Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Methionine aminopeptidase 2

Gene

TRV_05431

Organism
Trichophyton verrucosum (strain HKI 0517)
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 sitei199 – 1991SubstrateUniRule annotation
Metal bindingi219 – 2191Divalent metal cation 1UniRule annotation
Metal bindingi230 – 2301Divalent metal cation 1UniRule annotation
Metal bindingi230 – 2301Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi299 – 2991Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei307 – 3071SubstrateUniRule annotation
Metal bindingi335 – 3351Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi430 – 4301Divalent metal cation 1UniRule annotation
Metal bindingi430 – 4301Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

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
ORF Names:TRV_05431
OrganismiTrichophyton verrucosum (strain HKI 0517)
Taxonomic identifieri663202 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaeTrichophyton
ProteomesiUP000008383 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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 449449Methionine aminopeptidase 2PRO_0000407670Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi663202.XP_003020465.1.

Structurei

3D structure databases

ProteinModelPortaliD4DE65.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi61 – 7616Lys-richAdd
BLAST

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]
PANTHERiPTHR10804:SF9. PTHR10804:SF9. 1 hit.
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.

D4DE65-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQAAPELA KLDLNKNTGS VEANAVSAGG SEKEEAENEG DSEDDRDDEQ
60 70 80 90 100
AGGSAEVNAE KKKKKKRPKK KKKTAKVQSS PPRIPLTTLF PNNNFPEGEI
110 120 130 140 150
VEYLNENSYR TTNEEKRHLD RMNNDFLTEY RQAAEIHRQV RQYAQKELIK
160 170 180 190 200
PGATLTDIAE GIEDGVRHLT GHMGLEEGDS LVAGMGFPTG LNINHCAAHY
210 220 230 240 250
SPNAGNKVVL QHGDVMKVDF GVHINGRIVD SAFTVAFDPV FDPLLTAVKE
260 270 280 290 300
ATNTGIKEAG IDVRMSDIGA AIQETMESYE LELNGTSYPI KAIRNLNGHT
310 320 330 340 350
IGQYEIHGGV NGKSVPIVKG GDQTKMEEGE TYAIETFGST GKGYVRDDME
360 370 380 390 400
TSHYAKVPNA PSVPLRLSSA KNLYSLINKN FGTLPFCRRY LDRLGQEKYL
410 420 430 440
LGLNNLVSSG LVDAYPPLCD VKGSYTAQFE HTILLRPNVK EVISRGDDY
Length:449
Mass (Da):49,232
Last modified:May 3, 2011 - v2
Checksum:i7CB3434189AF910B
GO

Sequence cautioni

The sequence EFE39847.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ACYE01000286 Genomic DNA. Translation: EFE39847.1. Sequence problems.
RefSeqiXP_003020465.1. XM_003020419.1.

Genome annotation databases

GeneIDi9584204.
KEGGitve:TRV_05431.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ACYE01000286 Genomic DNA. Translation: EFE39847.1. Sequence problems.
RefSeqiXP_003020465.1. XM_003020419.1.

3D structure databases

ProteinModelPortaliD4DE65.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi663202.XP_003020465.1.

Protein family/group databases

MEROPSiM24.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi9584204.
KEGGitve:TRV_05431.

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]
PANTHERiPTHR10804:SF9. PTHR10804:SF9. 1 hit.
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: HKI 0517.

Entry informationi

Entry nameiMAP2_TRIVH
AccessioniPrimary (citable) accession number: D4DE65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 3, 2011
Last modified: June 24, 2015
This is version 36 of the entry and version 2 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

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.