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JJJ1_ARATH
ID   JJJ1_ARATH              Reviewed;         630 AA.
AC   Q9C911;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 144.
DE   RecName: Full=DNAJ protein JJJ1 homolog {ECO:0000305};
DE            Short=AtJJJ1 {ECO:0000305};
GN   Name=JJJ1 {ECO:0000305};
GN   OrderedLocusNames=At1g74250 {ECO:0000312|Araport:AT1G74250};
GN   ORFNames=F1O17.8 {ECO:0000312|EMBL:AAG52405.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   INTERACTION WITH REIL1 AND REIL2.
RX   PubMed=24603461; DOI=10.4161/psb.28224;
RA   Schmidt S., Dethloff F., Beine-Golovchuk O., Kopka J.;
RT   "REIL proteins of Arabidopsis thaliana interact in yeast-2-hybrid assays
RT   with homologs of the yeast Rlp24, Rpl24A, Rlp24B, Arx1, and Jjj1
RT   proteins.";
RL   Plant Signal. Behav. 9:E28224-E28224(2014).
CC   -!- SUBUNIT: Interacts with REIL1 AND REIL2. {ECO:0000269|PubMed:24603461}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130}.
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DR   EMBL; AC020579; AAG52405.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35570.1; -; Genomic_DNA.
DR   PIR; H96770; H96770.
DR   RefSeq; NP_177565.1; NM_106085.2.
DR   AlphaFoldDB; Q9C911; -.
DR   SMR; Q9C911; -.
DR   STRING; 3702.AT1G74250.1; -.
DR   iPTMnet; Q9C911; -.
DR   PaxDb; Q9C911; -.
DR   PRIDE; Q9C911; -.
DR   ProteomicsDB; 238991; -.
DR   EnsemblPlants; AT1G74250.1; AT1G74250.1; AT1G74250.
DR   GeneID; 843765; -.
DR   Gramene; AT1G74250.1; AT1G74250.1; AT1G74250.
DR   KEGG; ath:AT1G74250; -.
DR   Araport; AT1G74250; -.
DR   TAIR; locus:2019647; AT1G74250.
DR   eggNOG; KOG0717; Eukaryota.
DR   HOGENOM; CLU_009539_1_1_1; -.
DR   InParanoid; Q9C911; -.
DR   OMA; SEYSENC; -.
DR   OrthoDB; 858842at2759; -.
DR   PhylomeDB; Q9C911; -.
DR   PRO; PR:Q9C911; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C911; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR044648; JJJ1_plant.
DR   InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR   InterPro; IPR022755; Znf_C2H2_jaz.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR45495; PTHR45495; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF12171; zf-C2H2_jaz; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SMART; SM00451; ZnF_U1; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..630
FT                   /note="DNAJ protein JJJ1 homolog"
FT                   /id="PRO_0000435445"
FT   DOMAIN          11..81
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   ZN_FING         308..332
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         600..624
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          197..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..288
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..343
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..361
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..393
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..417
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..457
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..483
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..520
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..581
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   630 AA;  72476 MW;  BF2C0750BE682E72 CRC64;
     MASSSRSEKR CHYEVLGISK ESSPDEIRSS YRRLALQRHP DKLMKAAGLS EAEATAQFQE
     LVHAYEVLSD PKERAWYDSH RSQILFADHS SAGGSKSGGS VPDLFAFFSP TVYSGYSDTG
     KGFYKVYYDV FNSVYLNEIK FARTLGLRMD SVREAPIMGN LESPYAQVTA FYNYWLGFCT
     VMDFCWVDEY DVMGGPNRKS RRMMEEENKK SRKKAKREYN DTVRGLAEFV KKRDKRVIDM
     LVKKNAEMEK KKEEERERKK KMEKERLERA MNYEEPEWAK AHEGEDEGAG LSELEEEDDD
     AKRKNEQLYC IVCSKKFKSE KQWKNHEQSK KHKEKVAELR ESFTDYEEEN EEEEIDGPLD
     SPESVEELHE KLQEELNIDN EERDVKKEVV GEADETDDEY FVAEEDMQGS SESEDEDDEM
     TLLKKMVSGQ KNKQKNVVSK EEDEDETEVE IEGDTAEFSE FDNQKSTGRN KEAKEERNKQ
     NAGNDMADDT SKVQIPGEGG NPDENMNATE SASGALADSQ KDEANSMEYD NRKSTGRRRR
     SKKGKDKNNQ GELNEKSSEA DDTQYVNRDM ESQDYKKAPR SKKSTRGMKT KGTTKKNSSN
     ECDRCGEEFE SRTKLHKHLA DSGHATVKSR
 
 
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