ID A0A176WRH1_MARPO Unreviewed; 554 AA.
AC A0A176WRH1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=J domain-containing protein {ECO:0000259|PROSITE:PS50076};
GN ORFNames=AXG93_1550s1170 {ECO:0000313|EMBL:OAE35211.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE35211.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE35211.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE35211.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) 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:OAE35211.1}.
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DR EMBL; LVLJ01000228; OAE35211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176WRH1; -.
DR OrthoDB; 1214888at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
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 Gene3D; 1.10.287.110; DnaJ 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; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR24078:SF553; DNAJ HOMOLOG SUBFAMILY B MEMBER 13; 1.
DR PANTHER; PTHR24078; DNAJ HOMOLOG SUBFAMILY C MEMBER; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT DOMAIN 213..279
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 60619 MW; FB417304A71AFC2C CRC64;
MNAGQRGSGR GNHRRAGETR GLSRKFRTIL LGESGDGPHP RLAQRGGRPW AAVDAHRRRR
AAVSPALDLG FGFVSWAGDR RFLFRQAGSG ESGRASERAG GRAEADRTTY LAAKKPEQLQ
QHEARARKRS KGGAASEGWA ARQSMTANAN ANARPLQHRA RSEEAEAEVV VARVSGEEKE
AKANEEVEIE RGEGGNSKRK REEQSVELGM GVDYYNVLKV PKNASDDDLK KAYRKLAMKW
HPDKNPNNKK DAEAKFKQIS EAYEVLSDPQ KRAIYDQYGE EGLKGQVPPQ GAQQAGYSNG
GTTNTFRFNP RNAEDIFAEF FGGSPFGGMG GISGIGSRSG RGNFGDGMFG GFNTTENVFR
SFGEGAQSSG PRKAPPVENK LQCTLEELYN GSTRKMKISR NIADPSGKTM PVEEILTIEV
KPGWKKGTKI TFPEKGNEQP NVVPADLVFV IDERPHEIFK RDGNDLIMTH KVSLSEALTG
CTVNLTTLDG RLLNIPITEV INPGYEKVVQ KEGMPIAKES GKRGNLRIKF EIKFPARLSP
EQKQGLKRLL GGAG
//
