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Protein

Methionine aminopeptidase 2-1

Gene

BDCG_02379

Organism
Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces dermatitidis)
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 sitei196 – 1961SubstrateUniRule annotation
Metal bindingi216 – 2161Divalent metal cation 1UniRule annotation
Metal bindingi227 – 2271Divalent metal cation 1UniRule annotation
Metal bindingi227 – 2271Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi296 – 2961Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei304 – 3041SubstrateUniRule annotation
Metal bindingi332 – 3321Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi427 – 4271Divalent metal cation 1UniRule annotation
Metal bindingi427 – 4271Divalent 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 2-1UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2-1UniRule annotation
Short name:
MetAP 2-1UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
ORF Names:BDCG_02379
OrganismiAjellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces dermatitidis)
Taxonomic identifieri559297 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeBlastomyces
ProteomesiUP000002039: 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 – 446446Methionine aminopeptidase 2-1PRO_0000407594Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliC5GCN0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi58 – 7417Lys-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

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.

C5GCN0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQVTPELA NLNSKPEGGA PPKQVPVKDV PENEDVESDD DNEGDQGAGE
60 70 80 90 100
PGSTGAAKKK KKKKPKKKKK GGPKVQTEPP RVILSSIFPN NDYPVGELVE
110 120 130 140 150
YKDDNAYRTT NEEKRYLDRM NNDFLSEYRY AAEVHRQVRQ YAQKTIKPGQ
160 170 180 190 200
TLTEIAEGIE DSVRALTGHD GLTEGDNLLG GIAFPTGVNL NHCAAHYSPN
210 220 230 240 250
AGNKMVLQYE DVMKVDFGVH INGRIVDSAF TVAFDPVYDN LLAAVKDATN
260 270 280 290 300
TGIREAGIDV RMSDIGAAIQ ETMESYEVEI KGTTYPVKPI RNLNGHTIGQ
310 320 330 340 350
FEIHGGKNGK SVPIVKGGDQ SKMEEGEVYA IETFGSTGRG YVRDDMETSH
360 370 380 390 400
YAKVPDAPNV PLRLSSAKNL LNVITKNFGT LPFCRRYLDR LGQDKYLLGL
410 420 430 440
NNLVANGIVD AYPPLCDIKG SYTAQFEHTI LLRPNIKEVI SRGYDY
Length:446
Mass (Da):49,025
Last modified:July 28, 2009 - v1
Checksum:iAA100997CC8C860B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EQ999974 Genomic DNA. Translation: EEQ87259.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EQ999974 Genomic DNA. Translation: EEQ87259.1.

3D structure databases

ProteinModelPortaliC5GCN0.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

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. "The genome sequence of Blastomyces dermatitidis strain ER-3."
    Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Klein B., Goldman B., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Heiman D.I., Hepburn T.A., Saif S., Shea T.D., Shenoy N., Sykes S.
    , Galagan J.E., Nusbaum C., Birren B.W.
    Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ER-3 / ATCC MYA-2586.

Entry informationi

Entry nameiMAP21_AJEDR
AccessioniPrimary (citable) accession number: C5GCN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: July 28, 2009
Last modified: February 4, 2015
This is version 35 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

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.