ID A0A0N1ILU3_LEPSE Unreviewed; 128 AA.
AC A0A0N1ILU3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE RecName: Full=Prefoldin subunit 4 {ECO:0000256|PIRNR:PIRNR016477};
GN ORFNames=ABL78_2581 {ECO:0000313|EMBL:KPI88342.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI88342.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI88342.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI88342.1,
RC ECO:0000313|Proteomes:UP000038009};
RX PubMed=26317207;
RA Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA Yurchenko V.;
RT "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT donovani.";
RL PLoS Pathog. 11:E1005127-E1005127(2015).
CC -!- FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and
CC transfers target proteins to it. Binds to nascent polypeptide chain and
CC promotes folding in an environment in which there are many competing
CC pathways for nonnative proteins. {ECO:0000256|PIRNR:PIRNR016477}.
CC -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type
CC subunits. {ECO:0000256|PIRNR:PIRNR016477}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC {ECO:0000256|ARBA:ARBA00008045, ECO:0000256|PIRNR:PIRNR016477}.
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:KPI88342.1}.
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DR EMBL; LJSK01000054; KPI88342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1ILU3; -.
DR EnsemblProtists; KPI88342; KPI88342; ABL78_2581.
DR VEuPathDB; TriTrypDB:Lsey_0054_0190; -.
DR OMA; KFGRAIN; -.
DR OrthoDB; 5476468at2759; -.
DR Proteomes; UP000038009; Unassembled WGS sequence.
DR GO; GO:0016272; C:prefoldin complex; IEA:UniProtKB-UniRule.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR InterPro; IPR002777; PFD_beta-like.
DR InterPro; IPR016661; PFDN4.
DR PANTHER; PTHR21100; PREFOLDIN SUBUNIT 4; 1.
DR PANTHER; PTHR21100:SF9; PREFOLDIN SUBUNIT 4; 1.
DR Pfam; PF01920; Prefoldin_2; 1.
DR PIRSF; PIRSF016477; Prefoldin_subunit_4; 1.
DR SUPFAM; SSF46579; Prefoldin; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|PIRNR:PIRNR016477};
KW Coiled coil {ECO:0000256|SAM:Coils}.
FT COILED 26..114
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 128 AA; 14799 MW; 564990DB3D1B855F CRC64;
MTAVAAKKND VPIDVTWEDQ RNICIFSRLH RRVQALNRRL KLLSDDIEKL DDASTEVMIC
DQVKYVFGEA FVDVECDNAV ELLDTEKQRM EAEKEEVESE LRELATALND LKAQLYAKFG
SQIYLEEK
//
