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Q58725

- MAP2_METJA

UniProt

Q58725 - MAP2_METJA

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Protein

Methionine aminopeptidase

Gene

map

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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 Fe(2+)-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 sitei65 – 651SubstrateUniRule annotation
Metal bindingi85 – 851Divalent metal cation 1UniRule annotation
Metal bindingi96 – 961Divalent metal cation 1UniRule annotation
Metal bindingi96 – 961Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi156 – 1561Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei164 – 1641SubstrateUniRule annotation
Metal bindingi189 – 1891Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi279 – 2791Divalent metal cation 1UniRule annotation
Metal bindingi279 – 2791Divalent 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

Protein family/group databases

MEROPSiM24.035.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidaseUniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAPUniRule annotation
Short name:
MetAPUniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
Name:mapUniRule annotation
Ordered Locus Names:MJ1329
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
ProteomesiUP000000805: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 294294Methionine aminopeptidasePRO_0000148975Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi243232.MJ1329.

Structurei

3D structure databases

ProteinModelPortaliQ58725.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
InParanoidiQ58725.
KOiK01265.
OMAiERYKLHA.
PhylomeDBiQ58725.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_01975. MetAP_2_arc.
InterProiIPR028595. MetAP_archaeal.
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]
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.

Q58725-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEIEGYEKII EAGKIASKVR EEAVKLIXPG VKLLEVAEFV ENRIRELGGE
60 70 80 90 100
PAFPCNISIN EIAAHYTPKL NDNLEFKDDD VVKLDLGAHV DGYIADTAIT
110 120 130 140 150
VDLSNSYKDL VKASEDALYT VIKEINPPMN IGEMGKIIQE VIESYGYKPI
160 170 180 190 200
SNLSGHVMHR YELHTGISIP NVYERTNQYI DVGDLVAIEP FATDGFGMVK
210 220 230 240 250
DGNLGNIYKF LAKRPIRLPQ ARKLLDVISK NYPYLPFAER WVLKNESERL
260 270 280 290
ALNSLIRASC IYGYPILKER ENGIVGQAEH TILITENGVE ITTK
Length:294
Mass (Da):32,950
Last modified:November 1, 1997 - v1
Checksum:iAA28D37E2BF34186
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99338.1.
PIRiH64465.
RefSeqiNP_248330.1. NC_000909.1.
WP_010870846.1. NC_000909.1.

Genome annotation databases

EnsemblBacteriaiAAB99338; AAB99338; MJ_1329.
GeneIDi1452231.
KEGGimja:MJ_1329.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99338.1 .
PIRi H64465.
RefSeqi NP_248330.1. NC_000909.1.
WP_010870846.1. NC_000909.1.

3D structure databases

ProteinModelPortali Q58725.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243232.MJ1329.

Protein family/group databases

MEROPSi M24.035.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB99338 ; AAB99338 ; MJ_1329 .
GeneIDi 1452231.
KEGGi mja:MJ_1329.

Phylogenomic databases

eggNOGi COG0024.
InParanoidi Q58725.
KOi K01265.
OMAi ERYKLHA.
PhylomeDBi Q58725.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPi MF_01975. MetAP_2_arc.
InterProi IPR028595. MetAP_archaeal.
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: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.

Entry informationi

Entry nameiMAP2_METJA
AccessioniPrimary (citable) accession number: Q58725
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 26, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3