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Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Candida tropicalis (strain ATCC MYA-3404 / T1) (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 sitei183 – 1831SubstrateUniRule annotation
Metal bindingi203 – 2031Divalent metal cation 1UniRule annotation
Metal bindingi214 – 2141Divalent metal cation 1UniRule annotation
Metal bindingi214 – 2141Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi285 – 2851Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei293 – 2931SubstrateUniRule annotation
Metal bindingi318 – 3181Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi413 – 4131Divalent metal cation 1UniRule annotation
Metal bindingi413 – 4131Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

GO - Biological processi

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:CTRG_02746
OrganismiCandida tropicalis (strain ATCC MYA-3404 / T1) (Yeast)
Taxonomic identifieri294747 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
ProteomesiUP000002037 Componenti: Unassembled WGS sequence

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Methionine aminopeptidase 2PRO_0000407648Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliC5M8M4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi57 – 7115Lys-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.

C5M8M4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTASVDTKTV EGQINDLKID STESSTTIPN NGKQESDNED DEVDESSTTQ
60 70 80 90 100
LSSTGDKKKK KKKNNKKKKK KIVSIDSSYP DGVFPEGQWM EYPLEINSYR
110 120 130 140 150
TTSEEKRYLD RQENNKWEDF RKGAEIHRRV RHKAQSSIKP GMSMIEIADL
160 170 180 190 200
IEDSVRNYAA ADHTLKAGIG FPTGLSLNHV AAHYTPNTGD KLVLNKDDIM
210 220 230 240 250
KVDIGVHVNG RICDSAFTMT FNEEGKYDKI MEAVREATYT GIKEAGIDVR
260 270 280 290 300
LNDIGEAIQE VMESYEMEEN GKILPIKCIK NLNGHNIGDY VIHSGKTVPI
310 320 330 340 350
VANGDMTKME EGETFAIETF GSTGNGYVLP EGECSHYAMN TGVEHLKAPS
360 370 380 390 400
ERSKQLLQNI KDNFGTLPWC RRYLERAGEE KYLFALNQLV RHGIVEEYPP
410 420 430
IVDKRGSYTA QYEHTILLHP HKKEVVTKGD DY
Length:432
Mass (Da):48,681
Last modified:July 28, 2009 - v1
Checksum:i5D96C6A42548FB08
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GG692397 Genomic DNA. Translation: EER33928.1.
RefSeqiXP_002548449.1. XM_002548403.1.

Genome annotation databases

GeneIDi8298308.
KEGGictp:CTRG_02746.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GG692397 Genomic DNA. Translation: EER33928.1.
RefSeqiXP_002548449.1. XM_002548403.1.

3D structure databases

ProteinModelPortaliC5M8M4.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi8298308.
KEGGictp:CTRG_02746.

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-3404 / T1.

Entry informationi

Entry nameiMAP2_CANTT
AccessioniPrimary (citable) accession number: C5M8M4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: July 28, 2009
Last modified: January 7, 2015
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

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.