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Protein

Methionine aminopeptidase 2-2

Gene

PTRG_04371

Organism
Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus) (Drechslera tritici-repentis)
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:PTRG_04371
OrganismiPyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus) (Drechslera tritici-repentis)
Taxonomic identifieri426418 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePleosporaceaePyrenophora
ProteomesiUP000001471: Unassembled WGS sequence

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_0000407612Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB2W1N6.
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

InParanoidiB2W1N6.
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.

B2W1N6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAKVADDVA NLKLDDSNTK PASGAAENGD KPTGDAEHED SDDDNEAEEG
60 70 80 90 100
APEAGEGAAK KKKKRKPRKK KKAGAAGAGG AKTQTAPPRV RIDEVFPNDS
110 120 130 140 150
YPEGEIQEYV NENAYRTTNE EKRHLDRMNN DFLTEYRKGA EIHREVRQWA
160 170 180 190 200
QKWIKPGMGL TEIAEGIEDS VRALTGHQGL GNGDAQIAGM GFPTGLSINH
210 220 230 240 250
CAAHYTPNAG NKMVVNYEDV MKVDFGVHIN GRIVDSAFTL TFDPVYDNLV
260 270 280 290 300
NACKAATNAG IKEAGIDVRM SDIGAAIQEV MESYEVEIKG EMLPVKCIRN
310 320 330 340 350
LNGHSIGHYT IHGGKTVPIV KGGDQTKMEE GETFAIETFG STGKGYVRDD
360 370 380 390 400
METSHYAMKA DAPKVALRVS SAKTLLNSIT KNFGTLPFCR RYLDRMGHDK
410 420 430 440 450
YLLGLNNLVS AGIVEAYPPL CDIKGSYTAQ SEHTFVLRPT CKEVLSRGDD

Y
Length:451
Mass (Da):49,119
Last modified:July 1, 2008 - v1
Checksum:i282987C3F14707F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS231617 Genomic DNA. Translation: EDU47209.1.
RefSeqiXP_001934704.1. XM_001934669.1.

Genome annotation databases

EnsemblFungiiEDU47209; EDU47209; PTRG_04371.
GeneIDi6342609.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS231617 Genomic DNA. Translation: EDU47209.1.
RefSeqiXP_001934704.1. XM_001934669.1.

3D structure databases

ProteinModelPortaliB2W1N6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEDU47209; EDU47209; PTRG_04371.
GeneIDi6342609.

Phylogenomic databases

InParanoidiB2W1N6.
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. "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-repentis, reveals transduplication and the impact of repeat elements on pathogenicity and population divergence."
    Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B., Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H., Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W., Schwartz D.C., Spatafora J.W.
    , Turgeon B.G., Yandava C., Young S., Zhou S., Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.
    G3 (Bethesda) 3:41-63(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Pt-1C-BFP.

Entry informationi

Entry nameiMAP22_PYRTR
AccessioniPrimary (citable) accession number: B2W1N6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: July 1, 2008
Last modified: January 7, 2015
This is version 41 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.