ID A0A093Z1Y4_9PEZI Unreviewed; 506 AA.
AC A0A093Z1Y4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, 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=V492_05730 {ECO:0000313|EMBL:KFY08983.1};
OS Pseudogymnoascus sp. VKM F-4246.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY08983.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY08983.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY08983.1,
RC ECO:0000313|Proteomes:UP000029299};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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}.
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:KFY08983.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPJU01002037; KFY08983.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093Z1Y4; -.
DR STRING; 1420902.A0A093Z1Y4; -.
DR MEROPS; C01.085; -.
DR HOGENOM; CLU_038600_0_1_1; -.
DR Proteomes; UP000029299; 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:UP000029299};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|PIRNR:PIRNR005700}.
FT ACT_SITE 123
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 426
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 448
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
SQ SEQUENCE 506 AA; 56439 MW; 0AD80A3B31FFBF0F CRC64;
MGAQPSRPSH DDYTEKQAVE RMRQLALASP KDRRSYESEV DEKQRLRYVA DDTASLSLGD
VWRWQEKLMD DPKNRLALSA LSAADPKTVL QNRNVLTDNQ HIFNVKIPFE GGPITNQNSS
GRCWIFAATN VFRVALMKRH NLEAFELSQS YLFFWDKLEK ANYFLEQILD TADEDVEGRL
VQRLLQSPVG DGGQWDMIVN LVNKYGLVPQ VLYPDSFNAS HSGTINSLLT TKLRENALTL
RSLASTSSLS TIRSAKAKMM REVQLVLTLT LGPPPSPDSE FTWQYLDSSG AAKSLTTTPL
AFASELSSTP SIRTIGVDVN SMFSLINDPR NPPNTLLTVS RLGNVFGSTS RPVTYVNVAM
PTMKAAIIGM LKADIPVFFG CDVGQSSERA KGVMATGLVD FELGFNVKLG LTKRDRILSG
ESKMTHAMVL TAVHLDAEGK SVRWRVQNSW GEAQGDKGWF VMSDEWMDEF TYQAVVDPRF
VSKEVRDVLK QDPKVLPLWD PMGELA
//
