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Protein

Methionine aminopeptidase 2-2

Gene

PTT_01727

Organism
Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus) (Drechslera teres f. teres)
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 sitei210 – 2101SubstrateUniRule annotation
Metal bindingi231 – 2311Divalent metal cation 1UniRule annotation
Metal bindingi242 – 2421Divalent metal cation 1UniRule annotation
Metal bindingi242 – 2421Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi311 – 3111Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei319 – 3191SubstrateUniRule annotation
Metal bindingi344 – 3441Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi440 – 4401Divalent metal cation 1UniRule annotation
Metal bindingi440 – 4401Divalent 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:PTT_01727
OrganismiPyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus) (Drechslera teres f. teres)
Taxonomic identifieri861557 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePleosporaceaePyrenophora
ProteomesiUP000001067 Componenti: Unassembled WGS sequence

Subcellular locationi

  1. 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 – 459459Methionine aminopeptidase 2-2PRO_0000407635Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliE3RD74.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

KOiK01265.
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]
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.

E3RD74-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSKSPEDHR QGPDGGSADT AIAIVNPPKS AAASGLLQGM LEGQDEDGDD
60 70 80 90 100
DDDEKTGIDL KTNDGAKKKR KRNKKKSKKL SVVQQTSPPR VPLATLFDNQ
110 120 130 140 150
PYPEGQIVDY NVKDDNLQRT TAEELRHLAA VRDMDDDFLK DYRKAAEVHR
160 170 180 190 200
QVRRYAQAIA KPGVSMTRLA EEIDDGVRAL TGHEGLETGD ALKAGLAFPT
210 220 230 240 250
GLCLNHVGAH WTPNAGAKDV ILKHDDVLKV DFGVHVNGRI VDSAFTVAAN
260 270 280 290 300
PVYDNLLAAV KAATNTGLEE AGIDARIDHI SEAIQEVMES YEVELNGKTI
310 320 330 340 350
PIKAVRNITG HNILRYRIHG DKQVPFVKTK TDQRMEEGDI FAIETFGSTG
360 370 380 390 400
KAYLQDDVGV YGYGRNENMN PAVLHQSSAK SLLKTIDANF GTLVFARRQL
410 420 430 440 450
ERLPGVEKYH LGMRTLVNSG LVESYAPLVD IPGSYIAQFE HTVLLRPNCK

EIISRGEDY
Length:459
Mass (Da):50,347
Last modified:January 11, 2011 - v1
Checksum:iA1359C15ED0D28A5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GL532027 Genomic DNA. Translation: EFQ96321.1.
RefSeqiXP_003295579.1. XM_003295531.1.

Genome annotation databases

EnsemblFungiiEFQ96321; EFQ96321; PTT_01727.
GeneIDi10514965.
KEGGipte:PTT_01727.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GL532027 Genomic DNA. Translation: EFQ96321.1.
RefSeqiXP_003295579.1. XM_003295531.1.

3D structure databases

ProteinModelPortaliE3RD74.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFQ96321; EFQ96321; PTT_01727.
GeneIDi10514965.
KEGGipte:PTT_01727.

Phylogenomic databases

KOiK01265.
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]
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. "A first genome assembly of the barley fungal pathogen Pyrenophora teres f. teres."
    Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S., Oliver R.P., Friesen T.L.
    Genome Biol. 11:R109.1-R109.14(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 0-1.

Entry informationi

Entry nameiMAP22_PYRTT
AccessioniPrimary (citable) accession number: E3RD74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: January 11, 2011
Last modified: January 7, 2015
This is version 27 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.