ID   SDP_EIMBO               Reviewed;         596 AA.
AC   P42789;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Sporozoite developmental protein;
DE            EC=3.4.24.-;
OS   Eimeria bovis.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=5803;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Oocyst;
RX   PubMed=8426605; DOI=10.1016/0166-6851(93)90239-t;
RA   Abrahamsen M.S., Clark T.G., Mascolo P., Speer C.A., White M.W.;
RT   "Developmental gene expression in Eimeria bovis.";
RL   Mol. Biochem. Parasitol. 57:1-14(1993).
CC   -!- FUNCTION: May be involved in the degradation of a protein which is a
CC       component of the signal transduction pathway regulating oocyst
CC       sporulation.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- DEVELOPMENTAL STAGE: Expressed in sporulated oocysts.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR   EMBL; M98842; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P42789; -.
DR   SMR; P42789; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR032632; Peptidase_M16_M.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   Pfam; PF16187; Peptidase_M16_M; 1.
DR   SUPFAM; SSF63411; SSF63411; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           1..596
FT                   /note="Sporozoite developmental protein"
FT                   /id="PRO_0000074419"
FT   ACT_SITE        80
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         81
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
SQ   SEQUENCE   596 AA;  65280 MW;  4BF9A9B17B358AA0 CRC64;
     MRNAASVGLC VGLSALGAAA NDILKPEADY RDFRHYQLNN GMHAIAVHHP RSNESGFAVA
     ANTGSLYDPQ DVPGLAHFLE HMLFLGTSKY PEPESYDSFL TESGGANNAY TDEEKTVFFN
     KVTDSSFEEA LDRFSFKSPL FSRQYEEKEV NAIDAEHQKN IPNDDERAWY SIRSLAKGPM
     SRFATGNSST LSTTPKAKGI DLVDRLKDFH TQYYCGSNMV AVTISPRSLD EQEALIREKF
     EGVSAGHADW LGMVQCPGPM FDTVKPFDES NTGKFIHLQS FSSEPSLWVA FGLPPTLTSY
     KKQPISVLTY LLEYTGQGSL AKRLRLLGLA DGLSPVVDKN TVSTLLGIKV DLTQKGAAHR
     GLVLQEIFSY INFLRDHGVG HDLVSTLAQQ SRIDFHTTQP SSSIMEEAAG LAHNLLTYEP
     YHAIAGDSLL IDADPRLTNQ LLQQMSPSKA IIAFSDPQFT SKVEDFDTDP YYGVQFKVLD
     LPQHHAIAMA VLTATPNAFR MPPPLMHIPK ASDLKILPGL FGLSAPELIS DQGGNAGTAV
     WWQGQGAFAL PRIAVQLTGN ITKEKADLLS RTQGSVALAA LAEYLQEETW ISKTAG