Skip Header

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

Methionine aminopeptidase 2

Gene

MAP2

Organism
Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's yeast)
Status
Reviewed-Annotation score: -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 sitei174SubstrateUniRule annotation1
Metal bindingi194Divalent metal cation 1UniRule annotation1
Metal bindingi205Divalent metal cation 1UniRule annotation1
Metal bindingi205Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi274Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei282SubstrateUniRule annotation1
Metal bindingi307Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi402Divalent metal cation 1UniRule annotation1
Metal bindingi402Divalent metal cation 2; catalyticUniRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionAminopeptidase, Hydrolase, Protease
LigandMetal-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
ORF Names:EC1118_1B15_0199g
OrganismiSaccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's yeast)
Taxonomic identifieri643680 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000000286 Componenti: Chromosome II, Scaffold EC1118_1B15

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004076761 – 421Methionine aminopeptidase 2Add BLAST421

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei35PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiC8Z3V4

Structurei

3D structure databases

ProteinModelPortaliC8Z3V4
SMRiC8Z3V4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi41 – 57Lys-richAdd BLAST17

Sequence similaritiesi

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

Phylogenomic databases

OrthoDBiEOG092C3NQP

Family and domain databases

CDDicd01088 MetAP2, 1 hit
Gene3Di1.10.10.10, 1 hit
HAMAPiMF_03175 MetAP_2_euk, 1 hit
InterProiView protein in InterPro
IPR036005 Creatinase/aminopeptidase-like
IPR000994 Pept_M24
IPR001714 Pept_M24_MAP
IPR002468 Pept_M24A_MAP2
IPR018349 Pept_M24A_MAP2_BS
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF00557 Peptidase_M24, 1 hit
PRINTSiPR00599 MAPEPTIDASE
SUPFAMiSSF46785 SSF46785, 1 hit
SSF55920 SSF55920, 2 hits
TIGRFAMsiTIGR00501 met_pdase_II, 1 hit
PROSITEiView protein in PROSITE
PS01202 MAP_2, 1 hit

Sequencei

Sequence statusi: Complete.

C8Z3V4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDAEIENSP ASDLKELNLE NEGVEQQDQA KADESDPVES KKKKNKKKKK
60 70 80 90 100
KKSNVKKIEL LFPDGKYPEG AWMDYHQDFN LQRTTDEESR YLKRDLERAE
110 120 130 140 150
HWNDVRKGAE IHRRVRRAIK DRIVPGMKLM DIADMIENTT RKYTGAENLL
160 170 180 190 200
AMEDPKSQGI GFPTGLSLNH CAAHFTPNAG DKTVLKYEDV MKVDYGVQVN
210 220 230 240 250
GNIIDSAFTV SFDPQYDNLL AAVKDATYTG IKEAGIDVRL TDIGEAIQEV
260 270 280 290 300
MESYEVEING ETYQVKPCRN LCGHSIAPYR IHGGKSVPIV KNGDTTKMEE
310 320 330 340 350
GEHFAIETFG STGRGYVTAG GEVSHYARSA EDHQVMPTLD SAKNLLKTID
360 370 380 390 400
RNFGTLPFCR RYLDRLGQEK YLFALNNLVR HGLVQDYPPL NDIPGSYTAQ
410 420
FEHTILLHAH KKEVVSKGDD Y
Length:421
Mass (Da):47,518
Last modified:November 3, 2009 - v1
Checksum:i206E9651D88925A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN393060 Genomic DNA Translation: CAY77693.1

Genome annotation databases

EnsemblFungiiCAY77693; CAY77693; EC1118_1B15_0199g

Similar proteinsi

Entry informationi

Entry nameiMAP2_YEAS8
AccessioniPrimary (citable) accession number: C8Z3V4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: November 3, 2009
Last modified: May 23, 2018
This is version 50 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health