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Q8SR45

- MAP2_ENCCU

UniProt

Q8SR45 - MAP2_ENCCU

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Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

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).3 PublicationsUniRule 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

Kineticsi

  1. KM=1.95 mM for a Met-Ala-Ser peptide1 Publication

Vmax=7.3 nmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 8.5.1 Publication

Temperature dependencei

Optimum temperature is 37 degrees Celsius.1 Publication

Sites

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

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. 7412.

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
Ordered Locus Names:ECU10_0750
OrganismiEncephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
Taxonomic identifieri284813 [NCBI]
Taxonomic lineageiEukaryotaFungiMicrosporidiaUnikaryonidaeEncephalitozoon
ProteomesiUP000000819: Chromosome X

Organism-specific databases

EuPathDBiMicrosporidiaDB:ECU10_0750.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi241 – 2411A → T: Abolishes catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358Methionine aminopeptidase 2PRO_0000148985Add
BLAST

Expressioni

Developmental stagei

Expressed in late sporogonial stages.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi6035.ECU10_0750.

Structurei

Secondary structure

1
358
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi43 – 6523Combined sources
Helixi72 – 8615Combined sources
Turni87 – 893Combined sources
Helixi91 – 944Combined sources
Beta strandi95 – 1039Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi126 – 13510Combined sources
Beta strandi138 – 14710Combined sources
Helixi150 – 1523Combined sources
Helixi153 – 16917Combined sources
Helixi176 – 18712Combined sources
Beta strandi191 – 1933Combined sources
Beta strandi195 – 2006Combined sources
Beta strandi209 – 2135Combined sources
Beta strandi236 – 24914Combined sources
Beta strandi262 – 2643Combined sources
Helixi275 – 28713Combined sources
Turni288 – 2903Combined sources
Helixi295 – 3006Combined sources
Helixi309 – 3179Combined sources
Beta strandi320 – 3234Combined sources
Beta strandi335 – 34511Combined sources
Beta strandi348 – 3536Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FM3X-ray2.18A/B1-358[»]
3FMQX-ray2.50A/B1-358[»]
3FMRX-ray2.89A/B1-358[»]
ProteinModelPortaliQ8SR45.
SMRiQ8SR45. Positions 3-358.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8SR45.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
InParanoidiQ8SR45.
KOiK01265.
OMAiIQICEEL.
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.

Q8SR45-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKCILLNQAE ELPIEFLPKD GVYGKGKLFD SRNMEIENFT ESDILQDARR
60 70 80 90 100
AAEAHRRARY RVQSIVRPGI TLLEIVRSIE DSTRTLLKGE RNNGIGFPAG
110 120 130 140 150
MSMNSCAAHY TVNPGEQDIV LKEDDVLKID FGTHSDGRIM DSAFTVAFKE
160 170 180 190 200
NLEPLLVAAR EGTETGIKSL GVDVRVCDIG RDINEVISSY EVEIGGRMWP
210 220 230 240 250
IRPISDLHGH SISQFRIHGG ISIPAVNNRD TTRIKGDSFY AVETFATTGK
260 270 280 290 300
GSIDDRPPCS HFVLNTYKSR KLFNKDLIKV YEFVKDSLGT LPFSPRHLDY
310 320 330 340 350
YGLVKGGSLK SVNLLTMMGL LTPYPPLNDI DGCKVAQFEH TVYLSEHGKE

VLTRGDDY
Length:358
Mass (Da):39,975
Last modified:June 1, 2002 - v1
Checksum:i058A8AB457EC258F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti288 – 2881L → F in strain: ATCC 50502 / ECIII.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF440270 Genomic DNA. Translation: AAM49625.1.
AL590449 Genomic DNA. Translation: CAD25794.1.
AY339777 Genomic DNA. Translation: AAR04551.1.
AY339778 Genomic DNA. Translation: AAR04552.1.
AY339779 Genomic DNA. Translation: AAR04553.1.
RefSeqiNP_586190.1. NM_001042023.1.

Genome annotation databases

GeneIDi859839.
KEGGiecu:ECU10_0750.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF440270 Genomic DNA. Translation: AAM49625.1 .
AL590449 Genomic DNA. Translation: CAD25794.1 .
AY339777 Genomic DNA. Translation: AAR04551.1 .
AY339778 Genomic DNA. Translation: AAR04552.1 .
AY339779 Genomic DNA. Translation: AAR04553.1 .
RefSeqi NP_586190.1. NM_001042023.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3FM3 X-ray 2.18 A/B 1-358 [» ]
3FMQ X-ray 2.50 A/B 1-358 [» ]
3FMR X-ray 2.89 A/B 1-358 [» ]
ProteinModelPortali Q8SR45.
SMRi Q8SR45. Positions 3-358.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 6035.ECU10_0750.

Protein family/group databases

MEROPSi M24.002.

Protocols and materials databases

DNASUi 859839.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 859839.
KEGGi ecu:ECU10_0750.

Organism-specific databases

EuPathDBi MicrosporidiaDB:ECU10_0750.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000226278.
InParanoidi Q8SR45.
KOi K01265.
OMAi IQICEEL.
OrthoDBi EOG7BGHW3.

Enzyme and pathway databases

BRENDAi 3.4.11.18. 7412.

Miscellaneous databases

EvolutionaryTracei Q8SR45.

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], FUNCTION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: GB-M1.
  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 13-349.
    Strain: ATCC 50502 / ECIII, ATCC 50503 / ECI and ECII.
  4. "Characterization of recombinant microsporidian methionine aminopeptidase type 2."
    Weiss L.M., Zhou G.C., Zhang H.
    J. Eukaryot. Microbiol. 50:597-599(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "System for expression of microsporidian methionine amino peptidase type 2 (MetAP2) in the yeast Saccharomyces cerevisiae."
    Upadhya R., Zhang H.S., Weiss L.M.
    Antimicrob. Agents Chemother. 50:3389-3395(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ALA-241.
  6. "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi (microsporidia): a reference map for proteins expressed in late sporogonial stages."
    Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.
    Proteomics 6:3625-3635(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], DEVELOPMENTAL STAGE.
  7. "Structure of a microsporidian methionine aminopeptidase type 2 complexed with fumagillin and TNP-470."
    Alvarado J.J., Nemkal A., Sauder J.M., Russell M., Akiyoshi D.E., Shi W., Almo S.C., Weiss L.M.
    Mol. Biochem. Parasitol. 168:158-167(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) IN COMPLEX WITH IRON AND INHIBITOR, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiMAP2_ENCCU
AccessioniPrimary (citable) accession number: Q8SR45
Secondary accession number(s): Q6VH17, Q6VH18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: June 1, 2002
Last modified: November 26, 2014
This is version 96 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3