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
//