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B0YAX5

- MAP23_ASPFC

UniProt

B0YAX5 - MAP23_ASPFC

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Protein

Methionine aminopeptidase 2-3

Gene

AFUB_086160

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
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 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 2-3UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2-3UniRule annotation
Short name:
MetAP 2-3UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
ORF Names:AFUB_086160
OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Taxonomic identifieri451804 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000001699: Unassembled WGS sequence

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 – 446446Methionine aminopeptidase 2-3PRO_0000407621Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB0YAX5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi62 – 7413Poly-LysAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000226278.
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.

B0YAX5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTVDAPELLE KLRITDAGAN GADMSSSTSA AANGTGKEVD DGSDDDGTEN
60 70 80 90 100
PPAVAAEHST AKKKKNKKRK PKKKQPKVQT DPPSIPLSQL FPNNSYPKGE
110 120 130 140 150
EVEYKDENRY RTTSEEKRHL DNLNSDFLSD YRQAAEAHRQ VRQWAQRNIK
160 170 180 190 200
PGQTLLEIAN GIEESARCLV GHDGLTEGDS LIAGMGFPTG LNIDNIVAHY
210 220 230 240 250
SPNAGCKTVL AQNNVLKVDI GIHVGGRIVD SAFTMAFDPM YDNLLAAVKD
260 270 280 290 300
ATNTGVREAG IDVRVGELGG YIQEAMESYE CEIRGKTYPI KAIRNLCGHT
310 320 330 340 350
ILPYSIHGTK NVPFVKSNDM TKMEEGDVFA IETFGSTGSG RYVEGGEVSH
360 370 380 390 400
YALRGDADRK DLTLSSARSL LTAIKKNFST IPFCRRYLDR IGQEKYLLGL
410 420 430 440
NYLVKSGIVE DYPPLNEKPG TYTAQFEHTI LLRPTVKEVI SRGDDY
Length:446
Mass (Da):48,996
Last modified:May 3, 2011 - v2
Checksum:i69A91BEE68E78371
GO

Sequence cautioni

The sequence EDP49168.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499600 Genomic DNA. Translation: EDP49168.1. Sequence problems.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499600 Genomic DNA. Translation: EDP49168.1 . Sequence problems.

3D structure databases

ProteinModelPortali B0YAX5.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOGENOMi HOG000226278.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CEA10 / CBS 144.89 / FGSC A1163.

Entry informationi

Entry nameiMAP23_ASPFC
AccessioniPrimary (citable) accession number: B0YAX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 3, 2011
Last modified: November 26, 2014
This is version 45 of the entry and version 2 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