LipidDB ID

LipidDB-559292-00270

Entry Name

UniProt Accession

P25491; D6W1B6;

Theoretical PI

5.95

Molecular Weight

44670.74

Genbank Protein ID

CAA39910.1; AAB20771.1; AAA99647.1; CAA95937.1; DAA10482.1;

Genbank Nucleotide ID

X56560; S74758; U12141; Z71340; BK006947;

Protein Name

Mitochondrial protein import protein MAS5

Protein Synonyms/Alias

Yeast dnaJ protein 1;

Gene Name

YDJ1

Gene Synonyms/Alias

MAS5; YNL064C; N2418; YNL2418C;

Created Date

01-MAY-1992

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

NCBI Taxa ID

559292

Reference

[1] Caplan AJ, Tsai J, Casey PJ, Douglas MG. Farnesylation of YDJ1p is requiredfor function at elevated growth temperatures in Saccharomyces cerevisiae. J Biol Chem. 1992 Sep 15;267(26):18890-5.[PMID:1527016]
[2] Flom GA, Lemieszek M, Fortunato EA, Johnson JL. Farnesylation of Ydj1 isrequired for in vivo interaction with Hsp90 client proteins. Mol Biol Cell. 2008 Dec;19(12):5249-58. doi: 10.1091/mbc.E08-04-0435. Epub 2008 Oct 1.[PMID:18829866]

Functional Description

Probably involved in mitochondrial protein import. Is also required for efficient translocation of pre-pro-alpha-factor. Involved in heme regulation of HAP1, as a component of the high- molecular-weight (HMC) complex.

Sequence Annotation

Domain: 4 72 J.
Region: 1 172 Necessary for HAP1 repression in theabsence of heme.
Region: 135 137 Substrate binding.
Region: 215 216 Substrate binding.
Region: 247 249 Substrate binding.
Metal binding site: 143 143 Zinc 1.
Metal binding site: 146 146 Zinc 1.
Metal binding site: 159 159 Zinc 2.
Metal binding site: 162 162 Zinc 2.
Metal binding site: 185 185 Zinc 2.
Metal binding site: 188 188 Zinc 2.
Metal binding site: 201 201 Zinc 1.
Metal binding site: 204 204 Zinc 1.
Binding site: 116 116 Substrate; via amide nitrogen.
Functional site: 335 335 Involved in dimerization.
Modified residue: 406 406 Cysteine methyl ester.

Protein Length

409 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0005829; C:cytosol; IDA:SGD
GO:0048471; C:perinuclear region of cytoplasm; IDA:SGD
GO:0072380; C:TRC complex; IDA:SGD
GO:0005524; F:ATP binding; IEA:InterPro
GO:0001671; F:ATPase activator activity; IDA:SGD
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0051082; F:unfolded protein binding; IDA:SGD
GO:0006458; P:'de novo' protein folding; IMP:SGD
GO:0030433; P:ER-associated ubiquitin-dependent protein catabolic process; IMP:SGD
GO:0032781; P:positive regulation of ATPase activity; IDA:GOC
GO:0042026; P:protein refolding; IDA:SGD
GO:0045047; P:protein targeting to ER; IMP:SGD
GO:0006626; P:protein targeting to mitochondrion; IMP:SGD
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;