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B0XTJ7

- MAP21_ASPFC

UniProt

B0XTJ7 - MAP21_ASPFC

Protein

Methionine aminopeptidase 2-1

Gene

AFUB_018820

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (08 Apr 2008)
      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).UniRule 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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei238 – 2381SubstrateUniRule annotation
    Metal bindingi259 – 2591Divalent metal cation 1UniRule annotation
    Metal bindingi270 – 2701Divalent metal cation 1UniRule annotation
    Metal bindingi270 – 2701Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi339 – 3391Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei347 – 3471SubstrateUniRule annotation
    Metal bindingi372 – 3721Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi467 – 4671Divalent metal cation 1UniRule annotation
    Metal bindingi467 – 4671Divalent metal cation 2; catalyticUniRule annotation

    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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 2-1UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 2-1UniRule annotation
    Short name:
    MetAP 2-1UniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    ORF Names:AFUB_018820
    OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
    Taxonomic identifieri451804 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000001699: Unassembled WGS sequence

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 486486Methionine aminopeptidase 2-1PRO_0000407637Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliB0XTJ7.
    SMRiB0XTJ7. Positions 118-486.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi93 – 10816Lys-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000226278.
    OrthoDBiEOG7BGHW3.
    PhylomeDBiB0XTJ7.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPiMF_03175. MetAP_2_euk.
    InterProiIPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002468. Pept_M24A_MAP2.
    IPR018349. Pept_M24A_MAP2_BS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    PRINTSiPR00599. MAPEPTIDASE.
    SUPFAMiSSF55920. SSF55920. 2 hits.
    TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
    PROSITEiPS01202. MAP_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B0XTJ7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSKSPEGHR QAPHASNCNE LKPANPDPQI SQNGSGSADL DRGVIGDDDD    50
    DEDAEENGVN TETPNVGKLN QPPFPNLDQV HVTTTDGLCI TEKKKKRKKS 100
    NKKKKKTKSG ALPATELKQT SPPRVLVSTL FPSEYPVGEL VPYDCTARTT 150
    DEELRYNSRL WDDDFLPDYR QAAEIHRQVR QYAQKELIKP GATLLSIAEG 200
    IEDGVRALSG HQGLEPGDFF KAGMGFPTGL CLNHIAAHWT PNPREKDVIL 250
    DKGDVLKVDF GVHVNGRIVD SAFTVAFDDK YDNLLTAVRE ATNTGIKHAG 300
    VDARMSDIGA AIQEVMESYE VEIDGKVFPV KAIRNITGHD ILRYHIHGGK 350
    QIPFIKNNNQ DKMEEGEVYA IETFGSTGRG FLDDDVGVYG YGRNENMSGA 400
    NLRLSSAKSL LKTIDASFGS IVFSRRYLER LGVKNYLLGM KNLIDNGIVE 450
    CYSPLVDVKG SYTAQFEHTI LLHSGGKEVI SRGDDY 486
    Length:486
    Mass (Da):53,508
    Last modified:April 8, 2008 - v1
    Checksum:i940B4DC3289A7288
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS499595 Genomic DNA. Translation: EDP53838.1.

    Genome annotation databases

    EnsemblFungiiCADAFUBT00001876; CADAFUBP00001837; CADAFUBG00001876.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS499595 Genomic DNA. Translation: EDP53838.1 .

    3D structure databases

    ProteinModelPortali B0XTJ7.
    SMRi B0XTJ7. Positions 118-486.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUBT00001876 ; CADAFUBP00001837 ; CADAFUBG00001876 .

    Phylogenomic databases

    HOGENOMi HOG000226278.
    OrthoDBi EOG7BGHW3.
    PhylomeDBi B0XTJ7.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPi MF_03175. MetAP_2_euk.
    InterProi IPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002468. Pept_M24A_MAP2.
    IPR018349. Pept_M24A_MAP2_BS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    PRINTSi PR00599. MAPEPTIDASE.
    SUPFAMi SSF55920. SSF55920. 2 hits.
    TIGRFAMsi TIGR00501. met_pdase_II. 1 hit.
    PROSITEi PS01202. MAP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CEA10 / CBS 144.89 / FGSC A1163.

    Entry informationi

    Entry nameiMAP21_ASPFC
    AccessioniPrimary (citable) accession number: B0XTJ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: April 8, 2008
    Last modified: October 1, 2014
    This is version 43 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

    Complete proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3