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A1CYM1

- MAP22_NEOFI

UniProt

A1CYM1 - MAP22_NEOFI

Protein

Methionine aminopeptidase 2-2

Gene

NFIA_034070

Organism
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 52 (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 sitei215 – 2151SubstrateUniRule annotation
    Metal bindingi236 – 2361Divalent metal cation 1UniRule annotation
    Metal bindingi247 – 2471Divalent metal cation 1UniRule annotation
    Metal bindingi247 – 2471Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi316 – 3161Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei324 – 3241SubstrateUniRule annotation
    Metal bindingi349 – 3491Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi444 – 4441Divalent metal cation 1UniRule annotation
    Metal bindingi444 – 4441Divalent 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:NFIA_034070
    OrganismiNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus)
    Taxonomic identifieri331117 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeNeosartorya
    ProteomesiUP000006702: 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 – 463463Methionine aminopeptidase 2-2PRO_0000407639Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi36630.CADNFIAP00003719.

    Structurei

    3D structure databases

    ProteinModelPortaliA1CYM1.
    SMRiA1CYM1. Positions 95-463.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi69 – 8517Lys-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000226278.
    KOiK01265.
    OMAiNNCVAHY.
    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]
    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.

    A1CYM1-1 [UniParc]FASTAAdd to Basket

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    MGSKSPEGHW QAPHASNSNE LKPANPDPQT SQNGSGSADL DRGVIGDDDD    50
    DDEDAEENGV NTETPNVEKK KKRKKSNKKK KKKTKSGTLS VTELKQTSPP 100
    RVLVSTLFPS EYPVGELVPY DCTTRTTDEE SRYNSRLWDD DFLPDYRQAA 150
    EIHRQVRQYA QKELIKPGAT LLSIAEGIED GVRALSGHQG LEPGDFFKAG 200
    MGFPTGLCLN HIAAHWTPNP REKDVILDKG DVLKVDFGVH VNGRIVDSAF 250
    TVAFDDKYDN LLTAVREATN TGIKHAGVDA RMSDIGAAIQ EVMESYEVEI 300
    DGKVFPVKAI RNITGHDILR YHIHGGKQIP FIKNNNQDKM EEGEVYAIET 350
    FGSTGRGFLD DDVGVYGYGR NENMSGANLR LSSAKSLLKT IDANFGSIVF 400
    SRRYLERLGV KNYLLGMKNL VDNGIVECYS PLVDVKGSYT AQFEHTILLH 450
    SGGKEVISRG DDY 463
    Length:463
    Mass (Da):51,127
    Last modified:January 23, 2007 - v1
    Checksum:iC015237E375845F8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS027686 Genomic DNA. Translation: EAW23841.1.
    RefSeqiXP_001265738.1. XM_001265737.1.

    Genome annotation databases

    EnsemblFungiiCADNFIAT00003808; CADNFIAP00003719; CADNFIAG00003808.
    GeneIDi4592397.
    KEGGinfi:NFIA_034070.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS027686 Genomic DNA. Translation: EAW23841.1 .
    RefSeqi XP_001265738.1. XM_001265737.1.

    3D structure databases

    ProteinModelPortali A1CYM1.
    SMRi A1CYM1. Positions 95-463.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 36630.CADNFIAP00003719.

    Protein family/group databases

    MEROPSi M24.002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADNFIAT00003808 ; CADNFIAP00003719 ; CADNFIAG00003808 .
    GeneIDi 4592397.
    KEGGi nfi:NFIA_034070.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000226278.
    KOi K01265.
    OMAi NNCVAHY.
    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 ]
    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 1020 / DSM 3700 / FGSC A1164 / NRRL 181.

    Entry informationi

    Entry nameiMAP22_NEOFI
    AccessioniPrimary (citable) accession number: A1CYM1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 52 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