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Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (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)DescriptionActionsGraphical viewLength
Binding sitei197SubstrateUniRule annotation1
Metal bindingi217Divalent metal cation 1UniRule annotation1
Metal bindingi228Divalent metal cation 1UniRule annotation1
Metal bindingi228Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi299Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei307SubstrateUniRule annotation1
Metal bindingi332Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi427Divalent metal cation 1UniRule annotation1
Metal bindingi427Divalent metal cation 2; catalyticUniRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionAminopeptidase, Hydrolase, Protease
LigandMetal-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
Ordered Locus Names:CAALFM_C604080WA
ORF Names:CaO19.1214, CaO19.8802
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Chromosome 6

Organism-specific databases

CGDiCAL0000186537. orf19.1214.

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004076461 – 446Methionine aminopeptidase 2Add BLAST446

Proteomic databases

PRIDEiQ59LF9.

Structurei

3D structure databases

ProteinModelPortaliQ59LF9.
SMRiQ59LF9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi70 – 84Lys-richUniRule annotationAdd BLAST15

Sequence similaritiesi

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

Phylogenomic databases

InParanoidiQ59LF9.
KOiK01265.
OrthoDBiEOG092C3NQP.

Family and domain databases

CDDicd01088. MetAP2. 1 hit.
HAMAPiMF_03175. MetAP_2_euk. 1 hit.
InterProiView protein in InterPro
IPR036005. Creatinase/aminopeptidase-like.
IPR000994. Pept_M24.
IPR001714. Pept_M24_MAP.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
IPR036390. WH_DNA-bd_sf.
PfamiView protein in Pfam
PF00557. Peptidase_M24. 1 hit.
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
PROSITEiView protein in PROSITE
PS01202. MAP_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Q59LF9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGVTEGEDT KVIESKINEL NIDKPKLEDN NEAKGNGNGN ESGDDDDDDK
60 70 80 90 100
EEDDDNEITE PSTSTASGDE KKKKNKNKKK KKKKIVSIDS SYPEGIFPEG
110 120 130 140 150
QWMEYPLEDI NSYRTTSEEK RYLDRQQNNK WQDFRKGAEI HRRVRHKAQS
160 170 180 190 200
SIRPGMTMIE IANLIEDSVR NYSGNDHTLK AGIGFPTGLS LNHVAAHYTP
210 220 230 240 250
NTGDKLILKK DDIMKVDIGV HVNGRICDSA FTMTFNEDGK YDTIMQAVKE
260 270 280 290 300
ATYTGIKESG IDVRLNDIGA AIQEVMESYE MEENGKTYPI KCIKNLNGHN
310 320 330 340 350
IDDFVIHSGK SVPIIANGDM TKMEEGETFA IETFGSTGNG YVLPEGECSH
360 370 380 390 400
YAMNKGVEHL KPPSERSKQL LETIKQNFGT LPWCRRYLER TGEEKYLFAL
410 420 430 440
NQLVRHGIVE EYPPIVDKRG SYTAQFEHTI LLHPHKKEVV TKGDDY
Length:446
Mass (Da):50,379
Last modified:March 15, 2017 - v2
Checksum:i16950E829808285B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP017628 Genomic DNA. Translation: AOW30329.1.
RefSeqiXP_710564.2. XM_705472.2.

Genome annotation databases

EnsemblFungiiAOW30329; AOW30329; CAALFM_C604080WA.
GeneIDi3647837.
KEGGical:CAALFM_C604080WA.

Similar proteinsi

Entry informationi

Entry nameiMAP2_CANAL
AccessioniPrimary (citable) accession number: Q59LF9
Secondary accession number(s): A0A1D8PQC1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: March 15, 2017
Last modified: November 22, 2017
This is version 89 of the entry and version 2 of the sequence. See 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