Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q54VU7

- MAP12_DICDI

UniProt

Q54VU7 - MAP12_DICDI

Protein

Methionine aminopeptidase 1D, mitochondrial

Gene

metap1d

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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 sitei232 – 2321SubstrateUniRule annotation
    Metal bindingi249 – 2491Divalent metal cation 1UniRule annotation
    Metal bindingi260 – 2601Divalent metal cation 1UniRule annotation
    Metal bindingi260 – 2601Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi323 – 3231Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei330 – 3301SubstrateUniRule annotation
    Metal bindingi355 – 3551Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi389 – 3891Divalent metal cation 1UniRule annotation
    Metal bindingi389 – 3891Divalent 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

    MEROPSiM24.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 1D, mitochondrialUniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 1DUniRule annotation
    Short name:
    MetAP 1DUniRule annotation
    Alternative name(s):
    Methionyl aminopeptidase type 1D, mitochondrial
    Peptidase M 1DUniRule annotation
    Gene namesi
    Name:metap1d
    Synonyms:map1d
    ORF Names:DDB_G0280127
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 3, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0280127. map1d.

    Subcellular locationi

    Mitochondrion UniRule annotation

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5858MitochondrionUniRule annotationAdd
    BLAST
    Chaini59 – 404346Methionine aminopeptidase 1D, mitochondrialPRO_0000328514Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi44689.DDBDRAFT_0206394.

    Structurei

    3D structure databases

    ProteinModelPortaliQ54VU7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi27 – 359Poly-Ser
    Compositional biasi38 – 425Poly-Asn

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0024.
    KOiK01265.
    OMAiCANEFDS.
    PhylomeDBiQ54VU7.

    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.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q54VU7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKILKNIIN KSSINNVFKT SFNGGISSSS SSSSSYLNNN NNIIKSYNVQ    50
    QKQQQRYYSS FEDDLSPKKL KEKILENETE EIRDFVRSQR LTKKTASPLE 100
    GMNRKERRKM TTKLYRNPDN LIRGGIVSPQ PLIPAHIKKP KYVLGEPVID 150
    FEIDDPIEIH TAESIEHMRV VGKMAKEVLE YAGTLVRPGI TTDEIDKLVH 200
    QNIIDRGAYP SPLGYKGFPK SICTSINEVL CHGIPDDRPL EFGDIVKIDV 250
    TLYYNGYHGD TCATFPVGEI DSSSKRLIEA TEKALYAAIG EVKDGALFNK 300
    IGKKIQLVAN KYSLSVTPEF TGHGIGQLFH TAPFVFQCAN EFDSVMKEGM 350
    IFTIEPVLVE STSPYAEWKM WDDKWTVSSR EGGWSAQFEH TILVTKDGYE 400
    ILTK 404
    Length:404
    Mass (Da):45,549
    Last modified:May 24, 2005 - v1
    Checksum:iAC369296B3E58FD4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000035 Genomic DNA. Translation: EAL67290.1.
    RefSeqiXP_641258.1. XM_636166.1.

    Genome annotation databases

    EnsemblProtistsiDDB0235404; DDB0235404; DDB_G0280127.
    GeneIDi8622390.
    KEGGiddi:DDB_G0280127.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000035 Genomic DNA. Translation: EAL67290.1 .
    RefSeqi XP_641258.1. XM_636166.1.

    3D structure databases

    ProteinModelPortali Q54VU7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDBDRAFT_0206394.

    Protein family/group databases

    MEROPSi M24.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0235404 ; DDB0235404 ; DDB_G0280127 .
    GeneIDi 8622390.
    KEGGi ddi:DDB_G0280127.

    Organism-specific databases

    dictyBasei DDB_G0280127. map1d.

    Phylogenomic databases

    eggNOGi COG0024.
    KOi K01265.
    OMAi CANEFDS.
    PhylomeDBi Q54VU7.

    Miscellaneous databases

    PROi Q54VU7.

    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.
    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 nameiMAP12_DICDI
    AccessioniPrimary (citable) accession number: Q54VU7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: May 24, 2005
    Last modified: October 1, 2014
    This is version 71 of the entry and version 1 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