ID F2PN73_TRIEC Unreviewed; 646 AA.
AC F2PN73;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Heat shock protein hsp70 {ECO:0000313|EMBL:EGE03341.1};
GN ORFNames=TEQG_02374 {ECO:0000313|EMBL:EGE03341.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
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DR EMBL; DS995727; EGE03341.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PN73; -.
DR VEuPathDB; FungiDB:TEQG_02374; -.
DR eggNOG; KOG0102; Eukaryota.
DR HOGENOM; CLU_005965_2_1_1; -.
DR Proteomes; UP000009169; 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 CDD; cd11733; HSPA9-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 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:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 2.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
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 Stress response {ECO:0000313|EMBL:EGE03341.1}.
FT REGION 615..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 546..573
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 646 AA; 70499 MW; 9675957E17F2DF4A CRC64;
MLASRICRAA PRVPTQFIRS PAFRVPSTSF RRWNSTEGGE EKVKGQVIGI DLGTTNSAVA
VMEGKTPKIM ENSEGTRTTP SVVAFTKDGE RLVGVAAKRQ AVVNPENTLF ATKRLIGRKF
TDPECQRDLS EVPYKIVQHT NGDAWVEAQG QKYSPSQIGG FVLQKMKETA EGYLNKPIKN
GVVTVPAYFN DSQRQATKDA GQIAGLNVLR VVNEPTAAAL AYGLEKEQDR VIAVYDLGGG
TFDISILEIQ KGVFEVKSTN GDTHLGGEDF DITLVRNIVQ QFKKDSGIDL SGDRMAIQRI
REAAEKAKME LSSASQTEIN LPFITADSSG AKHINSKLTR SQLEALVDPL IQRTVEPVRK
ALKDANLTAK DIQEVILVGG MTRMPKVTES VKSIFGREPA KSVNPDEAVA IGAAIQGAVL
AGEVTDVLLL DKSQTFSTAA DFQTAVEIKV YQGERELVRD NKLLGNFQLV GIPPAHRGVP
QIEVTFDIDA DSIVHVHAKD KSTNKDQSIT IASGSGLSDS EIQNMVNDAE TYRAQDIERK
ALIEGANRAD SVLNDTEKAL KEFEEKLDKA EATQITEKIT ALREVVAKCQ SGESTITAEE
LKAKVDDLQT SSLTLFDKMH KARHEESQQQ QQQPPQGEEK PKDGSN
//
