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Q59LF9

- MAP2_CANAL

UniProt

Q59LF9 - MAP2_CANAL

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Protein
Methionine aminopeptidase 2
Gene
MAP2, CaO19.1214, CaO19.8802
Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
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) By similarity.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 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei198 – 1981Substrate By similarity
Metal bindingi218 – 2181Divalent metal cation 1 By similarity
Metal bindingi229 – 2291Divalent metal cation 1 By similarity
Metal bindingi229 – 2291Divalent metal cation 2; catalytic By similarity
Metal bindingi300 – 3001Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei308 – 3081Substrate By similarity
Metal bindingi333 – 3331Divalent metal cation 2; catalytic By similarity
Metal bindingi428 – 4281Divalent metal cation 1 By similarity
Metal bindingi428 – 4281Divalent metal cation 2; catalytic By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-HAMAP
  2. metalloaminopeptidase activity Source: UniProtKB-HAMAP
Complete GO annotation...

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 (EC:3.4.11.18)
Short name:
MAP 2
Short name:
MetAP 2
Alternative name(s):
Peptidase M
Gene namesi
Name:MAP2
ORF Names:CaO19.1214, CaO19.8802
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
ProteomesiUP000000559: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0002793. orf19.1214.

Subcellular locationi

Cytoplasm By similarity 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 – 447447Methionine aminopeptidase 2UniRule annotation
PRO_0000407646Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5476.CAL0002793.

Structurei

3D structure databases

ProteinModelPortaliQ59LF9.
SMRiQ59LF9. Positions 86-447.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi71 – 8515Lys-richUniRule annotation
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
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.

Q59LF9-1 [UniParc]FASTAAdd to Basket

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MTGVTEGGDT KVIESKINEL NIDKPKLEDN NEAKGNGNGN ESGGGDDDDK    50
EEDDDNDEIT EPSTSTASGD KKKKKNKNKK KKKKKIVSID SSYPEGIFPE 100
GQWMEYPLED INSYRTTSEE KRYLDRQQNN KWQDFRKGAE IHRRVRHKAQ 150
SSIRPGMTMI EIANLIEDSV RNYSGNDHTL KAGIGFPTGL SLNHVAAHYT 200
PNTGDKLILK KDDIMKVDIG VHVNGRICDS AFTMTFNEDG KYDTIMQAVK 250
EATYTGIKES GIDVRLNDIG AAIQEVMESY EMEENGKTYP IKCIKNLNGH 300
NIDDFVIHSG KSVPIIANGD MTKMEEGETF AIETFGSTGN GYVLPEGECS 350
HYAMNKGVEH LKPPSERSKQ LLETIKQNFG TLPWCRRYLE RTGEEKYLFA 400
LNQLVRHGIV EEYPPIVDKR GSYTAQFEHT ILLHPHKKEV VTKGDDY 447
Length:447
Mass (Da):50,335
Last modified:April 26, 2005 - v1
Checksum:i37DD37D9E03FDE2C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AACQ01000257 Genomic DNA. Translation: EAK91311.1.
AACQ01000256 Genomic DNA. Translation: EAK91323.1.
RefSeqiXP_710564.1. XM_705472.1.
XP_710575.1. XM_705483.1.

Genome annotation databases

GeneIDi3647819.
3647837.
KEGGical:CaO19.1214.
cal:CaO19.8802.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AACQ01000257 Genomic DNA. Translation: EAK91311.1 .
AACQ01000256 Genomic DNA. Translation: EAK91323.1 .
RefSeqi XP_710564.1. XM_705472.1.
XP_710575.1. XM_705483.1.

3D structure databases

ProteinModelPortali Q59LF9.
SMRi Q59LF9. Positions 86-447.
ModBasei Search...

Protein-protein interaction databases

STRINGi 5476.CAL0002793.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3647819.
3647837.
KEGGi cal:CaO19.1214.
cal:CaO19.8802.

Organism-specific databases

CGDi CAL0002793. orf19.1214.

Phylogenomic databases

eggNOGi COG0024.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SC5314 / ATCC MYA-2876.

Entry informationi

Entry nameiMAP2_CANAL
AccessioniPrimary (citable) accession number: Q59LF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: April 26, 2005
Last modified: May 14, 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. Candida albicans
    Candida albicans: entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi