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A7EZ86

- MAP2_SCLS1

UniProt

A7EZ86 - MAP2_SCLS1

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Protein
Methionine aminopeptidase 2
Gene
SS1G_10653
Organism
Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)
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 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
Complete GO annotation...

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 (EC:3.4.11.18)
Short name:
MAP 2
Short name:
MetAP 2
Alternative name(s):
Peptidase M
Gene namesi
ORF Names:SS1G_10653
OrganismiSclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)
Taxonomic identifieri665079 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeSclerotinia
ProteomesiUP000001312: 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 – 446446Methionine aminopeptidase 2UniRule annotation
PRO_0000407668Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi665079.A7EZ86.

Structurei

3D structure databases

ProteinModelPortaliA7EZ86.
SMRiA7EZ86. Positions 77-446.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
KOiK01265.
OMAiPVGECHD.
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.
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.

Sequencei

Sequence statusi: Complete.

A7EZ86-1 [UniParc]FASTAAdd to Basket

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MAAQVTDALK NLKVKDPNSV IESAAEAKSN GNTQAEAEDS DDEEEEPVNG    50
EGAGEGGAKK KRKRKKKPKK KAGANPKVQS SPPRVLLSNL FPSGEYPVGE 100
EVEYRDENNY RTTSEEKRYL DRMNNDFLQE YRQAAEIHRQ VRQYAKANIK 150
PGQTLTEIAE GIEDSVRALT GHPGLEEGDN IKGGVAFPTG VNLDHIAAHY 200
SPNAGNKTVL AYENVMKVDF GVHVNGRIVD SAFTIAFDPM YDNLLEAVKQ 250
ATNTGIKEAG IDARLGEIGE HIQETMESYE VEIKGQTYQV KPIRNLNGHD 300
ILQWKIHGGK SVPIVKSNDQ TKMEEGEVFA IETFGSTGNG YVRDDLECSH 350
YAKVADAPNV PLRIASAGKL LNVINKNFGT LPFCRRYLDR LGQDKYLLGL 400
NALVSHGIVQ DYPPLVDKKG SYTAQFEHTI VLRPNCKEVI SRGDDY 446
Length:446
Mass (Da):49,260
Last modified:September 11, 2007 - v1
Checksum:i0BC45FC3D04A2AF2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH476636 Genomic DNA. Translation: EDN94778.1.
RefSeqiXP_001588206.1. XM_001588156.1.

Genome annotation databases

GeneIDi5484447.
KEGGissl:SS1G_10653.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH476636 Genomic DNA. Translation: EDN94778.1 .
RefSeqi XP_001588206.1. XM_001588156.1.

3D structure databases

ProteinModelPortali A7EZ86.
SMRi A7EZ86. Positions 77-446.
ModBasei Search...

Protein-protein interaction databases

STRINGi 665079.A7EZ86.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5484447.
KEGGi ssl:SS1G_10653.

Phylogenomic databases

eggNOGi COG0024.
KOi K01265.
OMAi PVGECHD.
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.
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.
ProtoNeti Search...

Publicationsi

  1. "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia sclerotiorum and Botrytis cinerea."
    Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., Quevillon E.
    , Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.
    PLoS Genet. 7:E1002230-E1002230(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 18683 / 1980 / Ss-1.

Entry informationi

Entry nameiMAP2_SCLS1
AccessioniPrimary (citable) accession number: A7EZ86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: September 11, 2007
Last modified: May 14, 2014
This is version 44 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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