ID W3WMJ0_PESFW Unreviewed; 621 AA.
AC W3WMJ0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=PFICI_13614 {ECO:0000313|EMBL:ETS75130.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS75130.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
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DR EMBL; KI912119; ETS75130.1; -; Genomic_DNA.
DR RefSeq; XP_007840386.1; XM_007842195.1.
DR AlphaFoldDB; W3WMJ0; -.
DR STRING; 1229662.W3WMJ0; -.
DR GeneID; 19278627; -.
DR KEGG; pfy:PFICI_13614; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_006421_1_0_1; -.
DR InParanoid; W3WMJ0; -.
DR OMA; KQYYYIV; -.
DR OrthoDB; 2785398at2759; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd14096; STKc_RCK1-like; 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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24347:SF412; CALCIUM_CALMODULIN DEPENDENT PROTEIN KINASE I; 1.
DR PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000030651}.
FT DOMAIN 134..439
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 14..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 621 AA; 69626 MW; A0AB212FF768C21A CRC64;
MSTIQQLKNF IRHGKQARTN NNHDDSQRKN DHSPTNVPAQ QHKAMAHVTE PNLHVGGGGV
AAAHQVQPIP EAYSVQPGAG DAHNRVAQAN DVAAHHAEQR IDGSKSKDHH VAKLVEEEKA
SRSKFPKYPG LERWELTEKM GDGAFSNVYR ARDLTGDAGE VAIKVVRKFE MNNMQGQKHL
HPDFKKVPKA AERANILKEV QIMRQLDHPN IIKLIDFSES RQYYYIILEL APGGELFHQI
VRLTYFSEDL SRHVITQVAN ALEYLHEERG VVHRDIKPEN ILFEPIPVVP SKVPKPKQPG
DEDKVDEGEF ISGTGAGGIG RIKIADFGLS KIVWENSTMT PCGTVGYTAP EIVKDERYSK
SVDMWALGCV LYTLLCGFPP FYDESIEVLT EKVAKGQYTF LSPWWDDISK SAQDLISHLL
TVDPEKRYTI TEFLAHPWIR QGSGPTPREE KKALNNGDTL RAFDAGRLAD GDRRMDFRSP
GAVNLREIFD VGYSVHRQEE EAKRRKQVGS KGQAPSRLTD LNESEEDEKS DPEYVHKTDA
SQLEQRMRDT NLGKAQERGR ERERPEKEAR GYGQHSAAVA QAARQQVRDR NRAKGAFELS
LDGATLLGRR ANKPTARAGG A
//
