ID C9SI68_VERA1 Unreviewed; 372 AA.
AC C9SI68;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=VDBG_04750 {ECO:0000313|EMBL:EEY18641.1};
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN [1] {ECO:0000313|Proteomes:UP000008698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC {ECO:0000313|Proteomes:UP000008698};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; DS985218; EEY18641.1; -; Genomic_DNA.
DR RefSeq; XP_003005144.1; XM_003005098.1.
DR AlphaFoldDB; C9SI68; -.
DR GeneID; 9530363; -.
DR KEGG; val:VDBG_04750; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_744331_0_0_1; -.
DR OMA; PRFGIYY; -.
DR OrthoDB; 398606at2759; -.
DR Proteomes; UP000008698; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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:SF68; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000008698};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..372
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003001039"
FT DOMAIN 35..372
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 372 AA; 40495 MW; C427FC12E7E40E90 CRC64;
MAPPSMLLAV AAAAIPQLTA AVSVDLPITY YNSYSSVDVE IGKPSKTYRL HPDTGSSTTW
VVDKGCAEWC HNNTPTADIG YLGGYVAGDV VNDKFMVNNH TWRQPFLSTY YSDWNNMPTD
GFMGLAFDSI IVGDANNVLT MLMPNLDEPR FGIYLGDNDA ADKPGLLTIG SSKESEYSKA
ELTKIPIVKG PDGRYDVWRS TIKGVSFKGF DSSWSISIEF STPGVSEPIV LTASGEDLRK
PGFPAAPDAC WPPFEDSGAE GFTLIGTPFL RNFYTVWDFG AKDETDFEPT LGFAHLLEES
SVKFEVTNTS ANRRGAELIA MDTTSDFSPY RADGKLFRFV CVVTGASQPV GQAIIEGVWE
YVCSSKIPSS QC
//
