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B2W1N6

- MAP22_PYRTR

UniProt

B2W1N6 - MAP22_PYRTR

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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: 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) 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 sitei204 – 2041Substrate By similarity
Metal bindingi224 – 2241Divalent metal cation 1 By similarity
Metal bindingi235 – 2351Divalent metal cation 1 By similarity
Metal bindingi235 – 2351Divalent metal cation 2; catalytic By similarity
Metal bindingi304 – 3041Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei312 – 3121Substrate By similarity
Metal bindingi337 – 3371Divalent metal cation 2; catalytic By similarity
Metal bindingi432 – 4321Divalent metal cation 1 By similarity
Metal bindingi432 – 4321Divalent 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 2-2 (EC:3.4.11.18)
Short name:
MAP 2-2
Short name:
MetAP 2-2
Alternative name(s):
Peptidase M
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 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 – 451451Methionine aminopeptidase 2-2UniRule annotationPRO_0000407612Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB2W1N6.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi60 – 667Poly-LysUniRule annotation
Compositional biasi69 – 724Poly-LysUniRule annotation

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]
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

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MAAKVADDVA NLKLDDSNTK PASGAAENGD KPTGDAEHED SDDDNEAEEG    50
APEAGEGAAK KKKKRKPRKK KKAGAAGAGG AKTQTAPPRV RIDEVFPNDS 100
YPEGEIQEYV NENAYRTTNE EKRHLDRMNN DFLTEYRKGA EIHREVRQWA 150
QKWIKPGMGL TEIAEGIEDS VRALTGHQGL GNGDAQIAGM GFPTGLSINH 200
CAAHYTPNAG NKMVVNYEDV MKVDFGVHIN GRIVDSAFTL TFDPVYDNLV 250
NACKAATNAG IKEAGIDVRM SDIGAAIQEV MESYEVEIKG EMLPVKCIRN 300
LNGHSIGHYT IHGGKTVPIV KGGDQTKMEE GETFAIETFG STGKGYVRDD 350
METSHYAMKA DAPKVALRVS SAKTLLNSIT KNFGTLPFCR RYLDRMGHDK 400
YLLGLNNLVS AGIVEAYPPL CDIKGSYTAQ SEHTFVLRPT CKEVLSRGDD 450
Y 451
Length:451
Mass (Da):49,119
Last modified:July 1, 2008 - v1
Checksum:i282987C3F14707F5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
DS231617 Genomic DNA. Translation: EDU47209.1 .
RefSeqi XP_001934704.1. XM_001934669.1.

3D structure databases

ProteinModelPortali B2W1N6.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii EDU47209 ; EDU47209 ; PTRG_04371 .
GeneIDi 6342609.

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 ]
PANTHERi PTHR10804:SF9. PTHR10804:SF9. 1 hit.
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 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: May 14, 2014
This is version 37 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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