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Protein

Methionine aminopeptidase 2-2

Gene

Lema_P046670

Organism
Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8) (Blackleg fungus) (Phoma lingam)
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 sitei204SubstrateUniRule annotation1
Metal bindingi224Divalent metal cation 1UniRule annotation1
Metal bindingi235Divalent metal cation 1UniRule annotation1
Metal bindingi235Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi304Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei312SubstrateUniRule annotation1
Metal bindingi337Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi432Divalent metal cation 1UniRule annotation1
Metal bindingi432Divalent metal cation 2; catalyticUniRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionAminopeptidase, Hydrolase, Protease
LigandMetal-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:Lema_P046670
OrganismiLeptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8) (Blackleg fungus) (Phoma lingam)
Taxonomic identifieri985895 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaeLeptosphaeriaceaeLeptosphaeriaLeptosphaeria maculans species complex
Proteomesi
  • UP000002668 Componenti: Genome

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004076071 – 451Methionine aminopeptidase 2-2Add BLAST451

Proteomic databases

PRIDEiE5R4J3

Interactioni

Protein-protein interaction databases

STRINGi5022.CBX91961

Structurei

3D structure databases

ProteinModelPortaliE5R4J3
SMRiE5R4J3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi60 – 66Poly-Lys7
Compositional biasi69 – 72Poly-Lys4

Sequence similaritiesi

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

Phylogenomic databases

InParanoidiE5R4J3
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.

E5R4J3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQVEDDVA NLKLDDSTTK PTNGTSQPDS KLSAEAEDSD DDAEGDGNGT
60 70 80 90 100
GEAGADGAAK KKKKRKPRKK KKAGTSATAG AKSQTSPPRV LISDLFPNDS
110 120 130 140 150
YPEGEICEYR DENSYRTTNE EKRHLDRMNN DFLTDYRKGA EIHRQVRQWA
160 170 180 190 200
ANWIKPGMTL TEIAEGIEDS VRALTGHQGL EEGDAQKAGM GFPTGLSINH
210 220 230 240 250
CAAHYTPNAG NKVVVNYEDV MKVDFGVHIN GRIVDSAFTK TFDPVYDPLV
260 270 280 290 300
EACKAATNAG IKEAGIDVRM SDIGAAIQEV MESYEVEIGG KMLPVKCIRN
310 320 330 340 350
LNGHSIGHYT IHGGKTVPIV KGSDQTKMEE GETFAIETFG STGKGYVRDD
360 370 380 390 400
METSHYALRP DAPKVALRIS SAKSLLASIT KNFGTLPFCR RYLDRLGHDK
410 420 430 440 450
YLLGLNNLVS SGIVEAYPPL CDIKGSWTAQ SEHTFVLRPT CKEVLSRGDD

Y
Length:451
Mass (Da):49,158
Last modified:February 8, 2011 - v1
Checksum:i08407BBF6A063CA3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FP929083 Genomic DNA Translation: CBX91961.1
RefSeqiXP_003835326.1, XM_003835278.1

Genome annotation databases

EnsemblFungiiCBX91961; CBX91961; LEMA_P046670.1
GeneIDi13284777

Similar proteinsi

Entry informationi

Entry nameiMAP22_LEPMJ
AccessioniPrimary (citable) accession number: E5R4J3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: February 8, 2011
Last modified: May 23, 2018
This is version 42 of the entry and version 1 of the sequence. See 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

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