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Database: UniProt
Entry: A0A0G2HXF2_9PEZI
LinkDB: A0A0G2HXF2_9PEZI
Original site: A0A0G2HXF2_9PEZI 
ID   A0A0G2HXF2_9PEZI        Unreviewed;      1239 AA.
AC   A0A0G2HXF2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Putative int1 protein {ECO:0000313|EMBL:KKY39378.1};
GN   ORFNames=UCDDA912_g00589 {ECO:0000313|EMBL:KKY39378.1};
OS   Diaporthe ampelina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY39378.1, ECO:0000313|Proteomes:UP000034680};
RN   [1] {ECO:0000313|EMBL:KKY39378.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY39378.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY39378.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY39378.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) 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:KKY39378.1}.
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DR   EMBL; LCUC01000020; KKY39378.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2HXF2; -.
DR   STRING; 1214573.A0A0G2HXF2; -.
DR   OrthoDB; 2788168at2759; -.
DR   Proteomes; UP000034680; Unassembled WGS sequence.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   CDD; cd13278; PH_Bud4; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR012966; AHD.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR36100; BUD SITE SELECTION PROTEIN 4; 1.
DR   PANTHER; PTHR36100:SF1; BUD SITE SELECTION PROTEIN 4; 1.
DR   Pfam; PF08174; Anillin; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   4: Predicted;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034680}.
FT   DOMAIN          1067..1188
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          152..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          764..818
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          892..951
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..184
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..369
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..430
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..455
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..471
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..501
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..542
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..631
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        777..800
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        902..918
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        919..947
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1239 AA;  139542 MW;  B8E254B9F1645454 CRC64;
     MSSAIPRPLS EISPSEKRRN SPSWKEATKK MTLNTDSSPF QSSPLDGKAS PRLFWQSRNN
     ENSTYGSGSP SPTRRSSIER LQKASRVKNS NILALEQKQD RFKNSFDVDN ELNSSGSSYE
     DRELPSGMAL HRHAKSVTFD AAPPQVNEYE MATPDISSIA SSSREGSIDS EDDDEDDEEE
     HYFMGADDHD DSFDATLEDT VKTPVVLPDD WRQDMANPMD EVLEASPALD GFHNFPPGEI
     PQQDRTDSRN SNGDHRPLPP LPPPPGIFSE RRNSNSSAGL SATAERMIGS SRTLPSPPPA
     SSFTKSDIQN IGNGKMTLEE RLKLMMLSDD GKSAAEQQRE RRMRRAGTRD RADSQTPEAE
     LHDPLVSAEE DDTLPELSGL GDYELPTKIS RESIMRRVDG NQASEGGSDY NFSSPPPSSP
     ERPLPLDPDV PIPSTEGSAE DEIDHNAYLK HEEDEQDDKD EQDDKDEQDD DMSITDYYQH
     SESGVEDIEE YGKDDADKAD DSSSNYSGPE LPPTPQEEKS EEEQLTTPRA ASPTQQESSI
     DTITEKDLPD LPTNQKHNPF TDDLQSFMLP KPDEADAPQE TEAPTLQRPF TPKLTLSKPE
     YDGSGWGEPD EDEEEPKTPD SVIHRPLPSY DEEEELEEER HSPAIPETVA TIKSAAGSRL
     KTRPSATPSD MAAMREQRRQ VSCEVPNMPQ IPDRHRNRMS RDMDSEQHLA PDVTGDEYMQ
     RHPSFKSRSL TLDLDLGLSL DQDFERVIEA QKRGYLMRQN TKVVAASDKD NEDLRPSTRS
     AGNSPVKQTR PQSWTVEPWN GQVRKKSLRK RHTTEESGER GRVFVKVMGV KDLDLPMPKN
     ERTWFSLTLD NGVHCVTTAW LELARNAPIG QEFELVVPND LEFQLTLNVK LERPPPQRMA
     QSPASPRKTK TSTFSRVFAS PKKRKELELR QKEEDERLAR QQREAHARKT AANPTAWDLL
     SPLAAEDGSF ARAYVCLKEH EARCFGRPYV VDVACFNEWA TEEAGFASSV KSKRGSTSVV
     RKAPYKIGKL ELQLLFVPRP KGATDEDMPK SMNSCIREMK AAEERRSRNW EGPLSQQGGD
     CPYWRRRYFK LVGTKLTAYH EATRQPRATI NLANAKRLIN DRRALTEKEI TGKNGKRRRS
     AFAEEEEAYM FVEEGFRVRF NNGEIIDFYA DSPEDKEGWL KVLSDVIGRD NFGNDEDGLG
     GSSRAKGKWC ELVLKREDTL RRRAEARRPS HGRTKSSLV
//
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