ID A0A060SDV4_PYCCI Unreviewed; 705 AA.
AC A0A060SDV4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=J domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BN946_scf184636.g10 {ECO:0000313|EMBL:CDO70578.1};
OS Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO70578.1, ECO:0000313|Proteomes:UP000029665};
RN [1] {ECO:0000313|EMBL:CDO70578.1, ECO:0000313|Proteomes:UP000029665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM137 {ECO:0000313|EMBL:CDO70578.1,
RC ECO:0000313|Proteomes:UP000029665};
RA Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA Pontarotti P., Henrissat B., Record E.;
RT "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT breakdown.";
RL Submitted (JAN-2014) 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:CDO70578.1}.
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DR EMBL; CCBP010000086; CDO70578.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060SDV4; -.
DR STRING; 5643.A0A060SDV4; -.
DR HOGENOM; CLU_024340_0_0_1; -.
DR OMA; TAFICAK; -.
DR OrthoDB; 2785358at2759; -.
DR Proteomes; UP000029665; 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:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; 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 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 HAMAP; MF_01152; DnaJ; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
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 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 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00546}; Reference proteome {ECO:0000313|Proteomes:UP000029665};
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 10..276
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
FT DOMAIN 313..374
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 433..516
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 433..516
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 665..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 705 AA; 77683 MW; F52F58BDF0CFF75C CRC64;
MSSAPAFKPF NLALIQLGEV GPDKDANLKH AREMIRKAAS GSNGAVPKPD LVVLPECFNS
LYGVTYFPVY AETIGYTPGQ SYDVASSQSQ SVKMLSAAAR EERVWLIGGS IPERDAGTGK
LYNTATVYSP KGELVAMHRK VHLFDIDIPG KIKFKESEIL SAGNTINQFD TDFARIGLGI
CYDVRFPELA MTNTRRGCHM LIYPSAFNTT TGPLHWELLQ RARAVDNQVY FAMCSPARDL
NQSYHAWGHS MVVDPMGKVI AETEDEEDIV YAHIVALLHL SSPSQSFLSL ANPSAPSSSL
HLSVDPAMVK ETKYYDLLEV SPDASESELK KAYRKKALRL HPDKGGDPEL FKEVTHAYEV
LSDPQKRSIY DARGEAGLSD AGGMGGMDPQ DLFSQLFGGG GFFGGGGGRS PGPRKTKDLV
HRIHVTLEDL YKGKTTKLAL TRNVICPKCS GKGGKEGAVR PCTSCSGRGI KITLRQMGPM
IQQLQQPCDE CNGTGEIINQ KDRCKQCNGK KVVPEKKMLE VHIDKGMRGG QTITFSGESD
QAPGVTPGDV IIVIEEKPHE RFRRQDNDLF YEQEVDLLTA LGGGQFAIRH LDDRALIVNI
PPGEVLKNDD LKVIRGQGMP SQRHHEPGDL FVRIHVKFPD HIDPEVIPLL EKALPPRQPI
EKFPPSVLLE EVAMDEVDQR QRERATGEDA MDEDEDQPRV QCANQ
//
