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Database: UniProt
Entry: A0A286ULH3_9AGAM
LinkDB: A0A286ULH3_9AGAM
Original site: A0A286ULH3_9AGAM 
ID   A0A286ULH3_9AGAM        Unreviewed;       544 AA.
AC   A0A286ULH3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Cysteine proteinase 1, mitochondrial {ECO:0000256|ARBA:ARBA00016900};
DE            EC=3.4.22.40 {ECO:0000256|ARBA:ARBA00012465};
DE   AltName: Full=Bleomycin hydrolase {ECO:0000256|ARBA:ARBA00030627};
DE   AltName: Full=Homocysteine-thiolactonase {ECO:0000256|ARBA:ARBA00032353};
DE   AltName: Full=Leucine aminopeptidase 3 {ECO:0000256|ARBA:ARBA00031564};
DE   AltName: Full=Y3 {ECO:0000256|ARBA:ARBA00031859};
GN   ORFNames=PNOK_0293200 {ECO:0000313|EMBL:PAV20305.1};
OS   Pyrrhoderma noxium.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Hymenochaetales; Hymenochaetaceae; Pyrrhoderma.
OX   NCBI_TaxID=2282107 {ECO:0000313|EMBL:PAV20305.1, ECO:0000313|Proteomes:UP000217199};
RN   [1] {ECO:0000313|Proteomes:UP000217199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FFPRI411160 {ECO:0000313|Proteomes:UP000217199};
RA   Chung C.-L., Lee J.T., Akiba M., Lee H.-H., Kuo T.-H., Liu D., Ke H.-M.,
RA   Yokoi T., Roa M.B., Lu M.J., Chang Y.-Y., Ann P.-J., Tsai J.-N.,
RA   Chen C.-Y., Tzean S.-S., Ota Y., Hattori T., Sahashi N., Liou R.-F.,
RA   Kikuchi T., Tsai I.J.;
RT   "The Genomic Landscape Of Tree Rot In Phellinus noxius And Its
RT   Hymenochaetales Members.";
RL   bioRxiv 0:0-0(2017).
CC   -!- FUNCTION: The normal physiological role of the enzyme is unknown, but
CC       it is not essential for the viability of yeast cells. Has
CC       aminopeptidase activity, shortening substrate peptides sequentially by
CC       1 amino acid. Has bleomycin hydrolase activity, which can protect the
CC       cell from the toxic effects of bleomycin. Has homocysteine-
CC       thiolactonase activity, protecting the cell against homocysteine
CC       toxicity. Acts as a repressor in the GAL4 regulatory system, but this
CC       does not require either the peptidase or nucleic acid-binding
CC       activities. {ECO:0000256|ARBA:ARBA00025347}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by
CC         hydrolysis of a carboxyamide bond of beta-aminoalanine, but also
CC         shows general aminopeptidase activity. The specificity varies
CC         somewhat with source, but amino acid arylamides of Met, Leu and Ala
CC         are preferred.; EC=3.4.22.40;
CC         Evidence={ECO:0000256|ARBA:ARBA00000423};
CC   -!- SUBUNIT: Homohexamer. Binds to nucleic acids. Binds single-stranded DNA
CC       and RNA with higher affinity than double-stranded DNA.
CC       {ECO:0000256|ARBA:ARBA00026080}.
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:PAV20305.1}.
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DR   EMBL; NBII01000003; PAV20305.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286ULH3; -.
DR   STRING; 2282107.A0A286ULH3; -.
DR   InParanoid; A0A286ULH3; -.
DR   OrthoDB; 45184at2759; -.
DR   Proteomes; UP000217199; Chromosome 3.
DR   GO; GO:0070005; F:cysteine-type aminopeptidase activity; IEA:InterPro.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00585; Peptidase_C1B; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR004134; Peptidase_C1B.
DR   PANTHER; PTHR10363; BLEOMYCIN HYDROLASE; 1.
DR   PANTHER; PTHR10363:SF2; BLEOMYCIN HYDROLASE; 1.
DR   Pfam; PF03051; Peptidase_C1_2; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PAV20305.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217199};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
SQ   SEQUENCE   544 AA;  60856 MW;  3C11F20C885EFACC CRC64;
     MSLRDFFLVE DDLNCCCPQC ISCHIRPRNR TRARSNSCTG IRVTSMGAAQ STSAQSVSVA
     SSSLSEKVPA QEYSVQPSLK AATPLSPNGS ISLKNVAQWE EAAVDDLKVQ LARTVLVDTD
     YKSALATRSA RIADPHVFNV QLDFKTGPVT NQKSSGRCWL FATTNVLRHS IMQKLSLKEF
     QLSQSYLFFW DKLNKCNYYL ELSIETADLA LDDRIVNFLS NDLISDGGQW DMAVNLLETY
     GVVPQPIYPE SYSSSASSNL NKLLKLKLRE HALILRRLSA SLKGVTDKEQ ALSSIRAKKE
     ELMSEIWTIM TATLGVPPRP DDAFTWEYLD GDGKFRSWTG TPLEFYKAFT SRQYPPTDSF
     SIINDPRNEY KKLYTVDKLG NIWGGREVLY VNTHIDDLKN TIVKMLKAGQ PAFFGCDVNQ
     FSDSRGGILD TGLHKAAIEN AFNITLGLTK AERLEMNESS MTHAMVITAA HVDASGRPVR
     FRVENSWGPD SGEKGYLVMT DKWFDEFVYQ VVVPKSLAPK ELVKVFESRE KIVLPPWDPM
     GSLA
//
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