SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B2B738

- MAP2_PODAN

UniProt

B2B738 - MAP2_PODAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Methionine aminopeptidase 2
Gene
PODANS_2_9800
Organism
Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina)
Status
Reviewed - 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) By similarity.UniRule annotation

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation

Cofactori

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 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei198 – 1981Substrate By similarity
Metal bindingi218 – 2181Divalent metal cation 1 By similarity
Metal bindingi229 – 2291Divalent metal cation 1 By similarity
Metal bindingi229 – 2291Divalent metal cation 2; catalytic By similarity
Metal bindingi298 – 2981Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei306 – 3061Substrate By similarity
Metal bindingi331 – 3311Divalent metal cation 2; catalytic By similarity
Metal bindingi426 – 4261Divalent metal cation 1 By similarity
Metal bindingi426 – 4261Divalent metal cation 2; catalytic By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-HAMAP
  2. metalloaminopeptidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. protein initiator methionine removal Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2 (EC:3.4.11.18)
Short name:
MAP 2
Short name:
MetAP 2
Alternative name(s):
Peptidase M
Gene namesi
Ordered Locus Names:PODANS_2_9800
OrganismiPodospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina)
Taxonomic identifieri515849 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesLasiosphaeriaceaePodospora
ProteomesiUP000001197: Chromosome 2

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445Methionine aminopeptidase 2UniRule annotation
PRO_0000407665Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB2B738.
SMRiB2B738. Positions 77-445.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi61 – 7313Lys-richUniRule annotation
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

KOiK01265.

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.

B2B738-1 [UniParc]FASTAAdd to Basket

« Hide

MAAQAPVDEI AQLSVSDAAT TKPKPGLDSA TATNGNLNRD SDDSDDDAEN    50
AAPGAETGAA KKKKKRKPKK KKKNPTAQSD PPRVLISQLF PDKVYPKGEE 100
VEYVNENRYR TTNEEKRHLD NLKNDFYNDY RHAAEAHRQT RQWAQKNIKP 150
GWSLTDIANG IEDSVRALVG HQGLEEGDAL KAGMGFPTGL SLNHCAAHYN 200
PNAGNKMVLQ QDDVLKVDIG VHVNGNIVDS AFTLAFNPRY DPLLEACKAA 250
TNEGLKQAGI DARLGEIGGY IQEVMESYEV ELDGNTYQVK PIRNLNGHTI 300
LPYNIHGGKS VPIVKSNDQT KMEEGDVFAI ETFGSTGNGY VHEEGEISHY 350
AKRMDAPKVD LRLSSAKSLL NVINKNFGTL PFCRRYLDRL GQDKYLLGLN 400
SLVANGVVES YPPLVDKKGS YTAQFEHTIL IRPTVKEVIS RGDDY 445
Length:445
Mass (Da):49,022
Last modified:May 20, 2008 - v1
Checksum:iD4973E6DC966821E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU640366 Genomic DNA. Translation: CAP73616.1.
RefSeqiXP_001911788.1. XM_001911753.1.

Genome annotation databases

GeneIDi6196226.
KEGGipan:PODANSg8833.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU640366 Genomic DNA. Translation: CAP73616.1 .
RefSeqi XP_001911788.1. XM_001911753.1.

3D structure databases

ProteinModelPortali B2B738.
SMRi B2B738. Positions 77-445.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 6196226.
KEGGi pan:PODANSg8833.

Phylogenomic databases

KOi K01265.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPi MF_03175. MetAP_2_euk.
InterProi IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
PANTHERi PTHR10804:SF9. PTHR10804:SF9. 1 hit.
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SUPFAMi SSF55920. SSF55920. 2 hits.
TIGRFAMsi TIGR00501. met_pdase_II. 1 hit.
PROSITEi PS01202. MAP_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: S / ATCC MYA-4624 / DSM 980 / FGSC 10383.

Entry informationi

Entry nameiMAP2_PODAN
AccessioniPrimary (citable) accession number: B2B738
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 20, 2008
Last modified: May 14, 2014
This is version 41 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

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