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C0NIQ4

- MAP21_AJECG

UniProt

C0NIQ4 - MAP21_AJECG

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Protein
Methionine aminopeptidase 2-1
Gene
HCBG_02311
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) By similarity.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 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei198 – 1981Substrate By similarity
Metal bindingi218 – 2181Divalent metal cation 1 By similarity
Metal bindingi229 – 2291Divalent metal cation 1 By similarity
Metal bindingi229 – 2291Divalent metal cation 2; catalytic By similarity
Metal bindingi298 – 2981Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei306 – 3061Substrate By similarity
Metal bindingi334 – 3341Divalent metal cation 2; catalytic By similarity
Metal bindingi429 – 4291Divalent metal cation 1 By similarity
Metal bindingi429 – 4291Divalent metal cation 2; catalytic By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-HAMAP
  2. metalloaminopeptidase activity Source: UniProtKB-HAMAP
Complete GO annotation...

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 2-1 (EC:3.4.11.18)
Short name:
MAP 2-1
Short name:
MetAP 2-1
Alternative name(s):
Peptidase M
Gene namesi
ORF Names:HCBG_02311
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 By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Methionine aminopeptidase 2-1UniRule annotation
PRO_0000407593Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliC0NIQ4.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi60 – 7617Lys-richUniRule annotation
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

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.

C0NIQ4-1 [UniParc]FASTAAdd to Basket

« Hide

MAAQVIPELQ SLNLKTEGGA LPQELAPSGA PENEDGDSED DNGDDQGADE    50
SRTIEVLAAK KKKKKKPKKK KKDTQKAQTE PPRVILSALF PNNEYPVGEL 100
VEYKDENAYR TTNEEKRYLD RMNNDFLSEY RYAAEVHKQV RQYAQKTIKP 150
GQTLTEIAEG IEDSVRALTG HDGLTEGDNL LGGIAFPTGV NLNNCAAHYS 200
PNAGNKMVLQ YEDVMKVDFG VHMNGRIVDS AFTIAFDPVY DNLLAAVKDA 250
TNTGIREAGI DVRMSDIGAA IQEAMESYEV EIKGTTYPVK AIRNLNGHTI 300
GQFEIHGGKN GKSVPIVKGG DQSKMEEGEV YAIETFGSTG RGYVRDDMET 350
SHYAKVPDAP NVPLRLSSAK NLLNVITKNF GTLPFCRRYL DRLRQDKYLL 400
GLNNLVANGL VDAYPPLCDI KGSYTAQFEH TILLRPNIKE VISRGDDY 448
Length:448
Mass (Da):49,468
Last modified:May 5, 2009 - v1
Checksum:iA9D4636BE72A773C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GG663365 Genomic DNA. Translation: EEH08774.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GG663365 Genomic DNA. Translation: EEH08774.1 .

3D structure databases

ProteinModelPortali C0NIQ4.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

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: G186AR / H82 / ATCC MYA-2454 / RMSCC 2432.

Entry informationi

Entry nameiMAP21_AJECG
AccessioniPrimary (citable) accession number: C0NIQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 5, 2009
Last modified: May 14, 2014
This is version 31 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

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