ID A0A166MTZ9_9PEZI Unreviewed; 444 AA.
AC A0A166MTZ9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:KZL64997.1};
GN ORFNames=CT0861_02479 {ECO:0000313|EMBL:KZL64997.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL64997.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL64997.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL64997.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KZL64997.1}.
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DR EMBL; LFIV01000244; KZL64997.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166MTZ9; -.
DR STRING; 708197.A0A166MTZ9; -.
DR OrthoDB; 245129at2759; -.
DR Proteomes; UP000076552; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF1; ZGC:77287; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:KZL64997.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:KZL64997.1};
KW Transferase {ECO:0000313|EMBL:KZL64997.1}.
FT DOMAIN 207..444
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 444 AA; 48594 MW; 382F0FCADD02D6C2 CRC64;
MQDLATLRSG GYRGRGLQKL KLSEPLNGFP REILDLADTL EYLDLSGTGL STLPEDFSQL
QKLKIAFFSD CHFTVFPKQL AACPELEMVA FRSNAMAAIP EGALPFNLRW LILTNNRIEA
LPESIGRCSR LQKCMLAGNS LTTLPDGMSA CHKLGLLRLS ANKFAELPPW LFELPELAFL
SVAGNPCCAV SLDEELALLR KVGWHDLEIG SLLGHGASGD IFKARWVVAD SVVEQVAVKL
FKGEVTSDGT PLDEMAACLA AGSHGNLIST LASIQGHPEK HGLIMQLIPP HYQTLGLPPS
LQTCTRDRYE TDKPLSLETV LEILRGVAAA ARHLHSRKVS HCDLYAHNIL FNETGHALLG
DFGAATIYEH LDGFDFEKLE VLALGHLVED MLGLVNVKEE DSKGQKVLQE LRMLHTRCST
PIVRARPTFA EVVGGMQAAT RECQ
//
