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Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Komagataella pastoris (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris)
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 sitei198 – 1981SubstrateUniRule annotation
Metal bindingi218 – 2181Divalent metal cation 1UniRule annotation
Metal bindingi229 – 2291Divalent metal cation 1UniRule annotation
Metal bindingi229 – 2291Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi298 – 2981Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei306 – 3061SubstrateUniRule annotation
Metal bindingi331 – 3311Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi429 – 4291Divalent metal cation 1UniRule annotation
Metal bindingi429 – 4291Divalent metal cation 2; catalyticUniRule annotation

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 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:MAP2UniRule annotation
Ordered Locus Names:PAS_chr2-2_0159
OrganismiKomagataella pastoris (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris)
Taxonomic identifieri644223 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPhaffomycetaceaeKomagataella
ProteomesiUP000000314 Componenti: Chromosome 2

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 – 448448Methionine aminopeptidase 2PRO_0000407664Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi644223.PAS_chr2-2_0159.

Structurei

3D structure databases

ProteinModelPortaliC4R2P3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
InParanoidiC4R2P3.
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.

C4R2P3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSSVDKVSQ KVADVKLGSS KSTKNNKSKG KGKSNKNQVV EDDDEDDFEK
60 70 80 90 100
ALELAMQLDA QKLAQKKADD VPLVEEEEKK VEEKIEQQYD PISTFYPDGN
110 120 130 140 150
YPQGEVVDYK DDNLYRTTDE EKRALDREKN NKWNEFRKGA EIHRRVRKLA
160 170 180 190 200
KDEIKPGMSM IEIAELIENA VRGYSGEDGL KGGMGFPCGL SLNHCAAHYS
210 220 230 240 250
PNANDKLVLN YEDVMKVDFG VHVNGHIIDS AFTLTFDDKY DDLLKAVKDA
260 270 280 290 300
TNTGIREAGI DVRLTDIGEA IQEVMESYEV TLDGETYQVK PIKNLCGHNI
310 320 330 340 350
GQYRIHGGKS VPIVKNFDNT KMEEGETFAI ETFGSTGRGH VIGQGECSHY
360 370 380 390 400
AKNPDAPANA ISSIRVNRAK QLLKTIDENF GTLPFCRRYI DRLGEEKYLL
410 420 430 440
ALNQLVKSGV VSDYPPLVDV KGSYTAQYEH TILLRPNVKE VVSRGEDY
Length:448
Mass (Da):50,204
Last modified:July 7, 2009 - v1
Checksum:i6BCE8381B94A08F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN392320 Genomic DNA. Translation: CAY69767.1.
RefSeqiXP_002492047.1. XM_002492002.1.

Genome annotation databases

EnsemblFungiiCAY69767; CAY69767; PAS_chr2-2_0159.
GeneIDi8198269.
KEGGippa:PAS_chr2-2_0159.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN392320 Genomic DNA. Translation: CAY69767.1.
RefSeqiXP_002492047.1. XM_002492002.1.

3D structure databases

ProteinModelPortaliC4R2P3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi644223.PAS_chr2-2_0159.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAY69767; CAY69767; PAS_chr2-2_0159.
GeneIDi8198269.
KEGGippa:PAS_chr2-2_0159.

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
InParanoidiC4R2P3.
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: GS115 / ATCC 20864.

Entry informationi

Entry nameiMAP2_PICPG
AccessioniPrimary (citable) accession number: C4R2P3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: July 7, 2009
Last modified: April 1, 2015
This is version 42 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.