ID A0A439DCC9_9PEZI Unreviewed; 888 AA.
AC A0A439DCC9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=EKO27_g3045 {ECO:0000313|EMBL:RWA12064.1};
OS Xylaria grammica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Xylaria.
OX NCBI_TaxID=363999 {ECO:0000313|EMBL:RWA12064.1, ECO:0000313|Proteomes:UP000286045};
RN [1] {ECO:0000313|EMBL:RWA12064.1, ECO:0000313|Proteomes:UP000286045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHI A82 {ECO:0000313|EMBL:RWA12064.1,
RC ECO:0000313|Proteomes:UP000286045};
RA Buettner E., Kellner H.;
RT "Draft genome sequence of Xylaria grammica IHI A82.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00006529}.
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:RWA12064.1}.
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DR EMBL; RYZI01000061; RWA12064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A439DCC9; -.
DR STRING; 363999.A0A439DCC9; -.
DR Proteomes; UP000286045; 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:0000165; P:MAPK cascade; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd09534; SAM_Ste11_fungal; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 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; IPR000159; RA_dom.
DR InterPro; IPR029458; Ras-bd_By2.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR PANTHER; PTHR48016:SF29; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 1A; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF14847; Ras_bdg_2; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM01304; Ras_bdg_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
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:UP000286045}.
FT DOMAIN 66..129
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 241..331
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 614..884
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 16..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 643
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 888 AA; 98552 MW; 946990D1AE725AE4 CRC64;
MAMLASKTSF SASLSSSAST LVGNTPSSNM SHTRRAHTMP NSGQPFASPT ESEFSDIDGP
DVVKNWTEDQ VCEYLRSVKC GEYEKLFRKN NINGENLLEM DKEVLKEMGI DKVGDRVRLF
LGIKKLRTKA YANQKKRNRD SFAILDSQYT PSSASPRPPN SVSRSMPKRY SRQIEVSSLG
MNPALEVAKP ASRPESPLHT ADIRPARQHW YPQNQPYVIN TAPVMRGPTS PPETLASGRL
DQDFIRVIST GGITKVVKVA GCNTCEEVMR VTLRKFALRE DHDRNYCFWV LAGVDPDPRQ
CRRLGDTELW RIINDQKRPE RNRLILRKVP SGEPGESELL RAAAIGMEEA QQKHARALEN
VDKRSQLKVQ KLLGESWSEG LQQPLSPISV QVRERNLHNT ARDLERPAPS PTKAQPRRKG
ILRPFGGLRP PSELITSDLT SYFPDHPRED IDRTARLSMR RSTRLSKVNS RLSVASNFSF
ASSIQDAPPI PTIADSWLSN GHLAKVKARE AQGRLPHYRD SVTSSVLDTL QEESPIEPNR
KSYVSFADSG SDTNPVSITD PGGNIIRHSY FDETSTQGSE SLRDLTQALS EDGEDADEEL
ASFLAGESWD DNKWMKGALI GQGSFGSVYL ALHAVTGELL AVKQVEAPSP GANSQTDARK
KSMIEALKRE IGLLRDLRHP NIVQYLGCGS SNEYLNIFLE YVPGGSVQTM LNSYGALPEP
LVRSFVRQIL EGLSYLHNRD IIHRDIKGAN ILVDNKGTIK ISDFGISKKL EASNILNGAN
NNKNRPSLQG SVFWMAPEVV KQTSYTRKAD IWSLGCLVVE MMTGQHPFPD CSQLQAIFKI
GGGKAAPTIP DNASAEAVEF LSRTFEIDHN LRPSADDLRL SPFLTPIT
//
