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A2QHX0

- MAP22_ASPNC

UniProt

A2QHX0 - MAP22_ASPNC

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Protein

Methionine aminopeptidase 2-2

Gene

An04g01330

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 2 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

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 sitei184 – 1841SubstrateUniRule annotation
Metal bindingi204 – 2041Divalent metal cation 1UniRule annotation
Metal bindingi215 – 2151Divalent metal cation 1UniRule annotation
Metal bindingi215 – 2151Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi284 – 2841Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei292 – 2921SubstrateUniRule annotation
Metal bindingi317 – 3171Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi412 – 4121Divalent metal cation 1UniRule annotation
Metal bindingi412 – 4121Divalent 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:An04g01330
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706: Chromosome 6L

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 – 431431Methionine aminopeptidase 2-2PRO_0000407602Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00003753.

Structurei

3D structure databases

ProteinModelPortaliA2QHX0.
SMRiA2QHX0. Positions 62-431.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
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.

A2QHX0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAQASEKLQ KLDLNGQSGD AEADAPAAGQ TQAGEAEDDS DDDEVEDGNA
60 70 80 90 100
AGEGAASGGG AKVQSSPPRV PLSTLFAGKE YPEGEIVEYQ NENSYRTTNE
110 120 130 140 150
EKRYLDRMKN DFLQEYRQAA EVHRQVRQYA QKTIKPGQTL TEIAEGIEES
160 170 180 190 200
VRALTGHQGL EEGDNLKGGM GFPCGLSINH CAAHYTPNAG NKMVLQQGDV
210 220 230 240 250
MKVDFGAHIN GRIVDSAFTV AFDPVYDPLL AAVKDATNTG IREAGIDVRM
260 270 280 290 300
SDIGAAIQEA MESYEVEING TMYPVKCIRN LNGHNIDQHI IHGGKSVPIV
310 320 330 340 350
KGGDQTKMEE GEVFAIETFG STGKGYVRED METSHYALIP DHSQVPLRLS
360 370 380 390 400
SAKNLLNVIN KNFGTLPFCR RYLDRLGQDK YLLGLNNLVS SGIVQDYPPL
410 420 430
CDIKGSYTAQ YEHTIVLRPN VKEVISRGDD Y
Length:431
Mass (Da):46,964
Last modified:March 6, 2007 - v1
Checksum:i3C8063813B50BD68
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270069 Genomic DNA. Translation: CAK38590.1.

Genome annotation databases

EnsemblFungiiCADANGAT00003842; CADANGAP00003753; CADANGAG00003842.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270069 Genomic DNA. Translation: CAK38590.1 .

3D structure databases

ProteinModelPortali A2QHX0.
SMRi A2QHX0. Positions 62-431.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5061.CADANGAP00003753.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANGAT00003842 ; CADANGAP00003753 ; CADANGAG00003842 .

Phylogenomic databases

eggNOGi COG0024.
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.
IPR018349. Pept_M24A_MAP2_BS.
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.
PROSITEi PS01202. MAP_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513.

Entry informationi

Entry nameiMAP22_ASPNC
AccessioniPrimary (citable) accession number: A2QHX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: March 6, 2007
Last modified: October 29, 2014
This is version 51 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, 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