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Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii)
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 sitei210SubstrateUniRule annotation1
Metal bindingi230Divalent metal cation 1UniRule annotation1
Metal bindingi241Divalent metal cation 1UniRule annotation1
Metal bindingi241Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi312Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei320SubstrateUniRule annotation1
Metal bindingi345Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi440Divalent metal cation 1UniRule annotation1
Metal bindingi440Divalent metal cation 2; catalyticUniRule annotation1

GO - Molecular functioni

GO - Biological processi

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
Name:MAP2UniRule annotation
ORF Names:PGUG_05790
OrganismiMeyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii)
Taxonomic identifieri294746 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeMeyerozyma
Proteomesi
  • UP000001997 Componenti: Unassembled WGS sequence

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004076631 – 459Methionine aminopeptidase 2Add BLAST459

Interactioni

Protein-protein interaction databases

STRINGi4929.A5DR89

Structurei

3D structure databases

ProteinModelPortaliA5DR89
SMRiA5DR89
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi89 – 98Poly-Lys10

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2775 Eukaryota
COG0024 LUCA
InParanoidiA5DR89
KOiK01265
OMAiTINKHFG
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.

A5DR89-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKTRTNSET VSILHTLHTN QKAPGARVYR VFRFSHHPKM RSNMSQDKEA
60 70 80 90 100
NEIAVNTTET VVSTPTDVTT AETKTDGSPE TNAAPAAAKK KKNKKKKKIT
110 120 130 140 150
SIDSSYPDGV FPEGEWQEYP LEINSYRTSS EELRYLDNQR NNHWQDFRKG
160 170 180 190 200
AEIHRRVRHK AQSSIRPGMT MTEIADLIEN SVRSYAAADH TLKAGIGFPT
210 220 230 240 250
GLSLNEIAAH YTPNAGDKLV LGKDDVMKVD IGVHVNGHIV DSAFTMTFDD
260 270 280 290 300
DHKYDNLLKA VKEATNTGVR EAGIDVRLND IGAAVQEVME SYEMEIGGKT
310 320 330 340 350
YPIKCIRNLN GHNIGDYVIH SGKTVPIVAN GDMTKMEEGE TFAIETFGST
360 370 380 390 400
GNGYVIPTGE CSHYALSEEY KQARVGTDRA KQLLKTIESN FGTLPWCRRY
410 420 430 440 450
LDRVGEEKYL LALNQLVRAG AVQDYPPITD RAGSYTAQFE HTILLHPHKK

EVVSRGDDY
Length:459
Mass (Da):51,166
Last modified:July 22, 2008 - v2
Checksum:iBD5FDC3013D74BC1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH408162 Genomic DNA Translation: EDK41692.2
RefSeqiXP_001482027.1, XM_001481977.1

Genome annotation databases

EnsemblFungiiEDK41692; EDK41692; PGUG_05790
GeneIDi5123876
KEGGipgu:PGUG_05790

Entry informationi

Entry nameiMAP2_PICGU
AccessioniPrimary (citable) accession number: A5DR89
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: July 22, 2008
Last modified: March 28, 2018
This is version 67 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health