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Q4WAY7

- MAP21_ASPFU

UniProt

Q4WAY7 - MAP21_ASPFU

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Protein
Methionine aminopeptidase 2-1
Gene
AFUA_8G00410
Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (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) 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 sitei199 – 1991Substrate By similarity
Metal bindingi219 – 2191Divalent metal cation 1 By similarity
Metal bindingi230 – 2301Divalent metal cation 1 By similarity
Metal bindingi230 – 2301Divalent metal cation 2; catalytic By similarity
Metal bindingi299 – 2991Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei307 – 3071Substrate By similarity
Metal bindingi332 – 3321Divalent metal cation 2; catalytic By similarity
Metal bindingi427 – 4271Divalent metal cation 1 By similarity
Metal bindingi427 – 4271Divalent 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. fumagillin biosynthetic process Source: ASPGD
  2. protein initiator methionine removal Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Protein family/group databases

MEROPSiM24.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2-1 (EC:3.4.11.18)
Short name:
MAP 2-1
Short name:
MetAP 2-1
Alternative name(s):
Peptidase M
Gene namesi
ORF Names:AFUA_8G00410
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 8

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 – 446446Methionine aminopeptidase 2-1UniRule annotation
PRO_0000407623Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5085.CADAFUAP00000758.

Structurei

3D structure databases

ProteinModelPortaliQ4WAY7.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi62 – 7413Poly-LysUniRule annotation
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
KOiK01265.
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.

Q4WAY7-1 [UniParc]FASTAAdd to Basket

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MTVDAPELLE KLRITDAGAN GADMSSSTSA AANGTGKEVD DGSDDDGTEN    50
PPAVAAEHST AKKKKNKKRK PKKKQPKVQT DPPSIPLSQL FPNNSYPKGE 100
EVEYKDENRY RTTSEEKRHL DNLNSDFLSD YRQAAEAHRQ VRQWAQRNIK 150
PGQTLLEIAN GIEESARCLV GHDGLTEGDS LIAGMGFPTG LNIDNIVAHY 200
SPNAGCKTVL AQNNVLKVDI GIHVGGRIVD SAFTMAFDPM YDNLLAAVKD 250
ATNTGVREAG IDVRVGELGG YIQEAMESYE CEIRGKTYPI KAIRNLCGHT 300
ILPYSIHGTK NVPFVKSNDM TKMEEGDVFA IETFGSTGSG RYVEGGEVSH 350
YALRGDADRK DLTLSSARSL LTAIKKNFST IPFCRRYLDR IGQEKYLLGL 400
NYLVKSGIVE DYPPLNEKPG TYTAQFEHTI LLRPTVKEVI SRGDDY 446
Length:446
Mass (Da):48,996
Last modified:May 3, 2011 - v2
Checksum:i69A91BEE68E78371
GO

Sequence cautioni

The sequence EAL85125.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000014 Genomic DNA. Translation: EAL85125.1. Sequence problems.
RefSeqiXP_747163.1. XM_742070.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00000758; CADAFUAP00000758; CADAFUAG00000758.
GeneIDi3504499.
KEGGiafm:AFUA_8G00410.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000014 Genomic DNA. Translation: EAL85125.1 . Sequence problems.
RefSeqi XP_747163.1. XM_742070.1.

3D structure databases

ProteinModelPortali Q4WAY7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5085.CADAFUAP00000758.

Protein family/group databases

MEROPSi M24.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAFUAT00000758 ; CADAFUAP00000758 ; CADAFUAG00000758 .
GeneIDi 3504499.
KEGGi afm:AFUA_8G00410.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000226278.
KOi K01265.
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. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
    Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
    , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
    Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Entry informationi

Entry nameiMAP21_ASPFU
AccessioniPrimary (citable) accession number: Q4WAY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 3, 2011
Last modified: May 14, 2014
This is version 64 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, Reference 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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