E9E6S9 · PFF1_METAQ
- ProteinVacuolar membrane protease
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1029 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
May be involved in vacuolar sorting and osmoregulation.
Cofactor
Note: Binds 2 Zn2+ ions per subunit.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 194 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 206 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 206 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Active site | 240 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 241 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 266 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Site | 338 | Transition state stabilizer | ||||
Sequence: Y | ||||||
Binding site | 339 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | vacuolar membrane | |
Molecular Function | metal ion binding | |
Molecular Function | metalloexopeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameVacuolar membrane protease
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Clavicipitaceae > Metarhizium
Accessions
- Primary accessionE9E6S9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Vacuole membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-11 | Cytoplasmic | ||||
Sequence: MKLSNPFVFRP | ||||||
Transmembrane | 12-32 | Helical; Name=1 | ||||
Sequence: GPVSFWTTIVYLAIIIPLIYV | ||||||
Topological domain | 33-415 | Vacuolar | ||||
Sequence: QETVPPAPPEKDLPQGVNLTEAWLDLEVITRSYHPFNSHSNDIVRQYLVRRSRDILERNGIDYTTDLTGGVPWESRYLSSAEHPAQAAEASARPRGATLFDDRISNVTMTNPQPNDTMGRYFEGNNFYVYIHGSEDPEGDWWTSDNVQRVARNGAGVLVNCHFDSVSTGYGATDDGVACVSLLQLLSHFTSKGHQPKNGIVLLFNNAEEDGLLGAKAFGYSPLVQFCNTLVNLEGAGAGGRAMLFRTTDLEAAEAYSKSPHPFGSVVASNAFERGVIKSGTDYSVFVDNYGQRGLDIAFYSPRSRYHTEEDDARHTSVDSIWHMLSAALATTESLARTTSTKFNGPRSDGRKDLVQSGRPTAGVWFDWYGSSWSAFSLRGLFA | ||||||
Transmembrane | 416-436 | Helical; Name=2 | ||||
Sequence: WTLTLLITTPIVLFVVTYVLV | ||||||
Topological domain | 437-469 | Cytoplasmic | ||||
Sequence: RDDKWYFFATRVDSSVGDGEETVSFGGWKGFVR | ||||||
Transmembrane | 470-490 | Helical; Name=3 | ||||
Sequence: FPFALVVATALTIGSVFLLAK | ||||||
Topological domain | 491-493 | Vacuolar | ||||
Sequence: VNP | ||||||
Transmembrane | 494-514 | Helical; Name=4 | ||||
Sequence: LIIYSSGYSVWAMMLSLFYFV | ||||||
Topological domain | 515-532 | Cytoplasmic | ||||
Sequence: SWLLLRGAHFVRPSALQR | ||||||
Transmembrane | 533-553 | Helical; Name=5 | ||||
Sequence: GFTLIWLFIITWVLSVFAAVA | ||||||
Topological domain | 554-560 | Vacuolar | ||||
Sequence: EDRMNMG | ||||||
Transmembrane | 561-581 | Helical; Name=6 | ||||
Sequence: AVYSLAFLHTLVFAAVLISLL | ||||||
Topological domain | 582-698 | Cytoplasmic | ||||
Sequence: EQYALPAKQDFARQLSGENEEGEEQEQENLSGDGGNEQNHEDRGEADIAAAPTETTPLRADEEGQGSSEQTTTFANTYRRPVPETRGATHSGNNRKRSFPPYENEQAWSGRLPTWTW | ||||||
