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Database: UniProt
Entry: A0A2P7ZYA7_9PEZI
LinkDB: A0A2P7ZYA7_9PEZI
Original site: A0A2P7ZYA7_9PEZI 
ID   A0A2P7ZYA7_9PEZI        Unreviewed;      1626 AA.
AC   A0A2P7ZYA7;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   22-FEB-2023, entry version 15.
DE   SubName: Full=Anucleate primary sterigmata protein A {ECO:0000313|EMBL:PSK53200.1};
GN   ORFNames=B9Z65_3400 {ECO:0000313|EMBL:PSK53200.1};
OS   Elsinoe australis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX   NCBI_TaxID=40998 {ECO:0000313|EMBL:PSK53200.1, ECO:0000313|Proteomes:UP000243723};
RN   [1] {ECO:0000313|EMBL:PSK53200.1, ECO:0000313|Proteomes:UP000243723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NL1 {ECO:0000313|EMBL:PSK53200.1,
RC   ECO:0000313|Proteomes:UP000243723};
RA   Cheng Q.;
RT   "Draft genome sequence of Elsinoe australis.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:PSK53200.1}.
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DR   EMBL; NHZQ01000102; PSK53200.1; -; Genomic_DNA.
DR   STRING; 40998.A0A2P7ZYA7; -.
DR   Proteomes; UP000243723; Unassembled WGS sequence.
DR   GO; GO:0005938; C:cell cortex; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000243723}.
FT   DOMAIN          1277..1389
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          127..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          739..953
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          991..1010
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1015..1083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1106..1209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1418..1563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1583..1626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          212..341
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        564..586
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..649
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..687
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        758..778
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..829
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        860..874
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        908..936
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1022..1041
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1057..1083
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1106..1129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1189..1209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1444..1464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1478..1492
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1518..1543
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1583..1609
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1612..1626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1626 AA;  177346 MW;  709764D8F550E9B7 CRC64;
     MADISSSPAG ANSALEDPFI ETPPHAHPPQ PLRHAPFDPD AFSFHANSSP RQARRALEAH
     MKETDRRIQE ASKLGSTLVQ QRKDLAARIK EINDKKDSDE IGPDLGKKLA ELEREYTAVG
     RETARAVLPK SRLASSEHPD PAMSPAVFAG MSGPSPSKVA VPSRKQRNQP SNRVHDIEFA
     TEISTSLLAQ VRSLQAALVE KDDALKLETS ERAHLEGEYA SLRSRLRHLD DNEQKYKDEN
     WNLETQVQDI TAAMKLASEK EQRANQSLKS VQSEKESMLR ELEELKQNHG KLTDDYTAAK
     RAQEGDLHIL RRDLAGHEHE REQLQKKIEE LTSQNTELAR AISYRMNADG NGYDNQFGSG
     DDELTTDREF SEASPPASPT KRAPGQGVLE TETLRSSIQH AHRMIQTLKN NIHREKTEKL
     ELKRMLQDAR DELENKRGDN KQNNLKNRRS MQDAAKARRV RAEQLGANRV SREEIISDDP
     EWEDHEGDMS FRSATTARPR KLSMPGAYLP SEESTDAFET ANEKETSTET EAFQTGNEAF
     DDDSDGDATE TEGGTAKPDK TARRLTSFPS SIQTKRASFV STASTSADED DDNRTPVTGQ
     PKYKIKNIKT RSFLREGSAS ANNSPAFSSV YRNSPAYSQT SSNRGTPMAP GQSLGDELDG
     LSDDESTMDG TPSKRMSMIS ASSSPSKAGY AEEPVPAQRP AMVDFGMMTE PWEPEAKEEE
     KSHGVLAATA GALGGLGLGS LLSSKSDNEK ETEAETPSTP KAKSMFSSIL SRGTEPVQPA
     TPEQAPASPR HFASIASQDT EPVQTEPTPA SPRHFASVTS QTTEPIQTEP MPASPRHFAT
     FGAQSTGPVQ AEPVPESPRH FTTFGSQSTE PVQAEPEPAS PRHFATFASQ TTEPVQVEAP
     PASPRHFASI AAQTTEPAQA PPSPRNFASF KSQSTEPMEA FKPEPVPEPI HGFTTIRSHH
     TEPVATPEPE TVDESAFFAL SPIKSQAFEP WSPSENSVLF PPRRSSRRPN TAILVGDDEN
     MLRPQTAEKS MDTEAADEVA QENRSRAPFA EISNNAAGVQ RPASGTSNQS AKPRIVTSDE
     GTQTLVSSQE IDKLMRNKSA VTNGTAVAFA TPSSPRQMAN TSSPRRSSEP SVRADGLTIR
     RPGSSNSVRR SHEMPPPLPM DHNEKIVQAG GKPLQPSSGS MGPPLMPASA YRTNQQRDPS
     VRSRTSTINT AQKAPSFRNA ATAGSVRSEM RSPISRRSSV SSFASEVDQR LNPNGAFTYP
     ADLPPATDPR MITAITQTMI GEYLWKYTRN PLSSNTMSTN RHRRFFWVHP YTRTLYWSEH
     DPSTAGKQQL KAKSVAIDAV RVITDDNAYP PGLCAKSLVV VTPAREIVFT APTSQRHETW
     FNALSYLLLR TAPTADANTS AAVGGVVDSP VVLGGAASSS NNGELNDEDV AEFNPGYGTA
     TRPSARAGRQ SHLSVSSYGS ANTARSRPHY MDVPTLTPKN YNAEQPQWAQ SGTARRDGGR
     DAGGVISPEP ASPGVRSPSV SGRISSMMKS VGRRSVSSRR SATRVGDAES RAQGLRSESA
     ENIRRQIEEQ ERLERLENVR SCCDGKHDVG TLSRRQESFR GRGGRTHSHA HPQDPASVNS
     SVSSRT
//
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