ID G9MWD6_HYPVG Unreviewed; 823 AA.
AC G9MWD6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 08-NOV-2023, entry version 51.
DE SubName: Full=Serine threonine protein kinase CMGC group {ECO:0000313|EMBL:EHK21273.1};
GN Name=YAK1 {ECO:0000313|EMBL:EHK21273.1};
GN ORFNames=TRIVIDRAFT_52068 {ECO:0000313|EMBL:EHK21273.1};
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:EHK21273.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK21273.1, 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 -!- 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:EHK21273.1}.
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DR EMBL; ABDF02000073; EHK21273.1; -; Genomic_DNA.
DR RefSeq; XP_013955466.1; XM_014099991.1.
DR AlphaFoldDB; G9MWD6; -.
DR STRING; 413071.G9MWD6; -.
DR EnsemblFungi; EHK21273; EHK21273; TRIVIDRAFT_52068.
DR GeneID; 25795169; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_52068; -.
DR eggNOG; KOG0667; Eukaryota.
DR HOGENOM; CLU_000288_88_1_1; -.
DR InParanoid; G9MWD6; -.
DR OMA; QPYQDPL; -.
DR OrthoDB; 452107at2759; -.
DR Proteomes; UP000007115; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14212; PKc_YAK1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR24058; DUAL SPECIFICITY PROTEIN KINASE; 1.
DR PANTHER; PTHR24058:SF17; HOMEODOMAIN INTERACTING PROTEIN KINASE, ISOFORM D; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 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}; Kinase {ECO:0000313|EMBL:EHK21273.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000007115};
KW Transferase {ECO:0000313|EMBL:EHK21273.1}.
FT DOMAIN 228..559
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 823 AA; 92200 MW; 9CDB61B3922937B3 CRC64;
MHDAHDAHAG IKYPMRPHHQ AHLSGTRSQQ QHQQQPSSAA QRYSPMDTLS PTSPYSKAYT
SSPSQQTPPN ADYSSQYYVG RAPQLPPIAS YAHDGYPSSA VATLDGSFSD SKAPRRPNPP
MMKAVPEFKK IKSPAELQPK NTRQPRFRRA NPEGGFISPL QALTLHLPAT YRICNPSFKY
ESSRNPRRVL TKPSKGTKND GYDNEDSDYI LYVNDILGSE EAGHKNRYLI LDVLGQGTFG
QVVKCQNLKT QEVVAVKVIK NRTAYFNQSM MEVSVLDLLN TKLDKNDDHH LLRLKDTFIH
RQHLCLVFEL LSVNLYELIK QNQFRGLSTT LVRVFAQQLL NGLALLNKAR LIHCDLKPEN
ILLKNLESPI IKIIDFGSAC DERQTVYTYI QSRFYRSPEV LLGLPYSSAI DMWSLGCIVV
ELFLGLPLFP GSSEYNQIAR IVEMLGNPPN WMIDMGKQGL EFFERRQDEF GRRTYHMKSM
EQYSREHNTK EQPSKKYFQA NTLPEIIKSY PMPRKNMKQS EIDREMNNRI AFIDFVRGLL
NINPLERWSP QQAKLHPFIT QQKYTGPFVP PMNLKSSSLN RSPAPGTQQQ QQAEALSKQR
AAQAQAQAAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ ANSAQNAYAS SMGGGQYQPS
SHVPAPLYSN SAVYNPGAGH GNVPPQYGPP QTGQYGQMVM SQPPQQLPSG QYSNPAQPNM
YQQGGMRTNR QRASTMEQQQ SGIPPALQRV ASHLDPSQPI RLQPSPAYYP PTGEGLDNAP
GRAGRRGSRV QQGGARSNRD FIRNLEERTL EEGFMGSSQN PWH
//
