ID F2URJ7_SALR5 Unreviewed; 445 AA.
AC F2URJ7;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=bleomycin hydrolase {ECO:0000256|ARBA:ARBA00012465};
DE EC=3.4.22.40 {ECO:0000256|ARBA:ARBA00012465};
GN ORFNames=PTSG_10848 {ECO:0000313|EMBL:EGD80166.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|PIRNR:PIRNR005700}.
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DR EMBL; GL832991; EGD80166.1; -; Genomic_DNA.
DR RefSeq; XP_004988228.1; XM_004988171.1.
DR AlphaFoldDB; F2URJ7; -.
DR STRING; 946362.F2URJ7; -.
DR MEROPS; C01.084; -.
DR EnsemblProtists; EGD80166; EGD80166; PTSG_10848.
DR GeneID; 16068755; -.
DR KEGG; sre:PTSG_10848; -.
DR eggNOG; KOG4128; Eukaryota.
DR InParanoid; F2URJ7; -.
DR OMA; QSYTFFW; -.
DR OrthoDB; 45184at2759; -.
DR Proteomes; UP000007799; 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: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 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:UP000007799};
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 366
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 387
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
SQ SEQUENCE 445 AA; 51437 MW; 625F9F803C84FD55 CRC64;
MAGLEITTEL VDKARAEFDA EPRFKLSQNA VTRNDVKEVL PRHNITTTYE DKSFSTKLKE
MKATNQKSSG RCWLFAAANC MRLAMKEKYN LPDDFELSQS YLFFWDKLER ANYFTNAILE
TLDEDLDGRL VQHLLSDPLG DGGQWDMAVN IVLKYGIVPK SQYPESFSSC NTRHMNAFLT
AKLRDFACDL RATARELSKE ELAKKRDAFL AMVYRVLAIH LGTPPTTFDW CYTDTDKKFH
RISNLTPLQF YREYVPFKVE DYQSLIHDPR NAVERVYTVK YLGNVLGGDR ELVKHINVPI
DLIRSLCKKQ LDQGMPVWFG VDVGKEYHRK MAVMDTRLFD YDLVFGTRPA LSKADRLRYG
QSLMTHAMVF TGYNEADGKI DKWRVENSWG KDVGDSGYYL MTDEWFDEYL YQIVAPKAMV
EEMVKVDMKD VVELPPWDPM GALAC
//
