ID K1VMN8_TRIAC Unreviewed; 404 AA.
AC K1VMN8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=A1Q2_05115 {ECO:0000313|EMBL:EKD00627.1};
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:EKD00627.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKD00627.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD00627.1,
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M28 family.
CC {ECO:0000256|RuleBase:RU361240}.
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:EKD00627.1}.
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DR EMBL; AMBO01000338; EKD00627.1; -; Genomic_DNA.
DR AlphaFoldDB; K1VMN8; -.
DR STRING; 1220162.K1VMN8; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_025286_0_0_1; -.
DR InParanoid; K1VMN8; -.
DR OMA; SGSECHY; -.
DR OrthoDB; 1384212at2759; -.
DR Proteomes; UP000006757; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR PANTHER; PTHR12147:SF59; PEPTIDASE_M28 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU361240};
KW Metal-binding {ECO:0000256|RuleBase:RU361240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000006757};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..404
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012655367"
FT DOMAIN 250..402
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 404 AA; 43118 MW; 8FAC489BFE2CD58C CRC64;
MLPLALLALL SPASAGEVIF TPDAPTPSLP SCLRSAYHGE FGGKHVYLPT SECQQEFSSG
SIVEVGSDDA IVWVTRAGLE GDDNSLIGDL FAPSARAEDG AQAVMQAPSP LSFLHADDES
FFLSIPRSDL QRLDSLLPRH LSSVVLGGPV PLDGRWEVPK SARKHLTKLI DNLTFRPEVD
DLLDELNVDV VARHVRYLTG EAEDSPIRSR HAMHPDARLA GLYIRDKMTE AGFECSGFPV
LPEAGWSPSV VCALAGQDST DQVVISAHYD SRGSFGSVYA PGANDDASGT AHLLTLGEVI
GFNKLKFEKT LVLAFWSGEE QGLLGSHAAA EYLAKQNATV TINVQADMLG YHVPGEPPQL
ALPEKIATPE ASYLVSNVSA LYAPTLVVGR TGACCTDHQS FLTG
//
