ID A8N722_COPC7 Unreviewed; 667 AA.
AC A8N722;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Heat shock protein {ECO:0000313|EMBL:EAU91259.1};
GN ORFNames=CC1G_06894 {ECO:0000313|EMBL:EAU91259.1};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU91259.1, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU91259.1, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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:EAU91259.1}.
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DR EMBL; AACS02000003; EAU91259.1; -; Genomic_DNA.
DR RefSeq; XP_001830628.1; XM_001830576.1.
DR AlphaFoldDB; A8N722; -.
DR STRING; 240176.A8N722; -.
DR GeneID; 6007073; -.
DR KEGG; cci:CC1G_06894; -.
DR VEuPathDB; FungiDB:CC1G_06894; -.
DR eggNOG; KOG0102; Eukaryota.
DR InParanoid; A8N722; -.
DR OMA; GREQKMT; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000001861; 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 GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
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:UP000001861};
KW Stress response {ECO:0000313|EMBL:EAU91259.1}.
FT REGION 612..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 72085 MW; CDA0D3AA9D7FDEFD CRC64;
MFAAARSSLR SSVSRTGHYA ALPRTMIARN MNSKVNGPVV GIDLGTTNSC VAVMEGQSSR
VIENAEGART TPSVVAFTKH GERLVGLPAK RQAVVNAANT VFAFKRLVGR QYSDKEVQDD
AKHWPFQIVK KSDGHPAIEV DNGGKRQTFT PEELSSMVLV KMKETAEQYL NKKVNHAVVT
VPAYFNDAQR QATKDAGQIA GLDVLRVINE PTAAALAYGL DRADNSVIAV YDLGGGTFDI
SILEMQKGVF EVKSTNGDTH LGGEDFDVVL VEHILAEFQK ESGLDLKGDR MAIQRVREAA
EKAKIELSST QQTEINLPFI TADASGPKHI NLKLNRSQFE ALVDPLVKRT FDPCKKALSD
AGVKASEVNE VILVGGMTRM PKVVDTVKSI FGREPSKGVN PDEAVAIGAS IQGGVLAGNV
TDILLLDVTP LSLGIETLGG IMTKLINRNT TIPTKKSQVF STAADGQTAI EVKIYQGERE
LVRDNKLLGN FNLVGIPPAP KGVPQIEITF DIDADGIVNV SAKDKATNKD QSMTIASSSG
LSDKDIERMV AESEQYAEAD KARRALIEEG NKADSVCHDT EKAMNDFKDQ LDAAEKEKVS
KLLVELRELA TKGQAGDPSV TPEQIKEKIS ETQQASLGLF QKVYEKRAAE SSSSSSSESE
NKEEKKD
//
