ID A0A161YBM2_9PEZI Unreviewed; 614 AA.
AC A0A161YBM2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=non-chaperonin molecular chaperone ATPase {ECO:0000256|ARBA:ARBA00012554};
DE EC=3.6.4.10 {ECO:0000256|ARBA:ARBA00012554};
GN ORFNames=CI238_01698 {ECO:0000313|EMBL:KZL87132.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL87132.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL87132.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL87132.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
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:KZL87132.1}.
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DR EMBL; LFIW01000334; KZL87132.1; -; Genomic_DNA.
DR STRING; 1573173.A0A161YBM2; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000076584; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1270.10; -; 1.
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; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF467; RIBOSOME-ASSOCIATED MOLECULAR CHAPERONE SSB1-RELATED; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584}.
SQ SEQUENCE 614 AA; 66685 MW; 82F21EFBCFDA0265 CRC64;
MADEVYDGAI GIDLGTTYSC VATYEGTNVE IIANEQGSFT TPSFVSFTDK ERLIGEAAKN
QAAMNPINTV FDVKRLIGRR FDDPTVKKDI ESWPFKVVDD NGNPKVQVEY LGETKTFSPQ
EVSSMVLLKM KEIAEVKIGK KVEKAVITVP AYFNDNQRQA TKDAGAIAGL NVLRIINEPT
AAAIAYGLGA GKSGKERNVL IYDLGGGTFD VSLLNIQGGV FTVKATAGDT HLGGQDFDTN
LLDHCKKDFQ RKTKKDLSGD PRALRRLRTA CERAKRTLSS GAQTTIEIDS LFDGEDYTTQ
ITRARFEDLN AKAFNGTLEP VAQVLKDASI EKSGVDEIVL VGGSTRIPRI QKLLSEFFDG
KKLEKSINPD EAVAYGAAVQ AGILSGKATS AETADLLLLD VVPLSLGVAM EGNIFAPVVP
RGNTVPCLKK RTFTTVADNQ QTVQFPVFQG ERVNCEDNTS LGEFTLAPIP PMRAGEAVLE
VVFEVDVNGI LKVTATEKTS GRSANITISN SVGKLSSHEI ENMISDAEKF KSNDEAFSKR
FEAKQQLESY IGRVEEIISD PTLSLKLKRG QKDKIEQQVS EAMAALEITD AGADDLKKQE
LALKRLVTKA MSSR
//
