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E4ZYY3

- MAP21_LEPMJ

UniProt

E4ZYY3 - MAP21_LEPMJ

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Protein

Methionine aminopeptidase 2-1

Gene

Lema_P106830

Organism
Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8) (Blackleg fungus) (Phoma lingam)
Status
Reviewed - 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 Fe(2+)-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 sitei212 – 2121SubstrateUniRule annotation
Metal bindingi233 – 2331Divalent metal cation 1UniRule annotation
Metal bindingi244 – 2441Divalent metal cation 1UniRule annotation
Metal bindingi244 – 2441Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi313 – 3131Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei321 – 3211SubstrateUniRule annotation
Metal bindingi346 – 3461Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi441 – 4411Divalent metal cation 1UniRule annotation
Metal bindingi441 – 4411Divalent 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 2-1UniRule 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:Lema_P106830
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-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 460460Methionine aminopeptidase 2-1PRO_0000407629Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliE4ZYY3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi77 – 804Poly-Lys

Sequence similaritiesi

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

Phylogenomic databases

InParanoidiE4ZYY3.
OMAiHISECIQ.
OrthoDBiEOG7BGHW3.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_03175. MetAP_2_euk.
InterProiIPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
SUPFAMiSSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.

Sequencei

Sequence statusi: Complete.

E4ZYY3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSKSPNGED RGPNGPSAKK AVASINPPKS AAASGLLRGA LEDQDEDGDD
60 70 80 90 100
DEGKIGADMN VSEKTANGTK KRRRNNKKKK SAQAAQQTAP PRVEIATLFH
110 120 130 140 150
NRPYPEGEIV EYGINDENLV RTTDEEFRHL AVANNMNDEF LRDYRKAAEV
160 170 180 190 200
HRQVRQYAQT IAKPGISMTE LAREIEDGVR ALVGHQGIET GDSLKAGMGF
210 220 230 240 250
PTGLCINNVA AHWTPNPGAR EVVLQHDDVL SIDFGVHVNG RIVDSAFTVA
260 270 280 290 300
FNPMYDKLLT AVKAATNTGL KESGIDARMD YISETIQEVM ESYEVMINGK
310 320 330 340 350
PLPVKALSSL SGHNILRYKI HGDKQVPFVK TRTSQRMEEG DVFAIETFGS
360 370 380 390 400
TGIGRTRDDV GVYGYSRNEN VSTAGVHLAS AKSLLKAIDE NFGTLPFSRN
410 420 430 440 450
YLERIGVKNY HLGMRSLIAS GVVECYAPLV DTPGSYVAQF EHTVLLRPNC
460
KEIISRGDDY
Length:460
Mass (Da):50,338
Last modified:February 8, 2011 - v1
Checksum:iAE89CA76466A9747
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FP929129 Genomic DNA. Translation: CBX96418.1.
RefSeqiXP_003839897.1. XM_003839849.1.

Genome annotation databases

EnsemblFungiiCBX96418; CBX96418; LEMA_P106830.1.
GeneIDi13283230.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FP929129 Genomic DNA. Translation: CBX96418.1 .
RefSeqi XP_003839897.1. XM_003839849.1.

3D structure databases

ProteinModelPortali E4ZYY3.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CBX96418 ; CBX96418 ; LEMA_P106830.1 .
GeneIDi 13283230.

Phylogenomic databases

InParanoidi E4ZYY3.
OMAi HISECIQ.
OrthoDBi EOG7BGHW3.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPi MF_03175. MetAP_2_euk.
InterProi IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
SUPFAMi SSF55920. SSF55920. 2 hits.
TIGRFAMsi TIGR00501. met_pdase_II. 1 hit.
ProtoNeti Search...

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 nameiMAP21_LEPMJ
AccessioniPrimary (citable) accession number: E4ZYY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: February 8, 2011
Last modified: November 26, 2014
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