ID A0A316VSL6_9BASI Unreviewed; 549 AA.
AC A0A316VSL6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Cysteine proteinase 1, mitochondrial {ECO:0000256|ARBA:ARBA00016900};
DE EC=3.4.22.40 {ECO:0000256|ARBA:ARBA00012465};
DE AltName: Full=Bleomycin hydrolase {ECO:0000256|ARBA:ARBA00030627};
DE AltName: Full=Homocysteine-thiolactonase {ECO:0000256|ARBA:ARBA00032353};
DE AltName: Full=Leucine aminopeptidase 3 {ECO:0000256|ARBA:ARBA00031564};
DE AltName: Full=Y3 {ECO:0000256|ARBA:ARBA00031859};
GN ORFNames=IE81DRAFT_305279 {ECO:0000313|EMBL:PWN40360.1};
OS Ceraceosorus guamensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=1522189 {ECO:0000313|EMBL:PWN40360.1, ECO:0000313|Proteomes:UP000245783};
RN [1] {ECO:0000313|EMBL:PWN40360.1, ECO:0000313|Proteomes:UP000245783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4658 {ECO:0000313|EMBL:PWN40360.1,
RC ECO:0000313|Proteomes:UP000245783};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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 -!- 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}.
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DR EMBL; KZ819420; PWN40360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316VSL6; -.
DR STRING; 1522189.A0A316VSL6; -.
DR InParanoid; A0A316VSL6; -.
DR OrthoDB; 45184at2759; -.
DR Proteomes; UP000245783; Unassembled WGS sequence.
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 SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PWN40360.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000245783};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 61461 MW; B1F702BED76C35D5 CRC64;
MGSSASKPLP ASGEMSEKSA ATQSLERQLG RSGRASARPD ASLNLHHSTD RSYKIQASRL
VAHTAAAPQQ ESARDAGKAS SNITPTLLQY WSDTALKTTS AKLAARTLHN EQLALALRDR
RTEIEMGNHV FNVKVDLEGT PVCNQKSSGR CWLFATLNLL RVHAMKEYDV PALELSQSYL
HFYDKLEKAN TFLENTIDLA SEALDSRLYG YLKGDPVNDG GQWDMVVNLL RVYGIVPQVI
FPESFNSSNS DKINWLVTFQ LRQFALELRS LISQLRSQEG GARSLSPASE HSIVQQVRLT
KERQMKKIFE ILTIANGAAP PSPEQEFTWQ YYDSKGKYQE RRFTPKSFLQ SLKKRFDLDN
ACSLVNDPRA EEQKLITIDR LQNVWGARPV SYVNTSSQVM KESVIKSLRS NQAVFFGCDV
GQFSHTASGV MCPSLYQTGV EEAFDISLNL SKAERLQMGE SLMTHAMVIT GVQVDADGKP
TRYRVENSWS ETAGQKGYMI MSDAWFDQYV FQVVVRKQDM PAALWQLFDA GVNEETIVYP
PYDPFGSLA
//
