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Protein

Methionine aminopeptidase 2-2

Gene

MCYG_01318

Organism
Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis)
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 sitei197SubstrateUniRule annotation1
Metal bindingi217Divalent metal cation 1UniRule annotation1
Metal bindingi228Divalent metal cation 1UniRule annotation1
Metal bindingi228Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi297Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei305SubstrateUniRule annotation1
Metal bindingi333Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi428Divalent metal cation 1UniRule annotation1
Metal bindingi428Divalent 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:MCYG_01318
OrganismiArthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis)
Taxonomic identifieri554155 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaeArthroderma
Proteomesi
  • UP000002035 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_00004075971 – 447Methionine aminopeptidase 2-2Add BLAST447

Interactioni

Protein-protein interaction databases

STRINGi554155.XP_002851214.1.

Structurei

3D structure databases

ProteinModelPortaliC5FF46.
SMRiC5FF46.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi59 – 74Lys-richAdd BLAST16

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

C5FF46-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQTAPELA KLDLNKNSGS AEANVVSNGG SDKDDAENEG DSDDDKDEAG
60 70 80 90 100
GSAEVNTEKK KKKKRSKKKK KAAKVQSSPP RIPLTTLFPN NAFPEGEIVE
110 120 130 140 150
YLNDNSYRTT NEEKRHLDRM NNDFLTEYRQ AAEIHRQVRQ YAQKELIKPG
160 170 180 190 200
ATLTDIAEGI EDGVRHLTGH MGLEEGDSLI AGMGFPTGLN INHCAAHYSP
210 220 230 240 250
NAGNKVVLQH GDVMKVDFGV HVNGRIVDSA FTVAFDPVFD PLLTAVKEAT
260 270 280 290 300
NTGIKEAGID VRMSDIGAAI QETMESYELE INGTSYPIKA VRNLNGHTIG
310 320 330 340 350
QYEIHGGVNG KSVPIVKGGD QTKMEEGETY AIETFGSTGK GYVRDDMETS
360 370 380 390 400
HYAKVPNAPS VPLRLSSAKN LYSLINKNFG TLPFCRRYLD RLGQEKYLLG
410 420 430 440
LNNLVSSGLV DAYPPLCDVK GSYTAQFEHT ILLRPNVKEV ISRGDDY
Length:447
Mass (Da):48,883
Last modified:July 28, 2009 - v1
Checksum:i4C2792252B598045
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS995701 Genomic DNA. Translation: EEQ28430.1.
RefSeqiXP_002851214.1. XM_002851168.1.

Genome annotation databases

EnsemblFungiiEEQ28430; EEQ28430; MCYG_01318.
GeneIDi9228835.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS995701 Genomic DNA. Translation: EEQ28430.1.
RefSeqiXP_002851214.1. XM_002851168.1.

3D structure databases

ProteinModelPortaliC5FF46.
SMRiC5FF46.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi554155.XP_002851214.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEEQ28430; EEQ28430; MCYG_01318.
GeneIDi9228835.

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]
PANTHERiPTHR10804:SF9. PTHR10804:SF9. 1 hit.
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_ARTOC
AccessioniPrimary (citable) accession number: C5FF46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: July 28, 2009
Last modified: November 30, 2016
This is version 47 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

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.