ID A0A0G2FMG4_9PEZI Unreviewed; 407 AA.
AC A0A0G2FMG4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 30.
DE SubName: Full=Putative peptidase a1 {ECO:0000313|EMBL:KKY13148.1};
GN ORFNames=UCDDS831_g09268 {ECO:0000313|EMBL:KKY13148.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY13148.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY13148.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY13148.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY13148.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY13148.1};
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.
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:KKY13148.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LAQI01000401; KKY13148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2FMG4; -.
DR Proteomes; UP000034182; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR Pfam; PF00026; Asp; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 247..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..203
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 214..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 44818 MW; B405867E54DDBE37 CRC64;
MNRPQTSFLQ SLKDANNISS SENFFGSLVL GGYDSARFDN KSQITVPFNG DDEKDLTIQV
NTISTNISSD PLTTAAMNLV IDSTIPYLYL PESSYQLFEK AFGLEWNDTV ELYLINETHY
DNLVKQSAEL KFNVGTINTT EIVFPIAAFL LTASFPLLGD DSSTSYYFPI KRTNDKETFT
LGRAFLQEAY IIYDYERSFF TLAPCTWPSD TAASPPSAPT IIPSVNETSS HDSDNNNHNT
TNDTAGLSAA AIAGAAIGGI VAGLLLATLL ACIWLRRRRR LHSRRPSHST SASTTKFPPF
SPHTRHSSLT TLPPQSPRPR SGSRLIASFF RNPWASLSTE DEHVVYELAV DPSAPTPAER
AAGEHKRQLS SELDAEVCAV HEMFQPKAED VRSEMPGDGP LPTYESE
//