ID A9SLS0_PHYPA Unreviewed; 349 AA.
AC A9SLS0;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=J domain-containing protein {ECO:0000259|PROSITE:PS50076};
GN ORFNames=PHYPA_015967 {ECO:0000313|EMBL:PNR43586.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR43586.1};
RN [1] {ECO:0000313|EMBL:PNR43586.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c12_8210V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR43586.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c12_8210V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c12_8210V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
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DR EMBL; ABEU02000012; PNR43586.1; -; Genomic_DNA.
DR RefSeq; XP_001767250.1; XM_001767198.1.
DR AlphaFoldDB; A9SLS0; -.
DR STRING; 3218.A9SLS0; -.
DR PaxDb; 3218-PP1S91_238V6-1; -.
DR EnsemblPlants; Pp3c12_8210V3.1; Pp3c12_8210V3.1; Pp3c12_8210.
DR EnsemblPlants; Pp3c12_8210V3.2; Pp3c12_8210V3.2; Pp3c12_8210.
DR Gramene; Pp3c12_8210V3.1; Pp3c12_8210V3.1; Pp3c12_8210.
DR Gramene; Pp3c12_8210V3.2; Pp3c12_8210V3.2; Pp3c12_8210.
DR eggNOG; KOG0713; Eukaryota.
DR HOGENOM; CLU_017633_0_0_1; -.
DR InParanoid; A9SLS0; -.
DR OMA; LYITYNV; -.
DR OrthoDB; 2785358at2759; -.
DR Proteomes; UP000006727; Chromosome 12.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
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; PTHR44298; DNAJ HOMOLOG SUBFAMILY B MEMBER 11; 1.
DR PANTHER; PTHR44298:SF1; DNAJ HOMOLOG SUBFAMILY B MEMBER 11; 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:UP000006727};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..349
FT /note="J domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014297941"
FT DOMAIN 26..91
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
SQ SEQUENCE 349 AA; 39427 MW; CF3E72705FA4DC48 CRC64;
MWIGKVSVFL LLFSVSVVEL VSAGKSYYDI LQVSRQASDD QIKRSYRKLA LKFHPDKNPG
NEEATKKFAE INNAYEVLSD KEKRGIYDQY GEEGLREHQQ GGGRGGGGFG QDIFSQFFGG
GFRFGGEEEE EERTPKGEDV LVEIYATLED LYVGNSYQVW RDKNVVKPAS GKRRCNCKNK
VVHRQIGPGM YQQYTEQVCQ ECPNVKFERV GQFLTVDIEK GMRDGQEIIF YEDGEPIIDG
EPGDLKFIVR TKPHSRFRRE GNDLHVTVTL TLLESLVGFK KNIDHLDGHK VDVGSNLVTK
PKEVRKFPGE GMPLFESNKK GNLFVTFEVV FPSSLSDEQK SVISKTLGS
//
