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Database: UniProt
Entry: M5BMA8_THACB
LinkDB: M5BMA8_THACB
Original site: M5BMA8_THACB 
ID   M5BMA8_THACB            Unreviewed;       525 AA.
AC   M5BMA8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=DnaJ homolog subfamily A member 2 {ECO:0000313|EMBL:CCO28054.1};
DE            EC=3.5.1.3 {ECO:0000313|EMBL:CCO28054.1};
GN   ORFNames=BN14_02046 {ECO:0000313|EMBL:CCO28054.1};
OS   Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS   rot fungus) (Rhizoctonia solani).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX   NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO28054.1, ECO:0000313|Proteomes:UP000012065};
RN   [1] {ECO:0000313|EMBL:CCO28054.1, ECO:0000313|Proteomes:UP000012065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065};
RX   PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA   Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA   Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA   Schlueter A.S.;
RT   "Establishment and interpretation of the genome sequence of the
RT   phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL   J. Biotechnol. 0:0-0(2013).
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:CCO28054.1}.
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DR   EMBL; CAOJ01002781; CCO28054.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5BMA8; -.
DR   HOGENOM; CLU_024340_0_0_1; -.
DR   Proteomes; UP000012065; Unassembled WGS sequence.
DR   GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050152; F:omega-amidase activity; IEA:UniProtKB-EC.
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   CDD; cd10719; DnaJ_zf; 1.
DR   CDD; cd07572; nit; 1.
DR   Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 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   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
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   InterPro; IPR045254; Nit1/2_C-N_Hydrolase.
DR   InterPro; IPR001110; UPF0012_CS.
DR   PANTHER; PTHR43888:SF10; DNAJ-LIKE-2, ISOFORM A; 1.
DR   PANTHER; PTHR43888; DNAJ-LIKE-2, ISOFORM A-RELATED; 1.
DR   Pfam; PF00795; CN_hydrolase; 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; SSF56317; Carbon-nitrogen hydrolase; 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; PS50263; CN_HYDROLASE; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS01227; UPF0012; 1.
DR   PROSITE; PS51188; ZF_CR; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:CCO28054.1};
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          1..212
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
FT   DOMAIN          218..279
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          338..421
FT                   /note="CR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51188"
FT   ZN_FING         338..421
FT                   /note="CR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
SQ   SEQUENCE   525 AA;  57181 MW;  0553EEA1AB3CFF26 CRC64;
     MHFPNYAETI GYKHGEAYDV SASKSESVKA LSAMAKETGT WLLGGSIPER DESDGKLYNT
     ATVYNPQGEL IAIHRKVHLF DIDIPGGITF KESETLTGGT KLTSFQTEFG KIGLAICYDV
     RFPEMAMVAA RKGCVAMLYP GAFNLTTGPL HWELLQRARA VDNQIYVAMC SPARDMSAGY
     HAWGHSMVVD PMGKVIATTE HEEAIIHADI EFNNSISKFY DLLDVSPDCS DADLKKAFRK
     KALRLHPDKG GDPDLFKEVS HAYEVLADGQ KRAAYDRFGE AGLQDSGMPS DHQDLFSQLF
     GGGGGFFGGG GGSRNQGPRK GKDLHHRVAA SLEDLYKGKV TKLALTRHVI CSKCSGKGGK
     EGAVRKCGGC QGRGVKVMLR QMGPMLQQIQ QPCGECDGTG EVINQKDRCK TCNGKKVVSE
     RKFLEVHIDK GMKGGQPITF AGESDQAPGV EPGDVIIIVD EKPHERFKRE GNDLYAEVEL
     DLLTALGGGS FSILHLDDRA LNVPIHPGEV IKPGLLITFS REWGY
//
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