ID A0A164TGV0_9AGAM Unreviewed; 393 AA.
AC A0A164TGV0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=DnaJ-domain-containing protein {ECO:0000313|EMBL:KZS92351.1};
GN ORFNames=SISNIDRAFT_412505 {ECO:0000313|EMBL:KZS92351.1};
OS Sistotremastrum niveocremeum HHB9708.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314777 {ECO:0000313|EMBL:KZS92351.1, ECO:0000313|Proteomes:UP000076722};
RN [1] {ECO:0000313|EMBL:KZS92351.1, ECO:0000313|Proteomes:UP000076722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB9708 {ECO:0000313|EMBL:KZS92351.1,
RC ECO:0000313|Proteomes:UP000076722};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV419410; KZS92351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164TGV0; -.
DR STRING; 1314777.A0A164TGV0; -.
DR OrthoDB; 5491419at2759; -.
DR Proteomes; UP000076722; Unassembled WGS sequence.
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; IPR036869; J_dom_sf.
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; PF12874; zf-met; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076722};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 24..82
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 323..352
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 393 AA; 44779 MW; 1839DA8D532146A1 CRC64;
MGANASSHNH NDNTGAAPAE DQQDYYTLLG VSEDATSEDI KATFRKLALV HHPDKNADDI
EGATQRFAAI QQAYEERAWY DTHRSSLVPE ADAEDVLNDM RHGSGSNNKS SVPRGRGLTS
KHLMRFFDAT VWSGFDDSDS GFFNIYRNLF QRLAEDEEQH GSDVDYPSFG TSSWPWMPAE
KGLEHEAAKT FYNYWSSFAT AKEFVWMEQW NLQEAPDRRV RRLMEKDNKK ARDDAKRDYN
DTVRSLVMFI RKRDPRYKAH IASQASATNS GTSTPRHAVA ASAAAARKRA EASEAYVEQD
WQRVKPEDGA DGDWNDAEGA EEWECVACGK SFRSEAQWNS HERSRKHLKE VERCRYLAFQ
PEIFPLMHAN KVTTRNGARE RGTEFRGRTA RST
//