ID M7SY77_EUTLA Unreviewed; 916 AA.
AC M7SY77;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Putative calcium-independent protein kinase c protein {ECO:0000313|EMBL:EMR69247.1};
GN ORFNames=UCREL1_3735 {ECO:0000313|EMBL:EMR69247.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR69247.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
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=2.7.11.13;
CC Evidence={ECO:0000256|ARBA:ARBA00000946};
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=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569};
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DR EMBL; KB706115; EMR69247.1; -; Genomic_DNA.
DR RefSeq; XP_007791661.1; XM_007793470.1.
DR AlphaFoldDB; M7SY77; -.
DR STRING; 1287681.M7SY77; -.
DR KEGG; ela:UCREL1_3735; -.
DR eggNOG; KOG0694; Eukaryota.
DR HOGENOM; CLU_000288_54_0_1; -.
DR OMA; NRIYFAM; -.
DR OrthoDB; 21591at2759; -.
DR Proteomes; UP000012174; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd11620; HR1_PKC-like_2_fungi; 1.
DR CDD; cd05570; STKc_PKC; 1.
DR Gene3D; 1.10.287.160; HR1 repeat; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037312; PKC-like_HR1.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351:SF228; PROTEIN KINASE C; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF02185; HR1; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00742; Hr1; 2.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF46585; HR1 repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51860; REM_1; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01207, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EMR69247.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000012174};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..67
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 75..152
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 159..277
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 591..850
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 851..916
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 275..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 37..64
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 303..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 620
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 916 AA; 103231 MW; A131723BA8FACD96 CRC64;
MNEDEAMANI YRKIEREKVL LNGANAMRQQ TNNDAVRSRL DSQMREARRN IQFFEEKLRE
LQMKRMGQGM EDLIKYDTPY LGPRIQLMLS QIQFKLNVEE QYLKGIEKMV QLYGMEGDRK
SKADAAARRI ESKQKIQLLK QALKRYEELH IDDLESADSP DDDSINMPNL RKPLTGQLAI
RVVQVRDVDH ASTGRFSRGP ETFVAVKVED NIVARTRVSR NDKWEGEYHN IEVDKANEIE
LTVYDKPDTH ALPIAMLWVR ISDIVEEMRR KRIEAETSNS GWVSADRMGG HGSAPPPQFP
MSPQQQQFGG PPNSPGFSDQ PQQFPPQSAA PQITSQPIDA WFNLEPTGSI HLSLNFMKQN
KDRRPVDLGL GRKGAIRQRK EEVHEMYGHK FVQHQFYNIM RCAFVASQEA TDAAKAMYAS
QTSPSRPVYP DRASSTTTSA AAAAATAAMS GSMSSTSSRP GSIPDYASGR TNSYGGSTMD
GREDPYAAGQ GYGVPSQPKY NPAAYANVNN YPSQPAVLQH QPHPATQQYQ QPAPAQIQQP
MYPPTAAVPK PSAPLETPSP VSSSGVPVPS RKPLPLATDP GTGQRIGLDH FNFLAVLGKG
NFGKVMLAET KKGRKLYAIK VLKKEFIIEN DEVESIRSEK RVFLIANRER HPFLTNLHAC
FQTETRVYFV MEYISGGDLM LHIQRGQFGT KRAQFYAAEV CLALKYFHEN GVIYRDLKLD
NILLTLDGHI KIADYGLCKE DMWYGSTTST FCGTPEFMAP EILLDKKYGR AVDWWAFGVL
IYQMLLQQSP FRGEDEDEIY DAILADEPLY PIHMPRDSVS ILQKLLTREP DQRLGSGPTD
AQEVMNQPFF RNTVWDDIYH KRVAPPFMPT IKNATDTSNF DSEFTSVTPV LTPVQSVLSQ
AMQEEFRGFS YTADFD
//
