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Protein

Methionine aminopeptidase 2-2

Gene

BDBG_07768

Organism
Ajellomyces dermatitidis (strain SLH14081) (Blastomyces dermatitidis)
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)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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2-2UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2-2UniRule annotation
Short name:
MetAP 2-2UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
ORF Names:BDBG_07768
OrganismiAjellomyces dermatitidis (strain SLH14081) (Blastomyces dermatitidis)
Taxonomic identifieri559298 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeBlastomyces
Proteomesi
  • UP000002038 Componenti: Unassembled WGS sequence

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004076171 – 464Methionine aminopeptidase 2-2Add BLAST464

Interactioni

Protein-protein interaction databases

STRINGi559298.XP_002621929.1.

Structurei

3D structure databases

ProteinModelPortaliC5JYZ5.
SMRiC5JYZ5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi71 – 84Lys-richAdd BLAST14

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2775. Eukaryota.
COG0024. LUCA.
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.
IPR001714. Pept_M24_MAP.
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.
TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C5JYZ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSKTPNDHR RGPNESSPHA AIDTINPPKH AAASGLLHGP LEGETEDGED
60 70 80 90 100
EDDDKTGADL KSVGQLNNST KKKNKRKKNK KKKKTLLGGL QTTPPRVALS
110 120 130 140 150
SIFYNQRYPE AEIVGYTTNN DNLQRITAEE FRHLCVVNDM DDEFLNDYRK
160 170 180 190 200
AAEVHRQVRQ YVQTITKPGI AMSQLAQEIE DGVRALTDHQ GIETGDALKA
210 220 230 240 250
GMAFPTGLCL NNIGAHWTPN PGAKEVILQY DDVLKVDFGV HVNGRIVDSA
260 270 280 290 300
YTMAFNPVYD DLLTAVKAAT NTGLKEAGID ARIDCISEAI QEVMESYEVE
310 320 330 340 350
LNRKIIPVKA VRNITGHNIL RYKIHGDKQV PFVKTHTNQR MEEGDIFAIE
360 370 380 390 400
TFGSTGKAYL DDDIGIYGYF CDEHASAAGL HHSSAKSLLK TIKDNFGTLV
410 420 430 440 450
FSRRYLERLG VKSYHLGMRS LVSKGIVQSY APLVDVPGSY VAQFEHTVLL
460
RPNCKEVISR GDDY
Length:464
Mass (Da):51,413
Last modified:July 28, 2009 - v1
Checksum:i3F48E2F1AE45E115
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GG657467 Genomic DNA. Translation: EEQ73554.1.
RefSeqiXP_002621929.1. XM_002621883.1.

Genome annotation databases

EnsemblFungiiEEQ73554; EEQ73554; BDBG_07768.
GeneIDi8502192.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GG657467 Genomic DNA. Translation: EEQ73554.1.
RefSeqiXP_002621929.1. XM_002621883.1.

3D structure databases

ProteinModelPortaliC5JYZ5.
SMRiC5JYZ5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi559298.XP_002621929.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEEQ73554; EEQ73554; BDBG_07768.
GeneIDi8502192.

Phylogenomic databases

eggNOGiKOG2775. Eukaryota.
COG0024. LUCA.
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.
IPR001714. Pept_M24_MAP.
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.
TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMAP22_AJEDS
AccessioniPrimary (citable) accession number: C5JYZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: July 28, 2009
Last modified: November 30, 2016
This is version 45 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

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.