Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q4WNT9

- MAP23_ASPFU

UniProt

Q4WNT9 - MAP23_ASPFU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Methionine aminopeptidase 2-3

Gene

AFUA_4G06930

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).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 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

Protein family/group databases

MEROPSiM24.002.

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:AFUA_4G06930
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 4

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 – 472472Methionine aminopeptidase 2-3PRO_0000407601Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5085.CADAFUAP00008312.

Structurei

3D structure databases

ProteinModelPortaliQ4WNT9.
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

eggNOGiCOG0024.
HOGENOMiHOG000226278.
InParanoidiQ4WNT9.
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.
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.

Q4WNT9-1 [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 EAL90095.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000005 Genomic DNA. Translation: EAL90095.1. Sequence problems.
RefSeqiXP_752133.1. XM_747040.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00008312; CADAFUAP00008312; CADAFUAG00008312.
GeneIDi3509601.
KEGGiafm:AFUA_4G06930.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000005 Genomic DNA. Translation: EAL90095.1 . Sequence problems.
RefSeqi XP_752133.1. XM_747040.1.

3D structure databases

ProteinModelPortali Q4WNT9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5085.CADAFUAP00008312.

Protein family/group databases

MEROPSi M24.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAFUAT00008312 ; CADAFUAP00008312 ; CADAFUAG00008312 .
GeneIDi 3509601.
KEGGi afm:AFUA_4G06930.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000226278.
InParanoidi Q4WNT9.
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.
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. "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 nameiMAP23_ASPFU
AccessioniPrimary (citable) accession number: Q4WNT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 3, 2011
Last modified: October 29, 2014
This is version 70 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