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Database: UniProt
Entry: A0A0H2S5R1_9AGAM
LinkDB: A0A0H2S5R1_9AGAM
Original site: A0A0H2S5R1_9AGAM 
ID   A0A0H2S5R1_9AGAM        Unreviewed;       476 AA.
AC   A0A0H2S5R1;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Cysteine proteinase 1, mitochondrial {ECO:0000256|ARBA:ARBA00016900, ECO:0000256|PIRNR:PIRNR005700};
DE            EC=3.4.22.40 {ECO:0000256|ARBA:ARBA00012465, ECO:0000256|PIRNR:PIRNR005700};
GN   ORFNames=SCHPADRAFT_865050 {ECO:0000313|EMBL:KLO19552.1};
OS   Schizopora paradoxa.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Hymenochaetales; Schizoporaceae; Schizopora.
OX   NCBI_TaxID=27342 {ECO:0000313|EMBL:KLO19552.1, ECO:0000313|Proteomes:UP000053477};
RN   [1] {ECO:0000313|EMBL:KLO19552.1, ECO:0000313|Proteomes:UP000053477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KUC8140 {ECO:0000313|EMBL:KLO19552.1,
RC   ECO:0000313|Proteomes:UP000053477};
RG   DOE Joint Genome Institute;
RA   Min B., Park H., Jang Y., Kim J.-J., Kim K.H., Pangilinan J., Lipzen A.,
RA   Riley R., Grigoriev I.V., Spatafora J.W., Choi I.-G.;
RT   "Complete genome sequence of Schizopora paradoxa KUC8140, a cosmopolitan
RT   wood degrader in East Asia.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has aminopeptidase activity, shortening substrate peptides
CC       sequentially by 1 amino acid. Has bleomycin hydrolase activity, which
CC       can protect the cell from the toxic effects of bleomycin. Has
CC       homocysteine-thiolactonase activity, protecting the cell against
CC       homocysteine toxicity. {ECO:0000256|PIRNR:PIRNR005700}.
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         ECO:0000256|PIRNR:PIRNR005700};
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   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|PIRNR:PIRNR005700}.
CC       Cytoplasm {ECO:0000256|PIRNR:PIRNR005700}.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
CC       {ECO:0000256|PIRNR:PIRNR005700}.
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DR   EMBL; KQ085886; KLO19552.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H2S5R1; -.
DR   STRING; 27342.A0A0H2S5R1; -.
DR   InParanoid; A0A0H2S5R1; -.
DR   OrthoDB; 45184at2759; -.
DR   Proteomes; UP000053477; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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   PIRSF; PIRSF005700; PepC; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR005700};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005700};
KW   Mitochondrion {ECO:0000256|PIRNR:PIRNR005700};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR005700};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053477};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW   ECO:0000256|PIRNR:PIRNR005700}.
FT   ACT_SITE        80
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT   ACT_SITE        390
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT   ACT_SITE        412
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
SQ   SEQUENCE   476 AA;  54154 MW;  93FDEF749F5BC282 CRC64;
     MPTSNPISED GSITTFNIAG WEGDVSKNDK IKLSRTILVD ADFKVALVSR SKRVEDTHVF
     NHQIKLKTGP ITNQKASGRC WLFATTNILR YSIMEKLNLK EFELSQSYVL FWDKLNKANF
     YLENIIDTAD LPLDDRMVDY LSKNLINDSS QWDMAVNIIE ARGCTEGIVP QSIYPESFSS
     SSSRNLNALL RSKLREHALI LREYTTSLHQ RKPGLEKEDV VVCARAKKET LMKEVWAILT
     ITLGIPPNPD EKFTWDYYDK DDKSQTWTGT PVEYYKTFTS TDYPPSESFS LINDPRNSYK
     KLYSIDRFGN VWGGRSALYV NTEIDDLKAA VIKMIKAGEP VFFGCDYGQF SDTASGIMDL
     DLHQFETAFD ISFGLTKAQR LQLNESQMTH AMVISGVHLD ASEKPVRYKV ENSWGPNVGN
     KGYFVMTDAW FEQFVYQVVV PRSLAPKELV KVYDDGEKIM LPPWDPMGSV AESRAK
//
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