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Database: UniProt
Entry: A0A1I6LA34_9EURY
LinkDB: A0A1I6LA34_9EURY
Original site: A0A1I6LA34_9EURY 
ID   A0A1I6LA34_9EURY        Unreviewed;       129 AA.
AC   A0A1I6LA34;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Prefoldin subunit beta {ECO:0000256|ARBA:ARBA00016304, ECO:0000256|HAMAP-Rule:MF_00307};
DE   AltName: Full=GimC subunit beta {ECO:0000256|ARBA:ARBA00033461, ECO:0000256|HAMAP-Rule:MF_00307};
GN   Name=pfdB {ECO:0000256|HAMAP-Rule:MF_00307};
GN   ORFNames=SAMN05216559_2344 {ECO:0000313|EMBL:SFS00322.1};
OS   Halomicrobium zhouii.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halomicrobium.
OX   NCBI_TaxID=767519 {ECO:0000313|EMBL:SFS00322.1, ECO:0000313|Proteomes:UP000199062};
RN   [1] {ECO:0000313|EMBL:SFS00322.1, ECO:0000313|Proteomes:UP000199062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10457 {ECO:0000313|EMBL:SFS00322.1,
RC   ECO:0000313|Proteomes:UP000199062};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Molecular chaperone capable of stabilizing a range of
CC       proteins. Seems to fulfill an ATP-independent, HSP70-like function in
CC       archaeal de novo protein folding. {ECO:0000256|ARBA:ARBA00025077,
CC       ECO:0000256|HAMAP-Rule:MF_00307}.
CC   -!- SUBUNIT: Heterohexamer of two alpha and four beta subunits.
CC       {ECO:0000256|ARBA:ARBA00011716, ECO:0000256|HAMAP-Rule:MF_00307}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00307}.
CC   -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC       {ECO:0000256|ARBA:ARBA00008045, ECO:0000256|HAMAP-Rule:MF_00307}.
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DR   EMBL; FOZK01000002; SFS00322.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6LA34; -.
DR   STRING; 767519.SAMN05216559_2344; -.
DR   OrthoDB; 204796at2157; -.
DR   Proteomes; UP000199062; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016272; C:prefoldin complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.287.370; -; 1.
DR   HAMAP; MF_00307; PfdB; 1.
DR   InterPro; IPR002777; PFD_beta-like.
DR   InterPro; IPR012713; PfdB.
DR   InterPro; IPR009053; Prefoldin.
DR   NCBIfam; TIGR02338; gimC_beta; 1.
DR   PANTHER; PTHR20903:SF0; PREFOLDIN SUBUNIT 1; 1.
DR   PANTHER; PTHR20903; PREFOLDIN SUBUNIT 1-RELATED; 1.
DR   Pfam; PF01920; Prefoldin_2; 1.
DR   SUPFAM; SSF46579; Prefoldin; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00307};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00307};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199062}.
FT   REGION          20..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          108..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   129 AA;  14090 MW;  9ECCCAB9B915694E CRC64;
     MQGNLPPEAQ EKLEELQDLQ ETAQQVAAQK QQAETSLQES ETALNELDDI DEDATMYREV
     GELLVKTDYA EAQEDLEEKV DSLEVRTETL QKQEDRVREQ FEDLQSELQQ MLGGGGGPGG
     APGPGAGGA
//
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