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Q8SR45

- MAP2_ENCCU

UniProt

Q8SR45 - MAP2_ENCCU

Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).3 PublicationsUniRule annotation

    Catalytic activityi

    Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation

    Cofactori

    Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.UniRule annotation

    Kineticsi

    1. KM=1.95 mM for a Met-Ala-Ser peptide1 Publication

    Vmax=7.3 nmol/min/mg enzyme1 Publication

    pH dependencei

    Optimum pH is 8.5.1 Publication

    Temperature dependencei

    Optimum temperature is 37 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei109 – 1091Substrate
    Metal bindingi130 – 1301Divalent metal cation 1
    Metal bindingi141 – 1411Divalent metal cation 1
    Metal bindingi141 – 1411Divalent metal cation 2; catalytic
    Metal bindingi210 – 2101Divalent metal cation 2; catalytic; via tele nitrogen
    Binding sitei218 – 2181Substrate
    Metal bindingi243 – 2431Divalent metal cation 2; catalytic
    Metal bindingi339 – 3391Divalent metal cation 1
    Metal bindingi339 – 3391Divalent metal cation 2; catalytic

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-HAMAP
    2. metalloaminopeptidase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. protein initiator methionine removal Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    BRENDAi3.4.11.18. 7412.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 2UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 2UniRule annotation
    Short name:
    MetAP 2UniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    Name:MAP2UniRule annotation
    Ordered Locus Names:ECU10_0750
    OrganismiEncephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
    Taxonomic identifieri284813 [NCBI]
    Taxonomic lineageiEukaryotaFungiMicrosporidiaUnikaryonidaeEncephalitozoon
    ProteomesiUP000000819: Chromosome X

    Organism-specific databases

    EuPathDBiMicrosporidiaDB:ECU10_0750.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi241 – 2411A → T: Abolishes catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 358358Methionine aminopeptidase 2PRO_0000148985Add
    BLAST

    Expressioni

    Developmental stagei

    Expressed in late sporogonial stages.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi6035.ECU10_0750.

    Structurei

    Secondary structure

    1
    358
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi43 – 6523
    Helixi72 – 8615
    Turni87 – 893
    Helixi91 – 944
    Beta strandi95 – 1039
    Beta strandi106 – 1083
    Beta strandi126 – 13510
    Beta strandi138 – 14710
    Helixi150 – 1523
    Helixi153 – 16917
    Helixi176 – 18712
    Beta strandi191 – 1933
    Beta strandi195 – 2006
    Beta strandi209 – 2135
    Beta strandi236 – 24914
    Beta strandi262 – 2643
    Helixi275 – 28713
    Turni288 – 2903
    Helixi295 – 3006
    Helixi309 – 3179
    Beta strandi320 – 3234
    Beta strandi335 – 34511
    Beta strandi348 – 3536

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3FM3X-ray2.18A/B1-358[»]
    3FMQX-ray2.50A/B1-358[»]
    3FMRX-ray2.89A/B1-358[»]
    ProteinModelPortaliQ8SR45.
    SMRiQ8SR45. Positions 3-358.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8SR45.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000226278.
    KOiK01265.
    OMAiIQICEEL.
    OrthoDBiEOG7BGHW3.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPiMF_03175. MetAP_2_euk.
    InterProiIPR000994. Pept_M24_structural-domain.
    IPR002468. Pept_M24A_MAP2.
    IPR018349. Pept_M24A_MAP2_BS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PANTHERiPTHR10804:SF9. PTHR10804:SF9. 1 hit.
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    SUPFAMiSSF55920. SSF55920. 2 hits.
    TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
    PROSITEiPS01202. MAP_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8SR45-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKCILLNQAE ELPIEFLPKD GVYGKGKLFD SRNMEIENFT ESDILQDARR    50
    AAEAHRRARY RVQSIVRPGI TLLEIVRSIE DSTRTLLKGE RNNGIGFPAG 100
    MSMNSCAAHY TVNPGEQDIV LKEDDVLKID FGTHSDGRIM DSAFTVAFKE 150
    NLEPLLVAAR EGTETGIKSL GVDVRVCDIG RDINEVISSY EVEIGGRMWP 200
    IRPISDLHGH SISQFRIHGG ISIPAVNNRD TTRIKGDSFY AVETFATTGK 250
    GSIDDRPPCS HFVLNTYKSR KLFNKDLIKV YEFVKDSLGT LPFSPRHLDY 300
    YGLVKGGSLK SVNLLTMMGL LTPYPPLNDI DGCKVAQFEH TVYLSEHGKE 350
    VLTRGDDY 358
    Length:358
    Mass (Da):39,975
    Last modified:June 1, 2002 - v1
    Checksum:i058A8AB457EC258F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti288 – 2881L → F in strain: ATCC 50502 / ECIII.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF440270 Genomic DNA. Translation: AAM49625.1.
    AL590449 Genomic DNA. Translation: CAD25794.1.
    AY339777 Genomic DNA. Translation: AAR04551.1.
    AY339778 Genomic DNA. Translation: AAR04552.1.
    AY339779 Genomic DNA. Translation: AAR04553.1.
    RefSeqiNP_586190.1. NM_001042023.1.

