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Database: UniProt
Entry: A0A364NF31_9PLEO
LinkDB: A0A364NF31_9PLEO
Original site: A0A364NF31_9PLEO 
ID   A0A364NF31_9PLEO        Unreviewed;      1901 AA.
AC   A0A364NF31;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=WW domain containing protein {ECO:0000313|EMBL:RAR15918.1};
GN   ORFNames=DDE83_000715 {ECO:0000313|EMBL:RAR15918.1};
OS   Stemphylium lycopersici.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Stemphylium.
OX   NCBI_TaxID=183478 {ECO:0000313|EMBL:RAR15918.1, ECO:0000313|Proteomes:UP000249619};
RN   [1] {ECO:0000313|Proteomes:UP000249619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIDEFI 213 {ECO:0000313|Proteomes:UP000249619};
RA   Medina R., Franco M.E.E., Lucentini C.G., Saparrat M.C.N., Balatti P.A.;
RT   "Draft genome sequence of Stemphylium lycopersici strain CIDEFI 213.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
CC       {ECO:0000256|ARBA:ARBA00006141}.
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:RAR15918.1}.
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DR   EMBL; QGDH01000007; RAR15918.1; -; Genomic_DNA.
DR   STRING; 183478.A0A364NF31; -.
DR   Proteomes; UP000249619; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   CDD; cd07389; MPP_PhoD; 1.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 1.20.5.340; -; 1.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 1.20.190.20; 14-3-3 domain; 1.
DR   Gene3D; 3.60.21.70; PhoD-like phosphatase; 1.
DR   InterPro; IPR000308; 14-3-3.
DR   InterPro; IPR023409; 14-3-3_CS.
DR   InterPro; IPR036815; 14-3-3_dom_sf.
DR   InterPro; IPR023410; 14-3-3_domain.
DR   InterPro; IPR024461; CCDC90-like.
DR   InterPro; IPR018946; PhoD-like_MPP.
DR   InterPro; IPR038607; PhoD-like_sf.
DR   InterPro; IPR043904; PhoD_2-like.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR46689; MEMBRANE PROTEIN, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR46689:SF2; WW DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_6G06520); 1.
DR   Pfam; PF00244; 14-3-3; 1.
DR   Pfam; PF07798; CCDC90-like; 1.
DR   Pfam; PF19050; PhoD_2; 1.
DR   Pfam; PF00397; WW; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   SMART; SM00101; 14_3_3; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF48445; 14-3-3 protein; 1.
DR   SUPFAM; SSF51045; WW domain; 1.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249619};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          518..552
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   REGION          1..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1526..1604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1854..1901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..87
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..274
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..402
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..459
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..524
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1864..1885
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1901 AA;  208109 MW;  1B524C81C1240EFB CRC64;
     MDGRKQGRPE EELFLRYDSN PDTPTIPTVG PLRIQKGRDG KSPPPRTDSA GSSSQPAFSR
     PPPMPSFPAP PTSPPTAPLP YPDSDRPPNA EPTLGTGRYT PLSERERRSA NTTPAERREE
     VRRGSNATGP SPTSPSQRAR FDANDPNRPT ISGYAGRNPD GSVQPSRLAE RRGTAPKPLP
     ESPGPEAPDK EGLFQKAPQR QARADVAANS NPFPEYHQQY FPPPAAQPAP QPAQSNVVYT
     GPNQDEPALK VPTPVGVNRL SSTASTSTVR AQRGSPPPPE TPIIPPSGGG IEARFAAAGI
     AGTSTLTNLQ AQNLQNAAAA QRNQVYANQQ PRPSLGTPQP SQQQPARRPW TPTEQPGNMP
     HGPPAVYQGM DQVPPSSTPP QGPLPQAPNT RFSPPPANTN VPPEHPLNHD MGRMNLNEEP
     PPAYSSITTP PTGQAQSYPN EKGQQPAAQG VQFSDPNQGH PAFANDVRQQ AGPSQPATVV
     APTPTQNQFP PQIQTAQPAH TPSPAPAQGP GPGPASPPPL PEGWIAHLDP SSGQYYYIHL
     PTQSTQWEFP KGPTPLNLNE PMSPTGTFVG GPLASPSFGK APIASPGFAP QTATFPGDFG
     MAPLATPTTT GFTGPPPVAG VDQYKVAPTN GVYFGPYLRY TNMDIERGLW LGSILLITNT
     PHPPTIHIHQ STDLSPNPRQ LKANPIYTHQ TWIFYRYDID LRMEEDHAAK WTYAITSHLG
     CTRFEFLVAG RHETSWRFIA HSGNDFALNV NANERAKLGG VGLMWKDILQ KNAECGGFHV
     QLGLGGQIYA DRLWKELPLL KQWTATSGKE TRKNAPWTAK HEEDVCHAYF HYYTSHFDQP
     HLREAFAQIP HILALDDHDI FDGFGSYPEY MQFSNMFKNI GRLGIEMYLL FQHHTTLEIL
     RNVNNDMDLF TITGTGWHFI KYLGPCVTVV GPDCRSERNP HQVMAGPTYQ GIFPKVATLP
     PSVQHCIWMI PVPIVYPRLE SVEHLAHSMA TGKKAVTGTF NMLGKVTAGV AGVVGAKSVV
     GDGFNSVKKA IGKSGLMSGV LSPFGEIDLL DELRDQWTHD SKDLERTYLI RTLQGIAHNK
     SLRMTFMSGA VDCCGAGLVH DPSRPQDHKT MYQIISSSVV NGPPGNYVLR LLHNNRALYV
     PQNGHRSNNQ PTDTKEDMME IFTQDVNGQP REYKRLMGRR NYVACVIYDP DVVNGTFGQA
     VPGHGGGKLS LAVDFMVQND GGYSAPMKYG PVIVPSLENY NVGTMTAPSI QAMAIPRFLL
     PQLQWSARAS RPVALGAVEA RRYRSCSTSD RRTALPKPSP LQVQATKLWR QTSAQHRTSY
     ASTLELRRSF SATAKQDKDH HFDTLKFVQR MKEEGFTEEQ AEGMMRVLSD VIEESIQNLT
     RTMVLREDQE KATYTQKVDF AKLRSELMTA DSTESSLTRA SHERLTNELA KLNSRLRDEI
     QRTQASVRLD LNLEKGRIRE EANVQELKLK ETDTRIEQET AQLRERLEAV KFSTLQWLMG
     VCTGTAALML GQAVVWARHE SLQEATEVKG HDHVPAPHHG SLGTTCSRRD TNHGPESRST
     QEVPSKFSSC FQGALIGPHS DMGRPSRSQP LAGGRASEVP CPPTPNTHIN STITMATEAN
     LASPNSVRVI DMATARLSSP GCANRLSATM EVAKVAGELT VDERNLLSVA YKNVVGTRRA
     SWRIISSIEQ KEESKGTEKH VGTIRDYRQK IETELEEVCQ DVLNVLDDSL IPKAESGESK
     VFYHKMKGDY HRYLAEFASG EKRKVAATAA HEAYKTATDV AQTELTPTHP IRLGLALNFS
     VFYYEILNSP DRACHLAKQA FDDAIAELDS LSEESYRDST LIMQLLRDNL TLWTSSDGNE
     GEAAATDAPK EGETKTTEDA PAAAEAKTEE QPPAAAPAPA A
//
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