ID A0A0F4ZBD7_9PEZI Unreviewed; 495 AA.
AC A0A0F4ZBD7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=TD95_005437 {ECO:0000313|EMBL:KKA27605.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA27605.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA27605.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA27605.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-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:KKA27605.1}.
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DR EMBL; LAEV01001623; KKA27605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4ZBD7; -.
DR MEROPS; A01.077; -.
DR OrthoDB; 3087283at2759; -.
DR Proteomes; UP000033483; 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:SF51; 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; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000033483};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..495
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002482514"
FT DOMAIN 112..415
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 130
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 311
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 143..148
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 346..377
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 495 AA; 52064 MW; 7AC2987B306A4403 CRC64;
MRSPFLLAQA LALSSSASAF YIWKPCIEDG SCVDKTKIDI ARQRVTSRNK GLTLELVQRA
RPASSPLSRR LEAIRAADLE KRNTNSYDIM TAETPSYKHS VGIDQDGNDL SYFISVSIGS
NKTQMYMLVD TGAGSTWIMG DTCSTDACKM HSSFSPSEST TMTELDKTFS IAYGSGSVSG
RNVEDSLTVG DISVTMNFGL ANYTSSDFES FPFDGILGLS LNTGSTDSFT HKLNASSDIT
EKVFSVFLAR ASSGVNNGEL TLGGINPSRY TGAITYTDLE SASSGDWSIP MDSVSIGGKD
VGISSRTGYI DTGTSYIFGP PEDVKLMHSH IAGANTTDGS RWTVPCDTSE DLALSFGGKA
WTLQKSDWIS TARDGTCYSY VMGVEVVSNG WLLGDSFIKN VYTVFDMAER RIGFAAAKHD
SSSTASASGS TTIGGTAAQE TGGIGVISSN SASATAEAAH TTSPTSSSKS SAATSGLPIS
VAAVASSLLI SLMSL
//
