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A6RTU0

- MAP2_BOTFB

UniProt

A6RTU0 - MAP2_BOTFB

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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: 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 Fe(2+)-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

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

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

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

Interactioni

Protein-protein interaction databases

STRINGi332648.A6RTU0.

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.
OMAiIQICEEL.

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 .
RefSeqi XP_001557579.1. XM_001557529.1.

3D structure databases

ProteinModelPortali A6RTU0.
SMRi A6RTU0. Positions 79-448.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 332648.A6RTU0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5438178.
KEGGi bfu:BC1G_04189.

Phylogenomic databases

eggNOGi COG0024.
KOi K01265.
OMAi IQICEEL.

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: 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: November 26, 2014
This is version 52 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