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0AFG32_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameAFG3L2
DescriptionAfg3-like protein 2 (ec 3.4.24.-) (paraplegin-like protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005739 mitochondrion (TAS)
0051082 unfolded protein binding (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Metalloproteases are the most diverse of the four main types of protease.ith more than 30 families identified to date . In these enzymes. divalent cation.sually zinc.ctivates the water molecule. The metal ion is held in place by amino acid ligands.sually three in number. The known metal ligands are His.lu.sp or Lys and at least one other residue is required for catalysis.hich may play an electrophillic role. Of the known metalloproteases.round half contain an HEXXH motif.hich has been shown in crystallographic studies to form part of the metal-binding site . The HEXXH motif is relatively common.ut can be more stringently defined for metalloproteases as abXHEbbHbc.here a is most often valine or threonine and forms part of the S1 subsite in thermolysin and neprilysin. is an uncharged residue.nd c a hydrophobic residue. Proline is never found in this site.ossibly because it would break the helical structure adopted by this motif in metalloproteases .Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. This group of metallopeptidases belong to MEROPS peptidase family M41 (FtsH endopeptidase family.lan MA(E)). The predicted active site residues for members of this family and thermolysin.he type example for clan MA.ccur in the motif HEXXH.The peptidase M41 family belong to a larger family of zinc metalloproteases. This familyincludes the cell division protein FtsH.nd the yeast mitochondrial respiratory chain complexesassembly protein.hich is a putative ATP-dependent protease required for assembly of themitochondrial respiratory chain and ATPase complexes. FtsH is an integral membrane protein.hich seems to act as an ATP-dependent zinc metallopeptidase that binds one zinc ion.
  IPR000642:Peptidase M41
A large family of ATPases has been described whose key feature is that they share a conserved region of about 220 amino acids that contains an ATP-binding site. This family is now called AAA.or ATPases Associated with diverse cellular Activities. The proteins that belong to this family either contain one or two AAA domains.It is proposed that.n general.he AAA domains in these proteins act as ATP-dependent protein clamps .In addition to the ATP-binding A and B motifs (see the relevant entry ).hich are located in the N-terminal half of this domain.here is a highly conserved region located in the central part of the domain.
  IPR003959:AAA ATPase, central region
This domain is found in the FtsH family of proteins that include FtsH a membrane-bound ATP-dependent protease universally conserved in prokaryotes . The FtsH peptidases.hich belong to MEROPS peptidase family M41 (clan MA(E)).fficiently degrade proteins that have a low thermodynamic stability - e.g. they lack robust unfoldase activity. This feature may be key and implies that this could be a criterion for degrading a protein. In Oenococcus oeni FtsH is involved in protection against environmental stress .nd shows increased expression under heat or osmotic stress. These two lines of evidence suggest that it is a fundamental prokaryotic self-protection mechanism that checks if proteins are correctly folded. The precise function of this N-terminal region is unclear.
  IPR011546:Peptidase M41, FtsH extracellular
AAA ATPases form a large.unctionally diverse protein family belonging to the AAA+ superfamily of ring-shaped P-loop NTPases.hich exert their activity through the energy-dependent unfolding of macromolecules. AAA ATPases contain a P-loop NTPase domain.hich is the most abundant class of NTP-binding protein fold.nd is found throughout all kingdoms of life . P-loop NTPase domains act to hydrolyse the beta-gamma phosphate bond of bound nucleoside triphosphate. There are two classes of P-loop domains: the KG (kinase-GTPase) division.nd the ASCE division.he latter including the AAA+ group as well as several other ATPases.There are at least six major clades of AAA domains (metalloproteases.eiotic proteins.1 and D2 domains of ATPases with two AAA domains.roteasome subunits.nd BSC1).s well as several minor clades.ome of which consist of hypothetical proteins . The domain organisation of AAA ATPases consists of a non-ATPase N-terminal domain that acts in substrate recognition.ollowed by one or two AAA domains (D1 and D2).ne of which may be degenerate.
  IPR003593:AAA ATPase
Metalloproteases are the most diverse of the four main types of protease.ith more than 30 families identified to date . In these enzymes. divalent cation.sually zinc.ctivates the water molecule. The metal ion is held in place by amino acid ligands.sually three in number. The known metal ligands are His.lu.sp or Lys and at least one other residue is required for catalysis.hich may play an electrophillic role. Of the known metalloproteases.round half contain an HEXXH motif.hich has been shown in crystallographic studies to form part of the metal-binding site . The HEXXH motif is relatively common.ut can be more stringently defined for metalloproteases as abXHEbbHbc.here a is most often valine or threonine and forms part of the S1 subsite in thermolysin and neprilysin. is an uncharged residue.nd c a hydrophobic residue. Proline is never found in this site.ossibly because it would break the helical structure adopted by this motif in metalloproteases .Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. This group of metallopeptidases belong to MEROPS peptidase family M41 (FtsH endopeptidase family.lan MA(E)). The predicted active site residues for members of this family and thermolysin.he type example for clan MA.ccur in the motif HEXXH. FtsH is a membrane-anchored ATP-dependent protease that degrades misfolded or misassembled membrane proteins as well as a subset of cytoplasmic regulatory proteins. FtsH is a 647-residue protein of 70 kDa.ith two putative transmembrane segments towards its N terminus which anchor the protein to themembrane.iving rise to a periplasmic domain of 70 residues and a cytoplasmic segment of 520 residues containing the ATPase and protease domains .
  IPR005936:Peptidase M41, FtsH
IPR000642:Peptidase_M41 
Evalue:-110.075721740723 
Location:541-744IPR003959:AAA 
Evalue:-92.7958831787109 
Location:343-534IPR011546:FtsH_ext 
Evalue:-36.2146682739258 
Location:168-317
SequencesProtein: AFG32_HUMAN (797 aa)
mRNA: NM_006796
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentK01417
  Level 3 annotation:
    
  Level 2 annotation:
    Other enzymes
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 226 residues, 12319107-12319782Exon2: 67 residues, 12327339-12327534Exon3: 69 residues, 12330199-12330400Exon4: 40 residues, 12334130-12334246Exon5: 39 residues, 12338271-12338382Exon6: 44 residues, 12341083-12341209Exon7: 38 residues, 12341304-12341412Exon8: 53 residues, 12343003-12343157Exon9: 48 residues, 12346692-12346830Exon10: 93 residues, 12348668-12348942Exon11: 43 residues, 12349925-12350050Exon12: 27 residues, 12353780-12353855Exon13: 53 residues, 12356963-12357116Exon14: 37 residues, 12357274-12357381Exon15: 28 residues, 12360847-12360925Exon16: 35 residues, 12361590-12361690Exon17: 77 residues, 12366967-12367194Exon18: 2 residues, -Jump to AFG32_HUMAN  
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