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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: -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)DescriptionActionsGraphical viewLength
Binding sitei216SubstrateUniRule annotation1
Metal bindingi237Divalent metal cation 1UniRule annotation1
Metal bindingi248Divalent metal cation 1UniRule annotation1
Metal bindingi248Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi317Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei325SubstrateUniRule annotation1
Metal bindingi350Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi445Divalent metal cation 1UniRule annotation1
Metal bindingi445Divalent metal cation 2; catalyticUniRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionAminopeptidase, Hydrolase, Protease
LigandMetal-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
Proteomesi
  • UP000009297 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:HCAG_08694

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004076411 – 464Methionine aminopeptidase 2Add BLAST464

Proteomic databases

PRIDEiA6RGC8

Interactioni

Protein-protein interaction databases

STRINGi339724.XP_001536373.1

Structurei

3D structure databases

ProteinModelPortaliA6RGC8
SMRiA6RGC8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi78 – 82Poly-Lys5

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2775 Eukaryota
COG0024 LUCA
KOiK01265
OrthoDBiEOG092C3NQP

Family and domain databases

CDDicd01088 MetAP2, 1 hit
Gene3Di1.10.10.10, 1 hit
HAMAPiMF_03175 MetAP_2_euk, 1 hit
InterProiView protein in InterPro
IPR036005 Creatinase/aminopeptidase-like
IPR000994 Pept_M24
IPR001714 Pept_M24_MAP
IPR002468 Pept_M24A_MAP2
IPR018349 Pept_M24A_MAP2_BS
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF00557 Peptidase_M24, 1 hit
PRINTSiPR00599 MAPEPTIDASE
SUPFAMiSSF46785 SSF46785, 1 hit
SSF55920 SSF55920, 2 hits
TIGRFAMsiTIGR00501 met_pdase_II, 1 hit
PROSITEiView protein in PROSITE
PS01202 MAP_2, 1 hit

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

EnsemblFungiiEDN05040; EDN05040; HCAG_08694
GeneIDi5442741
KEGGiaje:HCAG_08694

Similar proteinsi

Entry informationi

Entry nameiMAP2_AJECN
AccessioniPrimary (citable) accession number: A6RGC8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: August 21, 2007
Last modified: May 23, 2018
This is version 68 of the entry and version 1 of the sequence. See 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
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