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Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
Status
Reviewed-Annotation score: 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).UniRule annotation3 Publications

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

Kineticsi

  1. KM=1.95 mM for a Met-Ala-Ser peptide1 Publication
  1. 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)DescriptionActionsGraphical viewLength
Binding sitei109SubstrateUniRule annotation1 Publication1
Metal bindingi130Divalent metal cation 1UniRule annotation1 Publication1
Metal bindingi141Divalent metal cation 1UniRule annotation1 Publication1
Metal bindingi141Divalent metal cation 2; catalyticUniRule annotation1 Publication1
Metal bindingi210Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1 Publication1
Binding sitei218SubstrateUniRule annotation1 Publication1
Metal bindingi243Divalent metal cation 2; catalyticUniRule annotation1 Publication1
Metal bindingi339Divalent metal cation 1UniRule annotation1 Publication1
Metal bindingi339Divalent metal cation 2; catalyticUniRule annotation1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BRENDAi3.4.11.18. 7412.

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
Proteomesi
  • UP000000819 Componenti: Chromosome X

Organism-specific databases

EuPathDBiMicrosporidiaDB:ECU10_0750.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi241A → T: Abolishes catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001489851 – 358Methionine aminopeptidase 2Add BLAST358

Expressioni

Developmental stagei

Expressed in late sporogonial stages.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi284813.NP_586190.1.

Structurei

Secondary structure

1358
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 65Combined sources23
Helixi72 – 86Combined sources15
Turni87 – 89Combined sources3
Helixi91 – 94Combined sources4
Beta strandi95 – 103Combined sources9
Beta strandi106 – 108Combined sources3
Beta strandi126 – 135Combined sources10
Beta strandi138 – 147Combined sources10
Helixi150 – 152Combined sources3
Helixi153 – 169Combined sources17
Helixi176 – 187Combined sources12
Beta strandi191 – 193Combined sources3
Beta strandi195 – 200Combined sources6
Beta strandi209 – 213Combined sources5
Beta strandi236 – 249Combined sources14
Beta strandi262 – 264Combined sources3
Helixi275 – 287Combined sources13
Turni288 – 290Combined sources3
Helixi295 – 300Combined sources6
Helixi309 – 317Combined sources9
Beta strandi320 – 323Combined sources4
Beta strandi335 – 345Combined sources11
Beta strandi348 – 353Combined sources6

3D structure databases

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

eggNOGiKOG2775. Eukaryota.
COG0024. LUCA.
HOGENOMiHOG000226278.
InParanoidiQ8SR45.
KOiK01265.
OMAiWEHTILL.
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.
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]
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.

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)DescriptionActionsGraphical viewLength
Natural varianti288L → F in strain: ATCC 50502 / ECIII. 1

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

EnsemblFungiiCAD25794; CAD25794; CAD25794.
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.
RefSeqiNP_586190.1. NM_001042023.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi284813.NP_586190.1.

Protocols and materials databases

DNASUi859839.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAD25794; CAD25794; CAD25794.
GeneIDi859839.
KEGGiecu:ECU10_0750.

Organism-specific databases

EuPathDBiMicrosporidiaDB:ECU10_0750.

Phylogenomic databases

eggNOGiKOG2775. Eukaryota.
COG0024. LUCA.
HOGENOMiHOG000226278.
InParanoidiQ8SR45.
KOiK01265.
OMAiWEHTILL.
OrthoDBiEOG092C3NQP.

Enzyme and pathway databases

BRENDAi3.4.11.18. 7412.

Miscellaneous databases

EvolutionaryTraceiQ8SR45.
PROiQ8SR45.

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.
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]
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_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 30, 2016
This is version 112 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

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.