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C4YSA9

- MAP2_CANAW

UniProt

C4YSA9 - MAP2_CANAW

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Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Candida albicans (strain WO-1) (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).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.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei198 – 1981SubstrateUniRule annotation
Metal bindingi218 – 2181Divalent metal cation 1UniRule annotation
Metal bindingi229 – 2291Divalent metal cation 1UniRule annotation
Metal bindingi229 – 2291Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi300 – 3001Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei308 – 3081SubstrateUniRule annotation
Metal bindingi333 – 3331Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi428 – 4281Divalent metal cation 1UniRule annotation
Metal bindingi428 – 4281Divalent 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:CAWG_04971
OrganismiCandida albicans (strain WO-1) (Yeast)
Taxonomic identifieri294748 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
ProteomesiUP000001429: Chromosome 6

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 – 447447Methionine aminopeptidase 2PRO_0000407645Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliC4YSA9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi71 – 8515Lys-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000226278.
OMAiIQICEEL.
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.

C4YSA9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGATEGEDT KVIESKINEL NIDKPKLEDN NEAKGNGNGN ESGGDDDDDK
60 70 80 90 100
EDDDDNDEIT EPSTSTSSGD KKKKKNKNKK KKKKKIVSID SSYPEGIFPE
110 120 130 140 150
GQWMEYPLED INSYRTTSEE KRYLDRQQNN KWQDFRKGAE IHRRVRHKAQ
160 170 180 190 200
SSIRPGMTMI EIANLIEDSV RNYSGNDHTL KAGIGFPTGL SLNHVAAHYT
210 220 230 240 250
PNTGDKLILK KDDIMKVDIG VHVNGRICDS AFTMTFNEDG KYDTIMQAVK
260 270 280 290 300
EATYTGIKES GIDVRLNDIG AAIQEVMESY EMEENGKTYP IKCIKNLNGH
310 320 330 340 350
NIDDFVIHSG KSVPIIANGD MTKMEEGETF AIETFGSTGN GYVLPEGECS
360 370 380 390 400
HYAMNKGVEH LKPPSERSKQ LLETIKQNFG TLPWCRRYLE RTGEEKYLFA
410 420 430 440
LNQLVRHGIV EEYPPIVDKR GSYTAQFEHT ILLHPHKKEV VTKGDDY
Length:447
Mass (Da):50,409
Last modified:July 28, 2009 - v1
Checksum:iEE7A3DE5AC911CD5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CM000312 Genomic DNA. Translation: EEQ46612.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CM000312 Genomic DNA. Translation: EEQ46612.1 .

3D structure databases

ProteinModelPortali C4YSA9.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOGENOMi HOG000226278.
OMAi IQICEEL.
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: WO-1.

Entry informationi

Entry nameiMAP2_CANAW
AccessioniPrimary (citable) accession number: C4YSA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: July 28, 2009
Last modified: October 29, 2014
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