ID W3WY85_PESFW Unreviewed; 783 AA.
AC W3WY85;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETS77851.1};
GN ORFNames=PFICI_09913 {ECO:0000313|EMBL:ETS77851.1};
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:ETS77851.1, 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).
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000256|ARBA:ARBA00006219}.
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DR EMBL; KI912115; ETS77851.1; -; Genomic_DNA.
DR RefSeq; XP_007836685.1; XM_007838494.1.
DR AlphaFoldDB; W3WY85; -.
DR GeneID; 19274926; -.
DR KEGG; pfy:PFICI_09913; -.
DR HOGENOM; CLU_357913_0_0_1; -.
DR InParanoid; W3WY85; -.
DR OMA; AGECHEN; -.
DR OrthoDB; 1659246at2759; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR21310:SF59; AMINOGLYCOSIDE PHOSPHOTRANSFERASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR21310; AMINOGLYCOSIDE PHOSPHOTRANSFERASE-RELATED-RELATED; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030651}.
FT REGION 104..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 89100 MW; 4E64BE8F1EA290D8 CRC64;
MERLKIPLGT LLDAVPPIRD MQDKLRETVV APLQDNIGDM VNKLADLALT TGSNIAAVSS
SSSTTRIPPF DPDNPSLDPH ANSACVPEAR ALLVKLRAEM GRNMPLDKQD KTQDPQNPAN
RAGKLADFGP VLARVDWAAV AAVAEDVAWR AGLASKYRGP VHVHVGEPRF GTMSVGFPLI
WQGSSSSSSG AGAGANSSKY GRKSSNRKDG DAKKWFIKIP INGTPNAWHS SDERALASEV
GTMRWLRREL GVHTNLNIPR VYHWDGSAGE TSRDGTRNRI RVPYMMMQYV DGISAHDAWF
TRWGPTGWWR PEAEELRRGI LSNVAAAMSE LRRFEFESGG APRYQFVRDA RGRETEELLG
VGPLRILDIE AMLDRWLCHL SPEEKLECKR TPIYRELGPW KGKDAVKNYY TSRIDCHNVR
ENSDFGSTML LESYFKWWHE SDTALGVGYD DESDEEDEEE LAIQRWNKGE KKPFVLTHHD
LNLHNIIIDQ QGKLWFIGWS GVACVPRAIG NEALPLWLVR DWNPFVYRWR DMDWPWRYRH
CPWRVPVTED NSTEEATWRL SGWRQYYAEC MNEAKKAWRD VEKDANERRE SREQESRPRA
RRKEAEESEF DRAELSSPKG EEERRGRPRY RFGEEPPEKS KTPPPGHQGV RHVSFASDTK
PAPGDRRPSS KSSPSSTNIK SCPRLNRTLL SALPLSLSAA ANDPRSRPFI LQELYHRAVP
SVPRWDNFAV SRLRHLAGEC HENVPSPFEI ESRELFYRTL LDCAGVARGR HRPWAARLGD
YND
//
