ID F2S1B5_TRIT1 Unreviewed; 656 AA.
AC F2S1B5;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Hsp70-like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TESG_04775 {ECO:0000313|EMBL:EGD97364.1};
OS Trichophyton tonsurans (strain CBS 112818) (Scalp ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=647933;
RN [1] {ECO:0000313|EMBL:EGD97364.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112818 {ECO:0000313|EMBL:EGD97364.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Henn M., Martinez D., Young S.K., Zeng Q., Gargeya S., Haas B.,
RA Alvarado L., Berlin A., Chapman S., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA Larson L., Mehta T., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., White T.C.,
RA Abdel-Rahman S., Graser Y., Gurr S.J., Kohler G., Martinez-Rossi N.,
RA Oliver B.C., Rossi A., Shelest E., Summerbell R., Lander E., Nusbaum C.,
RA Birren B.;
RT "Annotation of Trichophyton tonsurans strain CBS 112818.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG698501; EGD97364.1; -; Genomic_DNA.
DR AlphaFoldDB; F2S1B5; -.
DR HOGENOM; CLU_009958_6_2_1; -.
DR OrthoDB; 1377857at2759; -.
DR Proteomes; UP000009172; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd10229; HSPA12_like_NBD; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR14187; ALPHA KINASE/ELONGATION FACTOR 2 KINASE; 1.
DR PANTHER; PTHR14187:SF79; HSP70 FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G15200); 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 631..652
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 71314 MW; 58B9DCF0A2AA34F5 CRC64;
MDLMSSRFKL GFGNKRKSGS SLAPTTTATN TPPNGSPSQP SPPPGNTSNP NASSASLPMN
PQNHLGRPPS YTYAPGAPRP ASPLPPGGQH HPQQLAHHPP PLNTGVGVPY PTGGGMASAP
PPPGYGGYPP QSTGQGHGIP QPLAPFRGHT GELDNQARSK AQLIVGIDFG TTFSGVAYAF
ATNTEAREDI ITEWPGAGTH TKQKIPTVLY YDQYQKVVGW GPDIADALAP TGYPKAGVQK
VEWFKLQLMS SGGNTYIDPI NLPPLPPGKS EIDVAADYLF HLRGAMRNQL QKTLGEVFNR
EERNIRYFLT VPAIWNDAGK AATRAAAIQA GFLRDENDNR LTLITEPEAA AMFCAKTGLL
NLKIHDAILI VDCGGGTVDL IAYEVDEETP FSVCECTAGS GDSCGSTALN RNFSNILRAK
IRKMKLPDGS RTAGKVYAKC IMDFENRIKA DFRNNGQKWA VDVGIEADFP EAGIEEGYMT
FTNEEILQCF EPVVNRILEL VRNQIIAIQA QNRPLQNVLV VGGFGASEYL FQQIKLHVPP
QYQSKVVRPM DSVAAIVKGA VTAGITERVV TSRVARRHYL MATLQPFKEG HHPEQYRVPS
LDGKDRCKYT RQIFVQKGER IKNGEPVKVS FFRQVALGAT LMIHVMLSLF LFPFSS
//
