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Protein

Methionine aminopeptidase 2

Gene

Pa_2_9800

Organism
Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina)
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 sitei198SubstrateUniRule annotation1
Metal bindingi218Divalent metal cation 1UniRule annotation1
Metal bindingi229Divalent metal cation 1UniRule annotation1
Metal bindingi229Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi298Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei306SubstrateUniRule annotation1
Metal bindingi331Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi426Divalent metal cation 1UniRule annotation1
Metal bindingi426Divalent 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 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
Ordered Locus Names:Pa_2_9800
ORF Names:PODANS_2_9800
OrganismiPodospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina)
Taxonomic identifieri515849 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesLasiosphaeriaceaePodospora
Proteomesi
  • UP000001197 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)DescriptionActionsGraphical viewLength
ChainiPRO_00004076651 – 445Methionine aminopeptidase 2Add BLAST445

Interactioni

Protein-protein interaction databases

STRINGi515849.XP_001911788.1.

Structurei

3D structure databases

ProteinModelPortaliB2B738.
SMRiB2B738.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi61 – 73Lys-richAdd BLAST13

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2775. Eukaryota.
COG0024. LUCA.
KOiK01265.
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.

B2B738-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQAPVDEI AQLSVSDAAT TKPKPGLDSA TATNGNLNRD SDDSDDDAEN
60 70 80 90 100
AAPGAETGAA KKKKKRKPKK KKKNPTAQSD PPRVLISQLF PDKVYPKGEE
110 120 130 140 150
VEYVNENRYR TTNEEKRHLD NLKNDFYNDY RHAAEAHRQT RQWAQKNIKP
160 170 180 190 200
GWSLTDIANG IEDSVRALVG HQGLEEGDAL KAGMGFPTGL SLNHCAAHYN
210 220 230 240 250
PNAGNKMVLQ QDDVLKVDIG VHVNGNIVDS AFTLAFNPRY DPLLEACKAA
260 270 280 290 300
TNEGLKQAGI DARLGEIGGY IQEVMESYEV ELDGNTYQVK PIRNLNGHTI
310 320 330 340 350
LPYNIHGGKS VPIVKSNDQT KMEEGDVFAI ETFGSTGNGY VHEEGEISHY
360 370 380 390 400
AKRMDAPKVD LRLSSAKSLL NVINKNFGTL PFCRRYLDRL GQDKYLLGLN
410 420 430 440
SLVANGVVES YPPLVDKKGS YTAQFEHTIL IRPTVKEVIS RGDDY
Length:445
Mass (Da):49,022
Last modified:May 20, 2008 - v1
Checksum:iD4973E6DC966821E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU640366 Genomic DNA. Translation: CAP73616.1.
FO904937 Genomic DNA. Translation: CDP26018.1.
RefSeqiXP_001911788.1. XM_001911753.1.

Genome annotation databases

EnsemblFungiiCAP73616; CAP73616; PODANS_2_9800.
GeneIDi6196226.
KEGGipan:PODANSg8833.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU640366 Genomic DNA. Translation: CAP73616.1.
FO904937 Genomic DNA. Translation: CDP26018.1.
RefSeqiXP_001911788.1. XM_001911753.1.

3D structure databases

ProteinModelPortaliB2B738.
SMRiB2B738.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi515849.XP_001911788.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAP73616; CAP73616; PODANS_2_9800.
GeneIDi6196226.
KEGGipan:PODANSg8833.

Phylogenomic databases

eggNOGiKOG2775. Eukaryota.
COG0024. LUCA.
KOiK01265.
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 nameiMAP2_PODAN
AccessioniPrimary (citable) accession number: B2B738
Secondary accession number(s): A0A090D5L5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 20, 2008
Last modified: November 30, 2016
This is version 55 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.