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Q0UTI9

- MAP2_PHANO

UniProt

Q0UTI9 - MAP2_PHANO

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Protein
Methionine aminopeptidase 2
Gene
SNOG_04925
Organism
Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Septoria nodorum)
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 sitei199 – 1991Substrate By similarity
Metal bindingi219 – 2191Divalent metal cation 1 By similarity
Metal bindingi230 – 2301Divalent metal cation 1 By similarity
Metal bindingi230 – 2301Divalent metal cation 2; catalytic By similarity
Metal bindingi299 – 2991Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei307 – 3071Substrate By similarity
Metal bindingi332 – 3321Divalent metal cation 2; catalytic By similarity
Metal bindingi427 – 4271Divalent metal cation 1 By similarity
Metal bindingi427 – 4271Divalent 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 involved in protein maturation Source: EnsemblFungi
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2 (EC:3.4.11.18)
Short name:
MAP 2
Short name:
MetAP 2
Alternative name(s):
Peptidase M
Gene namesi
ORF Names:SNOG_04925
OrganismiPhaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Septoria nodorum)
Taxonomic identifieri321614 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePhaeosphaeriaceaeParastagonospora
ProteomesiUP000001055: 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 – 435435Methionine aminopeptidase 2UniRule annotation
PRO_0000407662Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ0UTI9.
SMRiQ0UTI9. Positions 77-430.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi55 – 617Poly-LysUniRule annotation
Compositional biasi64 – 674Poly-LysUniRule annotation

Sequence similaritiesi

Phylogenomic databases

KOiK01265.
OMAiIQICEEL.
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.

Q0UTI9-1 [UniParc]FASTAAdd to Basket

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MAAQVADGVA DLKLDDTKSK PTNGTTQNGD AEHEDSDDDN EGEEGAAEGG    50
EGAAKKKKKR KPRKKKKAGA AGASGPKTQT KPPRVPVHEI FLNDSYPEGE 100
IHEYLNENSY RTTSEEKRHL DRMNNDFLTD YRRGAEIHRT VRQWARDWIK 150
PGMSLTEIAE GIEDSVRALT GHQGLEDGDA QIAGMGFPTG LSINHCAAHY 200
TPNAGNKMVV NYEDVMKVDF GVHINGRIVD SAFTLTFDPV YDNLVEACKA 250
ATNAGIKEAG IDVRMSDIGA AIQEVMESYE VEIKGETFPV KCIRNLNGHS 300
IGHYTIHGGK TVPIVKGGDQ TKMEEGETFA IETFGSTGKG YVRDDMETSH 350
YAKRSDAPKV ALRVSSAKTL LNSITKNFGT LPFCRRYLDR LGHDKYLLGL 400
NNLVSAGIVE AYPPLCDIKG SYTAQSEHVS FFPSV 435
Length:435
Mass (Da):47,572
Last modified:September 5, 2006 - v1
Checksum:i769B7666F52B14E4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH445331 Genomic DNA. Translation: EAT87316.1.
RefSeqiXP_001795338.1. XM_001795286.1.

Genome annotation databases

EnsemblFungiiSNOT_04925; SNOT_04925; SNOG_04925.
GeneIDi5972213.
KEGGipno:SNOG_04925.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH445331 Genomic DNA. Translation: EAT87316.1 .
RefSeqi XP_001795338.1. XM_001795286.1.

3D structure databases

ProteinModelPortali Q0UTI9.
SMRi Q0UTI9. Positions 77-430.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SNOT_04925 ; SNOT_04925 ; SNOG_04925 .
GeneIDi 5972213.
KEGGi pno:SNOG_04925.

Phylogenomic databases

KOi K01265.
OMAi IQICEEL.
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. "Dothideomycete-plant interactions illuminated by genome sequencing and EST analysis of the wheat pathogen Stagonospora nodorum."
    Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L., Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E., Torriani S.F.F., McDonald B.A., Oliver R.P.
    Plant Cell 19:3347-3368(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SN15 / ATCC MYA-4574 / FGSC 10173.

Entry informationi

Entry nameiMAP2_PHANO
AccessioniPrimary (citable) accession number: Q0UTI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: September 5, 2006
Last modified: May 14, 2014
This is version 56 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

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