ID   U6LW50_9EIME            Unreviewed;       193 AA.
AC   U6LW50;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=26S protease regulatory subunit 4, related {ECO:0000313|EMBL:CDJ52010.1};
GN   ORFNames=EBH_0013020 {ECO:0000313|EMBL:CDJ52010.1};
OS   Eimeria brunetti.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=51314 {ECO:0000313|EMBL:CDJ52010.1};
RN   [1] {ECO:0000313|EMBL:CDJ52010.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDJ52010.1};
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:CDJ52010.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDJ52010.1};
RA   Aslett M.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; HG713058; CDJ52010.1; -; Genomic_DNA.
DR   AlphaFoldDB; U6LW50; -.
DR   EnsemblProtists; CDJ52010; CDJ52010; EBH_0013020.
DR   VEuPathDB; ToxoDB:EBH_0013020; -.
DR   OrthoDB; 1707207at2759; -.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR032501; Prot_ATP_ID_OB_2nd.
DR   Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:CDJ52010.1};
KW   Protease {ECO:0000313|EMBL:CDJ52010.1}.
FT   DOMAIN          113..159
FT                   /note="Proteasomal ATPase second OB"
FT                   /evidence="ECO:0000259|Pfam:PF16450"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   193 AA;  21780 MW;  52366E7602645CD3 CRC64;
     MGNAHGGFNL PGHPGAGDDK KDKKKEKKPL EAAPPSHVGR RKKPKGSTGA SKLPNVTPVT
     KCRMRLLKLE RVKDYLLLEE EYISNQEQHK PAEERNEEEV SRVDELRGSP LSVGTLEELI
     DEQHAIVSSS IGPEYYVNIL SFVDKDLLEP GSAVLLHNKE EKQQHNSNSQ QQHQQQQQQQ
     QQQQQQKQEQ GIV
//