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}.
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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
//