ID B8M6X9_TALSN Unreviewed; 577 AA.
AC B8M6X9;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Hsp70 chaperone (BiP), putative {ECO:0000313|EMBL:EED20199.1};
GN ORFNames=TSTA_034380 {ECO:0000313|EMBL:EED20199.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED20199.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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DR EMBL; EQ962654; EED20199.1; -; Genomic_DNA.
DR RefSeq; XP_002480633.1; XM_002480588.1.
DR AlphaFoldDB; B8M6X9; -.
DR STRING; 441959.B8M6X9; -.
DR GeneID; 8104280; -.
DR VEuPathDB; FungiDB:TSTA_034380; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_0_3_1; -.
DR InParanoid; B8M6X9; -.
DR OMA; DQVLMDH; -.
DR OrthoDB; 23943at2759; -.
DR PhylomeDB; B8M6X9; -.
DR Proteomes; UP000001745; 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; cd10232; ScSsz1p_like_NBD; 1.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR45639:SF32; HEAT SHOCK PROTEIN PDR13; 1.
DR PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT REGION 475..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..512
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 61925 MW; FD6A3701B2EDC6AA CRC64;
MSEETGAGER FAIGISFGNS SSSIAFTGPD GKAEVIANEE GDRQIPSILS YVDSEEFHGT
QAKAQLVRNS KNTVGYFRDY LGKDFKSIDP TPAHQSAHPQ QHESTVAFTI RDTDAETPST
VTVSEITTRH LRRLKQSASD FLGKTVNAAV ITVPTNFSDA QREALVAAAK NADIEALQLI
HEPVAALLAY DARPDAVVED KLVVIADFGG IRSDVAVVAS RGGMYSVLAT VHDYELGGAN
LDQVVIDHFA KEFIKKHKVD PREDARGLAK LKLEGEATKK ALSIGTNATL SIESLVNGID
YGSTINRTRY ELLSGKIFSQ FTGLVESAVK KAELDVLDID EVILAGGTSH TPKIARLLQN
VFPEKTKVLA PSTTPSAINP SELSARGAAY QASLIQEFDK EDIEQSLHPM VTVTPHLSKT
IGVQLVSADE NAEDAVFAPL VNAETALPAR RVAQYTVPKE GGDVLVRISE GEREIKVTKP
EPKPKAEKSE KDEEDSDSDS DFDSDEDEEE ETREIIWKST KTIAEAAIKG VKAGGKVEVT
ININPDLGLQ ITAREVGGKG GVRLAVEAPQ ASANGSA
//
