ID   HGLB_SCHJA              Reviewed;         423 AA.
AC   P42665;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Hemoglobinase;
DE            EC=3.4.22.34;
DE   AltName: Full=Antigen Sj32;
DE   Flags: Precursor;
GN   Name=HAEM;
OS   Schistosoma japonicum (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6182;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Chinese;
RX   PubMed=7899786;
RA   Merckelbach A., Hasse S., Dell R., Eschlbeck A., Ruppel A.;
RT   "cDNA sequences of Schistosoma japonicum coding for two cathepsin B-like
RT   proteins and Sj32.";
RL   Trop. Med. Parasitol. 45:193-198(1994).
CC   -!- FUNCTION: This protease is used by the parasite for degradation of the
CC       host globin.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins and small molecule substrates at
CC         -Asn-|-Xaa- bonds.; EC=3.4.22.34;
CC   -!- TISSUE SPECIFICITY: Gut.
CC   -!- SIMILARITY: Belongs to the peptidase C13 family. {ECO:0000305}.
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DR   EMBL; X70967; CAA50304.1; -; mRNA.
DR   PIR; S31908; S31908.
DR   AlphaFoldDB; P42665; -.
DR   SMR; P42665; -.
DR   MEROPS; C13.007; -.
DR   BRENDA; 3.4.22.34; 5607.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR   InterPro; IPR043577; AE.
DR   InterPro; IPR001096; Peptidase_C13.
DR   PANTHER; PTHR12000; PTHR12000; 1.
DR   Pfam; PF01650; Peptidase_C13; 1.
DR   PIRSF; PIRSF500139; AE; 1.
DR   PIRSF; PIRSF019663; Legumain; 1.
DR   PRINTS; PR00776; HEMOGLOBNASE.
PE   2: Evidence at transcript level;
KW   Hydrolase; Protease; Signal; Thiol protease.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..29
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026511"
FT   CHAIN           30..285
FT                   /note="Hemoglobinase"
FT                   /id="PRO_0000026512"
FT   PROPEP          286..423
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026513"
FT   REGION          286..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        186
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   423 AA;  48938 MW;  DF35CD475F4C8F03 CRC64;
     MFYSIFFIHI LRIVLVDCNE YSEENVDDRH KWAVLVAGSN GFENYRHQAD VCHAYHVLLS
     KGVKPEHIIT FMYDDIAHNK ENPFPGKIFN DYRHKDYYKG VVIDYKGKKV NPKTFLQVLK
     GDKRAGGKVL KSGKNDDVFI YFTDHGAPGI LAFPDDDLHA KPFINTLKYL RQHRRYSKLV
     IYVEACESGS MFAGLLPTDI NIYATTAARP DESSYATFCD DPRISSCLAD LYSYDWIVDS
     EKHQLTQRTL DQQYKEVKFE TNLSHVQRYG DKKMGKLYLS EFQGSRKKAS TEHDEPPMKP
     KDSIPSRDIP LHTLHRRIMM ANNMNDKTLL MKILGLKLKR RDLIKDTMEV IDQFMFNVKQ
     PNSNATIDET MDCIEVVYKE FQSKCFKIQQ APEITGYLST LYNYCQKGYS AENINGVIRK
     VCG