ID G9N999_HYPVG Unreviewed; 696 AA.
AC G9N999;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=TRIVIDRAFT_40990 {ECO:0000313|EMBL:EHK16520.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK16520.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK16520.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHK16520.1}.
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DR EMBL; ABDF02000090; EHK16520.1; -; Genomic_DNA.
DR RefSeq; XP_013950728.1; XM_014095253.1.
DR AlphaFoldDB; G9N999; -.
DR STRING; 413071.G9N999; -.
DR EnsemblFungi; EHK16520; EHK16520; TRIVIDRAFT_40990.
DR GeneID; 25793967; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_40990; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_3_1; -.
DR InParanoid; G9N999; -.
DR OMA; QNGRMKE; -.
DR OrthoDB; 5475340at2759; -.
DR Proteomes; UP000007115; Unassembled WGS sequence.
DR GO; GO:0000144; C:cellular bud neck septin ring; IEA:EnsemblFungi.
DR GO; GO:0005641; C:nuclear envelope lumen; IEA:EnsemblFungi.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IEA:EnsemblFungi.
DR GO; GO:0005774; C:vacuolar membrane; IEA:EnsemblFungi.
DR GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0061762; P:CAMKK-AMPK signaling cascade; IEA:EnsemblFungi.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:EnsemblFungi.
DR GO; GO:0071940; P:fungal-type cell wall assembly; IEA:EnsemblFungi.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IEA:EnsemblFungi.
DR GO; GO:0017148; P:negative regulation of translation; IEA:EnsemblFungi.
DR GO; GO:0075319; P:positive regulation of ascus development; IEA:EnsemblFungi.
DR GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IEA:EnsemblFungi.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:EnsemblFungi.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IEA:EnsemblFungi.
DR GO; GO:2000222; P:positive regulation of pseudohyphal growth; IEA:EnsemblFungi.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:2000217; P:regulation of invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:EnsemblFungi.
DR GO; GO:0006986; P:response to unfolded protein; IEA:EnsemblFungi.
DR GO; GO:0090606; P:single-species surface biofilm formation; IEA:EnsemblFungi.
DR GO; GO:0032933; P:SREBP signaling pathway; IEA:EnsemblFungi.
DR CDD; cd12122; AMPKA_C; 1.
DR CDD; cd14079; STKc_AMPK_alpha; 1.
DR CDD; cd14334; UBA_SNF1_fungi; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR032270; AMPK_C.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR013896; SNF1_UBA.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF82; SERINE_THREONINE-PROTEIN KINASE MARK-A-RELATED; 1.
DR Pfam; PF16579; AdenylateSensor; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08587; UBA_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; KA1-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000007115}.
FT DOMAIN 46..297
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 696 AA; 78117 MW; AEDFE8C2D54DA3EF CRC64;
MSSTHVRRHQ PQPQQEDVAT APKNIARADQ QPQEKKSRAE QRIGAYTVVR TLGEGSFGKV
RLAIHNGTGQ QVALKIITRK KLISRDMAGR VEREIEYLQL LRHPHIIKLY TVIKTPAEII
MVLEYAGGEL FDYIVQNGRM KEAEARRFFQ QMICAVEYCH RHKIVHRDLK PENLLLDENL
NVKIADFGLS NIMTDGNFLK TSCGSPNYAA PEVIGGKLYA GSEVDVWSCG VILYVLLVGR
LPFDDEHIPS LFAKIARGTY SMPQWMPAGA AALIKGMLVV NPVQRMTIDE IRADPWFNTD
LPAYLQPPVE EFFHTGVDPN KAIQKSDIAP NAPEKVQEKL HNEVTEKISK TMGYGKDDVE
EALQSEEPSA IKDAYMIVRE NKLMLANNPE SGLTGEEGSP MMSISSTRSA ISPGGTSPRP
YVNKVGILPS SLPAYHKDYM EREKNGIDHD PQPPAIAIND ELPATRTEAE KEEAARRLNP
HARPLRLDES SKRPQGMTPI TTPAKKPKPV RWQFGIRSRN APWEALLCIH KALHKLGASH
LRDEGYDEAH GRGDDAASRD GSFANGVPLA RESNLNDTDP TKRYKLPADP WHIQVRWPST
SMQKEAERRE DPEIKGGSPD SFHVYSPEDP TSRKDFVALH MDIQIYEMEQ GVYLVDFKCS
GYETQDGRLL EEKEVTSPFP FLDRAAKLIM QLAEAD
//
