ID A8HYV3_CHLRE Unreviewed; 679 AA.
AC A8HYV3;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PNW81520.1};
GN ORFNames=CHLRE_06g250100v5 {ECO:0000313|EMBL:PNW81520.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055 {ECO:0000313|EMBL:PNW81520.1, ECO:0000313|Proteomes:UP000006906};
RN [1] {ECO:0000313|EMBL:PNW81520.1, ECO:0000313|Proteomes:UP000006906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906};
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
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DR EMBL; CM008967; PNW81520.1; -; Genomic_DNA.
DR RefSeq; XP_001696432.1; XM_001696380.1.
DR AlphaFoldDB; A8HYV3; -.
DR STRING; 3055.A8HYV3; -.
DR PaxDb; 3055-EDP08409; -.
DR ProMEX; A8HYV3; -.
DR EnsemblPlants; PNW81520; PNW81520; CHLRE_06g250100v5.
DR GeneID; 5722220; -.
DR Gramene; PNW81520; PNW81520; CHLRE_06g250100v5.
DR KEGG; cre:CHLRE_06g250100v5; -.
DR eggNOG; KOG0102; Eukaryota.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; A8HYV3; -.
DR OMA; KRQGVVN; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000006906; Chromosome 6.
DR ExpressionAtlas; A8HYV3; baseline.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR NCBIfam; TIGR02350; prok_dnaK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
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, ECO:0000256|RuleBase:RU003322};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000006906}.
SQ SEQUENCE 679 AA; 71955 MW; 55E6914FA6B27AEA CRC64;
MPVQQMTSMR SQSLAGAPVA PVKAGRAGVS RRGLAVSVRA EKVVGIDLGT TNSAVAAMEG
GKPTIITNAE GGRTTPSVVA FTKTGDRLVG QIAKRQAVVN PENTFFSVKR FIGRRMSEVG
SESTQVPYRV IEDGGNVKIK CPNAGKDFAP EEISAQVLRK LTEDAAKFLN DKVEKAVITV
PAYFNDSQRQ ATKDAGKIAG LEVLRIINEP TAASLAYGFD KKANETILVF DLGGGTFDVS
VLEVGDGVFE VLSTSGDTHL GGDDFDKRIV DFLADDFKKS EGIDLRKDRQ ALQRLTEAAE
KAKIELSGMA QTSINLPFIT ATADGPKHID TQLTRAKFEE MCNDLLERCK VPVQQALRDA
KLSISDIQEV ILVGGSTRIP AVQEIVRKLS GGKDPNVTVN PDEVVALGAA VQAGVLAGEV
SDIVLLDVTP LSLGLETLGG VMTKLIPRNT TLPTSKSEVF STAADGQTSV EINVLQGERE
FARDNKSLGT FRLDGIPPAP RGVPQIEVKF DIDANGILSV TATDKGTSKK QDIRITGAST
LDKGDVERMV KEAEKFAGED KKRRESVETK NQAETMVYQT EKQLKEFEGK VPADIKAKVE
AKLGELKAAL PADDAEATKA AMNALQQEVM AMGQAMYSQA GAAPGGAPGA EPGAGAGAGG
APGGKKDDDV IDAEFTDKK
//