Transmembrane | 699-719 | Helical; Name=7 | ||||
Sequence: FIQLLLLVPLYVTVLGNLALV | ||||||
Topological domain | 720-735 | Vacuolar | ||||
Sequence: QTTSMGMTGTDGSSLL | ||||||
Transmembrane | 736-756 | Helical; Name=8 | ||||
Sequence: VPLMGVGILTILLLLPLTPFI | ||||||
Topological domain | 757-763 | Cytoplasmic | ||||
Sequence: HRVSHHV | ||||||
Transmembrane | 764-784 | Helical; Name=9 | ||||
Sequence: PLFLLLVFIGTLIYNLTAFPF | ||||||
Topological domain | 785-1029 | Vacuolar | ||||
Sequence: SANNRFKFYFKQVVDLDKGSNVVTLNGLEKFVRPVIGSLPTPAGQRIHCDEDPFLSNLRNCQYDASLLPPDVANGEKLENLISFEASKSKNGKTVLVSLDALNTRVCFLDTSSPIFGFSVDGGAKRDDRFGSFPPEGLQQIQLWRRDWEKGWNVTLYLGGNVLPTNQDSVEATEVDEVDDDPSGGELKRRAVREFVVTARCAWSDVNSANTIPAFHEVKQFMPRWAIVAKKSVGLVEITKKIKVT |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000411723 | 1-1029 | Vacuolar membrane protease | |||
Sequence: MKLSNPFVFRPGPVSFWTTIVYLAIIIPLIYVQETVPPAPPEKDLPQGVNLTEAWLDLEVITRSYHPFNSHSNDIVRQYLVRRSRDILERNGIDYTTDLTGGVPWESRYLSSAEHPAQAAEASARPRGATLFDDRISNVTMTNPQPNDTMGRYFEGNNFYVYIHGSEDPEGDWWTSDNVQRVARNGAGVLVNCHFDSVSTGYGATDDGVACVSLLQLLSHFTSKGHQPKNGIVLLFNNAEEDGLLGAKAFGYSPLVQFCNTLVNLEGAGAGGRAMLFRTTDLEAAEAYSKSPHPFGSVVASNAFERGVIKSGTDYSVFVDNYGQRGLDIAFYSPRSRYHTEEDDARHTSVDSIWHMLSAALATTESLARTTSTKFNGPRSDGRKDLVQSGRPTAGVWFDWYGSSWSAFSLRGLFAWTLTLLITTPIVLFVVTYVLVRDDKWYFFATRVDSSVGDGEETVSFGGWKGFVRFPFALVVATALTIGSVFLLAKVNPLIIYSSGYSVWAMMLSLFYFVSWLLLRGAHFVRPSALQRGFTLIWLFIITWVLSVFAAVAEDRMNMGAVYSLAFLHTLVFAAVLISLLEQYALPAKQDFARQLSGENEEGEEQEQENLSGDGGNEQNHEDRGEADIAAAPTETTPLRADEEGQGSSEQTTTFANTYRRPVPETRGATHSGNNRKRSFPPYENEQAWSGRLPTWTWFIQLLLLVPLYVTVLGNLALVQTTSMGMTGTDGSSLLVPLMGVGILTILLLLPLTPFIHRVSHHVPLFLLLVFIGTLIYNLTAFPFSANNRFKFYFKQVVDLDKGSNVVTLNGLEKFVRPVIGSLPTPAGQRIHCDEDPFLSNLRNCQYDASLLPPDVANGEKLENLISFEASKSKNGKTVLVSLDALNTRVCFLDTSSPIFGFSVDGGAKRDDRFGSFPPEGLQQIQLWRRDWEKGWNVTLYLGGNVLPTNQDSVEATEVDEVDDDPSGGELKRRAVREFVVTARCAWSDVNSANTIPAFHEVKQFMPRWAIVAKKSVGLVEITKKIKVT | ||||||
Glycosylation | 50 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 138 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 147 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 937 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 596-623 | Disordered | ||||
Sequence: LSGENEEGEEQEQENLSGDGGNEQNHED | ||||||
Region | 637-684 | Disordered | ||||
Sequence: TPLRADEEGQGSSEQTTTFANTYRRPVPETRGATHSGNNRKRSFPPYE | ||||||
Compositional bias | 641-660 | Polar residues | ||||
Sequence: ADEEGQGSSEQTTTFANTYR |
Sequence similarities
Belongs to the peptidase M28 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,029
- Mass (Da)114,089
- Last updated2011-04-05 v1
- ChecksumB57A6C7D5E7C6634
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 641-660 | Polar residues | ||||
Sequence: ADEEGQGSSEQTTTFANTYR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GL698512 EMBL· GenBank· DDBJ | EFY88368.1 EMBL· GenBank· DDBJ | Genomic DNA |