ID C5X4H2_SORBI Unreviewed; 678 AA.
AC C5X4H2;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EER99104.1};
GN ORFNames=SORBI_3002G249800 {ECO:0000313|EMBL:EER99104.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EER99104.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EER99104.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
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DR EMBL; CM000761; EER99104.1; -; Genomic_DNA.
DR RefSeq; XP_002462583.1; XM_002462538.1.
DR AlphaFoldDB; C5X4H2; -.
DR STRING; 4558.C5X4H2; -.
DR EnsemblPlants; EER99104; EER99104; SORBI_3002G249800.
DR GeneID; 8055880; -.
DR Gramene; EER99104; EER99104; SORBI_3002G249800.
DR KEGG; sbi:8055880; -.
DR eggNOG; KOG0102; Eukaryota.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; C5X4H2; -.
DR OMA; KRTIPPC; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000000768; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; 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; cd11733; HSPA9-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:SF356; OS09G0491772 PROTEIN; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768}.
FT REGION 639..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 297..324
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 652..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 678 AA; 72400 MW; F3E10D8D43FCFEB5 CRC64;
MAFGALVASR LARSGRTLAS AVAQGPVAQR TAPPLLSRLG AVARLLSTKP AAADVIGIDL
GTTNSCVSVM EGKTPRVIEN AEGARTTPSI VAKNQNGDLL IGITASRQAV TNAQNTIRGS
KRLIGRTFND PQTQKEMKMV PYKIVKAPNG DAWVEMGGQQ YSPSQIGAFV LTKMKETAEA
YLGKTVSKAV ITVPAYFNDA QRQATKDAGR IAGLEVMRII NEPTAAALSY GMNNKEGLIA
VFDLGGGTFD VSILEISNGV FEVKATNGDT FLGGEDFDGA LLEYLVSEFK KSDNIDLSQD
KLALQRLREA AEKAKVELSS TMQTEINLPF ITADASGAKH FNITLTRSKF ESLVSNLIER
TRIPCVNCLK DAGISAKEID EVLLVGGMTR VPKVQEVVSQ IFNKPPSKGV NPDEAVAMGA
AIQGGILRGD VKELLLLDVT PLSLGIETLG GIFTRLINRN TTIPTKKSQV FSTAADNQTQ
VGVKVLQGER EMATDNKLLG EFQLEGIPPA PRGMPQIEVT FDIDANGIVK VSARDKATGK
EQEITIKSSG GLSEGEIEKM VKEAELHAQK DQERKSLIDL KNSADTTIYT IEKSVSEYKD
KVPAEVTKEI ESAVSDLRAA MAEDDLEKIK QKLEAANKAV SKIGEHMQQG GGGGSAGSSS
GGDQTPEAEY QDAKEAKM
//
