ID U7PLD7_SPOS1 Unreviewed; 527 AA.
AC U7PLD7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=HMPREF1624_08055 {ECO:0000313|EMBL:ERS95539.1};
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:ERS95539.1, 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; KI440853; ERS95539.1; -; Genomic_DNA.
DR AlphaFoldDB; U7PLD7; -.
DR MEROPS; A01.081; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_035052_1_0_1; -.
DR OrthoDB; 4940213at2759; -.
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 CDD; cd05471; pepsin_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; 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:SF47; ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01220)-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 Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000018087};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..527
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004686335"
FT DOMAIN 142..513
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 95..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 402
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 527 AA; 54930 MW; 1F318AD70AC3B3F7 CRC64;
MAVLSVLLGS LAAASVVAGA PASSSASSET PHYGSHHRSG NHVLVSRAPA VALAEHTLPL
VRHVPGAQGR RARPRPWHNP DRAVWPLHAT WHEAVAAGGS PNGSNATNGT STSTSTTNSS
SSTPPAAISS GLAPSANHDI EYLTSVVAGT NNLSLVVDTG SSDTWFVRQG FSCIDPQYHE
PTLVAACRFG PEFKGDFPGG AIANQHLSVA YGSANGPFMQ GVLGYADLTV AGLTTRNQTI
GLGTRGFWDG DGISSGLLGL GLPGLTNALP GAVSTSRAGD LADQLRTPVE YSPLVATMAS
SSSGNNVTQF SLALSRDPQQ SFLAFGGAPA HIAVDPALGW VTTPIVKTVM RSVSASGSAS
RQARYMYYTI SIESLQYNSS LLRRSTLTMD QQPLRDVPII VDSGTTLNLF SYDVALAINQ
LYTPRAQFDP DQGAWIVRCD ATPPSLGVQI GDKTIWTDPK SMILPPPPGA GVGENLCLSG
VGARSELPYI LGDTFMQQLV TVFDVANKEI KFAKRLGTTA AAAPKSA
//