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Database: UniProt
Entry: A0A384A979_BALAS
LinkDB: A0A384A979_BALAS
Original site: A0A384A979_BALAS 
ID   A0A384A979_BALAS        Unreviewed;       455 AA.
AC   A0A384A979;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   08-NOV-2023, entry version 19.
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=BLMH {ECO:0000313|RefSeq:XP_007183900.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007183900.1};
RN   [1] {ECO:0000313|RefSeq:XP_007183900.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007183900.1};
RG   RefSeq;
RL   Submitted (JAN-2023) 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_007183900.1; XM_007183838.1.
DR   AlphaFoldDB; A0A384A979; -.
DR   GeneID; 103008350; -.
DR   CTD; 642; -.
DR   OrthoDB; 45184at2759; -.
DR   Proteomes; UP000261681; Unplaced.
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   Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW   ECO:0000256|PIRNR:PIRNR005700}.
FT   ACT_SITE        73
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT   ACT_SITE        372
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT   ACT_SITE        396
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
SQ   SEQUENCE   455 AA;  52300 MW;  8E508E04E5DB6389 CRC64;
     MNDAGLNSEK VAALLQKLNS DPQFVLAQNV GTTHDLLDIC LKRATVQGVQ HVFQHTVHPE
     GKPVTSQKSS GRCWIFSCLN VMRLPFMRKL NIEEFEFSQS YLFFWDKVER CYFFLNAFVD
     TAQKKEPEDG RLVQYLLTNP ANDGGQWDML VNIVEKYGVI PKKCFPESYT TEATKRMNDI
     LNHKMREFCL RLRNLVHSGA TKGEISATQD AMMEEIFRVV CICLGNPPET FTWEYRDKDK
     NYQKIGPITP LKFYKEHVKP LFNMEDKICL VNDPRPHHKY SRLYTVDYLS NMVGGRKTLY
     NNQPIDLLKK VVAASIKDGE AVWFGCDVGK HFNGKLGLSD MNVYDHELVF GVSMKNMNKA
     ERLTFGESLM THAMTFTAVS EKDDQEGAFV KWRVENSWGE DHGHKGYLCM TDEWFSEYVY
     EVVVDRKHIP EGVLAVLEQE PIVLPAWDPM GALAE
//
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