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Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus)
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 sitei224SubstrateUniRule annotation1
Metal bindingi244Divalent metal cation 1UniRule annotation1
Metal bindingi255Divalent metal cation 1UniRule annotation1
Metal bindingi255Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi326Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei334SubstrateUniRule annotation1
Metal bindingi359Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi454Divalent metal cation 1UniRule annotation1
Metal bindingi454Divalent 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
Name:MAP2UniRule annotation
ORF Names:LELG_04878
OrganismiLodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus)
Taxonomic identifieri379508 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeLodderomyces
Proteomesi
  • UP000001996 Componenti: Unassembled WGS sequence

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_00004076551 – 473Methionine aminopeptidase 2Add BLAST473

Interactioni

Protein-protein interaction databases

STRINGi379508.XP_001524065.1.

Structurei

3D structure databases

ProteinModelPortaliA5E5I9.
SMRiA5E5I9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi97 – 112Lys-richAdd BLAST16

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2775. Eukaryota.
COG0024. LUCA.
InParanoidiA5E5I9.
KOiK01265.
OMAiMIHICET.
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.

A5E5I9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTDTSIKAG IDSIRAKADD LHLAEDSSNG TQANLDKHQI KATTAVGQDN
60 70 80 90 100
GNNAGVADHK NDKNNKNNKN NNDDDDDDED DDVAAAAAAV GDAGSDKKKK
110 120 130 140 150
KKKSSNKKKK KKLVSIDQSY PDGVFPEGEW QEYGLDSNKY RTTSEEMRYL
160 170 180 190 200
DRQQNNKWED FRKGAEIHRR VRAKAKSSIR PGMTMIEIAD LIENSVRAYA
210 220 230 240 250
SADHTLKAGI GFPTGLSLNH VAAHYTPNTG DKLTLGKDDL MKVDIGVHVN
260 270 280 290 300
GRICDSAFTM TFNEDGKYDS IMQAVKEATN TGVKEAGIDV RLNDIGAAVQ
310 320 330 340 350
EVMESYEMEL DGKTYPIKCI KNLNGHNIGD FIIHSGKTVP IVANGDMTKM
360 370 380 390 400
EEGETFAIET FGSTGNGYVL PEGECSHYAL NSGVESIKPP SDKAKHLLNT
410 420 430 440 450
IQSNFGTLPW CRRYLERTGE EKYLFALNQL VKAGIVEDYP PIVDKRGSYT
460 470
AQFEHTILLH PHKKEVVTRG DDY
Length:473
Mass (Da):52,168
Last modified:June 12, 2007 - v1
Checksum:i276295946A163975
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH981530 Genomic DNA. Translation: EDK46697.1.
RefSeqiXP_001524065.1. XM_001524015.1.

Genome annotation databases

EnsemblFungiiEDK46697; EDK46697; LELG_04878.
GeneIDi5231111.
KEGGilel:LELG_04878.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH981530 Genomic DNA. Translation: EDK46697.1.
RefSeqiXP_001524065.1. XM_001524015.1.

3D structure databases

ProteinModelPortaliA5E5I9.
SMRiA5E5I9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi379508.XP_001524065.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEDK46697; EDK46697; LELG_04878.
GeneIDi5231111.
KEGGilel:LELG_04878.

Phylogenomic databases

eggNOGiKOG2775. Eukaryota.
COG0024. LUCA.
InParanoidiA5E5I9.
KOiK01265.
OMAiMIHICET.
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_LODEL
AccessioniPrimary (citable) accession number: A5E5I9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: June 12, 2007
Last modified: November 30, 2016
This is version 63 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.