ID U7PU02_SPOS1 Unreviewed; 545 AA.
AC U7PU02;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=HMPREF1624_05027 {ECO:0000313|EMBL:ERS98244.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS98244.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KI440846; ERS98244.1; -; Genomic_DNA.
DR AlphaFoldDB; U7PU02; -.
DR STRING; 1391915.U7PU02; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_4_1; -.
DR OrthoDB; 2686046at2759; -.
DR Proteomes; UP000018087; 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: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; 2.
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 Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000018087};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..545
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004685725"
FT DOMAIN 61..455
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 268..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 79
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 297
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 545 AA; 54747 MW; C6AE861492A67B2F CRC64;
MASRIANALT LLLAAAHVLA AETANGPVAL SLSATQAEGR TNGLSRRNAD IPLTNLSTVA
YLVTLSIGTP GQKVRVVVDT GSDELWVNPS CNSSSSASSG RSNGVTGVDQ KECLASGRYD
PGSSSTSINL NKSGKIQYAL GSVALDYYND TVAQPDSGVT LKSLQFGVAR QSEDLYEGIL
GLGFAENHNY TTFVSAAAEQ GAAGGPGKVF SIGLASANEL NAGTLVLGGL DTNRFTGPMM
GVPILPPPPS DTLVRYWVKL DSIGLTGSTV SSSSGTSSGS NNASKTYPNS GAPIVLDTGS
TLSILPFSIL AALAKDLGAS MTQGSRNEYA RLTGRAPDAA VNAAIFPVPC TALGLGADVH
SKENLAGLKR TVDFSFNNGA ALVRVPLSEF AIQITTDMCV LGGIAMDDGL SSSSSSGPGT
GIPQPDAGAT LLLGATFLRG AYVVYDQAAN SVFMAPYAHC NAGTANLQPL ASAKAGAAAG
FTGACSVADS LYGGGAGGFS AAAAATAPSS GDSGEDKKNA GRRSSSVSTI SLVAAVLSVL
AFLCT
//