ID A0A1V8U3V9_9PEZI Unreviewed; 1988 AA.
AC A0A1V8U3V9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=B0A51_14963 {ECO:0000313|EMBL:OQO18103.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO18103.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|Proteomes:UP000192386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
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 -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|RuleBase:RU003435}.
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:OQO18103.1}.
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DR EMBL; NAEU01000932; OQO18103.1; -; Genomic_DNA.
DR STRING; 1974281.A0A1V8U3V9; -.
DR Proteomes; UP000192386; 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:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06455; M3A_TOP; 1.
DR CDD; cd00585; Peptidase_C1B; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR024080; Neurolysin/TOP_N.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
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 Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000192386};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zinc {ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 495..986
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1305..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1414..1445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1988 AA; 220366 MW; E98D7E730CB6C3A9 CRC64;
MQLLQSERQL AHDGAHPDHK VDPQDGKCPS NSSYRVEHAP TFLHCDAFAS LTTHPDYASE
SFEVIRLRES IGGGRIVFDP PGDGASISLQ IAKLPFASHS RLPAAAIHCA TLALLRGSIQ
LGTIFIWAFS RSMTRAKGTG WQDSEAEKQN GIGKVLVQYT APVIPKSTAE PFDWRNFPVQ
SDIGPIFGIT SGSCFVAVPQ PRFSSPFAEP VRAGDNHDQE STPASAHHLP SVWGDVDNAT
ASTTAPSSEL VNRAHMHSSP STASDSLSNI DSVLEQLARL QQQLNEMQIS TRGLPTLDQI
VRSVDTALAE PTVIAEDDSV RSEGRARRVQ DDIVAAVTET TATFERQQIE FYAAVSIDAA
VREASQKASS LFDDFDTDAA ARQDVYDLLI AVRNSGEVLD AESQRWLTKF ISSSERNGLS
LSADGRACLK GINADLAELE RDYIARCDDT AELWCTREEL EGLDASLLDD MERGAGASEG
GIRVLLDSSL VHSILQRVHS SHTRWRVYEL AANTCQANVP LLRQVAALRL DKAKLLGHDS
YGSLRMAGRM DSDPVKMQRF FEDIVDRLAP AKDTLVSTCR EMKHDDLKSR QEVDDDNFYS
WDRPYYSEKL LSREYALDGK TISEYFALDE TVTRMLRIFE HVMSLTFQEF LKSDRDNLAS
DGNGDVFIWH DEVQVFAVWD TSSSSSASSK FLGWLHMDMH PREGKRSGFS DQPVCPAYTE
IDGGRRYAAT ALVCNFDRPT KQKPCLLSHN EVVLLFHELG HAMHDLVSQT QYARFSGASC
GDFNEAPSQM LEEWCWYPET LRLLSRHYSN LSPEYMQTWQ EDVDAGTSKA TGEPNVLPES
LIDALVRSKQ AKSAQRTLGL ANVSLFELAL TAPEAIEAVE ALDTTLLWHE TACRTFGFDM
PSEPVPAQAN QPMWFTIDGL YVYLATQVYS SDMYATIFKQ DPMSKEAGLR YRHTVLEKGG
SVDESELLKL LLGRAPSTDA LFESLGIRVP RKAEALQEGN ERQHTASPRK TAKKDANKER
NLPDILTPRR GRAVKFTYPH ESREFAHTQT GAFTIIGPAC FSHPGAAFSS NMKNLDDLLD
RTDKQDRRAH QLNSHKLAAD STGRWDLQPY LPKGVQISLP ARRKACKLLR HYEYESSDED
DDMVDESLDA QGSEDRVAAA ILRNKHRLRI LKASLTAAIA SRDTTVVRKS SQKQANGQKR
SSTPALMRAR TDSKSFEVKA SCETVTTAQI VARTDSKSPT AKPRPAARHI RELQIDMVNA
PNLRNSGAPR RMRSGHVSAD KWAVSRAVSV ARRSTQLNDQ IFEPAAPSTQ AVDDINRPKR
LSRPTEKVRL ARSPSPPVTH GHRASVKQHG DTIPVNKKER SSMVVLAFKS EQGQAKFSQL
VGSLSSSPTK FGPAHVTVTK LVSDQIVTRI ASTLGVQGSP STTSEMNDAS SRGRKRRAED
DSVTSFGVEP TKRLKLILRA HETAAAPTKR LRLVMSGDVV GQNSRSSPII TLRDENMGAA
QSAERPVRRV AIEPPPYTTL DEKFDAVQIS HGKISSITRG VSSSRDLSTV SASRVQEYIV
DILKDAKNQL SLAALSKNNI NAVLERPSTI VADRQVFNVS IPQEIAPVTN QRASGRCWIF
AATNVFRIAL SKKYRVDKFE LSQAYLFFWD KVEKANYFLE TTLLTADQDI DSRLVSTLTS
SPVGDGGQWD MLVNLVSKYG LVPQSLYPDS FNAKASRPMD SLITTKLRQD ALILRALQNK
GASVSDIAEA KQRMMQDIVR ILTITLGPPP PADKPFTWEY YDSKKSQRSV TMTPLEFAAP
IEVKKYFSLI NDPRNEYGQL LTVDLLGNVW QGQPITYVNV DRHILKSACV AMLKAGQPIF
FGSDVGKQSD SSYGIMDTDL IDYELGFDIK LGLTKAQRLQ TGESAMTHAM VLTAVHLDSD
GKPVRWRVEN SWSDTVGTDG YFVMSDKWMD EFVYQAVVHP DAVSKDVRDI LKQKPKVLPL
WDPMGALA
//
