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Database: UniProt
Entry: A0A3F3QEL7_9EURO
LinkDB: A0A3F3QEL7_9EURO
Original site: A0A3F3QEL7_9EURO 
ID   A0A3F3QEL7_9EURO        Unreviewed;      1629 AA.
AC   A0A3F3QEL7;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
GN   ORFNames=BDQ94DRAFT_157067 {ECO:0000313|EMBL:RDH37535.1};
OS   Aspergillus welwitschiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH37535.1, ECO:0000313|Proteomes:UP000253729};
RN   [1] {ECO:0000313|EMBL:RDH37535.1, ECO:0000313|Proteomes:UP000253729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH37535.1,
RC   ECO:0000313|Proteomes:UP000253729};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ852035; RDH37535.1; -; Genomic_DNA.
DR   STRING; 1341132.A0A3F3QEL7; -.
DR   OrthoDB; 1368013at2759; -.
DR   Proteomes; UP000253729; Unassembled WGS sequence.
DR   GO; GO:0005938; C:cell cortex; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR   GO; GO:0032065; P:maintenance of protein location in cell cortex; IEA:InterPro.
DR   CDD; cd13365; PH_PLC_plant-like; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR024774; PH_dom-Mcp5-type.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR28190; NUCLEAR MIGRATION PROTEIN NUM1; 1.
DR   PANTHER; PTHR28190:SF1; NUCLEAR MIGRATION PROTEIN NUM1; 1.
DR   Pfam; PF12814; Mcp5_PH; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          1346..1457
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          674..706
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1080..1099
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1174..1232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1244..1263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1268..1309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1463..1581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          43..87
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          188..236
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          272..338
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        344..365
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..477
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..522
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..547
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        634..659
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        685..699
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1181..1229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1270..1293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1483..1574
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1629 AA;  178882 MW;  DC2AEDC248C0AC6B CRC64;
     MSTIEDPFVS ASQEGAVPRE SHRYSSFDTQ LYSLDASSPA QAKRALEAHL AETERRLEEA
     SKLGTALIEQ QKELEEKLKE VEQQQEAGQI GPDLRQKLAD LEKEYNEIGR ETARAFLAPK
     RMAGGEDSHL GTPYEQKSPI SPALFAGQAT NSPSKVSVPS RKQRNQSSTR VHDIEFATEI
     STSLLAQVRQ LQALLAEREE ALKILNLEKS RLELEAEGYT QRIRALDESE ERYKDENWAL
     ETKTHELMAA VKEAADRESR LNSNLGLLAS EKGSVERELE DLKQVNAKLI EDHTAAQKAN
     DSEIHLLRRN LNAGDAEKLA LQKKVEELNL QNEELARAVA MRIRQHEAES TREVSRGHES
     DDQDQSTPEN SPPPSPNKFT PRHNHLETET LRSSLGHAHR MIQNLKSTIH REKTEKIDLK
     RMLQEARDEI EQRRREAAAP TNPSSKRQKT KAEAARKAPR PDLLGAGRKR AEIEIQDSDW
     EDNATEASPS HKPSMKLHQG RVGGQSSDEP SDAYQTATEA DDTFETANER ETATESEAFQ
     TGIESMADDS TDTDELTETE ERLQRTPRGR VSSLTLTKAR DRTSYQSTAS TSGDEDEDYD
     DGFPSPSQMS SPRYRLRKKR SVMRKIRPSG EAPMASNSRP SSARESPATS FTQGLPSSEG
     QSLFMELAEL DGEEDEGAFG PSMRFATGSQ ASTPRMLPTP DSRRPSEAIL DAVPKPVMVD
     SGVMTDPWVP TTVATTSLQD TNDEAARGLP TTPTKTVMSD ASTATEVEVP PQLAHAGTQW
     TPIETEVMEE QTVVNAEGVR PNGHPMPVME TDVSAVSFQE TVPVAPRLPE FSTSYAVGVT
     TEPVAFAVPE PPEVTLSSIC SELTEPADAK LPEPEPVYVA DMTVSAIEFQ STLPVAPALP
     EPAAPVLLSE HGTNTEMPEV SVSSILSQHT EPVEALLEPE APIPEAAVAY VEQAECPEIA
     LSSIVAQQTQ PAAAIPEPRE ITPVVAVEEQ MVPKVELVVS SISSQQTEPV DAVAPQPALP
     SLAISSTAFQ CTEPIPAQVP ELPVPLVSQV SLSSVSSVET LPVKSTPPPP AIPVLNFPDE
     NVAPESNEKA LNSSSIMEPP SLVVSEDTID DSTVNSAANI KLDDSLPLSA ISGNAVPRHA
     RKHSSSSRAD QGAQTILSSK QIDQILMDRI VARPLSPPDS DKAKEQNSSP FATPKARTRP
     THQPSATSLP SHKRPGSAVS QTSSIQSHPP LPMDHREAIM AAEKRSLDQR PSSPSLMGPP
     LAPASAYRTN VAQRPRTPND SNLQVGTATT TSRMKMRRES HVSRRSSVSS FASEIEERFN
     GHPNPALGPQ GYAAGTDPRM IQAITQTMIG EFLWKYTRKT VSGEISNSRH RRYFWLHPYT
     RTLYWSEQDP QSAGKSELRT KSVLIEAVRV VPDDNPYPPG LHCKSLEVVS PGRRIRFTAT
     TSQRHETWFN ALSYLLLRNS TENGEEQEGD ASLEDIDEFN PGFRSRSRQT SRLSFSSSRS
     RTSRNWPKQR AGSILSTRRA ATPGRSSPAL STPSHYSDQR HGSSSRLSTI LNTTIKGSFG
     RKGPNYATSS MHEGSLHTHD SEEDLRQMME RQDDRLENVR ACCDGKHDVG ALSRTSKYSP
     RVNRIHSHH
//
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