ID V6TT87_GIAIN Unreviewed; 315 AA.
AC V6TT87;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Proteasome subunit beta {ECO:0000256|RuleBase:RU004203};
GN ORFNames=GSB_12949 {ECO:0000313|EMBL:ESU41799.1};
OS Giardia intestinalis (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=5741 {ECO:0000313|EMBL:ESU41799.1, ECO:0000313|Proteomes:UP000018040};
RN [1] {ECO:0000313|Proteomes:UP000018040}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GS {ECO:0000313|Proteomes:UP000018040};
RA Adam R., Dahlstrom E., Martens C., Bruno D., Barbian K., Porcella S.F.,
RA Nash T.;
RT "Genome sequencing of Giardia lamblia Genotypes A2 and B isolates (DH and
RT GS) and comparative analysis with the genomes of Genotypes A1 and E (WB and
RT Pig).";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESU41799.1, ECO:0000313|Proteomes:UP000018040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS {ECO:0000313|EMBL:ESU41799.1,
RC ECO:0000313|Proteomes:UP000018040};
RX PubMed=24307482; DOI=10.1093/gbe/evt197;
RA Adam R.D., Dahlstrom E.W., Martens C.A., Bruno D.P., Barbian K.D.,
RA Ricklefs S.M., Hernandez M.M., Narla N.P., Patel R.B., Porcella S.F.,
RA Nash T.E.;
RT "Genome sequencing of Giardia lamblia genotypes A2 and B isolates (DH and
RT GS) and comparative analysis with the genomes of genotypes A1 and E (WB and
RT Pig).";
RL Genome Biol. Evol. 5:2498-2511(2013).
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:ESU41799.1}.
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DR EMBL; AHHH01000109; ESU41799.1; -; Genomic_DNA.
DR AlphaFoldDB; V6TT87; -.
DR EnsemblProtists; ESU41799; ESU41799; GSB_12949.
DR VEuPathDB; GiardiaDB:DHA2_12949; -.
DR VEuPathDB; GiardiaDB:GL50581_1384; -.
DR VEuPathDB; GiardiaDB:GL50803_0012949; -.
DR VEuPathDB; GiardiaDB:QR46_3124; -.
DR eggNOG; KOG0175; Eukaryota.
DR Proteomes; UP000018040; Unassembled WGS sequence.
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; cd03761; proteasome_beta_type_5; 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:SF0; ATP-DEPENDENT PROTEASE SUBUNIT HSLV; 1.
DR PANTHER; PTHR32194; METALLOPROTEASE TLDD; 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|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU004203};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleus {ECO:0000256|RuleBase:RU004203};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|RuleBase:RU004203};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT ACT_SITE 104
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600243-1"
SQ SEQUENCE 315 AA; 34594 MW; E57ACA42CECC3584 CRC64;
MTSLPVGYKK AKYSVLQKTF QMLSASEAIL MTRKTPFLHK RSERGYVPIS QWDTLVVPPN
GEHPKAFMKR ISAASGLGDN LSESLIKAHG SGPIVRRFHP NHGTTTVAFC FRGGILLAVD
SRSTQGQFVS SGVVQKVIEI TPHILGTIAG VAGDCQFWER DLGRKCRLYE LENGERIYAS
SASKLFISTL HSQSGTDMSV GAMISGFDST NHPCIYYCDS EGTRIGGYLY GAGSGSTFAF
GIVDTEYDFE MTEEQAIALG KKAIYHAVSR DAMSGGMLNI YVIRPSGWEH VLAMDNYEYY
RTMHPDAPEL PPPPQ
//
