BLH1_YEAS8
ID BLH1_YEAS8 Reviewed; 483 AA.
AC C8ZFZ7;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Cysteine proteinase 1, mitochondrial;
DE EC=3.4.22.40;
DE AltName: Full=Bleomycin hydrolase;
DE Short=BLM hydrolase;
DE AltName: Full=Homocysteine-thiolactonase;
DE Short=HTLase;
DE Short=Hcy-thiolactonase;
DE AltName: Full=Leucine aminopeptidase 3;
DE AltName: Full=Y3;
DE Flags: Precursor;
GN Name=LAP3; Synonyms=BLH1, GAL6, YCP1; ORFNames=EC1118_1N9_1035g;
OS Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=643680;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lalvin EC1118 / Prise de mousse;
RX PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
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 (By similarity). {ECO:0000250}.
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 -!- ACTIVITY REGULATION: Inhibited by E64, a specific inhibitor of cysteine
CC proteases, N-ethylmaleimide, iodacetamide, and mercury and zinc ions.
CC {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. Binds to nucleic acids. Binds single-stranded DNA
CC and RNA with higher affinity than double-stranded DNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Cytoplasm
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial;
CC IsoId=C8ZFZ7-1; Sequence=Displayed;
CC Name=Cytoplasmic;
CC IsoId=C8ZFZ7-2; Sequence=VSP_038915;
CC -!- PTM: The N-terminus of isoform Cytoplasmic is blocked. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAY82370.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; FN393086; CAY82370.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; C8ZFZ7; -.
DR SMR; C8ZFZ7; -.
DR MEROPS; C01.085; -.
DR EnsemblFungi; CAY82370; CAY82370; EC1118_1N9_1035g. [C8ZFZ7-2]
DR HOGENOM; CLU_038600_0_1_1; -.
DR Proteomes; UP000000286; Chromosome XIV, Scaffold EC1118_1N9.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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 InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR004134; Peptidase_C1B.
DR PANTHER; PTHR10363; PTHR10363; 1.
DR Pfam; PF03051; Peptidase_C1_2; 1.
DR PIRSF; PIRSF005700; PepC; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Alternative initiation; Cytoplasm; DNA-binding; Hydrolase; Mitochondrion;
KW Protease; Thiol protease; Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 31..482
FT /note="Cysteine proteinase 1, mitochondrial"
FT /id="PRO_0000393308"
FT PROPEP 483
FT /note="Removed in mature form; by autocatalysis"
FT /evidence="ECO:0000250"
FT /id="PRO_0000393309"
FT ACT_SITE 102
FT /evidence="ECO:0000250"
FT ACT_SITE 398
FT /evidence="ECO:0000250"
FT ACT_SITE 421
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform Cytoplasmic)"
FT /evidence="ECO:0000305"
FT /id="VSP_038915"
SQ SEQUENCE 483 AA; 55483 MW; BF92A6049F98DD3D CRC64;
MLPTSVSRSL YLKTFRSHLL RAPQIVLKRM SSSIDISKIN SWNKEFQSDL THQLATTVLK
NYNADDALLN KTRLQKQDNR VFNTVVSTDS TPVTNQKSSG RCWLFAATNQ LRLNVLSELN
LKEFELSQAY LFFYDKLEKA NYFLDQIVSS ADQDIDSRLV QYLLAAPTED GGQYSMFLNL
VKKYGLIPKD LYGDLPYSTT ASRKWNSLLT TKLREFAETL RTALKERSAD DSIIVTLREQ
MQREIFRLMS LFMDIPPVQP NEQFTWEYVD KDKKIHTIKS TPLEFASKYA KLDPSTPVSL
INDPRHPYGK LIKIDRLGNV LGGDAVIYLN VDNETLSKLV VKRLQNNKAV FFGSHTPKFM
DKKTGVMDIE LWNYPAIGYN LPQQKASRIR YHESLMTHAM LITGCHVDET SKLPLRYRVE
NSWGKDSGKD GLYVMTQKYF EEYCFQIVVD INELPKELAS KFTSGKEEPI VLPIWDPMGA
LAK
