ID A0A176W0R4_MARPO Unreviewed; 775 AA.
AC A0A176W0R4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=DnaJ homolog subfamily C member 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=AXG93_641s1050 {ECO:0000313|EMBL:OAE26664.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE26664.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE26664.1, 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:OAE26664.1};
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:OAE26664.1}.
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DR EMBL; LVLJ01002136; OAE26664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176W0R4; -.
DR OrthoDB; 168809at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IEA:InterPro.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd00167; SANT; 2.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR044634; Zuotin/DnaJC2.
DR PANTHER; PTHR43999; DNAJ HOMOLOG SUBFAMILY C MEMBER 2; 1.
DR PANTHER; PTHR43999:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 2; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS50090; MYB_LIKE; 2.
DR PROSITE; PS51293; SANT; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT DOMAIN 157..239
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 559..614
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 719..769
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 719..765
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 358..426
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 775 AA; 86575 MW; 584C21D4AA08A7F0 CRC64;
MKGGDGKGRE GRSERGGERR GASSVISPEE LISVLWDLGW LAYIGGASIG YGNSLEAASV
FLFGPVTHRL FLTYNSAELV DGAPLYVCSN GSPFQLKKEP AGHSFNEAAK RLLGCLNKVE
EDDTSASDKK EKGSSPSVDS YHFKGKKKGK DDGDQQDHYA LLGLSHLRFL ATEEQIRKSY
REVALKHHPD KQAALILQEE TEEAKQAKKE ETDRHFKAIQ EAYEVLIDPA KRRVYDSIDE
FDDEVPSECS PEDFFKVFGP VFARNGRWSV AQPVPSLGED ESTMADVDRF YDFWWSFKSW
REFPHADEFD LEQAESREHK RWMERQNTKL REKAKKEENG RIRTLIENAY KRDPRIVRRK
EEEKAEKLRK KQAKVLAKQE KELEAARLLE EEKLKKEVED KRIAEEAAAQ KKIREKEKKL
LRKERSRLRS AAAGVTSRKD FRVSDDSVET LCMSLEMVQL RCICEKLEEK KAVEEQAEML
KDIIKRVDDG TFTIEPSYSG SPPQRATTVE SATASTPSSV TEDQPKVSPV KADTGLPNGH
VSSTEPGEEV KKSVSALNGV EKKEKPWSKQ EVELLRKAVA KYPKGTSQRW EVVANYIGTG
RSVDEILKAI KTVLLQKPDS SKAFDSFLQK RKTADVSIAS PLSTREDIGD TGVNPNASTP
VIANGTGNKE KVEGLANGVA APEESSSEKK GPADTQPSSN GNASSAPNGT PGAAEQELWS
ETQELALVKA LKTFPKDTAQ RWERIAAAVP GKNKSQCFKK FAELRENFRS KKGTD
//
