ID A0A1E4IZU8_9BURK Unreviewed; 332 AA.
AC A0A1E4IZU8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Hsp33 chaperonin {ECO:0000313|EMBL:ODU15683.1};
GN ORFNames=ABS94_16910 {ECO:0000313|EMBL:ODU15683.1};
OS Variovorax sp. SCN 67-85.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1660152 {ECO:0000313|EMBL:ODU15683.1, ECO:0000313|Proteomes:UP000094461};
RN [1] {ECO:0000313|EMBL:ODU15683.1, ECO:0000313|Proteomes:UP000094461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
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:ODU15683.1}.
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DR EMBL; MEFM01000021; ODU15683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4IZU8; -.
DR Proteomes; UP000094461; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd00498; Hsp33; 1.
DR Gene3D; 1.10.287.480; helix hairpin bin; 1.
DR Gene3D; 3.55.30.10; Hsp33 domain; 1.
DR Gene3D; 3.90.1280.10; HSP33 redox switch-like; 1.
DR InterPro; IPR000397; Heat_shock_Hsp33.
DR InterPro; IPR016154; Heat_shock_Hsp33_C.
DR InterPro; IPR016153; Heat_shock_Hsp33_N.
DR InterPro; IPR023212; Hsp33_helix_hairpin_bin_dom_sf.
DR PANTHER; PTHR30111; 33 KDA CHAPERONIN; 1.
DR PANTHER; PTHR30111:SF1; 33 KDA CHAPERONIN; 1.
DR Pfam; PF01430; HSP33; 1.
DR PIRSF; PIRSF005261; Heat_shock_Hsp33; 1.
DR SUPFAM; SSF64397; Hsp33 domain; 1.
DR SUPFAM; SSF118352; HSP33 redox switch-like; 1.
PE 4: Predicted;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 332 AA; 36304 MW; ED27871916165521 CRC64;
MSELHKFLFD GLPVRGMIVR LTDAWQEILA RRASNTATGA YPPPVAELLG EMTAAATLMQ
ANIKFNGALI LQIFGDGPVK VAVAEAKPDL SLRATAKVIG ELPADARLPD MVNVNNKGRC
AITLDPKDKL PGTTPYQGVV PLFDDNGEKL GKLSDVLQHY MLQSEQLDTT LVLAADDKVA
AGLLIQRLPV KGEGNLEGTS SKDHDQANED QIGRNEDYNR ISILASSLTR DELLTLDIET
ILRRLFWEEK LLRFEPQAGL LGPHFACTCG RERVAQMIRG LGVEEAESIL AERGDIEVGC
DFCGKQYRFD AVDTAQIFRP PTDQIPGTPV VQ
//
