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C0NX86

- MAP22_AJECG

UniProt

C0NX86 - MAP22_AJECG

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Protein

Methionine aminopeptidase 2-2

Gene

HCBG_08078

Organism
Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432) (Darling's disease fungus) (Histoplasma capsulatum)
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 sitei217 – 2171SubstrateUniRule annotation
Metal bindingi238 – 2381Divalent metal cation 1UniRule annotation
Metal bindingi249 – 2491Divalent metal cation 1UniRule annotation
Metal bindingi249 – 2491Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi318 – 3181Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei326 – 3261SubstrateUniRule annotation
Metal bindingi351 – 3511Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi446 – 4461Divalent metal cation 1UniRule annotation
Metal bindingi446 – 4461Divalent 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 2-2UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2-2UniRule annotation
Short name:
MetAP 2-2UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
ORF Names:HCBG_08078
OrganismiAjellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432) (Darling's disease fungus) (Histoplasma capsulatum)
Taxonomic identifieri447093 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeAjellomyces
ProteomesiUP000001631: Unassembled WGS sequence

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 – 465465Methionine aminopeptidase 2-2PRO_0000407615Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliC0NX86.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi75 – 839Poly-Lys

Sequence similaritiesi

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

Phylogenomic databases

InParanoidiC0NX86.
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]
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.

C0NX86-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSKTPHNHR RGPNESSSPP AIDAINPPKQ AAASGLVHGS LEGESEGGED
60 70 80 90 100
EDDDKPGADL KAVGQIGNDG QKRNKRKKKK KKKNTKELEI LQTTPPRVAL
110 120 130 140 150
ANIFRSQRYP EAEIVKYSTD NDNLQRTTTE ELRHLSVLNA MDDEFLNDYR
160 170 180 190 200
KAAEVHRQVR QYVQTIIKPG IALSQLAPEI EDGVRALTNH QGLETGDALK
210 220 230 240 250
AGMAFPTGLC LNNIAAHWTP NPGAKEVILQ YDDVLKIDFG VHVNGRIVDS
260 270 280 290 300
AFTMAFNPVY DNLLAAVKDA TNAGLKEAGI DSRIAHISEA IQEVMESYEV
310 320 330 340 350
ELNRKVIPVK AVRNITGHNI LHYKIHGDKQ VPFVKTQTNQ RMEEGDVFAI
360 370 380 390 400
ETFGSTGKAY LDDATGIYGY GYDENSSTTG LHHSSAKSLL KTIKENFGTL
410 420 430 440 450
VFSRRYLERL GVQRYHLGMR SLVTNGIVQS YAPLVDVPGS YVAQFEHTVL
460
LRPNCKEVIS RGDDY
Length:465
Mass (Da):51,413
Last modified:May 5, 2009 - v1
Checksum:iE835F35500BAC179
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GG663375 Genomic DNA. Translation: EEH03952.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GG663375 Genomic DNA. Translation: EEH03952.1 .

3D structure databases

ProteinModelPortali C0NX86.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

InParanoidi C0NX86.
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 ]
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: G186AR / H82 / ATCC MYA-2454 / RMSCC 2432.

Entry informationi

Entry nameiMAP22_AJECG
AccessioniPrimary (citable) accession number: C0NX86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 5, 2009
Last modified: October 29, 2014
This is version 34 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