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Protein

Methionine aminopeptidase 2-1

Gene

An01g11360

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

Co2+UniRule annotation, Zn2+UniRule annotation, Mn2+UniRule annotation, Fe2+UniRule annotationNote: 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 sitei211 – 2111SubstrateUniRule annotation
Metal bindingi232 – 2321Divalent metal cation 1UniRule annotation
Metal bindingi243 – 2431Divalent metal cation 1UniRule annotation
Metal bindingi243 – 2431Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi312 – 3121Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei320 – 3201SubstrateUniRule annotation
Metal bindingi345 – 3451Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi456 – 4561Divalent metal cation 1UniRule annotation
Metal bindingi456 – 4561Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Protein family/group databases

MEROPSiM24.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2-1UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2-1UniRule annotation
Short name:
MetAP 2-1UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
ORF Names:An01g11360
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706 Componenti: Chromosome 2R

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 475475Methionine aminopeptidase 2-1PRO_0000407624Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliA2QAF9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi70 – 756Poly-Lys

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
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.

A2QAF9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSKSPEGHR QTPDASNSSE LKPANPNPKP ARNGSQSADL DGGNLDDDND
60 70 80 90 100
DDGEANEEAG VKTSADSTDK KKKRKRSKKK TKKGTLPLKQ SSPPRVLVSS
110 120 130 140 150
LFPSGYPIGE CVPYQDDNTS RTTDEELRYN SRLWDKDFLD EYRQAAEIHR
160 170 180 190 200
QVRQYAQNEL IKPGASLTTI AEGIEDGVRA LSGHQGLEPG DGFKAGMGFP
210 220 230 240 250
TGLCLNNVAA HWTPNPGAKD VFLDKSDVLK VDFGVHVNGR IVDSAFTVAF
260 270 280 290 300
DHTYDNLLTA VKEATNTGIM HAGIDARVSE IGAAIQEVME SYEVEIAGKT
310 320 330 340 350
HPVKAIRNIT GHDILRYNIH GGKQVPFIKN DRPDKMEEGE VFAIETFGST
360 370 380 390 400
GRGVLHDDVG LCLSNVFSKA NAPQVGVYGY GRNTDVSGAN LRLSSAKNLL
410 420 430 440 450
KTIDANFGSL VFCRRYLERL GVEKYHLGMR HLIDNGIVEY YEPLVDVKGS
460 470
YTAQFEHTIL LHNGGKEVIS RGDDY
Length:475
Mass (Da):51,977
Last modified:March 6, 2007 - v1
Checksum:iB76FFBA77D325599
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM269981 Genomic DNA. Translation: CAK44040.1.

Genome annotation databases

EnsemblFungiiCADANGAT00001134; CADANGAP00001099; CADANGAG00001134.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM269981 Genomic DNA. Translation: CAK44040.1.

3D structure databases

ProteinModelPortaliA2QAF9.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM24.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANGAT00001134; CADANGAP00001099; CADANGAG00001134.

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
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]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513.

Entry informationi

Entry nameiMAP21_ASPNC
AccessioniPrimary (citable) accession number: A2QAF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: March 6, 2007
Last modified: July 22, 2015
This is version 56 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.