ID A0A2H3IG60_9EURO Unreviewed; 528 AA.
AC A0A2H3IG60;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Heat shock protein DnaJ {ECO:0000313|EMBL:PCH02283.1};
GN ORFNames=PENO1_038750 {ECO:0000313|EMBL:PCH02283.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH02283.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCH02283.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCH02283.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PCH02283.1}.
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DR EMBL; NPFK01000086; PCH02283.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IG60; -.
DR STRING; 290292.A0A2H3IG60; -.
DR OrthoDB; 5491419at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR041661; ZN622/Rei1/Reh1_Znf-C2H2.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR44029; DNAJ HOMOLOG SUBFAMILY C MEMBER 21; 1.
DR PANTHER; PTHR44029:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 21; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF12756; zf-C2H2_2; 1.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW Stress response {ECO:0000313|EMBL:PCH02283.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 23..89
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 319..343
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 485..514
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 361..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 59642 MW; 6C3FA0E6A3C3ED46 CRC64;
MGQSQSTGAN KDDTGQEAER RIDYYELLGV ERDATDDEIK KAYRRKALEL HPDRNYGQVE
AATKLFAEVQ CAYEVLSDPQ ERAWYDSHQY AELTEDGAAA AGGQQPASGG FKMTASGITS
LVMNFNPHME FSDSPSGFFG GLRDIFDQIA MDEGIAYRWD GSEPVDYPSF GAKEDSYEDV
VRPFYAVWTS FSTKKSFAWM DKYKYSEAPD RRIRRLMEKE NKKMREDGIR EYNDAVRSLV
AFVKKRDPRY KSNIQTEAER QRMLRESAAA QAARSRAANQ AKMQDHVIPE WAQTHESQPG
EDEHEGHFFS SSESEVEHFE CVVCNKLFKS QKQFEAHEKS KKHIKAVKQL RKEMLLEDEE
LNLDVDEEPE AKLVESEEDI VSTHDTPNAE VDDDIGETEV NDKDIPATAS RSPSPSASDD
EDEDYIDPDR TKPEHTPLSS SEIANEDGNE DLESKPTTAK LGKAKQKRAK KLAAQQAASS
IDAQNKCAHC QATFTSRTQL FSHLRETGHA QPVQTAQSKS KKGKKSRK
//
