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Q7ZWV9

- MAP1_XENLA

UniProt

Q7ZWV9 - MAP1_XENLA

Protein

Methionine aminopeptidase 1

Gene

metap1

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 2 (18 Mar 2008)
      Previous versions | rss
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    • Comment

    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 sitei203 – 2031SubstrateUniRule annotation
    Metal bindingi220 – 2201Divalent metal cation 1UniRule annotation
    Metal bindingi231 – 2311Divalent metal cation 1UniRule annotation
    Metal bindingi231 – 2311Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi294 – 2941Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei301 – 3011SubstrateUniRule annotation
    Metal bindingi327 – 3271Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi358 – 3581Divalent metal cation 1UniRule annotation
    Metal bindingi358 – 3581Divalent 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

    Protein family/group databases

    MEROPSiM24.017.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 1UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 1UniRule annotation
    Short name:
    MetAP 1UniRule annotation
    Alternative name(s):
    Peptidase M 1UniRule annotation
    Gene namesi
    Name:metap1
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-6254194. metap1.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytosolic ribosome Source: UniProtKB-HAMAP

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 385385Methionine aminopeptidase 1PRO_0000323738Add
    BLAST

    Interactioni

    Subunit structurei

    Associates with the 60S ribosomal subunit of the 80S translational complex.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliQ7ZWV9.
    SMRiQ7ZWV9. Positions 81-385.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni9 – 5244Zinc finger-like; important for proper ribosome associationUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

    Phylogenomic databases

    HOVERGENiHBG067178.

    Family and domain databases

    Gene3Di3.90.230.10. 1 hit.
    HAMAPiMF_01974. MetAP_1.
    InterProiIPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002467. Pept_M24A_MAP1.
    [Graphical view]
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    PRINTSiPR00599. MAPEPTIDASE.
    SUPFAMiSSF55920. SSF55920. 1 hit.
    TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
    PROSITEiPS00680. MAP_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q7ZWV9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAVESRVCE TEGCSSEAKL QCPTCIKLGI QGSYFCSQEC FKGSWATHKL    50
    LHKKAKDDKI KPEVSPWTMD GEVNTDPWPG YRYTGKLRPH YPLTPMRPVP 100
    SYIQRPDYAD HPLGMSESEQ TLKGTSQIKT LSPEDIEGMR VVCRLAREVL 150
    GVAAMMVKSG ITTEEIDHAV HLACISRNCY PSPLNYYNFP KSCCTSVNEV 200
    ICHGIPDRRP LQDGDIVNVD ITVYRDGYHG DLNETFYVGD VDEGAKRLVE 250
    TTYECLMQAI DEVKPGVRYR ELGNIIQKHA QANGFSIVRS YCGHGIHKLF 300
    HTAPNVPHYG KNKAVGVMKP GHVFTIEPMI CEGGWQDETW PDGWTAITRD 350
    GKRSAQFEHT LLVTETGCEI LTCRLEENGR PYFIS 385
    Length:385
    Mass (Da):43,196
    Last modified:March 18, 2008 - v2
    Checksum:iE3CCA9B269376EEF
    GO

    Sequence cautioni

    The sequence AAH46685.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC046685 mRNA. Translation: AAH46685.1. Different initiation.
    BC070567 mRNA. Translation: AAH70567.1.
    UniGeneiXl.76058.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC046685 mRNA. Translation: AAH46685.1 . Different initiation.
    BC070567 mRNA. Translation: AAH70567.1 .
    UniGenei Xl.76058.

    3D structure databases

    ProteinModelPortali Q7ZWV9.
    SMRi Q7ZWV9. Positions 81-385.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M24.017.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Xenbasei XB-GENE-6254194. metap1.

    Phylogenomic databases

    HOVERGENi HBG067178.

    Family and domain databases

    Gene3Di 3.90.230.10. 1 hit.
    HAMAPi MF_01974. MetAP_1.
    InterProi IPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002467. Pept_M24A_MAP1.
    [Graphical view ]
    Pfami PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    PRINTSi PR00599. MAPEPTIDASE.
    SUPFAMi SSF55920. SSF55920. 1 hit.
    TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
    PROSITEi PS00680. MAP_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. NIH - Xenopus Gene Collection (XGC) project
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryo.

    Entry informationi

    Entry nameiMAP1_XENLA
    AccessioniPrimary (citable) accession number: Q7ZWV9
    Secondary accession number(s): Q6NRY8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 18, 2008
    Last sequence update: March 18, 2008
    Last modified: October 1, 2014
    This is version 72 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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