ID   HGLB_SCHMA              Reviewed;         429 AA.
AC   P09841;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 3.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Hemoglobinase;
DE            EC=3.4.22.34;
DE   AltName: Full=Antigen SM32;
DE   Flags: Precursor;
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 32-57.
RX   PubMed=2382765; DOI=10.4269/ajtmh.1990.43.67;
RA   el Meanawy M.A., Aji T., Phillips N.F.B., Davis R.E., Salata R.A.,
RA   Malchotra I., McClain D., Aikawa M., Davis A.H.;
RT   "Definition of the complete Schistosoma mansoni hemoglobinase mRNA sequence
RT   and gene expression in developing parasites.";
RL   Am. J. Trop. Med. Hyg. 43:67-78(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2725581; DOI=10.1016/0166-6851(89)90025-x;
RA   Klinkert M.-Q., Felleisen R., Link G., Ruppel A., Beck E.;
RT   "Primary structures of Sm31/32 diagnostic proteins of Schistosoma mansoni
RT   and their identification as proteases.";
RL   Mol. Biochem. Parasitol. 33:113-122(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 77-429.
RX   PubMed=3305515; DOI=10.1016/s0021-9258(18)45284-2;
RA   Davis A.H., Nanduri J., Watson D.C.;
RT   "Cloning and gene expression of Schistosoma mansoni protease.";
RL   J. Biol. Chem. 262:12851-12855(1987).
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   -!- SIMILARITY: Belongs to the peptidase C13 family. {ECO:0000305}.
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DR   EMBL; M21308; AAA29895.1; -; mRNA.
DR   EMBL; M17423; AAA29916.1; -; mRNA.
DR   PIR; A60145; A60145.
DR   AlphaFoldDB; P09841; -.
DR   SMR; P09841; -.
DR   STRING; 6183.Smp_075800.1; -.
DR   MEROPS; C13.007; -.
DR   eggNOG; KOG1348; Eukaryota.
DR   HOGENOM; CLU_024160_0_0_1; -.
DR   BRENDA; 3.4.22.34; 5608.
DR   Proteomes; UP000008854; Unassembled WGS sequence.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Reference proteome; Signal;
KW   Thiol protease.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..31
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026508"
FT   CHAIN           32..291
FT                   /note="Hemoglobinase"
FT                   /id="PRO_0000026509"
FT   PROPEP          292..429
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026510"
FT   REGION          288..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..309
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        151
FT                   /evidence="ECO:0000255"
FT   CONFLICT        91
FT                   /note="P -> L (in Ref. 2; AAA29895)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        115
FT                   /note="N -> K (in Ref. 2; AAA29895)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        216
FT                   /note="S -> P (in Ref. 2; AAA29895)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        297
FT                   /note="S -> T (in Ref. 2; AAA29895)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        302
FT                   /note="P -> S (in Ref. 2; AAA29895)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        310
FT                   /note="I -> V (in Ref. 3; AAA29916)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   429 AA;  49032 MW;  333C9DA086C83B0F CRC64;
     MMLFSLFLIS ILHILLVKCQ LDTNYEVSDE TVSDNNKWAV LVAGSNGYPN YRHQADVCHA
     YHVLRSKGIK PEHIITMMYD DIAYNLMNPF PGKLFNDYNH KDWYEGVVID YRGKNVNSKT
     FLKVLKGDKS AGGKVLKSGK NDDVFIYFTD HGAPGLIAFP DDELYAKEFM STLKYLHSHK
     RYSKLVIYIE ANESGSMFQQ ILPSNLSIYA TTAANSTECS YSTFCGDPTI TTCLADLYSY
     NWIVDSQTHH LTQRTLDQQY KEVKRETDLS HVQRYGDTRM GKLYVSEFQG SRDKSSSEND
     EPPMKPRHSI ASRDIPLHTL HRQIMMTNNA EDKSFLMQIL GLKLKRRDLI EDTMKLIVKV
     MNNEEIPNTK ATIDQTLDCT ESVYEQFKSK CFTLQQAPEV GGHFSTLYNY CADGYTAETI
     NEAIIKICG