    Genome annotation databases

    GeneIDi859839.
    KEGGiecu:ECU10_0750.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF440270 Genomic DNA. Translation: AAM49625.1 .
    AL590449 Genomic DNA. Translation: CAD25794.1 .
    AY339777 Genomic DNA. Translation: AAR04551.1 .
    AY339778 Genomic DNA. Translation: AAR04552.1 .
    AY339779 Genomic DNA. Translation: AAR04553.1 .
    RefSeqi NP_586190.1. NM_001042023.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3FM3 X-ray 2.18 A/B 1-358 [» ]
    3FMQ X-ray 2.50 A/B 1-358 [» ]
    3FMR X-ray 2.89 A/B 1-358 [» ]
    ProteinModelPortali Q8SR45.
    SMRi Q8SR45. Positions 3-358.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 6035.ECU10_0750.

    Protocols and materials databases

    DNASUi 859839.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 859839.
    KEGGi ecu:ECU10_0750.

    Organism-specific databases

    EuPathDBi MicrosporidiaDB:ECU10_0750.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000226278.
    KOi K01265.
    OMAi IQICEEL.
    OrthoDBi EOG7BGHW3.

    Enzyme and pathway databases

    BRENDAi 3.4.11.18. 7412.

    Miscellaneous databases

    EvolutionaryTracei Q8SR45.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPi MF_03175. MetAP_2_euk.
    InterProi IPR000994. Pept_M24_structural-domain.
    IPR002468. Pept_M24A_MAP2.
    IPR018349. Pept_M24A_MAP2_BS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    PANTHERi PTHR10804:SF9. PTHR10804:SF9. 1 hit.
    Pfami PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55920. SSF55920. 2 hits.
    TIGRFAMsi TIGR00501. met_pdase_II. 1 hit.
    PROSITEi PS01202. MAP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Investigations into microsporidian methionine aminopeptidase type 2: a therapeutic target for microsporidiosis."
      Zhang H., Huang H., Cali A., Takvorian P.M., Feng X., Zhou G., Weiss L.M.
      Folia Parasitol. 52:182-192(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: GB-M1.
    3. "Phylogenetic relationships of methionine aminopeptidase 2 among Encephalitozoon species and genotypes of microsporidia."
      Pandrea I., Mittleider D., Brindley P.J., Didier E.S., Robertson D.L.
      Mol. Biochem. Parasitol. 140:141-152(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-349.
      Strain: ATCC 50502 / ECIII, ATCC 50503 / ECI and ECII.
    4. "Characterization of recombinant microsporidian methionine aminopeptidase type 2."
      Weiss L.M., Zhou G.C., Zhang H.
      J. Eukaryot. Microbiol. 50:597-599(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "System for expression of microsporidian methionine amino peptidase type 2 (MetAP2) in the yeast Saccharomyces cerevisiae."
      Upadhya R., Zhang H.S., Weiss L.M.
      Antimicrob. Agents Chemother. 50:3389-3395(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ALA-241.
    6. "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi (microsporidia): a reference map for proteins expressed in late sporogonial stages."
      Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.
      Proteomics 6:3625-3635(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], DEVELOPMENTAL STAGE.
    7. "Structure of a microsporidian methionine aminopeptidase type 2 complexed with fumagillin and TNP-470."
      Alvarado J.J., Nemkal A., Sauder J.M., Russell M., Akiyoshi D.E., Shi W., Almo S.C., Weiss L.M.
      Mol. Biochem. Parasitol. 168:158-167(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) IN COMPLEX WITH IRON AND INHIBITOR, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiMAP2_ENCCU
    AccessioniPrimary (citable) accession number: Q8SR45
    Secondary accession number(s): Q6VH17, Q6VH18
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3