ID U4LK24_PYROM Unreviewed; 492 AA.
AC U4LK24;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=PCON_07046 {ECO:0000313|EMBL:CCX29720.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX29720.1};
RN [1] {ECO:0000313|EMBL:CCX29720.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX29720.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX29720.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
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; HF935352; CCX29720.1; -; Genomic_DNA.
DR AlphaFoldDB; U4LK24; -.
DR STRING; 1076935.U4LK24; -.
DR MEROPS; C01.085; -.
DR eggNOG; KOG4128; Eukaryota.
DR OMA; QSYTFFW; -.
DR OrthoDB; 45184at2759; -.
DR Proteomes; UP000018144; 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; 2.
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; 2.
DR PIRSF; PIRSF005700; PepC; 3.
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 Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|PIRNR:PIRNR005700}.
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 109
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 413
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 434
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
SQ SEQUENCE 492 AA; 54802 MW; DC733F2619B763E9 CRC64;
MGNSHSKRSK TITYPVARKS KPAPSRDSDV TLTDSICDPS PTVNISNVCK WEDKLLSDPK
NRLALGALTT HAATAILQNP SILLQDTHIF SNKLDMGAPV TNQRSSGRCW LFAATNVFRV
GLIRKYKLNG FELSQSYLFF WDKLEKANFF LEQIIDTVKE PLDSRLIQYL MHGPVGDGGQ
WDMVVNLVEK YGLVPQAIYP DSFNAKASGR INWLITAKLR EAALHLRQLA NAKEKVSSDL
IYRYKAKVMQ EIYGVLVLSL GAPPKPNDTF TWIFVDKDQK HQTITTTPLE FYHANVGAVS
NLATLSQPLH IPALTNLAPA GGRGGVKNRF SLVNDPRNPY MRLLTVERLG NIYGGKGVEQ
ARPSLFGCDV GKYSDPQKGI LDTAQFDYEL GFNITLNLTK AQRLETGESS MTHAMVLSGV
NLVDDKPTKW RVENSWGDAN GDKGYLVMSD AWFDEFVYQI VVSPDFVDEE VVKVLDQDPI
TLPIWDPMGS LA
//
