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Q4WII3

- MAP22_ASPFU

UniProt

Q4WII3 - MAP22_ASPFU

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Protein

Methionine aminopeptidase 2-2

Gene

AFUA_2G01750

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

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 sitei238 – 2381SubstrateUniRule annotation
Metal bindingi259 – 2591Divalent metal cation 1UniRule annotation
Metal bindingi270 – 2701Divalent metal cation 1UniRule annotation
Metal bindingi270 – 2701Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi339 – 3391Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei347 – 3471SubstrateUniRule annotation
Metal bindingi372 – 3721Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi467 – 4671Divalent metal cation 1UniRule annotation
Metal bindingi467 – 4671Divalent 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 2-2UniRule 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:AFUA_2G01750
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 2

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 – 486486Methionine aminopeptidase 2-2PRO_0000407638Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5085.CADAFUAP00003355.

Structurei

3D structure databases

ProteinModelPortaliQ4WII3.
SMRiQ4WII3. Positions 118-486.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi93 – 10816Lys-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
InParanoidiQ4WII3.
KOiK01265.
OMAiRNISAHN.
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]
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.

Q4WII3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSKSPEGHR QAPHASNCNE LKPANPDPQI SQNGSGSADL DRGVIGDDDD
60 70 80 90 100
DEDAEENGVN TETPNVGKLN QPPFPNLDQV HVTTTDGLCI TEKKKKRKKS
110 120 130 140 150
NKKKKKTKSG ALPATELKQT SPPRVLVSTL FPSEYPVGEL VPYDCTARTT
160 170 180 190 200
DEELRYNSRL WDDDFLPDYR QAAEIHRQVR QYAQKELIKP GATLLSIAEG
210 220 230 240 250
IEDGVRALSG HQGLEPGDFF KAGMGFPTGL CLNHIAAHWT PNPREKDVIL
260 270 280 290 300
DKGDVLKVDF GVHVNGRIVD SAFTVAFDDK YDNLLTAVRE ATNTGIKHAG
310 320 330 340 350
VDARMSDIGA AIQEVMESYE VEIDGKVFPV KAIRNITGHD ILRYHIHGGK
360 370 380 390 400
QIPFIKNNNQ DKMEEGEVYA IETFGSTGRG FLDDDVGVYG YGRNENMSGA
410 420 430 440 450
NLRLSSAKSL LKTIDASFGS IVFSRRYLER LGVKNYLLGM KNLIDNGIVE
460 470 480
CYSPLVDVKG SYTAQFEHTI LLHSGGKEVI SRGDDY
Length:486
Mass (Da):53,508
Last modified:July 5, 2005 - v1
Checksum:i940B4DC3289A7288
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000008 Genomic DNA. Translation: EAL87272.1.
RefSeqiXP_749310.1. XM_744217.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00003355; CADAFUAP00003355; CADAFUAG00003355.
GeneIDi3506721.
KEGGiafm:AFUA_2G01750.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000008 Genomic DNA. Translation: EAL87272.1 .
RefSeqi XP_749310.1. XM_744217.1.

3D structure databases

ProteinModelPortali Q4WII3.
SMRi Q4WII3. Positions 118-486.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5085.CADAFUAP00003355.

Protein family/group databases

MEROPSi M24.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAFUAT00003355 ; CADAFUAP00003355 ; CADAFUAG00003355 .
GeneIDi 3506721.
KEGGi afm:AFUA_2G01750.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000226278.
InParanoidi Q4WII3.
KOi K01265.
OMAi RNISAHN.
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 ]
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 nameiMAP22_ASPFU
AccessioniPrimary (citable) accession number: Q4WII3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: July 5, 2005
Last modified: November 26, 2014
This is version 68 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