ID G0VHE0_NAUCC Unreviewed; 456 AA.
AC G0VHE0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
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 Name=NCAS0G03590 {ECO:0000313|EMBL:CCC71246.1};
GN OrderedLocusNames=NCAS_0G03590 {ECO:0000313|EMBL:CCC71246.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC71246.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC71246.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) 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; HE576758; CCC71246.1; -; Genomic_DNA.
DR RefSeq; XP_003677598.1; XM_003677550.1.
DR AlphaFoldDB; G0VHE0; -.
DR STRING; 1064592.G0VHE0; -.
DR MEROPS; C01.085; -.
DR GeneID; 11527741; -.
DR KEGG; ncs:NCAS_0G03590; -.
DR eggNOG; KOG4128; Eukaryota.
DR HOGENOM; CLU_038600_0_1_1; -.
DR InParanoid; G0VHE0; -.
DR OMA; DDGGWWQ; -.
DR OrthoDB; 45184at2759; -.
DR Proteomes; UP000001640; Chromosome 7.
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:UP000001640};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|PIRNR:PIRNR005700}.
FT ACT_SITE 75
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 371
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 394
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
SQ SEQUENCE 456 AA; 52630 MW; 01882777BA6A23DB CRC64;
MQRSLDSATL AQWTQELRTD PTYQLSSTVL KNGNADDLLL DKLRLLQIDQ PVYNITVTDL
DKVAPITNQK ASGRCWLFAA TNELRINIAK RLNLKEFELS QGYLFFYDKL EKANYFLDQI
IDTCDEDEDS RLVQYLLSAP VQDGGQYSMF FNLVRKYGLV PKAIYDDRNY SITASRKLNG
LLTTKLREFA EVLRDAIAQK KDVAPLRNSM QKEIYKLLSM FLNIPSVQPN ETFKWSYTDK
DKKVQTLECT PLEFASKQAG LNLQDSLKTP VSLINDPRHE YGRLIKIDRL GNVIDGDDVL
YLNVDNETLS KLVVKRLQND KAVFFGSHTP KYMNKEHGIM DIQLWNYEAI DYNLNQSKSS
RIKYHESMMT HAMLIRACNV EEGEQLPSRY CVENSWGKDS GRDGLYLMTQ EYFEEYCFQI
VVDLDELPKD LAEKFTSKEE KPIVLPIWDP MGALAD
//
