ID A0A1I8Q0X7_STOCA Unreviewed; 455 AA.
AC A0A1I8Q0X7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 08-NOV-2023, entry version 25.
DE RecName: Full=Bleomycin hydrolase {ECO:0000256|ARBA:ARBA00022227, ECO:0000256|PIRNR:PIRNR005700};
DE EC=3.4.22.40 {ECO:0000256|ARBA:ARBA00012465, ECO:0000256|PIRNR:PIRNR005700};
GN Name=106087831 {ECO:0000313|EnsemblMetazoa:SCAU012839-PA};
OS Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Stomoxys.
OX NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU012839-PA, ECO:0000313|Proteomes:UP000095300};
RN [1] {ECO:0000313|EnsemblMetazoa:SCAU012839-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU012839-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR005700}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|PIRNR:PIRNR005700}.
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DR RefSeq; XP_013108460.1; XM_013253006.1.
DR AlphaFoldDB; A0A1I8Q0X7; -.
DR STRING; 35570.A0A1I8Q0X7; -.
DR EnsemblMetazoa; SCAU012839-RA; SCAU012839-PA; SCAU012839.
DR GeneID; 106087831; -.
DR KEGG; scac:106087831; -.
DR VEuPathDB; VectorBase:SCAU012839; -.
DR OrthoDB; 45184at2759; -.
DR Proteomes; UP000095300; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, 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 ACT_SITE 74
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 374
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 396
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
SQ SEQUENCE 455 AA; 52058 MW; 7640A09492638677 CRC64;
MSSTSAITQD KLDKWRQNFY SEPKNVLAQN VCSRFDPFDV CLSRKCLETT NHVFTHKVEM
EGKPVTNQRS SGRCWLFAAL NCLRLPLMKE YNLDEFEFSQ AYLFYWDKIE RCNYFLNNIV
KTSKRGEKVD GRLVSFLLND PTSDGGQWDM LVNLITKHGL MPKKCFPESF SCESSMRMNG
VLKSKLREYA KVLRVLMDTN PSDEQVNAKI DEMMEEIYKV VGICLGIPAK EFTWEYYDKT
KNYNAVGPIT PLEFYNTKVK PLFNVEDKMC LVTDPRPSSE YNQAYTVDCL GNVVDGRPVL
YNNQPVEILL EMVAASLKAG EPVWFGCEVS KRFAGKQGIE DLNVHDFKLV FDVDIQNTMT
KADRLIYGES AMTHAMVFTA ISLDENGLAK KLRVENSWGE DRGEKGYLVM SAEWFKEFGF
EVVVDKKFLP ASVLSVFDQD PIVLPAWDPM GTLAQ
//
