ID A0A395GTD7_9EURO Unreviewed; 1076 AA.
AC A0A395GTD7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
GN ORFNames=BO80DRAFT_427517 {ECO:0000313|EMBL:RAK98218.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAK98218.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAK98218.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAK98218.1,
RC ECO:0000313|Proteomes:UP000249402};
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 (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ824455; RAK98218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395GTD7; -.
DR STRING; 1448316.A0A395GTD7; -.
DR VEuPathDB; FungiDB:BO80DRAFT_427517; -.
DR OrthoDB; 1360556at2759; -.
DR Proteomes; UP000249402; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:1902657; P:protein localization to prospore membrane; IEA:InterPro.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR040345; Mug56/Spo71.
DR InterPro; IPR039486; Mug56/Spo71_PH.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR029217; Spo7_2_N.
DR PANTHER; PTHR28076:SF1; PROSPORE MEMBRANE ADAPTER PROTEIN SPO71; 1.
DR PANTHER; PTHR28076; SPORULATION-SPECIFIC PROTEIN 71; 1.
DR Pfam; PF15404; PH_4; 1.
DR Pfam; PF15407; Spo7_2_N; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM01316; Spo7_2_N; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000249402};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 621..828
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 891..1062
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 99..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..133
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1076 AA; 123216 MW; 55CAF298260808C1 CRC64;
MASRLSPDQH ASDNMATDSH AAFQCRRHHG LDTDSHTAEK LHHASPRHMH MTSRRFFIGP
IPQGWLQNHR KSWWRTRMKF GKYSSKTVTF SADPIVAHYT QGSDTDQDDS APEESPAATD
TTEDEWTERE QEDETSDQEA RPQSDLRTVP YTLAEDHDIS RITTTASDTA ISHQGDNEHD
WNPSMGKRDG SSAYYTAREQ EPNDAAGASS STMNAEQLEQ GSSKQTLSTP SQNGASQSSP
LAPASDYGST TALLRPDSRS KGKGRVPTTS SMNLEQQEPQ VETAEEEPLR NGRRSRMDPL
HPFSRKAAKH NLDDNLLDKQ QRVLSRISRT QAKLSRNLPH RRKMKEGEVI KAEKMLVRIE
ETVQEKLPDD YSENDSYKME TRVVDHWREY LVACRLASDE DAPFSLQMYK TRVIPEVQKA
GTRVAPVYEV PLGRKRTKVN LYSHLDKAIV LWGPCKHGTK IYIIRPKSSA HAVEWFTFLS
QVMGRRRPSS LPIHVPDLGV SLVFNNPFGQ LEAALDSQKK NTGILSRAVI HEESAATAIV
QGCLKLLENR PEWAEVLQRW SKTEIMGLAW KRYDRLEWIL GANEERMYGS LAMHTSHELE
LRPRQHYNTY IKRDGEKADE PEPVEGFLVR LTSQRGVHQR MNKMFFKRLY FFTQDHYLFF
CRPSKSLPPA PPRLCRSGSD MPSTQQILDA SPLSYEVDPY PLQDGDISWL LSGNKEHIRK
HDEEAFVQRQ RNIHNLEHAD GFIDLSKVQE VRNVRRGSCP ADPNIEAGPD VEFHPDSRDT
HRDDGATRQF DDDRTFEMLL DNKLVVRFQA YNETTKNEWM QRLEALVKYW KDKIATDAAE
IKALRQRNLE LLGIDEELES IMGQFAKKWE VKKAEASPLL HNVCLLSGCR TIKISGQLYR
KPRRHSTFKK THVVLTAGKL LIFRSSLRKR NGVEVPHIHQ NLETSIDLND CYIYSGLLTD
SDLLYANQTF DSNHPGHHSL PRVYLSSDVY TSSDEDTAIT FVIWQPLKKN LFRAREHGLT
GQTKQRLKQV STLGVHGRTI VFKARSRIEK DRWVLSIASE INRLQEDQPE DVRIIT
//
