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A5E5I9

- MAP2_LODEL

UniProt

A5E5I9 - MAP2_LODEL

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Protein

Methionine aminopeptidase 2

Gene
MAP2, LELG_04878
Organism
Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus)
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 sitei224 – 2241Substrate By similarity
Metal bindingi244 – 2441Divalent metal cation 1 By similarity
Metal bindingi255 – 2551Divalent metal cation 1 By similarity
Metal bindingi255 – 2551Divalent metal cation 2; catalytic By similarity
Metal bindingi326 – 3261Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei334 – 3341Substrate By similarity
Metal bindingi359 – 3591Divalent metal cation 2; catalytic By similarity
Metal bindingi454 – 4541Divalent metal cation 1 By similarity
Metal bindingi454 – 4541Divalent 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:LELG_04878
OrganismiLodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus)
Taxonomic identifieri379508 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeLodderomyces
ProteomesiUP000001996: Unassembled WGS sequence

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 – 473473Methionine aminopeptidase 2UniRule annotationPRO_0000407655Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi36914.A5E5I9.

Structurei

3D structure databases

ProteinModelPortaliA5E5I9.
SMRiA5E5I9. Positions 112-473.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi97 – 11216Lys-richUniRule annotationAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
KOiK01265.
OMAiIQICEEL.
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.

A5E5I9-1 [UniParc]FASTAAdd to Basket

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MSTDTSIKAG IDSIRAKADD LHLAEDSSNG TQANLDKHQI KATTAVGQDN    50
GNNAGVADHK NDKNNKNNKN NNDDDDDDED DDVAAAAAAV GDAGSDKKKK 100
KKKSSNKKKK KKLVSIDQSY PDGVFPEGEW QEYGLDSNKY RTTSEEMRYL 150
DRQQNNKWED FRKGAEIHRR VRAKAKSSIR PGMTMIEIAD LIENSVRAYA 200
SADHTLKAGI GFPTGLSLNH VAAHYTPNTG DKLTLGKDDL MKVDIGVHVN 250
GRICDSAFTM TFNEDGKYDS IMQAVKEATN TGVKEAGIDV RLNDIGAAVQ 300
EVMESYEMEL DGKTYPIKCI KNLNGHNIGD FIIHSGKTVP IVANGDMTKM 350
EEGETFAIET FGSTGNGYVL PEGECSHYAL NSGVESIKPP SDKAKHLLNT 400
IQSNFGTLPW CRRYLERTGE EKYLFALNQL VKAGIVEDYP PIVDKRGSYT 450
AQFEHTILLH PHKKEVVTRG DDY 473
Length:473
Mass (Da):52,168
Last modified:June 12, 2007 - v1
Checksum:i276295946A163975
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH981530 Genomic DNA. Translation: EDK46697.1.
RefSeqiXP_001524065.1. XM_001524015.1.

Genome annotation databases

GeneIDi5231111.
KEGGilel:LELG_04878.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH981530 Genomic DNA. Translation: EDK46697.1 .
RefSeqi XP_001524065.1. XM_001524015.1.

3D structure databases

ProteinModelPortali A5E5I9.
SMRi A5E5I9. Positions 112-473.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 36914.A5E5I9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5231111.
KEGGi lel:LELG_04878.

Phylogenomic databases

eggNOGi COG0024.
KOi K01265.
OMAi IQICEEL.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239.

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: May 14, 2014
This is version 48 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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