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Protein

Methionine aminopeptidase 2

Gene

BC1G_04189

Organism
Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
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 sitei201 – 2011SubstrateUniRule annotation
Metal bindingi221 – 2211Divalent metal cation 1UniRule annotation
Metal bindingi232 – 2321Divalent metal cation 1UniRule annotation
Metal bindingi232 – 2321Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi301 – 3011Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei309 – 3091SubstrateUniRule annotation
Metal bindingi334 – 3341Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi429 – 4291Divalent metal cation 1UniRule annotation
Metal bindingi429 – 4291Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

GO - Biological processi

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:BC1G_04189
OrganismiBotryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
Taxonomic identifieri332648 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeBotrytis

Organism-specific databases

EuPathDBiFungiDB:BC1G_04189.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Methionine aminopeptidase 2PRO_0000407644Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliA6RTU0.
SMRiA6RTU0. Positions 79-448.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
KOiK01265.
OMAiWCRRYLE.

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.

A6RTU0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQVTDALK NLKVKDPNAV VESAAEAKAN GNAQPEAEAE DSDDDDEEPV
60 70 80 90 100
NGEGAGEGGA KKKRKRKKKP KKKAGANPKV QSSPPRVLLS NLFPSGEYPV
110 120 130 140 150
GEEVEYRDEN NYRTTSEEKR YLDRMNNDFL QEYRQGAEIH RQVRQYAKAN
160 170 180 190 200
IKPGQTLTEI AEGIEDSVRA LTGHPGLEEG DNIKGGVAFP TGVNLDHIAA
210 220 230 240 250
HYSPNAGNKT VLAYENVMKV DFGVHINGRI VDSAFTIAFD PMYDNLLEAV
260 270 280 290 300
KQATNTGIKE AGIDARLGEI GEHIQETMES YEVEIKGQTY QVKPIRNLNG
310 320 330 340 350
HDILQWKIHG GKSVPIVKSN DQTKMEEGEV FAIETFGSTG NGYVRDDLEC
360 370 380 390 400
SHYAKVADAP NVPLRIASAG KLLNVINKNF GTLPFCRRYL DRLGQDKYLL
410 420 430 440
GLNALVSHGI VQDYPPLVDK KGSYTAQFEH TIVLRPNCKE VISRGDDY
Length:448
Mass (Da):49,382
Last modified:August 21, 2007 - v1
Checksum:iBAE7123D8B732BAB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476856 Genomic DNA. Translation: EDN21182.1.
RefSeqiXP_001557579.1. XM_001557529.1.

Genome annotation databases

GeneIDi5438178.
KEGGibfu:BC1G_04189.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476856 Genomic DNA. Translation: EDN21182.1.
RefSeqiXP_001557579.1. XM_001557529.1.

3D structure databases

ProteinModelPortaliA6RTU0.
SMRiA6RTU0. Positions 79-448.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5438178.
KEGGibfu:BC1G_04189.

Organism-specific databases

EuPathDBiFungiDB:BC1G_04189.

Phylogenomic databases

eggNOGiCOG0024.
KOiK01265.
OMAiWCRRYLE.

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: B05.10.

Entry informationi

Entry nameiMAP2_BOTFB
AccessioniPrimary (citable) accession number: A6RTU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: August 21, 2007
Last modified: July 22, 2015
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

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.