Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-3553-00610
Entry Name
UniProt Accession
Theoretical PI
6.11
Molecular Weight
46565.84
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
DnaJ protein homolog ANJ1
Protein Synonyms/Alias
Gene Name
Gene Synonyms/Alias
Created Date
01-NOV-1995
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
414
Canonical
AGGQRVQCAQQ****
[1]
S-Farnesylation
Organism
Atriplex nummularia (Old man saltbush) (Atriplex johnstonii)
NCBI Taxa ID
3553
Reference
[1] Ziegelhoffer EC, Medrano LJ, Meyerowitz EM. Cloning of the Arabidopsis WIGGUM gene identifies a role for farnesylation in meristem development. Proc Natl Acad Sci U S A. 2000 Jun 20;97(13):7633-8.[PMID:10840062]
Functional Description
Have a continuous role in plant development probably in the structural organization of compartments.
Sequence Annotation
Domain: 11 76 J.
Modified residue: 414 414 Cysteine methyl ester.
Protein Length
417 AA.
Protein Sequence
(Canonical)
MFGRAPKKSD STRYYEILGV PKDASPEDLK KAYKKAAIKN HPDKGGDPEK FKELAHAYEV  60
LSDPEKREIY DQYGEDALKE GMGGGGGMHD PFDIFQSFFG GSPFGGVGSS RGRRQRRGED  120
VVHPLKVSLE DLFTGTTKKL SLSRNVICSK CTGKGSKSGA SMKCSGCQGT GMKVSIRHLG  180
PSMIQQMQHP CNECKGTGET INDKDRCPQC KGEKVVQEKK VLEVVVEKGM QHGQKITFPG  240
EADEAPDTVT GDIVFVLQQK EHPKFKRKGE DLFYEHTLSL TEALCGFRFV LTHLDGRQLL  300
IKSNLGEVVK PDQFKAIEDE GMPIYQRPFM KGKMYIHFTV EFPDSLNPDQ VKSLEAILPP  360
KPSMSLTYME LDECEETTLH NVNIEEEMKR KQTQAQQEAY DEDDEPAGGQ RVQCAQQ     417
FASTA
(Canonical)
>LipidDB-3553-00610|P43644
MFGRAPKKSDSTRYYEILGVPKDASPEDLKKAYKKAAIKNHPDKGGDPEKFKELAHAYEV
LSDPEKREIYDQYGEDALKEGMGGGGGMHDPFDIFQSFFGGSPFGGVGSSRGRRQRRGED
VVHPLKVSLEDLFTGTTKKLSLSRNVICSKCTGKGSKSGASMKCSGCQGTGMKVSIRHLG
PSMIQQMQHPCNECKGTGETINDKDRCPQCKGEKVVQEKKVLEVVVEKGMQHGQKITFPG
EADEAPDTVTGDIVFVLQQKEHPKFKRKGEDLFYEHTLSLTEALCGFRFVLTHLDGRQLL
IKSNLGEVVKPDQFKAIEDEGMPIYQRPFMKGKMYIHFTVEFPDSLNPDQVKSLEAILPP
KPSMSLTYMELDECEETTLHNVNIEEEMKRKQTQAQQEAYDEDDEPAGGQRVQCAQQ
Gene Ontology
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0005524; F:ATP binding; IEA:InterPro
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0006457; P:protein folding; IEA:InterPro
GO:0009408; P:response to heat; IEA:InterPro
Interpro
InterPro; IPR012724; DnaJ
InterPro; IPR002939; DnaJ_C
InterPro; IPR001623; DnaJ_domain
InterPro; IPR018253; DnaJ_domain_CS
InterPro; IPR008971; HSP40/DnaJ_pept-bd
InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom
Pfam
Pfam; PF01556; CTDII;
Pfam; PF00226; DnaJ;
Pfam; PF00684; DnaJ_CXXCXGXG;
SMART
SMART; SM00271; DnaJ;
PROSITE
PROSITE; PS00636; DNAJ_1;
PROSITE; PS50076; DNAJ_2;
PROSITE; PS51188; ZF_CR;
PRINTS
PRINTS; PR00625; JDOMAIN;