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Protein

Methionine aminopeptidase 2

Gene

HCAG_08694

Organism
Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus) (Histoplasma capsulatum)
Status
Reviewed-Annotation score: 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 Fe2+-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 sitei216 – 2161SubstrateUniRule annotation
Metal bindingi237 – 2371Divalent metal cation 1UniRule annotation
Metal bindingi248 – 2481Divalent metal cation 1UniRule annotation
Metal bindingi248 – 2481Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi317 – 3171Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei325 – 3251SubstrateUniRule annotation
Metal bindingi350 – 3501Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi445 – 4451Divalent metal cation 1UniRule annotation
Metal bindingi445 – 4451Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

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
ORF Names:HCAG_08694
OrganismiAjellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus) (Histoplasma capsulatum)
Taxonomic identifieri339724 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeHistoplasma
ProteomesiUP000009297 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:HCAG_08694.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 464464Methionine aminopeptidase 2PRO_0000407641Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi339724.XP_001536373.1.

Structurei

3D structure databases

ProteinModelPortaliA6RGC8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi78 – 825Poly-Lys

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.
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]
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.

A6RGC8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSKTPGNHR RGPNESSPHP AIDAINPPKQ AAASRLVHSS LEGESEGGED
60 70 80 90 100
EDDDKPGADL KAVGQIGNNG QKRNKRRKKK KKNTKELEIL QTTPPRVALA
110 120 130 140 150
NIFRSQRYPE AEIVKYSTDN DNLQRTTAEE LRHISVLNAM DDEFLNDYRK
160 170 180 190 200
AAEVHRQVRQ YVQTIIKPGI ALSQLAEEIE DGVRALTNHQ GLETGDALKA
210 220 230 240 250
GMAFPTGLCL NNIAAHWTPN PGAKEVILKY DDVLKIDFGV HVNGRIVDSA
260 270 280 290 300
FTIAFNPVYD NLLAAVKDAT NAGLKEAGID ARIAHISETI QNVMESYEVE
310 320 330 340 350
LNQKVIPVKA VRNITGHNVL HYKIHGDKQV PFVKTQTNQR MEEGDVFAIE
360 370 380 390 400
TFGSTGKAYL DDATGIYGYG YDENASTAGL HHSSAKSLLK TIKENFGTLV
410 420 430 440 450
FSRRYLERLG VQRYHLGMRS LVTNGIVQSY APLVDVPGSY VAQFEHTVLL
460
RPNCKEVISR GDDY
Length:464
Mass (Da):51,306
Last modified:August 21, 2007 - v1
Checksum:iA07E43839397E551
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476666 Genomic DNA. Translation: EDN05040.1.
RefSeqiXP_001536373.1. XM_001536323.1.

Genome annotation databases

GeneIDi5442741.
KEGGiaje:HCAG_08694.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476666 Genomic DNA. Translation: EDN05040.1.
RefSeqiXP_001536373.1. XM_001536323.1.

3D structure databases

ProteinModelPortaliA6RGC8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi339724.XP_001536373.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5442741.
KEGGiaje:HCAG_08694.

Organism-specific databases

EuPathDBiFungiDB:HCAG_08694.

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.
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]
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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NAm1 / WU24.

Entry informationi

Entry nameiMAP2_AJECN
AccessioniPrimary (citable) accession number: A6RGC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: August 21, 2007
Last modified: June 24, 2015
This is version 51 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, Reference 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

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 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.