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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: 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei199 – 1991SubstrateUniRule annotation
Metal bindingi219 – 2191Divalent metal cation 1UniRule annotation
Metal bindingi230 – 2301Divalent metal cation 1UniRule annotation
Metal bindingi230 – 2301Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi299 – 2991Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei307 – 3071SubstrateUniRule annotation
Metal bindingi332 – 3321Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi427 – 4271Divalent metal cation 1UniRule annotation
Metal bindingi427 – 4271Divalent metal cation 2; catalyticUniRule annotation

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 2UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2UniRule annotation
Short name:
MetAP 2UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
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 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 2PRO_0000407668Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi665079.A7EZ86.

Structurei

3D structure databases

ProteinModelPortaliA7EZ86.
SMRiA7EZ86. Positions 77-446.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
InParanoidiA7EZ86.
KOiK01265.
OMAiSTRMEED.
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

« Hide

        10         20         30         40         50
MAAQVTDALK NLKVKDPNSV IESAAEAKSN GNTQAEAEDS DDEEEEPVNG
60 70 80 90 100
EGAGEGGAKK KRKRKKKPKK KAGANPKVQS SPPRVLLSNL FPSGEYPVGE
110 120 130 140 150
EVEYRDENNY RTTSEEKRYL DRMNNDFLQE YRQAAEIHRQ VRQYAKANIK
160 170 180 190 200
PGQTLTEIAE GIEDSVRALT GHPGLEEGDN IKGGVAFPTG VNLDHIAAHY
210 220 230 240 250
SPNAGNKTVL AYENVMKVDF GVHVNGRIVD SAFTIAFDPM YDNLLEAVKQ
260 270 280 290 300
ATNTGIKEAG IDARLGEIGE HIQETMESYE VEIKGQTYQV KPIRNLNGHD
310 320 330 340 350
ILQWKIHGGK SVPIVKSNDQ TKMEEGEVFA IETFGSTGNG YVRDDLECSH
360 370 380 390 400
YAKVADAPNV PLRIASAGKL LNVINKNFGT LPFCRRYLDR LGQDKYLLGL
410 420 430 440
NALVSHGIVQ DYPPLVDKKG SYTAQFEHTI VLRPNCKEVI SRGDDY
Length:446
Mass (Da):49,260
Last modified:September 11, 2007 - v1
Checksum:i0BC45FC3D04A2AF2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
CH476636 Genomic DNA. Translation: EDN94778.1.
RefSeqiXP_001588206.1. XM_001588156.1.

3D structure databases

ProteinModelPortaliA7EZ86.
SMRiA7EZ86. Positions 77-446.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi665079.A7EZ86.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5484447.
KEGGissl:SS1G_10653.

Phylogenomic databases

eggNOGiCOG0024.
InParanoidiA7EZ86.
KOiK01265.
OMAiSTRMEED.
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.
ProtoNetiSearch...

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: January 7, 2015
This is version 48 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

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 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.