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Q55C21

- MAP2_DICDI

UniProt

Q55C21 - MAP2_DICDI

Protein

Methionine aminopeptidase 2

Gene

metap2

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 3 (28 Jul 2009)
      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 sitei191 – 1911SubstrateUniRule annotation
    Metal bindingi211 – 2111Divalent metal cation 1UniRule annotation
    Metal bindingi222 – 2221Divalent metal cation 1UniRule annotation
    Metal bindingi222 – 2221Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi291 – 2911Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei299 – 2991SubstrateUniRule annotation
    Metal bindingi324 – 3241Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi417 – 4171Divalent metal cation 1UniRule annotation
    Metal bindingi417 – 4171Divalent 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 2UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 2UniRule annotation
    Short name:
    MetAP 2UniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    Name:metap2
    ORF Names:DDB_G0270264
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 1, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0270264. metap2.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. phagocytic vesicle Source: dictyBase

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 436436Methionine aminopeptidase 2PRO_0000328464Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi44689.DDBDRAFT_0190923.

    Structurei

    3D structure databases

    ProteinModelPortaliQ55C21.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi44 – 5512Poly-LysAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    KOiK01265.
    OMAiIQICEEL.
    PhylomeDBiQ55C21.

    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.

    Q55C21-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEIQPKTEV PPKTVEEEEE SDDEEDNTKV TEGGNPTGGE GAAKKKKKKN    50
    KKKKKAAPVA SAADIIDSKP IPSGLVQTNP PTIPVSKQFS NGVYPMGEIQ 100
    EYRDSNSYRT TSEEKRLEER IHANIYNDVR RAAEVHRQVR KYVQGIVKPG 150
    LGLTELVESL ENASRTLIEA DGLKAGIAFP TGVSLNHIAA HFTPNTGDKT 200
    VLKKDDVLKI DFGTHVNGYI IDCAFTVTFD EKYDKLKDAV REATNTGIYH 250
    AGIDARLGEI GAAIQEVMES HEIELNGKTY PIRSIRNLNG HSIRPYVIHG 300
    GKTVPIVRGG EMTKMEEGEF YAIETFGSTG RAQVIEDLEC SHYMKTDYQT 350
    TVRLPKAKQL LQYINKNYDT LCFCRRWLDR AGEDKHILAL NNLCDLGIIQ 400
    RHAPLVDSKG SYVAQYEHTL LLKPTAKEVL SRGDDY 436
    Length:436
    Mass (Da):48,561
    Last modified:July 28, 2009 - v3
    Checksum:i586AE79EF89454CF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000005 Genomic DNA. Translation: EAL72482.3.
    RefSeqiXP_646660.3. XM_641568.3.

    Genome annotation databases

    EnsemblProtistsiDDB0304991; DDB0304991; DDB_G0270264.
    GeneIDi8617632.
    KEGGiddi:DDB_G0270264.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000005 Genomic DNA. Translation: EAL72482.3 .
    RefSeqi XP_646660.3. XM_641568.3.

    3D structure databases

    ProteinModelPortali Q55C21.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDBDRAFT_0190923.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0304991 ; DDB0304991 ; DDB_G0270264 .
    GeneIDi 8617632.
    KEGGi ddi:DDB_G0270264.

    Organism-specific databases

    dictyBasei DDB_G0270264. metap2.

    Phylogenomic databases

    eggNOGi COG0024.
    KOi K01265.
    OMAi IQICEEL.
    PhylomeDBi Q55C21.

    Miscellaneous databases

    PROi Q55C21.

    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. "The genome of the social amoeba Dictyostelium discoideum."
      Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
      , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
      Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.

    Entry informationi

    Entry nameiMAP2_DICDI
    AccessioniPrimary (citable) accession number: Q55C21
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 73 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Dictyostelium discoideum
      Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3