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Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841) (Yeast)
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 sitei203 – 2031SubstrateUniRule annotation
Metal bindingi223 – 2231Divalent metal cation 1UniRule annotation
Metal bindingi234 – 2341Divalent metal cation 1UniRule annotation
Metal bindingi234 – 2341Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi305 – 3051Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei313 – 3131SubstrateUniRule annotation
Metal bindingi338 – 3381Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi433 – 4331Divalent metal cation 1UniRule annotation
Metal bindingi433 – 4331Divalent 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
Name:MAP2UniRule annotation
ORF Names:CD36_64570
OrganismiCandida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841) (Yeast)
Taxonomic identifieri573826 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
ProteomesiUP000002605: Chromosome 6

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 – 452452Methionine aminopeptidase 2PRO_0000407647Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi573826.CD36_64570.

Structurei

3D structure databases

ProteinModelPortaliB9WJA2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi74 – 9017Lys-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
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.

B9WJA2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTGVTGTEDT KVIESKINEL NIDKSKPEKT NKVNKSDDVD NDDVDNDDND
60 70 80 90 100
DEDNDDDDDE ITESGNSASS SGDKKKKKNK NKNKKKKKKK IISIDSSYPE
110 120 130 140 150
GIFPEGQWME YPLEDINSYR ITSEEKRYLD RQQNNKWQDF RKGAEIHRRV
160 170 180 190 200
RHKAQSSIKP GMTMIEIANL IEDSIRNYSN NDHTLKSGIG FPTGLSLNHV
210 220 230 240 250
AAHYTPNTGD KLILKKDDIM KVDIGIHVNG RICDSAFTMT FNDEGKYDNI
260 270 280 290 300
MKAVKEATYT GIKESGIDVR LNDIGAAIQE VMESYEMEEN GKIYPIKCIK
310 320 330 340 350
NLNGHNIDDF IIHSGKSVPI IANGDMTKME EGEIFAIETF GSTGNGYVLP
360 370 380 390 400
EGECSHYAMN KNIQHLKPPS ERSKQLLESI KQNFGTLPWC RRYLERTGEE
410 420 430 440 450
KYLFALNQLV RHGIIEEYPP IVDKRGSYTA QYEHTILLHP HKKEVVTKGD

DY
Length:452
Mass (Da):51,409
Last modified:March 24, 2009 - v1
Checksum:iE9BA5A87E7D7FAF9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM992693 Genomic DNA. Translation: CAX41324.1.
RefSeqiXP_002421164.1. XM_002421119.1.

Genome annotation databases

GeneIDi8048936.
KEGGicdu:CD36_64570.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM992693 Genomic DNA. Translation: CAX41324.1.
RefSeqiXP_002421164.1. XM_002421119.1.

3D structure databases

ProteinModelPortaliB9WJA2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi573826.CD36_64570.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi8048936.
KEGGicdu:CD36_64570.

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
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: CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841.

Entry informationi

Entry nameiMAP2_CANDC
AccessioniPrimary (citable) accession number: B9WJA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: March 24, 2009
Last modified: January 7, 2015
This is version 41 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

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.