ID A0A2J6TJZ1_9HELO Unreviewed; 444 AA.
AC A0A2J6TJZ1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JUN-2023, entry version 20.
DE SubName: Full=DnaJ-domain-containing protein {ECO:0000313|EMBL:PMD63331.1};
GN ORFNames=K444DRAFT_522983 {ECO:0000313|EMBL:PMD63331.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD63331.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD63331.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD63331.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-2016) 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; KZ613782; PMD63331.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6TJZ1; -.
DR STRING; 1095630.A0A2J6TJZ1; -.
DR InParanoid; A0A2J6TJZ1; -.
DR OrthoDB; 168809at2759; -.
DR Proteomes; UP000235371; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IEA:InterPro.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 1.10.8.840; Ribosome-associated complex head domain; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR032003; RAC_head.
DR InterPro; IPR042569; RAC_head_sf.
DR InterPro; IPR044634; Zuotin/DnaJC2.
DR PANTHER; PTHR43999; DNAJ HOMOLOG SUBFAMILY C MEMBER 2; 1.
DR PANTHER; PTHR43999:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 2; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF16717; RAC_head; 1.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 4: Predicted;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000235371}.
FT DOMAIN 101..171
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT REGION 50..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 50427 MW; 5A92D9A9DE6DFA90 CRC64;
MATHTQVNLP LPVLPETWSG EKDFKAIGKL SAATQRSIEP VGPHFLAHAR RARHKRTFSE
DDRIQAQENV KKVEDDDSGE ISEPEDPMML SRDAKDWKSQ DHYAVLGLSK YRYKATEEQI
KRAHRKKVLR HHPDKKAAAG STEDDSFFKC IQKATEILLD PVKRRQFDSV DEHADLEPPT
KKQLKEGKYY KLWSNVFKSE GRFSRVQPVP KFGDEKSNKE DVDTFYNFFY NFDSWRSFEY
QDEDVPDDNE NRDQKRHMER KNNNARKKKK TEDSARLRRL VDDAMAGDER IKRFRQEANA
SKNKKRLDKE AAEKKALDDA KAAKEAEAKA AKEAEEKAKA EREQGKKAKE AAKAAVKKNR
RVLKGSVKDA NYFVSGVAPA SVIDAVLNDV ELVQGKIDAD ETAALAGKLN GLKIADEIKG
VWSSEVKRLV SAGKIKDSDV KGLA
//
