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Q4WII3

- MAP22_ASPFU

UniProt

Q4WII3 - MAP22_ASPFU

Protein

Methionine aminopeptidase 2-2

Gene

AFUA_2G01750

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (05 Jul 2005)
      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

    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:AFUA_2G01750
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530: Chromosome 2

    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 2-2PRO_0000407638Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi5085.CADAFUAP00003355.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4WII3.
    SMRiQ4WII3. 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

    eggNOGiCOG0024.
    HOGENOMiHOG000226278.
    KOiK01265.
    OMAiRNISAHN.
    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.

    Q4WII3-1 [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:July 5, 2005 - v1
    Checksum:i940B4DC3289A7288
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000008 Genomic DNA. Translation: EAL87272.1.
    RefSeqiXP_749310.1. XM_744217.1.

    Genome annotation databases

    EnsemblFungiiCADAFUAT00003355; CADAFUAP00003355; CADAFUAG00003355.
    GeneIDi3506721.
    KEGGiafm:AFUA_2G01750.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000008 Genomic DNA. Translation: EAL87272.1 .
    RefSeqi XP_749310.1. XM_744217.1.

    3D structure databases

    ProteinModelPortali Q4WII3.
    SMRi Q4WII3. Positions 118-486.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5085.CADAFUAP00003355.

    Protein family/group databases

    MEROPSi M24.002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUAT00003355 ; CADAFUAP00003355 ; CADAFUAG00003355 .
    GeneIDi 3506721.
    KEGGi afm:AFUA_2G01750.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000226278.
    KOi K01265.
    OMAi RNISAHN.
    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. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
      Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
      , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
      Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

    Entry informationi

    Entry nameiMAP22_ASPFU
    AccessioniPrimary (citable) accession number: Q4WII3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 66 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