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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: 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 sitei204 – 2041SubstrateUniRule annotation
Metal bindingi224 – 2241Divalent metal cation 1UniRule annotation
Metal bindingi235 – 2351Divalent metal cation 1UniRule annotation
Metal bindingi235 – 2351Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi304 – 3041Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei312 – 3121SubstrateUniRule annotation
Metal bindingi337 – 3371Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi432 – 4321Divalent metal cation 1UniRule annotation
Metal bindingi432 – 4321Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-HAMAP
  2. metalloaminopeptidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. protein initiator methionine removal Source: UniProtKB-HAMAP
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: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 complex
ProteomesiUP000002668: Whole genome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Methionine aminopeptidase 2-2PRO_0000407607Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliE5R4J3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi60 – 667Poly-Lys
Compositional biasi69 – 724Poly-Lys

Sequence similaritiesi

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

Phylogenomic databases

InParanoidiE5R4J3.
OMAiSTRMEED.
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.

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliE5R4J3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCBX91961; CBX91961; LEMA_P046670.1.
GeneIDi13284777.

Phylogenomic databases

InParanoidiE5R4J3.
OMAiSTRMEED.
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: JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8.

Entry informationi

Entry nameiMAP22_LEPMJ
AccessioniPrimary (citable) accession number: E5R4J3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: February 8, 2011
Last modified: January 7, 2015
This is version 25 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.