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Database: UniProt
Entry: J4DPT8_THEOR
LinkDB: J4DPT8_THEOR
Original site: J4DPT8_THEOR 
ID   J4DPT8_THEOR            Unreviewed;       495 AA.
AC   J4DPT8;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   08-NOV-2023, entry version 46.
DE   SubName: Full=Pepsinogen {ECO:0000313|EMBL:BAM41279.1};
GN   ORFNames=TOT_030000542 {ECO:0000313|EMBL:BAM41279.1};
OS   Theileria orientalis strain Shintoku.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM41279.1, ECO:0000313|Proteomes:UP000003786};
RN   [1] {ECO:0000313|EMBL:BAM41279.1, ECO:0000313|Proteomes:UP000003786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shintoku {ECO:0000313|EMBL:BAM41279.1,
RC   ECO:0000313|Proteomes:UP000003786};
RX   PubMed=22951932;
RA   Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA   Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA   Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA   Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA   Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT   "Comparative genome analysis of three eukaryotic parasites with differing
RT   abilities to transform leukocytes reveals key mediators of Theileria-
RT   induced leukocyte transformation.";
RL   MBio 3:e00204-e00212(2012).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; AP011948; BAM41279.1; -; Genomic_DNA.
DR   RefSeq; XP_009691580.1; XM_009693285.1.
DR   AlphaFoldDB; J4DPT8; -.
DR   STRING; 869250.J4DPT8; -.
DR   MEROPS; A01.A95; -.
DR   EnsemblProtists; BAM41279; BAM41279; TOT_030000542.
DR   GeneID; 20715712; -.
DR   KEGG; tot:TOT_030000542; -.
DR   VEuPathDB; PiroplasmaDB:TOT_030000542; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   OrthoDB; 46443at2759; -.
DR   Proteomes; UP000003786; Chromosome 3.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003786};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..495
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003778837"
FT   DOMAIN          152..473
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        358
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        183..188
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   495 AA;  55073 MW;  27C67AB7C8A169B9 CRC64;
     MFVSKIILNV VLPLSVINIS LGRVDGETNN YVSQIKRCSD CSWSTVDGCR VCLHEGHNSQ
     RYGKSGSESV STIQLAKDNL ELFKNGKISF ALRSEGPFGS LGFNEKLHGS NFANVYNNEP
     KNTSRLRHHS SVLSADEVNE YIPLNQIKDS LYVGSMYVGS PPQLMHPIFD TGSTNMWVVG
     TNCDSETCKK VKRFNPSLSN TFKALAKPKR IHIRFGTGEI EGKPAKDVVK IGGMSFEQAF
     AVVEKENDPG SDFNVFERIN FEGIVGLAFS EMSSIKAPSV LENLTKLNLL SHNEFSFYIG
     EDTRDALLMF GGANSEFYEG ELKMFPVVRE HYWEVALDEI YLGAEKICCK EKSYLIFDSG
     TSLNSVPSSE YSDFLSMIDK VRPQFPNSCF RSASVISTVS PSPTCWLGGE KIVIEPSQYI
     YKQGDHCTPA YMQLDVPSQF GHAYVLGSSG FMRYYFTLFR MGSGERPSMV GVAPAKRGPE
     VSKRARELAL MNSEF
//
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