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
//