ID F2TJ85_AJEDA Unreviewed; 410 AA.
AC F2TJ85;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=DnaJ like subfamily A member 2 {ECO:0000313|EMBL:EGE83298.1};
GN ORFNames=BDDG_06242 {ECO:0000313|EMBL:EGE83298.1};
OS Ajellomyces dermatitidis (strain ATCC 18188 / CBS 674.68) (Blastomyces
OS dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=653446 {ECO:0000313|EMBL:EGE83298.1};
RN [1] {ECO:0000313|EMBL:EGE83298.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18188 {ECO:0000313|EMBL:EGE83298.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease.;
RA Cuomo C., Klein B., Sullivan T., Heitman J., Young S., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A.M., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Blastomyces dermatitidis strain ATCC 18188.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GG749447; EGE83298.1; -; Genomic_DNA.
DR AlphaFoldDB; F2TJ85; -.
DR HOGENOM; CLU_017633_10_2_1; -.
DR Proteomes; UP000007802; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10747; DnaJ_C; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1.
DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR HAMAP; MF_01152; DnaJ; 1.
DR InterPro; IPR012724; DnaJ.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR044713; DNJA1/2-like.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR43888:SF10; DNAJ-LIKE-2, ISOFORM A; 1.
DR PANTHER; PTHR43888; DNAJ-LIKE-2, ISOFORM A-RELATED; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00546}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00546};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00546}.
FT DOMAIN 6..71
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 132..215
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 132..215
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 354..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 410 AA; 45273 MW; AECB6EE0141244EF CRC64;
MVKETKYYDI LGVSPNATDA ELKTAYKKGA LKHHPDKNAH NPEAAEKFKD LSHAYEILSD
SQKRQIYDQY GEEGLEQGGA GGGMQAEDLF AQFFGGSAFG GMFGGGMRDT GPKKARTIVH
PLKVSLEDIY RGKISKLALK KSVICPGCDG IGGKPGSVKQ CGPCGGTGKR TMMRQMGPMI
QRFVVECSDC DRTGQVINER DRCKKCKGNK VIIERKVLHV HIDRGVKPGH KIDFRGEGDQ
APGVITGDVQ FEIDQQPHPR FQRKDDDLFY QADIDLLTAL AGGTINVEHL DDRWLTVQIA
PGEPITPGQI KVIKGQGMPS FRHHDFGNLY IQFNVKFPEK EDIRNVELLE QVLPPRPLQP
QPPADSMVED FNLEDVEDSG RARAHGAVHM GDEDDDDIPP GAERMQCASQ
//
