A0A223P3D8 · A0A223P3D8_9SPHI
- ProteinAminopeptidase N
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids831 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Catalytic activity
- Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
Cofactor
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | metalloaminopeptidase activity | |
Molecular Function | peptide binding | |
Molecular Function | zinc ion binding | |
Biological Process | peptide catabolic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAminopeptidase N
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Sphingobacteriia > Sphingobacteriales > Sphingobacteriaceae > Mucilaginibacter
Accessions
- Primary accessionA0A223P3D8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MIKTKTISAFVLSGLFVGLTIA | ||||||
Chain | PRO_5012103952 | 23-831 | Aminopeptidase N | |||
Sequence: ATAQTTQPADPALKIYRATPPKINDLVHTKLDVRFDYKKRYMYGKEWVTLKPHFYPTDTLRLDAKGMDLKTIAVVKNGKNVPLKFKYEDSLSVNIQLDKVYHNNESYTLYIDYTAKPNEIKQHGSAAITDAKGLYFINPDGTEKDKPTQIWTQGESESSSCWFPTIDKPEQKTTDEISMTVPAKYVTLSNGRLAAQKVNADGTRTDTWKQELPHSPYLFMMAVGDFKIYKDKWRNKEVSYYLEPKYAPYAKQIFGMTPELIEFYSTTLGVDFPWYKYSQIVVRDYVSGAMENTSATLHGEYVQETPRELIDAGYDAGRSTIAHELFHQWFGDFVTAESWSNLTVNESFADFSEMLWAEHKYGKDEADAHSNDAMQSYLGSPDAKTKNLVRFHYNNEMDMFDVVTYQKGGRILNMLRNYLGKDAFYKGLNIYLKTNAYKTGEAQQLRLAEEEASGLDLNWFFNQWYYGAGNPELKISYKYDEATKTETVYLAQTQEGQIFKLPMAIDIYAGGKKNRYKVWMNDKADTLNFQSATKPDLVNVDGDKVLLAKKTDDKTLDEYAFQYFNAPLYMDRFEAITFAATHQSDKAGQKVIIAALKDKYYGLRIKAIKALNMSNDEIHNAALPVLASLAQTDENTLVRAAAITALGKLKASGNLTLFKQALTSQSYAVQGAALNAIALLEPAQSVALAKGFEQDNKGALSQAIVTVYATNGDGEQWPYVYQKFSDAGPQAKFALTRSFAAMTGRVEKPEFAQQGINAIKDLGVKYKQFGIGPFITGLLTDIKTARTKLNDAASATAADDAIKAVNDAK |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 50-240 | Aminopeptidase N-like N-terminal | ||||
Sequence: HTKLDVRFDYKKRYMYGKEWVTLKPHFYPTDTLRLDAKGMDLKTIAVVKNGKNVPLKFKYEDSLSVNIQLDKVYHNNESYTLYIDYTAKPNEIKQHGSAAITDAKGLYFINPDGTEKDKPTQIWTQGESESSSCWFPTIDKPEQKTTDEISMTVPAKYVTLSNGRLAAQKVNADGTRTDTWKQELPHSPYL | ||||||
Domain | 278-486 | Peptidase M1 membrane alanine aminopeptidase | ||||
Sequence: MTPELIEFYSTTLGVDFPWYKYSQIVVRDYVSGAMENTSATLHGEYVQETPRELIDAGYDAGRSTIAHELFHQWFGDFVTAESWSNLTVNESFADFSEMLWAEHKYGKDEADAHSNDAMQSYLGSPDAKTKNLVRFHYNNEMDMFDVVTYQKGGRILNMLRNYLGKDAFYKGLNIYLKTNAYKTGEAQQLRLAEEEASGLDLNWFFNQW |
Sequence similarities
Belongs to the peptidase M1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length831
- Mass (Da)93,242
- Last updated2017-10-25 v1
- Checksum675338AD719B7BCE
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP022743 EMBL· GenBank· DDBJ | ASU36331.1 EMBL· GenBank· DDBJ | Genomic DNA |