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Protein

Methionine aminopeptidase 2

Gene

PAAG_07566

Organism
Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides brasiliensis)
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 sitei195 – 1951SubstrateUniRule annotation
Metal bindingi215 – 2151Divalent metal cation 1UniRule annotation
Metal bindingi226 – 2261Divalent metal cation 1UniRule annotation
Metal bindingi226 – 2261Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi295 – 2951Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei303 – 3031SubstrateUniRule annotation
Metal bindingi331 – 3311Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi426 – 4261Divalent metal cation 1UniRule annotation
Metal bindingi426 – 4261Divalent 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 2UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2UniRule annotation
Short name:
MetAP 2UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
ORF Names:PAAG_07566
OrganismiParacoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides brasiliensis)
Taxonomic identifieri502779 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesParacoccidioides
ProteomesiUP000002059 Componenti: Partially assembled WGS

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 – 445445Methionine aminopeptidase 2PRO_0000407659Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliC1HAB2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi58 – 7316Lys-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

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.

C1HAB2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQVASGVG NLNLNSEGGA AAKNRPAQGS PENEARESDG EYDDDQGAPE
60 70 80 90 100
LGNTTAAKKK KKKTKKKKKC TSKVQTEPPR IILSSLFPNN QYPEGEIVEY
110 120 130 140 150
QNENAYRTTN EEKRHLDRMN NDFLAEYRYA AEVHRQVRQY SQKAIKPGQT
160 170 180 190 200
LTEIAEGIEE SVRALTGHPG LEEGDNLRGG IAFPTGVNLN HCAAHYTPNA
210 220 230 240 250
GNKMVLQYED VMKVDFGVHI NGRIVDSAFT IAFDPVYDNL LAAVKDATNT
260 270 280 290 300
GIKQAGIDVR MSDIGAAIQE AMESYEVEIK GTSYPVKAIR NLNGHTIGRY
310 320 330 340 350
EIHGGKNGKS VPIVKGGDQT KMEEGEVYAI ETFGSTGRGY VRDDMETSHY
360 370 380 390 400
AKIPDAPNVP LRLSSAKNLL NVITKNFGTL PFCRRYLDRL GQDKYLLGLN
410 420 430 440
NLVANGIVDA YPPLCDVKGS YTAQFEHTIL LRPNVKEIIS RGDDY
Length:445
Mass (Da):48,945
Last modified:May 25, 2009 - v1
Checksum:i9842168F931D0254
GO

Sequence cautioni

The sequence EEH37285.2 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KN294017 Genomic DNA. Translation: EEH37285.2. Sequence problems.
RefSeqiXP_002790267.1. XM_002790221.1.

Genome annotation databases

GeneIDi9093508.
KEGGipbl:PAAG_07566.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KN294017 Genomic DNA. Translation: EEH37285.2. Sequence problems.
RefSeqiXP_002790267.1. XM_002790221.1.

3D structure databases

ProteinModelPortaliC1HAB2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi9093508.
KEGGipbl:PAAG_07566.

Phylogenomic databases

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-826 / Pb01.

Entry informationi

Entry nameiMAP2_PARBA
AccessioniPrimary (citable) accession number: C1HAB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2011
Last sequence update: May 25, 2009
Last modified: March 31, 2015
This is version 39 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.