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Protein

Methionine aminopeptidase 2

Gene

MGG_00966

Organism
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae)
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 sitei196 – 1961SubstrateUniRule annotation
Metal bindingi216 – 2161Divalent metal cation 1UniRule annotation
Metal bindingi227 – 2271Divalent metal cation 1UniRule annotation
Metal bindingi227 – 2271Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi296 – 2961Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei304 – 3041SubstrateUniRule annotation
Metal bindingi329 – 3291Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi424 – 4241Divalent metal cation 1UniRule annotation
Metal bindingi424 – 4241Divalent 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 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
ORF Names:MGG_00966
OrganismiMagnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae)
Taxonomic identifieri242507 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeMagnaporthalesMagnaporthaceaeMagnaporthe
ProteomesiUP000009058 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiFungiDB:MGG_00966.

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 – 443443Methionine aminopeptidase 2PRO_0000407656Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliA4RDI6.
SMRiA4RDI6. Positions 76-443.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi58 – 7114Lys-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
InParanoidiA4RDI6.
KOiK01265.
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]
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.

A4RDI6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQVPTEEL KKLKVAAKSD DPAAANGANG NTANDSDGSD DDDEPEDAGA
60 70 80 90 100
AAGGEGAKKK KKRKPRKKKK KNANGQTDPP RIPISQLFPD NSYPKGQEVE
110 120 130 140 150
YLGENTYRTT NEEKRHLDSL NSDLLTDYRH GAEAHRQARR WAHKHVKPGM
160 170 180 190 200
SLTDIANGIE DSVRALVGHS GLEEGDAIIA GMGFPTGLSI NHCAAHYTPN
210 220 230 240 250
AGNKMVLEHD DVLKVDIGVH VNGRIVDSAF TVAFNPRYDN LLAAVKDATN
260 270 280 290 300
TGIREAGIDA RLGEIGEAIQ ETMESYEVEI DGETYPVKPI RNLNGHTIDR
310 320 330 340 350
YTIHGGKSVP IVKSADQTKM EEGEIYAIET FGSTGLGYVR DEGEVSHYAK
360 370 380 390 400
RADAPNVALR LTSAQKILNV INKNFGTLPF CRRYLDRLGQ DKYLLGLNNL
410 420 430 440
VSNGIVEAYP PLVDKKGSYT AQYEHTILLR PTVKEVISRG DDY
Length:443
Mass (Da):48,388
Last modified:May 15, 2007 - v1
Checksum:i1C082CDAC42FC28A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM001235 Genomic DNA. Translation: EHA48400.1.
RefSeqiXP_003717984.1. XM_003717936.1.

Genome annotation databases

EnsemblFungiiMGG_00966T0; MGG_00966T0; MGG_00966.
GeneIDi2674877.
KEGGimgr:MGG_00966.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM001235 Genomic DNA. Translation: EHA48400.1.
RefSeqiXP_003717984.1. XM_003717936.1.

3D structure databases

ProteinModelPortaliA4RDI6.
SMRiA4RDI6. Positions 76-443.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM24.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiMGG_00966T0; MGG_00966T0; MGG_00966.
GeneIDi2674877.
KEGGimgr:MGG_00966.

Organism-specific databases

EuPathDBiFungiDB:MGG_00966.

Phylogenomic databases

eggNOGiCOG0024.
InParanoidiA4RDI6.
KOiK01265.
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]
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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 70-15 / ATCC MYA-4617 / FGSC 8958.

Entry informationi

Entry nameiMAP2_MAGO7
AccessioniPrimary (citable) accession number: A4RDI6
Secondary accession number(s): G4ND58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 15, 2007
Last modified: July 22, 2015
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

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.