ID K1VWX9_TRIAC Unreviewed; 513 AA.
AC K1VWX9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Endopeptidase {ECO:0000313|EMBL:EKD01343.1};
GN ORFNames=A1Q2_04369 {ECO:0000313|EMBL:EKD01343.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD01343.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKD01343.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD01343.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
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:EKD01343.1}.
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DR EMBL; AMBO01000320; EKD01343.1; -; Genomic_DNA.
DR AlphaFoldDB; K1VWX9; -.
DR STRING; 1220162.K1VWX9; -.
DR MEROPS; A01.078; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_1_2_1; -.
DR InParanoid; K1VWX9; -.
DR OMA; ATMHASA; -.
DR OrthoDB; 1203010at2759; -.
DR Proteomes; UP000006757; 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:SF92; 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:UP000006757};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..513
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003854082"
FT DOMAIN 106..455
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 197..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 124
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 339
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 513 AA; 54847 MW; 9E73363E92D16920 CRC64;
MRTTTTAAAL LALAAATHAA PTAEAEKLNV IGGEPVAVPL VHRRTGQYRT PEERMAWAEG
QAMAMRAKYG SFLNEEERSL LKRTLHEKRQ NVGSLPLVDI GIDSTYAGQI DIGTPAQPFY
CIMDTGSSDL WVLDDDCNDC EGISTFKLHE SSTLQETNDP FGVKYGSGMV KGGIVRDTVT
MGGFTVQEQT FGVVNYTKQT NPTSSSGESG GSQPGQESSG PASGIIQAPI SGLMGLAWKA
IANSGATPMW QTLAASKWQQ KEFGVFMVRH RGDEWARQFE ENGGQILFGG TNNTLYKGDL
NYVSIPDQDK DYWRLKLEGI NVQGNDLGYS TEWASAAIDT GTTLIGAPPD MVRAVFDQIE
GSRPLASVSP TMAGYYAYPC ETRVELLLKF GNKWYPVSNE DFNLGSIERT GTWCMGAVFE
FGASQNSPVN WIIGAAFLKN VYTAFRYEPA AVGFAELADG VQNSDANTSS WTTSGGGGVI
SGDGKSQGGH SDAGRALPSL LAVIAVALAA ALL
//
