ID M7SDG2_EUTLA Unreviewed; 675 AA.
AC M7SDG2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=UCREL1_8775 {ECO:0000313|EMBL:EMR64259.1};
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:EMR64259.1, 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=2.7.11.1;
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. COT1 subfamily. {ECO:0000256|ARBA:ARBA00038271}.
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DR EMBL; KB707098; EMR64259.1; -; Genomic_DNA.
DR RefSeq; XP_007796640.1; XM_007798449.1.
DR AlphaFoldDB; M7SDG2; -.
DR STRING; 1287681.M7SDG2; -.
DR KEGG; ela:UCREL1_8775; -.
DR eggNOG; KOG0605; Eukaryota.
DR HOGENOM; CLU_000288_67_4_1; -.
DR OMA; KLRVDQF; -.
DR OrthoDB; 10768at2759; -.
DR Proteomes; UP000012174; Unassembled WGS sequence.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd21776; MobB_Sid2p-like; 1.
DR CDD; cd05600; STKc_Sid2p_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; PTHR24356:SF417; CELL CYCLE PROTEIN KINASE DBF2-RELATED; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EMR64259.1};
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 Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 277..580
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 581..660
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 306
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 675 AA; 76567 MW; FA355D31FDB195BF CRC64;
MASYITSMFP SAPGKDLKSP ATERPGTPGT PGMPSTPTTN NFLNPISTPQ GSPSKKTIPP
GAHDLTTAFD SALKLNTSAL DSPIQLGRPQ TQTQTTPLSP TKGNLQSTDN VRPGNGSPTF
DESIIHKSGS RPGSPLKKQQ GQENTPPSRI PIAESLYQHN HAAASRQEVY NLRDRPYTPT
NKKFNTHRGL TPEELETLKK PSVRRLVNVT QLYFLDYYFD LLTYVGSRQT RLNAFKAEVP
SPPQTDEEEY KKLWSKYSGR ERAALRKRRV RLRHGDFQIL TQVGQGGYGQ VYLAQKKDTK
EVCALKVMNK KLLFKLDEVR HVLTERDILT TANSEWLVRL LYSFQDDKSI YLAMEYVPGG
DFRTLLNNTG VLSNRHARFY IAEMFCSVDA LHKLGYIHRD LKPENFLVDS TGHIKLTDFG
LAAGNIASSK INSMRVRLEK ATEADVPFGK AMDQRTIAER REGYQSMREK DVNYAKSIVG
SPDYMAPEVL RGEEYDFTVD YWSLGCMLFE ALTGFPPFAG ANADETWRNL KHWKEVLKRP
VWEDPNYFLS NRTWGFITTC INSRSKRFSN INDIKQHHYF AEVNWETLRQ TKAPFVPELD
SETDAGYFDD FSSEADMAKY KEVHEKQQAL ETMADREDSM SKGLFVGFTF RHRKATSEDS
TPRKSIQTDT FGTML
//
