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Database: UniProt
Entry: A0A0G2EQJ0_9EURO
LinkDB: A0A0G2EQJ0_9EURO
Original site: A0A0G2EQJ0_9EURO 
ID   A0A0G2EQJ0_9EURO        Unreviewed;       790 AA.
AC   A0A0G2EQJ0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   08-NOV-2023, entry version 34.
DE   SubName: Full=Putative eukaryotic aspartyl protease family protein {ECO:0000313|EMBL:KKY25057.1};
GN   ORFNames=UCRPC4_g02114 {ECO:0000313|EMBL:KKY25057.1};
OS   Phaeomoniella chlamydospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX   NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY25057.1, ECO:0000313|Proteomes:UP000053317};
RN   [1] {ECO:0000313|EMBL:KKY25057.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY25057.1};
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:KKY25057.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY25057.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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:KKY25057.1}.
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DR   EMBL; LCWF01000050; KKY25057.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2EQJ0; -.
DR   OrthoDB; 1831139at2759; -.
DR   Proteomes; UP000053317; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR   Pfam; PF00026; Asp; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KKY25057.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KKY25057.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..790
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002543708"
FT   TRANSMEM        453..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          59..412
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          518..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          684..790
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        518..532
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..593
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..616
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..669
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        684..711
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..745
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        767..790
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   790 AA;  86144 MW;  C386664DF3321F74 CRC64;
     MHWMLVNMLA FTFGNSNLRR FYQFALLTLF ADICTAKSPS PLSVPVDSSQ WLGYDGNWSP
     VILRAGTPEQ WVYVLPNILS SETWVIGPDG CDGTYTCETE RGGIFNASES TTWDEIGNYE
     LGFDNALGVT GTADYGDDTL ALSDSVVAED QIVGILTSTQ FWTGLMGLGV EESDFTGSAQ
     KTFLSTLVEN DSLVPSHSYG YTAGAYYRLK GVPASLTFGG VDTNRYVAND VSFALNANSQ
     PVVAINSIKV TAQSSSETSL RNWTSPLTLQ NKSSAAKYTI DSSTPFLWMP GEVCDAFAEA
     LGLYYNETLE LYTFEGNSTV PSLLENWNLT FTFDIADTPR SSNSVELTLP YDAFNLELTY
     PFPNLWANYT SPATKYFPLR RATDSTQYTI GRMFLQETYL TVDYERGNFS LSQAVFSYSA
     QTDINLAEIT RPSNSSYDGP KESNSGLSTG AKAGIGVAVA VGVLLFLCLI ALLVLLRRQK
     KANAGSEKST SEHRRGFLQL LSLNGSRSVQ NVQQIAPTEL PASKQQPTEV PADVSASRFE
     LPGSTPIEME GSLVPLSYYA KEDHRSNPPV ELPSNRRFSM SKSPSGSSGR TCQEDSHDLP
     RYTPMADNDR HADSISPDSP TRSGNYPTYS SSGPISPNTI HPDPDTGSGG NSFSPVSPDT
     STGSNSNTHT NSLAATIIRA ASYSSPNNNS NTHLSVPGAT EQGSVARSQS TRSSRFREEG
     IDLNPLVNAQ EELRRHEDEL GSDSGYRIRD PVGDGAQRKL SRISRMIRPR SRADGEGGGE
     QRRRFSWEQE
//
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