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B2VW14

- MAP21_PYRTR

UniProt

B2VW14 - MAP21_PYRTR

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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: 2 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) By similarity.UniRule annotation

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation

Cofactori

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 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei210 – 2101Substrate By similarity
Metal bindingi231 – 2311Divalent metal cation 1 By similarity
Metal bindingi242 – 2421Divalent metal cation 1 By similarity
Metal bindingi242 – 2421Divalent metal cation 2; catalytic By similarity
Metal bindingi311 – 3111Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei319 – 3191Substrate By similarity
Metal bindingi344 – 3441Divalent metal cation 2; catalytic By similarity
Metal bindingi440 – 4401Divalent metal cation 1 By similarity
Metal bindingi440 – 4401Divalent metal cation 2; catalytic By similarity

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 2-1 (EC:3.4.11.18)
Short name:
MAP 2-1
Short name:
MetAP 2-1
Alternative name(s):
Peptidase M
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
ProteomesiUP000001471: Unassembled WGS sequence

Subcellular locationi

Cytoplasm By similarity 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 2-1UniRule annotationPRO_0000407634Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB2VW14.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

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.

B2VW14-1 [UniParc]FASTAAdd to Basket

« Hide

MGSKSPEDHR QGPDGGSADA AVTIINPPKS AAASGLLQGM LEGQDEDGDD    50
DDDEKTGINV KTYDGAKKKR KRNKKKSKKV AVIQQTFPPR IPLATLFDNQ 100
PYPEGQIVDH VVKDDNIKRT TTEELRHVAA LNDMDDDFLK DYRKAAEVHR 150
QVRHHAQTIA KPGVSMTRLA EEIDEGVRAL TGHTGLETGD ALKAGLAFPT 200
GLCLNHVGAH WTPNAGAKEV ILKHDDVLKV DFGVHVNGRI VDSAFTVAAN 250
PVYDNLLAAV KAATNTGLGE AGIDARIDHI SEAIQEVMES YEVELNGKTI 300
PVKAVRNITG HNILRYRIHG DKQVPFVKTK TDQRMEEGDI FAIETFGSTG 350
KAHLRDDVGV YGYGRNENMS PAVLHQSSAK SLLKTIDANF GTLVFARRQL 400
ERLPGVEKYH LGMRTLVNSG LVESYAPLVD ITGSYIAQFE HTVLLRPNCK 450
EIISRGDDY 459
Length:459
Mass (Da):50,250
Last modified:July 1, 2008 - v1
Checksum:i273AECA2B59CE3E8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
DS231615 Genomic DNA. Translation: EDU40814.1 .
RefSeqi XP_001931709.1. XM_001931674.1.

3D structure databases

ProteinModelPortali B2VW14.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii EDU40814 ; EDU40814 ; PTRG_01376 .
GeneIDi 6338328.

Phylogenomic databases

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 IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SUPFAMi SSF55920. SSF55920. 2 hits.
TIGRFAMsi TIGR00501. met_pdase_II. 1 hit.
PROSITEi PS01202. MAP_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 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: June 11, 2014
This is version 38 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

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

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