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Q6XMH6

- MAP2_ENCHA

UniProt

Q6XMH6 - MAP2_ENCHA

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Protein
Methionine aminopeptidase 2
Gene
MAP2, EHEL_100750
Organism
Encephalitozoon hellem (strain ATCC 50504) (Microsporidian parasite)
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).1 Publication

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.

Enzyme regulationi

Irreversibly inhibited by the fungal metabolite fumagillin and the fumagillin analog TNP470, antiangiogenic drugs.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091Substrate By similarity
Metal bindingi130 – 1301Divalent metal cation 1 By similarity
Metal bindingi141 – 1411Divalent metal cation 1 By similarity
Metal bindingi141 – 1411Divalent metal cation 2; catalytic By similarity
Metal bindingi210 – 2101Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei218 – 2181Substrate By similarity
Metal bindingi243 – 2431Divalent metal cation 2; catalytic By similarity
Metal bindingi339 – 3391Divalent metal cation 1 By similarity
Metal bindingi339 – 3391Divalent 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

Enzyme and pathway databases

BRENDAi3.4.11.18. 8141.

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
Ordered Locus Names:EHEL_100750
OrganismiEncephalitozoon hellem (strain ATCC 50504) (Microsporidian parasite)
Taxonomic identifieri907965 [NCBI]
Taxonomic lineageiEukaryotaFungiMicrosporidiaUnikaryonidaeEncephalitozoon
ProteomesiUP000010086: Chromosome X

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 – 358358Methionine aminopeptidase 2UniRule annotation
PRO_0000148986Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ6XMH6.
SMRiQ6XMH6. Positions 4-358.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK01265.
OrthoDBiEOG7BGHW3.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_03175. MetAP_2_euk.
InterProiIPR000994. 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]
SUPFAMiSSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6XMH6-1 [UniParc]FASTAAdd to Basket

« Hide

MKFILMNQAA ELPIEFLPRD GAYRKGRLLD SKNAEVENTT ESDILQDARR    50
AAEAHRRVRY KVQSIIKPGM TLLEIVKSIE DSTRILLSGE RNNGIGFPAG 100
MSMNSCAAHY SVNPGEKDII LTENDVLKID FGTHSNGRIM DSAFTIAFKE 150
EFEPLLMAAK EGTETGIRSL GIDARVCDIG RDINEVISSY EMEVDGKKWA 200
IRPVSDLHGH SISQFKIHGG ISIPAVNNRD PTRITGDTFY AVETFATTGE 250
GFINDRSPCS HFMINTHKSR KLYNKDLIKV YEFVRDSFGT LPFSPRHLDY 300
YNLVEGSALK SVNLLTMMGL FTPYPPLNDI DGSKVAQFEH TVYLSESGKE 350
ILTRGDDY 358
Length:358
Mass (Da):40,071
Last modified:July 5, 2004 - v1
Checksum:i1EF1C9B28E0E8C39
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY224694 Genomic DNA. Translation: AAP51023.1.
CP002723 Genomic DNA. Translation: AFM99168.1.
AY339780 Genomic DNA. Translation: AAR04554.1.
RefSeqiXP_003888149.1. XM_003888100.1.

Genome annotation databases

GeneIDi13466604.
KEGGiehe:EHEL_100750.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY224694 Genomic DNA. Translation: AAP51023.1 .
CP002723 Genomic DNA. Translation: AFM99168.1 .
AY339780 Genomic DNA. Translation: AAR04554.1 .
RefSeqi XP_003888149.1. XM_003888100.1.

3D structure databases

ProteinModelPortali Q6XMH6.
SMRi Q6XMH6. Positions 4-358.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 13466604.
KEGGi ehe:EHEL_100750.

Phylogenomic databases

KOi K01265.
OrthoDBi EOG7BGHW3.

Enzyme and pathway databases

BRENDAi 3.4.11.18. 8141.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPi MF_03175. MetAP_2_euk.
InterProi 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 ]
SUPFAMi SSF55920. SSF55920. 2 hits.
TIGRFAMsi TIGR00501. met_pdase_II. 1 hit.
PROSITEi PS01202. MAP_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Investigations into microsporidian methionine aminopeptidase type 2: a therapeutic target for microsporidiosis."
    Zhang H., Huang H., Cali A., Takvorian P.M., Feng X., Zhou G., Weiss L.M.
    Folia Parasitol. 52:182-192(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Gain and loss of multiple functionally related, horizontally transferred genes in the reduced genomes of two microsporidian parasites."
    Pombert J.-F., Selman M., Burki F., Bardell F.T., Farinelli L., Solter L.F., Whitman D.W., Weiss L.M., Corradi N., Keeling P.J.
    Proc. Natl. Acad. Sci. U.S.A. 109:12638-12643(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 50504.
  3. "Phylogenetic relationships of methionine aminopeptidase 2 among Encephalitozoon species and genotypes of microsporidia."
    Pandrea I., Mittleider D., Brindley P.J., Didier E.S., Robertson D.L.
    Mol. Biochem. Parasitol. 140:141-152(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-343.
    Strain: ATCC 50504.
  4. "Microsporidian methionine aminopeptidase type 2."
    Weiss L.M., Costa S.F., Zhang H.
    J. Eukaryot. Microbiol. 48:88S-90S(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.

Entry informationi

Entry nameiMAP2_ENCHA
AccessioniPrimary (citable) accession number: Q6XMH6
Secondary accession number(s): I6UP09, Q6VH16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 62 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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