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Protein

Methionine aminopeptidase 2-2

Gene

AFLA_092260

Organism
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
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)DescriptionActionsGraphical viewLength
Binding sitei219SubstrateUniRule annotation1
Metal bindingi240Divalent metal cation 1UniRule annotation1
Metal bindingi251Divalent metal cation 1UniRule annotation1
Metal bindingi251Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi320Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei328SubstrateUniRule annotation1
Metal bindingi353Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi449Divalent metal cation 1UniRule annotation1
Metal bindingi449Divalent metal cation 2; catalyticUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

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:AFLA_092260
OrganismiAspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Taxonomic identifieri332952 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000001875 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:AFLA_092260.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004076221 – 468Methionine aminopeptidase 2-2Add BLAST468

Structurei

3D structure databases

ProteinModelPortaliB8NLL0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi78 – 81Poly-Lys4

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000226278.
KOiK01265.
OMAiPSIPNRH.
OrthoDBiEOG092C3NQP.

Family and domain databases

CDDicd01088. MetAP2. 1 hit.
Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_03175. MetAP_2_euk. 1 hit.
InterProiIPR000994. Pept_M24.
IPR001714. Pept_M24_MAP.
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.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B8NLL0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSKTFEGEG QRGGNDPSNS TSPNSAGGEP RGAHLSRDGD GSLGDGDGDD
60 70 80 90 100
GADGDEKDGA VTTTPLTEQQ PSSETTSKKK KRRKPKKKIS ALKQSSPPRV
110 120 130 140 150
PLDDLFPTGQ FPVGETHEYG SVVEGTARTT SEEVRYLSRN YLQDDSVLTD
160 170 180 190 200
YRKAAEIHRQ VRHWTQENVR PGQTLTEIAV GIEDGVRALL DNAGLETGQC
210 220 230 240 250
LQSGMGFPTG LALNDCVAHY TPNPGQKDIV LQASDVMKVD FGVHINGWIV
260 270 280 290 300
DSAFTMSFDP TYDNLLAAVK DATNTGIKNA GIDVRISDVS AAIQEAMESY
310 320 330 340 350
EVEIGGKVFP VKPVRDISGH NINRYQIHGG KSIPFVKNSS QTKMEEGEIF
360 370 380 390 400
AIETFGSTGR GSTVEGFGVY GYGKDPNAPK KVSSPLASAR SLYKTINENF
410 420 430 440 450
GSIVFCRRYL ERLGVERYLA GMNSLVNNGI VEQYAPLMDM KGSYSAQFEH
460
TILLRESCKE VVSRGNDY
Length:468
Mass (Da):50,724
Last modified:March 3, 2009 - v1
Checksum:i7290AC2351FFEFF9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EQ963480 Genomic DNA. Translation: EED49145.1.
RefSeqiXP_002381046.1. XM_002381005.1.

Genome annotation databases

EnsemblFungiiEED49145; EED49145; AFLA_092260.
GeneIDi7918359.
KEGGiafv:AFLA_092260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EQ963480 Genomic DNA. Translation: EED49145.1.
RefSeqiXP_002381046.1. XM_002381005.1.

3D structure databases

ProteinModelPortaliB8NLL0.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEED49145; EED49145; AFLA_092260.
GeneIDi7918359.
KEGGiafv:AFLA_092260.

Organism-specific databases

EuPathDBiFungiDB:AFLA_092260.

Phylogenomic databases

HOGENOMiHOG000226278.
KOiK01265.
OMAiPSIPNRH.
OrthoDBiEOG092C3NQP.

Family and domain databases

CDDicd01088. MetAP2. 1 hit.
Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_03175. MetAP_2_euk. 1 hit.
InterProiIPR000994. Pept_M24.
IPR001714. Pept_M24_MAP.
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.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMAP22_ASPFN
AccessioniPrimary (citable) accession number: B8NLL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: March 3, 2009
Last modified: November 30, 2016
This is version 53 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

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 one 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.