ID K1V8X4_TRIAC Unreviewed; 725 AA.
AC K1V8X4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:EKD00455.1};
GN ORFNames=A1Q2_05292 {ECO:0000313|EMBL:EKD00455.1};
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:EKD00455.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKD00455.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD00455.1,
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:EKD00455.1}.
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DR EMBL; AMBO01000341; EKD00455.1; -; Genomic_DNA.
DR AlphaFoldDB; K1V8X4; -.
DR STRING; 1220162.K1V8X4; -.
DR eggNOG; ENOG502SUZ7; Eukaryota.
DR HOGENOM; CLU_024069_0_0_1; -.
DR InParanoid; K1V8X4; -.
DR OMA; SMCLAWP; -.
DR OrthoDB; 1696312at2759; -.
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:SF74; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00026; Asp; 2.
DR SUPFAM; SSF50630; Acid proteases; 2.
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..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..725
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003854003"
FT DOMAIN 65..596
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 195..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 73981 MW; 87B3AC673C27335A CRC64;
MLVPLSTLAI AGLVAAELGD PQSLRPHPRR ANVPRADIGV GGVDLALHKR EVDPAVVKRG
LNGSVIALGA IHNPSRAYPL QLDTASADLL IASTKCGKEC PAPTKENPYY DMMSSDFKEV
NGNSTYWRTQ YADKSFASGF VARDQVMIAA HLVDDQVIGL ITATNMSLPE QDISGVLGLG
FPRLSTLGRA LLQDSVPSSD RSPLTSSAAP AGASSPSGSA SAPSESGASG SAVASPSSGM
ERRQESSSDS SGTASVTSSS APAAAVPSSS AAYMPTLLEN LITTPSIPYP AFALALSPPL
NASQATALKS LHPEPAPRYS LSSGSLTLGG VSALYVSDDP STGRTVNDIE WWPVVPFGRA
SNGVSRSNAT TIDVSAMSTS ATPAAAGEPA SASGSGASAP SSPSASSSGS SAPGSNLLQD
NGMGAIGTPG KRGLPKTPAE LESEAYLYWA LQLSKVSVNG TGFALNSTYA NLGVPPIALL
DVGTNGIYGP EDDVAKLFSG IKDARMVSTG QWAVPCDTRV TLGFSFGENG GSVEIPPSDW
IYAAVPESSM CLAWPVAVPA TGDGLDWQLG TPFLKNVYTV FSYGVDGGQP PQIGFLPLTD
KANGTQPISA ATPSQTVNTK LPHVLLSPPN YPTPSYAFST PVPTLGVPQA LGLGNASAYP
SAAVPVVSIP VPKASASDDH QAIPGWPGDS SQATVENAAT KRQTLPAASV ALPSILIVLS
HLLLL
//