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Protein

Methionine aminopeptidase 2-2

Gene

AFUB_064000

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
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 sitei225 – 2251SubstrateUniRule annotation
Metal bindingi245 – 2451Divalent metal cation 1UniRule annotation
Metal bindingi256 – 2561Divalent metal cation 1UniRule annotation
Metal bindingi256 – 2561Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi325 – 3251Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei333 – 3331SubstrateUniRule annotation
Metal bindingi358 – 3581Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi453 – 4531Divalent metal cation 1UniRule annotation
Metal bindingi453 – 4531Divalent 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 2-2UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2-2UniRule annotation
Short name:
MetAP 2-2UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
ORF Names:AFUB_064000
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-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 472472Methionine aminopeptidase 2-2PRO_0000407599Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB0Y5N4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi88 – 9912Poly-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.
IPR018349. Pept_M24A_MAP2_BS.
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.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B0Y5N4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQVSEKLQ DLHLNGLNGD AKSNATVIGQ TEAGEAEDDS DDEKEDGNTA
60 70 80 90 100
PEAGAGGGAY LHVWVIFEMP VSQALGMLAY NSRIPAAKKK KRKSKKKKKG
110 120 130 140 150
GAKVQSSPPR VPVSNLFPNN QYPEGEIVEY KNENSYRTTN EEKRYLDRMN
160 170 180 190 200
NNFLQEYRQA AEVHRQVRQY AQKTIKPGQT LTEIAEGIED AVRALTGHQG
210 220 230 240 250
LEEGDNLKGG MGFPCGLSIN HCAAHYTPNA GNKMVLQQGD VMKVDFGAHI
260 270 280 290 300
NGRIVDSAFT MTFDPVYDPL LEAVKDATNT GIREAGIDVR MSDIGAAIQE
310 320 330 340 350
AMESYEVELN GTMYPVKCIR NLNGHNIDRH IIHGGKSVPI VKGSDQTKME
360 370 380 390 400
EGETFAIETF GSTGKGYVRE DMETSHYALI PDAPSVPLRL SSAKNLLNVI
410 420 430 440 450
NKNFGTLPFC RRYLDRLGQE KYLLGLNNLV SSGIVQDYPP LCDVKGSYTA
460 470
QFEHTILLRP TVKEVISRGD DY
Length:472
Mass (Da):51,959
Last modified:May 3, 2011 - v2
Checksum:i07C2C43062731656
GO

Sequence cautioni

The sequence EDP50069.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499598 Genomic DNA. Translation: EDP50069.1. Sequence problems.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499598 Genomic DNA. Translation: EDP50069.1. Sequence problems.

3D structure databases

ProteinModelPortaliB0Y5N4.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.
IPR018349. Pept_M24A_MAP2_BS.
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.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

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

Entry informationi

Entry nameiMAP22_ASPFC
AccessioniPrimary (citable) accession number: B0Y5N4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 3, 2011
Last modified: January 7, 2015
This is version 47 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

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.