ID A0A179FX62_METCM Unreviewed; 500 AA.
AC A0A179FX62;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=VFPPC_02502 {ECO:0000313|EMBL:OAQ69957.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ69957.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ69957.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ69957.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
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:OAQ69957.1}.
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DR EMBL; LSBJ02000002; OAQ69957.1; -; Genomic_DNA.
DR RefSeq; XP_018146494.1; XM_018282143.1.
DR AlphaFoldDB; A0A179FX62; -.
DR STRING; 1380566.A0A179FX62; -.
DR GeneID; 28846137; -.
DR KEGG; pchm:VFPPC_02502; -.
DR OrthoDB; 45184at2759; -.
DR Proteomes; UP000078397; Chromosome 2.
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:UP000078397};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|PIRNR:PIRNR005700}.
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 110
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 411
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 434
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
SQ SEQUENCE 500 AA; 56267 MW; 251B22275E148C98 CRC64;
MENQSSISYR LAKDQGANDP DGQGNWKDGN SNGVSTRRTL EPLPFEVVSS FPKTLLEKSQ
NRLAVNALSS ADPSEVIKIV SSRVDNPQVF NTKIPLEGAP ITNQRATGRC WLFAATNVFR
VPIMKKRKLE SLELSQKYLF YYDKLEKSNF FLEQIIDTAE EDVDSRIVQR LLEGIVADGG
QWDMVYNLVK KYGLVPQAIY PETWSAQNSR FLKAILGTKL REFALKLRNL SRADGTTAEA
DLIHSKAEMM QEIQKILTLL LGAPPHPMQE FTWEYTDKDG KTQEVRTTPM SFAEETCYSD
LDCNINNMAS LVHDPRHDPL RLLTVSRLGN VIGGRDTTYV NVDMDTLKTA CVAMIQAGQP
IFFGCDFGKF RDKATGILDM GNFDYESGFG TDMLGMSKEE RLVMGESRLT HAMILTAVHL
CESTGKPIRW KIQNSHGPDS GSKGCYVMTD AWMDEFVYQV VIDLRFVDEK VRDVMKQDPI
VLPLWDPIGA LAQLQESTIL
//
