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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)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

GO - Biological processi

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
Proteomesi
  • UP000001471 Componenti: Unassembled WGS sequence

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004076121 – 451Methionine aminopeptidase 2-2Add BLAST451

Interactioni

Protein-protein interaction databases

STRINGi426418.XP_001934704.1.

Structurei

3D structure databases

ProteinModelPortaliB2W1N6.
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

eggNOGiKOG2775. Eukaryota.
COG0024. LUCA.
InParanoidiB2W1N6.
OrthoDBiEOG092C3NQP.

Family and domain databases

CDDicd01088. MetAP2. 1 hit.
Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_03175. MetAP_2_euk. 1 hit.
InterProiIPR000994. Pept_M24.
IPR001714. Pept_M24_MAP.
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.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55920. 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...

Protein-protein interaction databases

STRINGi426418.XP_001934704.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEDU47209; EDU47209; PTRG_04371.
GeneIDi6342609.

Phylogenomic databases

eggNOGiKOG2775. Eukaryota.
COG0024. LUCA.
InParanoidiB2W1N6.
OrthoDBiEOG092C3NQP.

Family and domain databases

CDDicd01088. MetAP2. 1 hit.
Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_03175. MetAP_2_euk. 1 hit.
InterProiIPR000994. Pept_M24.
IPR001714. Pept_M24_MAP.
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.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 49 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

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 one 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.