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
//