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Protein

Methionine aminopeptidase 2-1

Gene

MGYG_01664

Organism
Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum gypseum)
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 sitei219 – 2191SubstrateUniRule annotation
Metal bindingi240 – 2401Divalent metal cation 1UniRule annotation
Metal bindingi251 – 2511Divalent metal cation 1UniRule annotation
Metal bindingi251 – 2511Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi320 – 3201Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei328 – 3281SubstrateUniRule annotation
Metal bindingi353 – 3531Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi448 – 4481Divalent metal cation 1UniRule annotation
Metal bindingi448 – 4481Divalent 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 2-1UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2-1UniRule annotation
Short name:
MetAP 2-1UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
ORF Names:MGYG_01664
OrganismiArthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum gypseum)
Taxonomic identifieri535722 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaeMicrosporum
ProteomesiUP000002669 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 – 467467Methionine aminopeptidase 2-1PRO_0000407618Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi535722.XP_003177594.1.

Structurei

3D structure databases

ProteinModelPortaliE5R278.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi83 – 886Poly-Lys

Sequence similaritiesi

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

Phylogenomic databases

InParanoidiE5R278.
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.

E5R278-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSKSPDGHR QGPNAESPSS SVAATTNPPK PAAASGLVQG MLDGDDEDED
60 70 80 90 100
GDDDGDNQRI GADLKSGVLP NNDGKKRKRK SNKKKKKKTS KGQQTTPPRV
110 120 130 140 150
SLPSIFHDQR YPEGEIVEYA ARNDNLQRTT AEELRHQAAI HNMDDEFLTD
160 170 180 190 200
YRQAAEVHRQ VRQYVQSIAK PGILMSELAE EIETGVRALT GHQGIETGDA
210 220 230 240 250
LKAGLAFPTG LCLNNVAAHW TPNPGAKEVI LKHDDVLKID FGVHVNGRIV
260 270 280 290 300
DSAFTVASNP VYDNLLTAVK AATNTGLKEA GIDARIDHIS GEIQEVMESY
310 320 330 340 350
EVEINGKAIP VKALRSLTGH NILRYKIHGE KQVPFVKSKT TQRMEEGDVF
360 370 380 390 400
AIETFGSTGK GYTRDEVGVY GYGLNEHAST AGLHHASAKS LLKTIRENFG
410 420 430 440 450
TLVFSRRYLE HMGVKNYHLG MRSLISNDIV ECYAPLVDVP GSYVAQFEHT
460
VLLRPNCKEI ISRGDDY
Length:467
Mass (Da):51,146
Last modified:February 8, 2011 - v1
Checksum:iFF54B66A7F399579
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS989822 Genomic DNA. Translation: EFQ98642.1.
RefSeqiXP_003177594.1. XM_003177546.1.

Genome annotation databases

GeneIDi10032929.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS989822 Genomic DNA. Translation: EFQ98642.1.
RefSeqiXP_003177594.1. XM_003177546.1.

3D structure databases

ProteinModelPortaliE5R278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi535722.XP_003177594.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi10032929.

Phylogenomic databases

InParanoidiE5R278.
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: ATCC MYA-4604 / CBS 118893.

Entry informationi

Entry nameiMAP21_ARTGP
AccessioniPrimary (citable) accession number: E5R278
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: February 8, 2011
Last modified: June 24, 2015
This is version 27 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.