ID A0A1L9TIP7_9EURO Unreviewed; 480 AA.
AC A0A1L9TIP7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Cysteine proteinase 1, mitochondrial {ECO:0000256|PIRNR:PIRNR005700};
DE EC=3.4.22.40 {ECO:0000256|PIRNR:PIRNR005700};
GN ORFNames=ASPSYDRAFT_79039 {ECO:0000313|EMBL:OJJ59173.1};
OS Aspergillus sydowii CBS 593.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036612 {ECO:0000313|EMBL:OJJ59173.1, ECO:0000313|Proteomes:UP000184356};
RN [1] {ECO:0000313|Proteomes:UP000184356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 593.65 {ECO:0000313|Proteomes:UP000184356};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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 -!- 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|PIRNR:PIRNR005700};
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV878586; OJJ59173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9TIP7; -.
DR STRING; 1036612.A0A1L9TIP7; -.
DR VEuPathDB; FungiDB:ASPSYDRAFT_79039; -.
DR OrthoDB; 45184at2759; -.
DR Proteomes; UP000184356; 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: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; 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; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR005700};
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:UP000184356};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|PIRNR:PIRNR005700}.
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 120
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 401
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 422
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
SQ SEQUENCE 480 AA; 54294 MW; DF64B865A6469A05 CRC64;
MGSSYSIPER PVNEKSARGK VDTVQRSPDG HIEESATVDS PPPYQIEERE PSVSLRRLQD
WNDALLDDPK NRLAISSLAG ASYADVLSNR SAIKSDTQVF NIKVPIEGAP ITNQRSSGRC
WLFAQAYLFY WDKIEKANWF FETIIKTAHE DVSDRLVQKL LQDPVTDGGQ WDMVANLVKK
YGLVPHDVYP DNFNAQNSGK MNWLLTATLR EYAFALRKIA RSPQLKDRVQ LGNSKERFLK
EIHSLVTILL GPPPNPDEPF TWQYYNAEGK TREIRQTPLE FGRQAFSQTS RSRVSPDRLF
SLVNDPRNEY NRLLTVDKLG NVVEGQPLTY VNVQMNVLKN AAISMLKAGH PVFFGCDVGK
FSNNTSGIMD PDLVDLSLGF NISLGLNKAE RLASGESAMT HAMVITAVHV EQGRPVRWRV
ENSWGETAGD KGWFVMTDRW MDEYTFQVVM DFNLVSSEVR DVLRQEPQVL PRWDPLGVLA
//
