ID A0A0L0D751_THETB Unreviewed; 476 AA.
AC A0A0L0D751;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Cytoplasmic ATPase that is a ribosome-associated molecular chaperone {ECO:0000313|EMBL:KNC47926.1};
GN ORFNames=AMSG_04161 {ECO:0000313|EMBL:KNC47926.1};
OS Thecamonas trahens ATCC 50062.
OC Eukaryota; Apusozoa; Apusomonadida; Apusomonadidae; Thecamonas.
OX NCBI_TaxID=461836 {ECO:0000313|EMBL:KNC47926.1, ECO:0000313|Proteomes:UP000054408};
RN [1] {ECO:0000313|EMBL:KNC47926.1, ECO:0000313|Proteomes:UP000054408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50062 {ECO:0000313|EMBL:KNC47926.1,
RC ECO:0000313|Proteomes:UP000054408};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA Borenstein D., Chapman S., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA Burger G., Gray M.W., Holland P.W.H., King N., Lang F.B.F., Roger A.J.,
RA Ruiz-Trillo I., Lander E., Nusbaum C.;
RT "The Genome Sequence of Thecamonas trahens ATCC 50062.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381}.
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DR EMBL; GL349449; KNC47926.1; -; Genomic_DNA.
DR RefSeq; XP_013758945.1; XM_013903491.1.
DR AlphaFoldDB; A0A0L0D751; -.
DR STRING; 461836.A0A0L0D751; -.
DR EnsemblProtists; KNC47926; KNC47926; AMSG_04161.
DR GeneID; 25563716; -.
DR eggNOG; KOG0101; Eukaryota.
DR OMA; THCKELF; -.
DR OrthoDB; 103654at2759; -.
DR Proteomes; UP000054408; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375:SF395; HEAT SHOCK 70 KDA PROTEIN COGNATE 1-RELATED; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054408}.
FT REGION 431..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 476 AA; 50613 MW; 3140770708F97492 CRC64;
MAATNETPTS EEVCIGIDLG TTYSCVGVWQ NDRVEIIANE QGDRTTPSCV AFTSEGRLVG
KAAANQAGMN PTNTVFDAKR LIGRLVDDAV IKQDLEHWAF KVVGNSDHKP LIEVADAGED
KQFTPEEISS MVLMKMKETA EAYLGKAVTS AVITVPAYFN DSQRRATQDA GVIAGLKVLR
IINEPTAAAI AYGLDKSAEK GSKNVLIFDL GGGTFDVSLL NINNGIFSVL ATAGDTHLGG
EDFDNNMVAH CQAILTKKHS KDISGNPRAL RRLRTACERA KRALSASTSA VIDVESLVDG
IDFRTKVSRA KFEAMNESLF QACLEPVGRV LADAGMAKGE VTDVVLVGGS TRIPKIQEML
RDFFGGKELN QSINPDEAVA YGAAVQAAII TGQSTGASKD LLLLDVTPLS LGVDTIGGVM
NVVIPRNTKI PCKKEDFSPP PRTARPRLTL TSTRASARTS TRTTSSAALP SAASRP
//