Q9FV51 (AMP1C_ARATH) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 71.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Methionine aminopeptidase 1C, chloroplastic/mitochondrial Short name=MAP 1C Short name=MetAP 1C EC=3.4.11.18 Alternative name(s): Peptidase M 1C | ||||||
| Gene names |
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| Organism | Arabidopsis thaliana (Mouse-ear cress) | ||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis |
Protein attributes
| Sequence length | 344 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Removes the amino-terminal methionine from nascent proteins By similarity. |
| Catalytic activity | Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. |
| Cofactor | Binds 2 cobalt ions per subunit. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions By similarity. |
| Subcellular location | |
| Tissue specificity | Ubiquitous. Ref.1 |
| Sequence similarities | Belongs to the peptidase M24A family. |
| Sequence caution | The sequence BAA95761.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Chloroplast Mitochondrion Plastid |
| Domain | Transit peptide |
| Ligand | Cobalt Metal-binding |
| Molecular function | Aminopeptidase Hydrolase Protease |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | N-terminal protein amino acid modification Traceable author statement. Source: TAIR proteolysisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | chloroplast Traceable author statement. Source: TAIR mitochondrionInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – ? | Chloroplast and mitochondrion Potential | |||||||
| Chain | ? – 344 | Methionine aminopeptidase 1C, chloroplastic/mitochondrial | PRO_0000045806 | ||||||
Sites | |||||||||
| Metal binding | 189 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 200 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 200 | 1 | Cobalt 2 By similarity | ||||||
| Metal binding | 262 | 1 | Cobalt 2 By similarity | ||||||
| Metal binding | 296 | 1 | Cobalt 2 By similarity | ||||||
| Metal binding | 327 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 327 | 1 | Cobalt 2 By similarity | ||||||
| Binding site | 172 | 1 | Substrate By similarity | ||||||
| Binding site | 269 | 1 | Substrate By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 264 | 1 | V → L in AAG33976. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms." Giglione C., Serero A., Pierre M., Boisson B., Meinnel T. EMBO J. 19:5916-5929(2000) [PubMed: 11060042] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION. |
| [2] | "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones." Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S. DNA Res. 7:131-135(2000) [PubMed: 10819329] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia. |
| [3] | The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF250962 mRNA. Translation: AAG33976.1. AB028607 Genomic DNA. Translation: BAA95761.1. Sequence problems. CP002686 Genomic DNA. Translation: AEE77063.1. |
| IPI | IPI00533123. |
| RefSeq | NP_189202.1. NM_113473.2. |
| UniGene | At.16911. |
3D structure databases | |
| ProteinModelPortal | Q9FV51. |
| SMR | Q9FV51. Positions 16-343. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9FV51. |
Protein family/group databases | |
| MEROPS | M24.A07. |
Proteomic databases | |
| PRIDE | Q9FV51. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblPlants | AT3G25740.1; AT3G25740.1; AT3G25740. |
| GeneID | 822165. |
| GenomeReviews | Gene locus AT3G25740 in contig BA000014_GR. |
| KEGG | ath:AT3G25740. |
| NMPDR | fig|3702.1.peg.14832. |
Organism-specific databases | |
| GeneFarm | 2287. 184. |
| TAIR | At3g25740. |
Phylogenomic databases | |
| GeneTree | EPGT00050000011147. |
| HOGENOM | HBG299384. |
| InParanoid | Q9FV51. |
| OMA | MERFIGH. |
| PhylomeDB | Q9FV51. |
| ProtClustDB | CLSN2915435. |
Gene expression databases | |
| Genevestigator | Q9FV51. |
| GermOnline | AT3G25740. Arabidopsis thaliana. |
Family and domain databases | |
| InterPro | IPR001714. Pept_M24_MAP. IPR000994. Pept_M24_structural-domain. IPR002467. Pept_M24A_MAP1. [Graphical view] |
| Gene3D | G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit. |
| Pfam | PF00557. Peptidase_M24. 1 hit. [Graphical view] |
| PRINTS | PR00599. MAPEPTIDASE. |
| SUPFAM | SSF55920. Peptidase_M24_cat_core. 1 hit. |
| TIGRFAMs | TIGR00500. Met_pdase_I. 1 hit. |
| PROSITE | PS00680. MAP_1. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AMP1C_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q9FV51 Secondary accession number(s): Q9LS05 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with