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Database: UniProt
Entry: A0A2N5SBH2_9BASI
LinkDB: A0A2N5SBH2_9BASI
Original site: A0A2N5SBH2_9BASI 
ID   A0A2N5SBH2_9BASI        Unreviewed;       491 AA.
AC   A0A2N5SBH2;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=J domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PCANC_23148 {ECO:0000313|EMBL:PLW10600.1};
OS   Puccinia coronata f. sp. avenae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW10600.1, ECO:0000313|Proteomes:UP000235388};
RN   [1] {ECO:0000313|EMBL:PLW10600.1, ECO:0000313|Proteomes:UP000235388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12NC29 {ECO:0000313|EMBL:PLW10600.1};
RA   Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA   Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA   Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT   "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT   Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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:PLW10600.1}.
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DR   EMBL; PGCJ01001053; PLW10600.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5SBH2; -.
DR   STRING; 200324.A0A2N5SBH2; -.
DR   Proteomes; UP000235388; 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:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 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   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; 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   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00546}; Reference proteome {ECO:0000313|Proteomes:UP000235388};
KW   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          71..134
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          222..306
FT                   /note="CR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51188"
FT   ZN_FING         222..306
FT                   /note="CR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT   REGION          26..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   491 AA;  54296 MW;  6B128CEF500F95A3 CRC64;
     MVDGRGERVP PWPVLEESSV LPGYPWTHSR NEPLPISHSE SHRTKRKRSQ HILIPLGTHS
     PASMASPSQQ DLYDILELPQ SASRSEIRAA YHRLAKRSHP DKNPGADPAV FHALQQAYET
     LSDPQRRAEY DARPKKASMV PSSQHPHPFG SAFESLFTSM FRDDLADGFF AGHPFFPSHH
     HPFHPPWNHR STPQPPKWSS PQVKSPDLNI DFQCTLDDIM NGRTVITEIP RQVGCQLCHA
     TGFHPNAAPR HCRHCDGKGY QSCTQAFHGL VTHTQSTCSR CNGTGSKMSS DDCCSQCRGS
     CIITETVAIE WEIVKGMLPG QMMTLSEMGN TLPGHLAGDV VICLCVAPHR SFKMISPDSR
     DLILGLSLTL SESLLGVDRV LFRHLDGRDI RVSLPGPHQQ GHSVIKPGDI KAIRGMGLPG
     HSPAEPHGDL WIKFDIEWPS SEWIRSQDFS LLQNALPPAL PDLPHSDAPQ EYAILESAVL
     NTETAKAADL T
//
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