ID B6AHY4_CRYMR Unreviewed; 442 AA.
AC B6AHY4;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Eukaryotic aspartyl protease family protein {ECO:0000313|EMBL:EEA07825.1};
DE EC=3.4.23.- {ECO:0000313|EMBL:EEA07825.1};
GN ORFNames=CMU_028990 {ECO:0000313|EMBL:EEA07825.1};
OS Cryptosporidium muris (strain RN66).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=441375 {ECO:0000313|Proteomes:UP000001460};
RN [1] {ECO:0000313|EMBL:EEA07825.1, ECO:0000313|Proteomes:UP000001460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RN66 {ECO:0000313|EMBL:EEA07825.1,
RC ECO:0000313|Proteomes:UP000001460};
RA Lorenzi H., Inman J., Miller J., Schobel S., Amedeo P., Caler E.V.,
RA da Silva J.;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; DS989735; EEA07825.1; -; Genomic_DNA.
DR RefSeq; XP_002142174.1; XM_002142138.1.
DR AlphaFoldDB; B6AHY4; -.
DR STRING; 441375.B6AHY4; -.
DR EnsemblProtists; EEA07825; EEA07825; CMU_028990.
DR GeneID; 6997347; -.
DR VEuPathDB; CryptoDB:CMU_028990; -.
DR eggNOG; KOG1339; Eukaryota.
DR OMA; IGWTEYD; -.
DR OrthoDB; 335768at2759; -.
DR Proteomes; UP000001460; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR13683; ASPARTYL PROTEASES; 1.
DR PANTHER; PTHR13683:SF375; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000313|EMBL:EEA07825.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:EEA07825.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001460};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..401
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 60
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 278
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 73..105
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 442 AA; 51336 MW; EE75C7277A4D3DB0 CRC64;
MRIRIGIKVE LWIWIFIYGV ILPTRSYLSV ELHGSMNMHG YYFVDVYIGT PTQKQSLIID
TGSSHIGFSC ATCLQCGKHD VQPYNLSKST TAKWCNLSEN NHNICKYVQI YNEGSIVSGE
YFEDILSFEE PNSDVKYFFN GFRMHYNKLG CHEIETQLFI NQNASGIMGL GIRNKDLQDN
FINFLLLSVS RYYENENSDI ILSLCLLKDG GIMNIGRYND DIIEFDPENN IEIKNQILWI
PLVLDTSVYR IKLEIIMKSS DILWAFGNTE DAIGVVIDTG STFSHFPKSI YKLIRKNFDQ
LCTAIDQKFG TCRIVHDILC WTNIKDINNK FPNITMKFLG QPNYITWTYH SYLYKTNSGL
WCLAIEEHKF QSYEDDIILG MSFLKNRQII LDPKNRMIGI NSLLLKQCKK NRDWIRNKES
KYKSNLELGY NLFGIISTIY LI
//
