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B8NLL0

- MAP22_ASPFN

UniProt

B8NLL0 - MAP22_ASPFN

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Protein
Methionine aminopeptidase 2-2
Gene
AFLA_092260
Organism
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
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 sitei219 – 2191Substrate By similarity
Metal bindingi240 – 2401Divalent metal cation 1 By similarity
Metal bindingi251 – 2511Divalent metal cation 1 By similarity
Metal bindingi251 – 2511Divalent metal cation 2; catalytic By similarity
Metal bindingi320 – 3201Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei328 – 3281Substrate By similarity
Metal bindingi353 – 3531Divalent metal cation 2; catalytic By similarity
Metal bindingi449 – 4491Divalent metal cation 1 By similarity
Metal bindingi449 – 4491Divalent 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 Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2-2 (EC:3.4.11.18)
Short name:
MAP 2-2
Short name:
MetAP 2-2
Alternative name(s):
Peptidase M
Gene namesi
ORF Names:AFLA_092260
OrganismiAspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Taxonomic identifieri332952 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000001875: 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 – 468468Methionine aminopeptidase 2-2UniRule annotation
PRO_0000407622Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5059.CADAFLAP00008911.

Structurei

3D structure databases

ProteinModelPortaliB8NLL0.
SMRiB8NLL0. Positions 93-468.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi78 – 814Poly-LysUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
KOiK01265.
OMAiNNCVAHY.
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]
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.

B8NLL0-1 [UniParc]FASTAAdd to Basket

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MGSKTFEGEG QRGGNDPSNS TSPNSAGGEP RGAHLSRDGD GSLGDGDGDD    50
GADGDEKDGA VTTTPLTEQQ PSSETTSKKK KRRKPKKKIS ALKQSSPPRV 100
PLDDLFPTGQ FPVGETHEYG SVVEGTARTT SEEVRYLSRN YLQDDSVLTD 150
YRKAAEIHRQ VRHWTQENVR PGQTLTEIAV GIEDGVRALL DNAGLETGQC 200
LQSGMGFPTG LALNDCVAHY TPNPGQKDIV LQASDVMKVD FGVHINGWIV 250
DSAFTMSFDP TYDNLLAAVK DATNTGIKNA GIDVRISDVS AAIQEAMESY 300
EVEIGGKVFP VKPVRDISGH NINRYQIHGG KSIPFVKNSS QTKMEEGEIF 350
AIETFGSTGR GSTVEGFGVY GYGKDPNAPK KVSSPLASAR SLYKTINENF 400
GSIVFCRRYL ERLGVERYLA GMNSLVNNGI VEQYAPLMDM KGSYSAQFEH 450
TILLRESCKE VVSRGNDY 468
Length:468
Mass (Da):50,724
Last modified:March 3, 2009 - v1
Checksum:i7290AC2351FFEFF9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EQ963480 Genomic DNA. Translation: EED49145.1.
RefSeqiXP_002381046.1. XM_002381005.1.

Genome annotation databases

EnsemblFungiiCADAFLAT00008911; CADAFLAP00008911; CADAFLAG00008911.
GeneIDi7918359.
KEGGiafv:AFLA_092260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EQ963480 Genomic DNA. Translation: EED49145.1 .
RefSeqi XP_002381046.1. XM_002381005.1.

3D structure databases

ProteinModelPortali B8NLL0.
SMRi B8NLL0. Positions 93-468.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5059.CADAFLAP00008911.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAFLAT00008911 ; CADAFLAP00008911 ; CADAFLAG00008911 .
GeneIDi 7918359.
KEGGi afv:AFLA_092260.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000226278.
KOi K01265.
OMAi NNCVAHY.
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 ]
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. "Genome sequence of Aspergillus flavus strain NRRL 3357."
    Payne W.G.A., Dean R.A., Nierman W.C., Amedeo P., Caler E.G.A., Fedorova N.D., Maiti R., Joardar V., Inman J., Galinsky K.J., Yu J., Bhatnagar D., Cleveland T.E.
    Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167.

Entry informationi

Entry nameiMAP22_ASPFN
AccessioniPrimary (citable) accession number: B8NLL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: March 3, 2009
Last modified: June 11, 2014
This is version 38 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

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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