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A1CH02

- MAP22_ASPCL

UniProt

A1CH02 - MAP22_ASPCL

Protein

Methionine aminopeptidase 2-2

Gene

ACLA_046220

Organism
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (23 Jan 2007)
      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 sitei197 – 1971SubstrateUniRule annotation
    Metal bindingi217 – 2171Divalent metal cation 1UniRule annotation
    Metal bindingi228 – 2281Divalent metal cation 1UniRule annotation
    Metal bindingi228 – 2281Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi297 – 2971Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei305 – 3051SubstrateUniRule annotation
    Metal bindingi330 – 3301Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi425 – 4251Divalent metal cation 1UniRule annotation
    Metal bindingi425 – 4251Divalent 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

    MEROPSiM24.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 2-2UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 2-2UniRule annotation
    Short name:
    MetAP 2-2UniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    ORF Names:ACLA_046220
    OrganismiAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
    Taxonomic identifieri344612 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006701: 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 – 435435Methionine aminopeptidase 2-2PRO_0000407598Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi5057.CADACLAP00004837.

    Structurei

    3D structure databases

    ProteinModelPortaliA1CH02.
    SMRiA1CH02. Positions 75-430.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi60 – 7112Poly-LysAdd
    BLAST

    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.
    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]
    PANTHERiPTHR10804:SF9. PTHR10804:SF9. 1 hit.
    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.

    A1CH02-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAQTTEKLQ KLDLNGQSGD AKADAPAAGQ AEAGEAEEDS DDEKDDGNAA    50
    PEAGAGGAAK KKKRKSKKKK KGGAKVQSSP PRVPVSNLFP NNQYPEGEIV 100
    EYTNENSYRT TNEEKRYLDR MNNDFLQEYR QAAEVHRQVR QYAQKNIKPG 150
    QTLTEIAEGI EDAVRALTGH QGLEEGDNLK GGMGFPCGLS INHCAAHYTP 200
    NAGNKMVLQQ GDVMKVDFGA QINGRIVDSA FTMTFDPVYD PLLEAVKDAT 250
    NTGIREAGID VRMSDIGAAI QEAMESYEIE LNGTMYPVKC IRNLNGHNID 300
    QHVIHGGKSV PIVKGGDQTK MEEGETFAIE TFGSTGKGYV REDMETSHYA 350
    LVPDAPSVPL RLSSAKNLLN VINKNFGTLP FCRRYLDRLG QDKYLLGLNN 400
    LVSSGIVQDY PPLCDIKGSY TAQFEHVQIP SHSHP 435
    Length:435
    Mass (Da):47,491
    Last modified:January 23, 2007 - v1
    Checksum:i2D152BB644700084
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS027054 Genomic DNA. Translation: EAW10157.1.
    RefSeqiXP_001271583.1. XM_001271582.1.

    Genome annotation databases

    EnsemblFungiiCADACLAT00004938; CADACLAP00004837; CADACLAG00004938.
    GeneIDi4704294.
    KEGGiact:ACLA_046220.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS027054 Genomic DNA. Translation: EAW10157.1 .
    RefSeqi XP_001271583.1. XM_001271582.1.

    3D structure databases

    ProteinModelPortali A1CH02.
    SMRi A1CH02. Positions 75-430.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5057.CADACLAP00004837.

    Protein family/group databases

    MEROPSi M24.002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADACLAT00004938 ; CADACLAP00004837 ; CADACLAG00004938 .
    GeneIDi 4704294.
    KEGGi act:ACLA_046220.

    Phylogenomic databases

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

    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 ]
    PANTHERi PTHR10804:SF9. PTHR10804:SF9. 1 hit.
    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: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

    Entry informationi

    Entry nameiMAP22_ASPCL
    AccessioniPrimary (citable) accession number: A1CH02
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 49 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, Reference 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