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Database: UniProt
Entry: A0A3P9BFU3_9CICH
LinkDB: A0A3P9BFU3_9CICH
Original site: A0A3P9BFU3_9CICH 
ID   A0A3P9BFU3_9CICH        Unreviewed;       452 AA.
AC   A0A3P9BFU3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 23.
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};
OS   Maylandia zebra (zebra mbuna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX   NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005008758.1, ECO:0000313|Proteomes:UP000265160};
RN   [1] {ECO:0000313|Ensembl:ENSMZEP00005008758.1, ECO:0000313|Proteomes:UP000265160}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25186727; DOI=10.1038/nature13726;
RA   Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA   Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA   Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA   Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA   Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA   Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA   Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA   Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA   Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA   Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA   Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA   Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA   Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA   Di Palma F.;
RT   "The genomic substrate for adaptive radiation in African cichlid fish.";
RL   Nature 513:375-381(2014).
RN   [2] {ECO:0000313|Ensembl:ENSMZEP00005008758.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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_004567058.1; XM_004567001.3.
DR   AlphaFoldDB; A0A3P9BFU3; -.
DR   STRING; 106582.ENSMZEP00005008758; -.
DR   Ensembl; ENSMZET00005009098.1; ENSMZEP00005008758.1; ENSMZEG00005006646.1.
DR   GeneID; 101466499; -.
DR   KEGG; mze:101466499; -.
DR   CTD; 642; -.
DR   GeneTree; ENSGT00390000001735; -.
DR   OrthoDB; 45184at2759; -.
DR   Proteomes; UP000265160; LG14.
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:UP000265160};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW   ECO:0000256|PIRNR:PIRNR005700}.
FT   ACT_SITE        72
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT   ACT_SITE        371
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT   ACT_SITE        394
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
SQ   SEQUENCE   452 AA;  52201 MW;  9D73A89CA1733517 CRC64;
     METGLSQEKV ATFVKRMRSE PRYLLAQNVS TCIDPLEVCL HRQTVQDTVH IFQHSIPTEG
     KPITNQKNSG RCWIFSCLNV MRLPFMKKFN IEEFEFSQSY LFFWDKIERC YYFLQACVET
     AQRKEPVDGR LVQFLLSNPT NDGGQWDMLV NLIEKYGVIP KKCFPESHSS EASRRMNDIL
     NHKLREYCLR LRNMVASDAS KGELSEAMDS MIEEVFRVAS VCLGSPPETI CWEYRDKDKN
     FNRMGPLTPQ EFYRKHVKPL YNIQDKVCLV NDPRPQNPYG KLYSVEFLGN MVGGRSTLYN
     NQPIQLLKKA AAESIKDGEA VWFGCDVGKH FHSKLGINDM NVFNHELVFG VSVKNLSKAE
     RLIYGDSLMT HAMILTAVTD KDGKEGYEKW RVENSWGDDR GNKGYLIMTD DWFSEYVYEV
     VVDKRFLTDD VLEVMQQDPI VLPAWDPMGS LA
//
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