ID G2X6R6_VERDV Unreviewed; 472 AA.
AC G2X6R6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Candidapepsin-3 {ECO:0000313|EMBL:EGY14684.1};
GN ORFNames=VDAG_05848 {ECO:0000313|EMBL:EGY14684.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY14684.1};
RN [1] {ECO:0000313|EMBL:EGY14684.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY14684.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL Submitted (MAR-2008) 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; DS572705; EGY14684.1; -; Genomic_DNA.
DR RefSeq; XP_009653540.1; XM_009655245.1.
DR AlphaFoldDB; G2X6R6; -.
DR EnsemblFungi; EGY14684; EGY14684; VDAG_05848.
DR GeneID; 20707311; -.
DR KEGG; vda:VDAG_05848; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_3_1; -.
DR InParanoid; G2X6R6; -.
DR OMA; CNVTLGT; -.
DR OrthoDB; 615305at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05474; SAP_like; 1.
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 InterPro; IPR033876; SAP-like.
DR PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..472
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003438989"
FT TRANSMEM 452..471
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..397
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 87
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 280
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 472 AA; 50042 MW; A6212557E21407E1 CRC64;
MRTIPIWVLS SLLLSSTGEA VALRKRDGSP ARVIGFDLES KIIQAPNDKN GMRRRNTVTA
SLDNLQTLYF VNATLGNPPQ QFRLHLDTGS SDLWVNTANS QLCQEVPNPC ALSGMYAANQ
SSSYNYLGSY FNISYVDGSG ATGDYVTDDF NIGGTVLTDF QFGIGYESSA AQGILGVGYP
INEVQVGRAG MDPYDNIAAK MKAQGLIQSN AFSLYLNSLS ASTGSILFGG VDTEHFVGEL
QTLPIQMHAD IHSEFLVTLT DVTLGSTTMG SDLAIAVLLD SGSSLSYLPD AMVKEIYSMV
GAVYQEEQAV AFVPCALRQS PANMTFTFSK PKITVPISEL VLDLFKITGR QPTFSNGAPA
CLFGLAPAGA GTHVLGDTFM RSAYIVYDME NNEISLAQTR FNTSRSNILE IGTGRSSVPS
AITVAEPVAA THGLRGGGAA AAHSTAHVLT PLAGPFLAGV ISGILGFVSF FI
//
