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   20-JAN-2009, entry version 60.
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; Platyhelminthes; Trematoda; Digenea; Strigeidida;
OC   Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 32-57.
RX   MEDLINE=90342941; PubMed=2382765;
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
RT   sequence and gene expression in developing parasites.";
RL   Am. J. Trop. Med. Hyg. 43:67-78(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89261925; 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
RT   mansoni and their identification as proteases.";
RL   Mol. Biochem. Parasitol. 33:113-122(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 77-429.
RX   MEDLINE=87308326; PubMed=3305515;
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
CC       the host globin.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of proteins and small molecule
CC       substrates at -Asn-|-Xaa- bonds.
CC   -!- SIMILARITY: Belongs to the peptidase C13 family.
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DR   EMBL; M21308; AAA29895.1; -; mRNA.
DR   EMBL; M17423; AAA29916.1; -; mRNA.
DR   PIR; A60145; A60145.
DR   BRENDA; 3.4.22.34; 1460.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR001096; Peptidase_C13.
DR   PANTHER; PTHR12000; Peptidase_C13; 1.
DR   Pfam; PF01650; Peptidase_C13; 1.
DR   PRINTS; PR00776; HEMOGLOBNASE.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Signal;
KW   Thiol protease.
FT   SIGNAL        1     19       Potential.
FT   PROPEP       20     31       Potential.
FT                                /FTId=PRO_0000026508.
FT   CHAIN        32    291       Hemoglobinase.
FT                                /FTId=PRO_0000026509.
FT   PROPEP      292    429       Potential.
FT                                /FTId=PRO_0000026510.
FT   ACT_SITE    151    151       Potential.
FT   CONFLICT     91     91       P -> L (in Ref. 2; AAA29895).
FT   CONFLICT    115    115       N -> K (in Ref. 2; AAA29895).
FT   CONFLICT    216    216       S -> P (in Ref. 2; AAA29895).
FT   CONFLICT    297    297       S -> T (in Ref. 2; AAA29895).
FT   CONFLICT    302    302       P -> S (in Ref. 2; AAA29895).
FT   CONFLICT    310    310       I -> V (in Ref. 3; AAA29916).
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
//