GenomeNet

Database: UniProt
Entry: A0A0G4N2C0_9PEZI
LinkDB: A0A0G4N2C0_9PEZI
Original site: A0A0G4N2C0_9PEZI 
ID   A0A0G4N2C0_9PEZI        Unreviewed;       380 AA.
AC   A0A0G4N2C0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   22-FEB-2023, entry version 39.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
DE   Flags: Fragment;
GN   ORFNames=BN1708_016810 {ECO:0000313|EMBL:CRK40499.1};
OS   Verticillium longisporum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK40499.1, ECO:0000313|Proteomes:UP000044602};
RN   [1] {ECO:0000313|EMBL:CRK40499.1, ECO:0000313|Proteomes:UP000044602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VL1 {ECO:0000313|EMBL:CRK40499.1};
RA   Wang D.B., Wang M.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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; CVQH01026405; CRK40499.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4N2C0; -.
DR   STRING; 100787.A0A0G4N2C0; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000044602; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
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; 2.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 2.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 2.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000044602}.
FT   DOMAIN          1..94
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DOMAIN          93..380
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          328..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        124..129
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   NON_TER         380
FT                   /evidence="ECO:0000313|EMBL:CRK40499.1"
SQ   SEQUENCE   380 AA;  41724 MW;  C6B6ACAEA8A229F0 CRC64;
     MLNNEIGAKK GYNGQWSVEC DKRASLPDIT FNLAGYNFSI SAYDYILEVS GSCISTFQGM
     DFPEPVGPLV ILGDAFLRRW YSIYDLGKNT VPDFSEITIG TPPQTFKVVL DTGSSNLWVP
     SQQCSSIACY LHTKYDSSDS STYKANGSEF EIHYGSGSLT GFVSQDTVTI GDIKIKNQDF
     AEATSEPGLA FAFGRFDGIL GLGYDTISVN KIVPPFYQMV NQKAVDEPVF AFYLGDTNEQ
     GDESEVVFGG VDESHYEGKI TTIPLRRKAV TDQNQQRLLE QARARAAAQQ NSNVFGDKMQ
     QGGMANQTSY NPAQLAAQQA RLVNNVANKP QSPAPRQGQN GTPTIPARVT PVPVPVIPGA
     QQQQQQQQQQ QQQQQQQQQQ
//
DBGET integrated database retrieval system