VSTIYEVRPL LNNGLGNLPM ALKQTVIRTT NKDPKKFSLQ VQNLESRLMD LKSVKQFHHP
HLVQVLGFKV QDSPMDPAIA DTCTISILLP WADWGSLQEL LELSTPGIGK VRSWTRDLLD
ALHFLHDKKL VHGDIHSGNI LLFRESNGQT VPKISDAWYQ SEIHSISSNK PGRLQQKTGK
SAYWLPPEIA GRSNPVYTSK TDIWDFGVVF VQMIFGFNVQ QTFTSPKILM ESFALSLPLK
ELLSKFFKED EQERPRAYVF GPSEFLATDA RILLENSPAA PSTNPSVLPP DFGERDLLNL
TARQRSSRSR YEDDFIEEAK LGKGGFGEVV KARMKLDGQV YAIKKIKTRS ETNLDELIKE
VQLLSRLNHP AVVRYNNTWV ERLPGHSDTE DCTSTSDPSE EDSEGNLSAD IEFESTNNTG
GLDFMSSNAN VVYGDDDSDG SEDDETEEEA GSEDGMFDHN ELSSVDGGTN ARVSRLARSR
RSIITTLYIA MEYCEKRTLR DIIARDLYKD TLAIWHLFSQ IVEGLAHIHG LGIVHRDLKP
ENIFITSSPD RIGNVKIGDF GLAIRGQFSV ERANENGMEP DDMTRSIGTA YYSAPEIRST
VHGIYNTKVD MYSLGIIFFE MCYHPMLGME KDTVLGQLRQ PKPVLPLDFK PSDNSQTNVV
LSLVNHNPNE RPSSTNLLED KELPIQLETR KGKRALTMLT NPRSSHYHEV ISRLFSVPME
PIKDFAWDMS VKTLSPQELH KQGLVKQELI SIFRLHGALE TPQSSIHPRS PHYGDNAFQL
LDSKGNLLQL PYDLTLGKAR MMAKRSNDPI AERTYTFGNV FRDKNDGGHP LMIGEADFDI
FTTQTSDLSF DDAEVLKVMD EIVHAFPSLS TTPMCFHLGH SDLLQLIFDY CGVQPSSRPA
AADVLSKLNV RGHNWQKIKA ELRSQSVNVF SMSVSDLQKF DFRDTPNKTF SRLKTLFEGS
DMYQRASPTI AHLKEVIEYC KRLGVGTKIY INPLNSFRES FYKGGILISC LYDTKAKEVF
AAGGRYDQLI KECRPSVGGQ IGNKHAVGIS LAWERLAKIP KAGGRSFLKK PEDESSGIFN
SRRCDCLVAS FDAAVLRSSG AEMLQTLWAN NISAELADNA GSLEDLLSKH DEEEYSWLII
IKQDAMLKIK SLGRKDVPDT DIPTTQLLSW LRNEFRDRDS RTVVKLRGNS SADTNGPGEK
EEQEVRVLVA QTRSKKFNRR TVVEQAQSTA SSLVQSFLDG PILAIETTDQ VMDLIRGTCL
SEVDGWRQVE QSVTNTERKY IREIHDELDN LRFKYQKKGG GDGSRHAFVY NFRSGNCVYY
DLGA
//
