ID F8PY62_SERL3 Unreviewed; 517 AA.
AC F8PY62;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=J domain-containing protein {ECO:0000259|PROSITE:PS50076};
GN ORFNames=SERLA73DRAFT_73414 {ECO:0000313|EMBL:EGN98825.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
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DR EMBL; GL945480; EGN98825.1; -; Genomic_DNA.
DR AlphaFoldDB; F8PY62; -.
DR STRING; 936435.F8PY62; -.
DR eggNOG; KOG0714; Eukaryota.
DR HOGENOM; CLU_031313_0_0_1; -.
DR InParanoid; F8PY62; -.
DR OMA; KDAMHIK; -.
DR OrthoDB; 1341614at2759; -.
DR Proteomes; UP000008063; Unassembled WGS sequence.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10747; DnaJ_C; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR24078; DNAJ HOMOLOG SUBFAMILY C MEMBER; 1.
DR PANTHER; PTHR24078:SF538; PROTEIN SIS1; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008063}.
FT DOMAIN 11..81
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT REGION 78..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 56949 MW; D1CC7766D878AEA0 CRC64;
MSHPPGLEKN DRYVVLGLSP DATDDEIRSA YKKLALKWHP DRHTVDKEHA AQMFIEVNAA
YRALMDGKET IHSKLAEDTA KSASGSDGHS THSSSKHETH SKSSAGKEHE TSSDTSASPK
PDSEFGTKNT HSSTAKSNSK SSYSGSSSRS SKTPNTRSRP KHDHPSSMPS HATPSESHST
NSSREHIHSS YKMDDHQARS TSSRRHHGSA HTSASPPSGT HSEKDKDTHP PSSHTHFSAT
STATPAESGT SVRSKTSRSR GIRTNVSNSS KPVIPPISQL HKSSRFGFGD DFVQKLSKGK
PKTPKRRKAE DGSDSEDEGA PVYGSPLRPL TSPRGSSKEW IFPLPLTLDD MYHGTNFRFR
IIREMLSRQK KEVEIEIDIP PGCRSGTRIV CPGTGHERKD GTLQDVVFLV EEVSHDRFSR
VKDDLFLDIC VPWVDSLADQ GGELCVEGIN GEEIMFSLPY PLQDQATEGK IIIKRAGMPV
FHTGKTKGRG DLIIRWQVVF SNPSKWQSLK KVFHLKA
//
