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Protein

Methionine aminopeptidase 2-1

Gene

PTRG_01376

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 sitei210SubstrateUniRule annotation1
Metal bindingi231Divalent metal cation 1UniRule annotation1
Metal bindingi242Divalent metal cation 1UniRule annotation1
Metal bindingi242Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi311Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei319SubstrateUniRule annotation1
Metal bindingi344Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi440Divalent metal cation 1UniRule annotation1
Metal bindingi440Divalent 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 2-1UniRule 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:PTRG_01376
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_00004076341 – 459Methionine aminopeptidase 2-1Add BLAST459

Interactioni

Protein-protein interaction databases

STRINGi426418.XP_001931709.1.

Structurei

3D structure databases

ProteinModelPortaliB2VW14.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2775. Eukaryota.
COG0024. LUCA.
InParanoidiB2VW14.
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]
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.

B2VW14-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSKSPEDHR QGPDGGSADA AVTIINPPKS AAASGLLQGM LEGQDEDGDD
60 70 80 90 100
DDDEKTGINV KTYDGAKKKR KRNKKKSKKV AVIQQTFPPR IPLATLFDNQ
110 120 130 140 150
PYPEGQIVDH VVKDDNIKRT TTEELRHVAA LNDMDDDFLK DYRKAAEVHR
160 170 180 190 200
QVRHHAQTIA KPGVSMTRLA EEIDEGVRAL TGHTGLETGD ALKAGLAFPT
210 220 230 240 250
GLCLNHVGAH WTPNAGAKEV ILKHDDVLKV DFGVHVNGRI VDSAFTVAAN
260 270 280 290 300
PVYDNLLAAV KAATNTGLGE AGIDARIDHI SEAIQEVMES YEVELNGKTI
310 320 330 340 350
PVKAVRNITG HNILRYRIHG DKQVPFVKTK TDQRMEEGDI FAIETFGSTG
360 370 380 390 400
KAHLRDDVGV YGYGRNENMS PAVLHQSSAK SLLKTIDANF GTLVFARRQL
410 420 430 440 450
ERLPGVEKYH LGMRTLVNSG LVESYAPLVD ITGSYIAQFE HTVLLRPNCK

EIISRGDDY
Length:459
Mass (Da):50,250
Last modified:July 1, 2008 - v1
Checksum:i273AECA2B59CE3E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS231615 Genomic DNA. Translation: EDU40814.1.
RefSeqiXP_001931709.1. XM_001931674.1.

Genome annotation databases

EnsemblFungiiEDU40814; EDU40814; PTRG_01376.
GeneIDi6338328.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS231615 Genomic DNA. Translation: EDU40814.1.
RefSeqiXP_001931709.1. XM_001931674.1.

3D structure databases

ProteinModelPortaliB2VW14.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi426418.XP_001931709.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEDU40814; EDU40814; PTRG_01376.
GeneIDi6338328.

Phylogenomic databases

eggNOGiKOG2775. Eukaryota.
COG0024. LUCA.
InParanoidiB2VW14.
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]
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 nameiMAP21_PYRTR
AccessioniPrimary (citable) accession number: B2VW14
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.