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Database: UniProt
Entry: Q5CUK0_CRYPI
LinkDB: Q5CUK0_CRYPI
Original site: Q5CUK0_CRYPI 
ID   Q5CUK0_CRYPI            Unreviewed;       279 AA.
AC   Q5CUK0;
DT   12-APR-2005, integrated into UniProtKB/TrEMBL.
DT   12-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=Proteasome subunit beta {ECO:0000256|RuleBase:RU004203};
GN   ORFNames=cgd3_2530 {ECO:0000313|EMBL:EAK89067.1};
OS   Cryptosporidium parvum (strain Iowa II).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=353152 {ECO:0000313|EMBL:EAK89067.1, ECO:0000313|Proteomes:UP000006726};
RN   [1] {ECO:0000313|EMBL:EAK89067.1, ECO:0000313|Proteomes:UP000006726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Iowa II {ECO:0000313|Proteomes:UP000006726};
RX   PubMed=15044751; DOI=10.1126/science.1094786;
RA   Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA   Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA   Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA   Anantharaman V., Aravind L., Kapur V.;
RT   "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL   Science 304:441-445(2004).
CC   -!- FUNCTION: Component of the proteasome, a multicatalytic proteinase
CC       complex which is characterized by its ability to cleave peptides with
CC       Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
CC       slightly basic pH. The proteasome has an ATP-dependent proteolytic
CC       activity. {ECO:0000256|RuleBase:RU004203}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of peptide bonds with very broad specificity.;
CC         EC=3.4.25.1; Evidence={ECO:0000256|ARBA:ARBA00001198};
CC   -!- SUBUNIT: Component of the proteasome complex.
CC       {ECO:0000256|RuleBase:RU004203}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004203}.
CC       Nucleus {ECO:0000256|RuleBase:RU004203}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family.
CC       {ECO:0000256|RuleBase:RU004203}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAK89067.1}.
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DR   EMBL; AAEE01000004; EAK89067.1; -; Genomic_DNA.
DR   RefSeq; XP_626814.1; XM_626814.1.
DR   AlphaFoldDB; Q5CUK0; -.
DR   STRING; 353152.Q5CUK0; -.
DR   EnsemblProtists; EAK89067; EAK89067; cgd3_2530.
DR   GeneID; 3373907; -.
DR   KEGG; cpv:cgd3_2530; -.
DR   VEuPathDB; CryptoDB:cgd3_2530; -.
DR   InParanoid; Q5CUK0; -.
DR   OMA; KQHLFRH; -.
DR   OrthoDB; 5485745at2759; -.
DR   Proteomes; UP000006726; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR   CDD; cd03763; proteasome_beta_type_7; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR000243; Pept_T1A_subB.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1.
DR   PANTHER; PTHR32194:SF4; PROTEASOME SUBUNIT BETA TYPE-7; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   PRINTS; PR00141; PROTEASOME.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU004203};
KW   Hydrolase {ECO:0000313|EMBL:EAK89067.1};
KW   Nucleus {ECO:0000256|RuleBase:RU004203};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|RuleBase:RU004203};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006726}.
FT   ACT_SITE        42
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600243-1"
SQ   SEQUENCE   279 AA;  30406 MW;  2A486EC06C4B6215 CRC64;
     MNAYLNAYFS EKSTNGFLFE NNIATAPCLS DSTELKTVKT GTTIVGVACN DCVVLGADTR
     ATNGPIVADK DCEKIHRLSD NIFAAGAGTA ADLDHVTSLI EGNLELQKLQ MNRKPRVAHA
     VSMLSDHLYK YQGYIGAHLI VAGSDSTGNF VFQVSANGCI MQLPFTSMGS GSLCARSILE
     ARYRDGLTES ECVELVSDAI RAGIYNDLYS GSNVNILIIK NNYVKHFRHF DTKASERIYR
     QPKPISFPVG TTPIIAEKTE DLSSFVVEVS EVQIDENMD
//
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