ID K1VXR2_TRIAC Unreviewed; 824 AA.
AC K1VXR2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 28-JUN-2023, entry version 47.
DE SubName: Full=Endopeptidase {ECO:0000313|EMBL:EKD04292.1};
GN ORFNames=A1Q2_01323 {ECO:0000313|EMBL:EKD04292.1};
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:EKD04292.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKD04292.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD04292.1,
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, ECO:0000256|RuleBase:RU000454}.
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:EKD04292.1}.
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DR EMBL; AMBO01000227; EKD04292.1; -; Genomic_DNA.
DR AlphaFoldDB; K1VXR2; -.
DR STRING; 1220162.K1VXR2; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_343608_0_0_1; -.
DR InParanoid; K1VXR2; -.
DR OMA; STACTTH; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000006757; 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; 2.60.40.1960; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 4.
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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 2.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 2.
DR PROSITE; PS00141; ASP_PROTEASE; 4.
DR PROSITE; PS51767; PEPTIDASE_A1; 2.
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:UP000006757}.
FT DOMAIN 236..546
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 537..824
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 254
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 433
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 824 AA; 90248 MW; 560CA085D780F994 CRC64;
MVCPFARSSD RRRRAIRVDH TGRAVRLEAP LMLRLFHELK FESIWHMHEL GGRTRAGTDR
AVHVLEQAGC TLRMGDELIA EGSHKPSSLS SILLITDGYI PSVDTHCPYH PPPLLDINPP
ALLDVMKTAA LIAVLAALGS VDAAVHRMKL QKRDPASLLD HDVAKEVEFL MQKHAGAFMQ
DTAQKVLGGF GGAGRPLRTN KGDGERLWAQ MIEEENENAL KGGHGVPLSN YMNAQYYAPI
TIGTPPQEFG VVLDTGSSNL WVPSVQCSSI ACFKYDNSQS STYKANGSEF AIRYGSGSLE
GFVSEDTLEI AGLKVKDQLF AEATKEPGMA FVFGKFDGIL GLGYNTISVN QIPPPFYNMI
DQNLLDEKVF SFRLGSSEDD GGECIFGGYD KKWSDEKPIY VPVRRKGYWE VELEGIKFGD
EELPLENTGA AIDTGTSLIA LPTDIAEILN KEIGAEKSWN GQYTVDCSKV PSLPDLTFNF
GGKKFPIKGE DYVLGRPLRT NKGDGERLWA QMIEEENENA LKGGHGVPLS NYMNAQYYAP
ITIGTPPQEF GVVLDTGSSN LWVPSVQCSS IACFKYDNSQ SSTYKANGSE FAIRYGSGSL
EGFVSEDTLE IAGLKVKDQL FAEATKEPGM AFVFGKFTVS FGLGYNTISV NQIPPPFYNM
IDQNLLDEKV FSFRLGSSED DGGECIFGGY DKKWSDEKPI YVPVRRKGYW EVELEGIKFG
DEELPLENTG AAIDTGTSLI ALPTDIAEIL NKEIGAEKSW NGQYTVDCSK VPSLPDLTFN
FGGKKFPIKG EDYVLNAGGT CISAFMGMDI PPPMGPIWII GDAL
//