Detail Information for IndEnz0002018750
IED ID IndEnz0002018750
Enzyme Type ID protease018750
Protein Name AFG3-like protein spg-7
EC 3.4.24.-
Gene Name spg-7 Y47G6A.10
Organism Caenorhabditis elegans
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans
Enzyme Sequence MWRLYRKTPKQLRNSVESCFKSVNSRQFSVSSFSAVAKDDKSVLKQQEVLHLLAKDQRFEERFFNQVQQTIRYFASKPNDLKKFFRKEASTDNKESSSSSDKKDSKGNKGEDNNPFNQFPGGWQQIAVSVGILLALYAFMDYQSYREISWKEFYSDFLEAGLVERLEVVDKRWVRIVSSSGKYAGQTCYFNIGSVDSFERSLGAAQHHLQYDADRQIPVLYKSEFNFKREIPNLISVAFPLLFGYYIYRMLKGGGAAGGAGRAGGGGLGGMFGGFGQSTARVINREDIKVKFADVAGCEEAKIEIMEFVNFLKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDMFSMARKNSPCILFIDEIDAVGRKRGGKGGMGGHSEQENTLNQLLVEMDGFTTDESSVIVIAATNRVDILDSALLRPGRFDRQIYVPVPDIKGRASIFRVHLGPLRTSLDKTVLSRKLAAHTPGFSGADISNVCNEAALIAARDANHEISNKHFEQAIERVVAGMEKKTQVLQKEEKKTVAYHEAGHAIAGWFLQHADPLLKVSIIPRGKGLGYAQYLPKEQYLYSKDQLLDRMCMTLGGRVAEEIFFGRITTGAQDDLQKVTQMAYSQVVKFGMSEKVGPLSFETPAPGEMAFDKPYSEATAQLIDQEVRDLVMNALRRTRDLLLEKRSDIERVALRLLEKEILNREDMIELVGKRPFVEKNTYEEMVSGTGGLDENVELPKGLENWNKESEKKKKDEEKKKNDE
Enzyme Length 782
Uniprot Accession Number Q9N3T5
Absorption
Active Site ACT_SITE 560; /evidence=ECO:0000250|UniProtKB:Q9WZ49
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: Acts as a component of the m-AAA protease complex which is an ATP-dependent metalloprotease mediating degradation of non-assembled mitochondrial inner membrane proteins (By similarity). The complex is necessary for the assembly of mitochondrial respiratory chain and ATPase complexes (By similarity). Functions both in post-translational assembly and in the turnover of mistranslated or misfolded polypeptides (PubMed:22700657, PubMed:25274306, PubMed:25773600). Plays a role in male tail tip morphogenesis (PubMed:21408209). {ECO:0000250|UniProtKB:P39925, ECO:0000269|PubMed:21408209, ECO:0000305|PubMed:22700657, ECO:0000305|PubMed:25274306, ECO:0000305|PubMed:25773600}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 333..340; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00499
Features Active site (1); Chain (1); Compositional bias (2); Metal binding (3); Nucleotide binding (1); Region (2); Topological domain (3); Transmembrane (2)
Keywords ATP-binding;Hydrolase;Membrane;Metal-binding;Metalloprotease;Mitochondrion;Mitochondrion inner membrane;Nucleotide-binding;Protease;Reference proteome;Transmembrane;Transmembrane helix;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P39925}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P39925}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10778742; 11099033; 11231151; 11381264; 11483502; 14551910; 15084750; 15280428; 15489339; 15791247; 16816413; 16854972; 17164286; 17411345; 17704769; 17925224; 19343510; 20089839; 20188671; 20439774; 20439776; 21085631; 21177967; 21367940; 21529718; 22220943; 22267497; 22286215; 22347378; 22500807; 22560298; 22719267; 23800452; 24884423; 25215496; 25487147; 25979236; 26913604; 27129311; 27459203; 29348603; 30929899; 6593563;
Motif
Gene Encoded By
Mass 87,469
Kinetics
Metal Binding METAL 559; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9WZ49; METAL 563; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9WZ49; METAL 634; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9WZ49
Rhea ID
Cross Reference Brenda