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C8Z3V4

- MAP2_YEAS8

UniProt

C8Z3V4 - MAP2_YEAS8

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Protein

Methionine aminopeptidase 2

Gene
MAP2, EC1118_1B15_0199g
Organism
Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's yeast)
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 sitei174 – 1741Substrate By similarity
Metal bindingi194 – 1941Divalent metal cation 1 By similarity
Metal bindingi205 – 2051Divalent metal cation 1 By similarity
Metal bindingi205 – 2051Divalent metal cation 2; catalytic By similarity
Metal bindingi274 – 2741Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei282 – 2821Substrate By similarity
Metal bindingi307 – 3071Divalent metal cation 2; catalytic By similarity
Metal bindingi402 – 4021Divalent metal cation 1 By similarity
Metal bindingi402 – 4021Divalent 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
Name:MAP2
ORF Names:EC1118_1B15_0199g
OrganismiSaccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's yeast)
Taxonomic identifieri643680 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000000286: Chromosome II, Scaffold EC1118_1B15

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 – 421421Methionine aminopeptidase 2UniRule annotationPRO_0000407676Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliC8Z3V4.
SMRiC8Z3V4. Positions 61-421.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi41 – 5717Lys-richUniRule annotationAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

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.

C8Z3V4-1 [UniParc]FASTAAdd to Basket

« Hide

MTDAEIENSP ASDLKELNLE NEGVEQQDQA KADESDPVES KKKKNKKKKK    50
KKSNVKKIEL LFPDGKYPEG AWMDYHQDFN LQRTTDEESR YLKRDLERAE 100
HWNDVRKGAE IHRRVRRAIK DRIVPGMKLM DIADMIENTT RKYTGAENLL 150
AMEDPKSQGI GFPTGLSLNH CAAHFTPNAG DKTVLKYEDV MKVDYGVQVN 200
GNIIDSAFTV SFDPQYDNLL AAVKDATYTG IKEAGIDVRL TDIGEAIQEV 250
MESYEVEING ETYQVKPCRN LCGHSIAPYR IHGGKSVPIV KNGDTTKMEE 300
GEHFAIETFG STGRGYVTAG GEVSHYARSA EDHQVMPTLD SAKNLLKTID 350
RNFGTLPFCR RYLDRLGQEK YLFALNNLVR HGLVQDYPPL NDIPGSYTAQ 400
FEHTILLHAH KKEVVSKGDD Y 421
Length:421
Mass (Da):47,518
Last modified:November 3, 2009 - v1
Checksum:i206E9651D88925A8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FN393060 Genomic DNA. Translation: CAY77693.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FN393060 Genomic DNA. Translation: CAY77693.1 .

3D structure databases

ProteinModelPortali C8Z3V4.
SMRi C8Z3V4. Positions 61-421.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

OrthoDBi EOG7BGHW3.

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. "Eukaryote-to-eukaryote gene transfer events revealed by the genome sequence of the wine yeast Saccharomyces cerevisiae EC1118."
    Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B., Legras J.-L., Wincker P., Casaregola S., Dequin S.
    Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Lalvin EC1118 / Prise de mousse.

Entry informationi

Entry nameiMAP2_YEAS8
AccessioniPrimary (citable) accession number: C8Z3V4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: November 3, 2009
Last modified: May 14, 2014
This is version 30 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

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