Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Methionine aminopeptidase 2

Gene

CPC735_002850

Organism
Coccidioides posadasii (strain C735) (Valley fever fungus)
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 sitei202 – 2021SubstrateUniRule annotation
Metal bindingi222 – 2221Divalent metal cation 1UniRule annotation
Metal bindingi233 – 2331Divalent metal cation 1UniRule annotation
Metal bindingi233 – 2331Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi302 – 3021Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei310 – 3101SubstrateUniRule 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

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
ORF Names:CPC735_002850
OrganismiCoccidioides posadasii (strain C735) (Valley fever fungus)
Taxonomic identifieri222929 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesCoccidioides
ProteomesiUP000009084 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:CPC735_002850.

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 – 452452Methionine aminopeptidase 2PRO_0000407650Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi222929.XP_003068261.1.

Structurei

3D structure databases

ProteinModelPortaliC5P8Q4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi63 – 7917Lys-richAdd
BLAST

Sequence similaritiesi

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

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.

C5P8Q4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVQALPEIN KLSVSEEGAA NAAAKGQAAQ GTAGNDDAEN DESDEDKEDE
60 70 80 90 100
QEVADGAAAA GGKKKKKKTK KKKKKGTAKV QSDPPRVPLS TLFPNNNYPE
110 120 130 140 150
GEIVEYKDDN AYRTTNEEKR YLDRMNNDFL TDYRKSAEIH RQVRQYAQKE
160 170 180 190 200
LLKPGRSLTE IAEGIEDSVR ALTGHMGLEE GDSLVAGMGF PTGLNINHCA
210 220 230 240 250
AHYSPNAGNK MVLQYGDVMK VDFGVHVNGR IVDSAFTVAF DPVYDNLLNA
260 270 280 290 300
VKDATNTGIR EAGIDVRMSD IGAAIQETME SYEVEINGTI YPVKAIRNLN
310 320 330 340 350
GHTIGHYLIH GGSTGKSVPI VKGGDQTKME EGETYAIETF GSTGKGFVRD
360 370 380 390 400
DMEVSHYAKV PDAPNVPLRL SSAKNLLNVI TKNFGTLPFC RRYLDRLGQE
410 420 430 440 450
KYLLGLNNLV SSGLVDAYPP LVDVKGSYTA QFEHTILLRP NVKEVITRGD

DY
Length:452
Mass (Da):49,394
Last modified:May 3, 2011 - v2
Checksum:i9E4A3B36E989C61F
GO

Sequence cautioni

The sequence EER26116.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ACFW01000030 Genomic DNA. Translation: EER26116.1. Different initiation.
RefSeqiXP_003068261.1. XM_003068215.1.
UniGeneiCpo.1088.

Genome annotation databases

GeneIDi9693744.
KEGGicpw:CPC735_002850.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ACFW01000030 Genomic DNA. Translation: EER26116.1. Different initiation.
RefSeqiXP_003068261.1. XM_003068215.1.
UniGeneiCpo.1088.

3D structure databases

ProteinModelPortaliC5P8Q4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi222929.XP_003068261.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi9693744.
KEGGicpw:CPC735_002850.

Organism-specific databases

EuPathDBiFungiDB:CPC735_002850.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C735.

Entry informationi

Entry nameiMAP2_COCP7
AccessioniPrimary (citable) accession number: C5P8Q4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 3, 2011
Last modified: June 24, 2015
This is version 43 of the entry and version 2 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.