ID A0A0D2GZ39_9EURO Unreviewed; 614 AA.
AC A0A0D2GZ39;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=non-chaperonin molecular chaperone ATPase {ECO:0000256|ARBA:ARBA00012554};
DE EC=3.6.4.10 {ECO:0000256|ARBA:ARBA00012554};
GN ORFNames=Z517_03121 {ECO:0000313|EMBL:KIW83875.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW83875.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW83875.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW83875.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-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}.
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DR EMBL; KN846970; KIW83875.1; -; Genomic_DNA.
DR RefSeq; XP_013287683.1; XM_013432229.1.
DR AlphaFoldDB; A0A0D2GZ39; -.
DR STRING; 1442368.A0A0D2GZ39; -.
DR GeneID; 25302611; -.
DR VEuPathDB; FungiDB:Z517_03121; -.
DR HOGENOM; CLU_005965_0_1_1; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000053029; 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:UP000053029}.
SQ SEQUENCE 614 AA; 66899 MW; C5C52F7014D96E25 CRC64;
MADEVYEGAI GIDLGTTYSC VAVYEGTNVE IIANEQGSFT TPSFVSFTDE ERLIGEAAKN
QAAMNPENTV FDVKRLIGRR FDDPTVKKDI ESWPFKVVDQ GGNPMVQVQY LGETKTFSPQ
EISSMVLMKM KEVAETKLGK KVSKAVVTVP AYFNDNQRQA TKDAGAISGL NVLRIINEPT
AAAIAYGLGS GKSDKERNVL IYDLGGGTFD VSLLNIQGGV FTVKATAGDT HLGGQDFDTN
LLEHFKKEFT RKTKKDLSGD ARALRRLRTA CERAKRTLSN GTQATVEIDS LFDGEDFNAT
ITRARFEDLN AKIFNGTLEP VQQVLKDANI EKSKVDEIVL VGGSTRIPRI QKLLSDFFDG
KKLEKSINPD EAVAYGAAVQ AGILSGKATS AETADLLLLD VVPLSLGVAM EGNIFAPVVP
RGNTVPCIKK RTFTTVVDNQ QTVQFPVYQG ERTNCEDNTS LGEFTLSPIP PMRAGDAALE
VVFEVDVNGI LKVTATEKSS GRSANITISN AVGKLSTTEI EKMVEDAAKF KTSDEAFTKK
FEAKQQLESY IGRVEELIND PGLSMKMKRG NKAKIEEALS DAMQQLEVDD STPDDLKKKE
LALKRAMTKA MATR
//
