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Q6XMH7

- MAP2_ENCIT

UniProt

Q6XMH7 - MAP2_ENCIT

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Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Encephalitozoon intestinalis (strain ATCC 50506) (Microsporidian parasite) (Septata intestinalis)
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).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 Fe(2+)-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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091SubstrateUniRule annotation
Metal bindingi130 – 1301Divalent metal cation 1UniRule annotation
Metal bindingi141 – 1411Divalent metal cation 1UniRule annotation
Metal bindingi141 – 1411Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi210 – 2101Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei218 – 2181SubstrateUniRule annotation
Metal bindingi243 – 2431Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi339 – 3391Divalent metal cation 1UniRule annotation
Metal bindingi339 – 3391Divalent metal cation 2; catalyticUniRule annotation

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. 8683.

Protein family/group databases

MEROPSiM24.002.

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
OrganismiEncephalitozoon intestinalis (strain ATCC 50506) (Microsporidian parasite) (Septata intestinalis)
Taxonomic identifieri876142 [NCBI]
Taxonomic lineageiEukaryotaFungiMicrosporidiaUnikaryonidaeEncephalitozoon
ProteomesiUP000002313: Chromosome X

Organism-specific databases

EuPathDBiMicrosporidiaDB:Eint_100700.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358Methionine aminopeptidase 2PRO_0000148987Add
BLAST

Proteomic databases

PRIDEiQ6XMH7.

Structurei

3D structure databases

ProteinModelPortaliQ6XMH7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

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.

Q6XMH7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKFILIDQAP ELPIEFLPKG DCYRKGRLFG PKGEEIENTT DCDLLQDARR
60 70 80 90 100
AAEAHRRARY KVQSIIRPGI TLLEIVRSIE DSTRTLLEGE RNNGIGFPAG
110 120 130 140 150
MSMNSCAAHY TVNPGEEDIV LKEDDVLKVD FGTHSNGRIM DSAFTVAFQE
160 170 180 190 200
NLQPLLMAAR EGTETGIRSL GIDARVCDIG RDINEVITSY EVEIEGKTWP
210 220 230 240 250
IRPVSDLHGH SISQFKIHGG ISIPAVNNRD TTRIKGDTFY AVETFATTGK
260 270 280 290 300
GFINDRSPCS HFMLNVHKSR KLFNKDLIKV YEFVKSSFGT LPFSPRHLDH
310 320 330 340 350
YNLVEGGSLK SVNLLTMMGL FTPYPPLNDI DGSKVAQFEH TVYLSENGKE

ILTRGDDY
Length:358
Mass (Da):40,058
Last modified:July 24, 2013 - v2
Checksum:iDA38CFE92BAA9362
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111E → K in AAP51022. (PubMed:16004378)Curated
Sequence conflicti24 – 241R → K in AAP51022. (PubMed:16004378)Curated
Sequence conflicti27 – 271R → K in AAP51022. (PubMed:16004378)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY224693 Genomic DNA. Translation: AAP51022.1.
CP001951 Genomic DNA. Translation: ADM12396.1.
AY339781 Genomic DNA. Translation: AAR04555.1.
RefSeqiXP_003073756.1. XM_003073710.1.

Genome annotation databases

GeneIDi9699461.
KEGGiein:Eint_100700.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY224693 Genomic DNA. Translation: AAP51022.1 .
CP001951 Genomic DNA. Translation: ADM12396.1 .
AY339781 Genomic DNA. Translation: AAR04555.1 .
RefSeqi XP_003073756.1. XM_003073710.1.

3D structure databases

ProteinModelPortali Q6XMH7.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M24.002.

Proteomic databases

PRIDEi Q6XMH7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 9699461.
KEGGi ein:Eint_100700.

Organism-specific databases

EuPathDBi MicrosporidiaDB:Eint_100700.

Phylogenomic databases

KOi K01265.
OrthoDBi EOG7BGHW3.

Enzyme and pathway databases

BRENDAi 3.4.11.18. 8683.

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].
    Strain: CDC.
  2. "The complete sequence of the smallest known nuclear genome from the microsporidian Encephalitozoon intestinalis."
    Corradi N., Pombert J.-F., Farinelli L., Didier E.S., Keeling P.J.
    Nat. Commun. 1:77-77(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 50506.
  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 14-331.
    Strain: ATCC 50506.

Entry informationi

Entry nameiMAP2_ENCIT
AccessioniPrimary (citable) accession number: Q6XMH7
Secondary accession number(s): E0S9L1, Q6VH15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 24, 2013
Last modified: November 26, 2014
This is version 67 of the entry and version 2 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