ID U6MU62_9EIME Unreviewed; 294 AA.
AC U6MU62;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CDJ67767.1};
DE Flags: Fragment;
GN ORFNames=ENH_00041260 {ECO:0000313|EMBL:CDJ67767.1};
OS Eimeria necatrix.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51315 {ECO:0000313|EMBL:CDJ67767.1};
RN [1] {ECO:0000313|EMBL:CDJ67767.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ67767.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ67767.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ67767.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DDI1 family.
CC {ECO:0000256|ARBA:ARBA00009136}.
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DR EMBL; HG724796; CDJ67767.1; -; Genomic_DNA.
DR RefSeq; XP_013436234.1; XM_013580780.1.
DR AlphaFoldDB; U6MU62; -.
DR GeneID; 25474283; -.
DR VEuPathDB; ToxoDB:ENH_00041260; -.
DR OrthoDB; 891597at2759; -.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00303; retropepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR12917; ASPARTYL PROTEASE DDI-RELATED; 1.
DR PANTHER; PTHR12917:SF1; AT13091P; 1.
DR Pfam; PF13650; Asp_protease_2; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
PE 3: Inferred from homology;
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 294
FT /evidence="ECO:0000313|EMBL:CDJ67767.1"
SQ SEQUENCE 294 AA; 32771 MW; 732CD8220AA3ABA4 CRC64;
MSKEHEEETR PLKEMRWKSG PTSILSEETP DATTDSRRKS AEATKEGHGS DVTEILPHWW
RETCMKESYD QGGALCCVGA TAVLRVELVG SPCEALLDTG ASRSFISPKT VERRQLKVRM
LPRERRFTVA TGAQLRIDRA VTGLTLWCGH ARFSGNFLVG PVPYDLVLGL DWLTEHKVAW
YFQSDKLRTY VDGQWCELPV VRTGEATLRG DSSIAAHPKT PAEQAYEILA KQLAGMSAEE
AAIFLRPPAR RYKPHAKKKA KARITSLVRQ AAEDTKDLKA PMHGLHLILA LPEA
//
