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Protein

Methionine aminopeptidase

Gene

map

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: 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 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 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 bindingi284 – 2841Divalent metal cation 1UniRule annotation
Metal bindingi284 – 2841Divalent 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

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-93-MONOMER.

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:SSO0098
ORF Names:C04024, C05_012
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000001974: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 301301Methionine aminopeptidasePRO_0000148981Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi273057.SSO0098.

Structurei

3D structure databases

ProteinModelPortaliP95963.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226277.
InParanoidiP95963.
KOiK01265.
OMAiRTIDENF.

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.

P95963-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTEDELNKLL LAGKIAAKAR DEVSLDVKAS AKVLDICEEV ESIIIENKAF
60 70 80 90 100
PSFPCNISIN SEAAHYSPTI NDEKRIPEGA VVKLDLGAHI DGFISDTAIT
110 120 130 140 150
ISLDSRYQRL LDASKTALEA AITNFKAGLS IGEIGRVIEK VIRAQGYKPI
160 170 180 190 200
RNLGGHLIRR YELHAGVFIP NVYERGLGVI QSDSVYAIEP FATDGGGEVV
210 220 230 240 250
EGKSITIYSL KNPNIKGLSS RENELIDFIY TRFNYLPFSE RWLKEFSTNV
260 270 280 290 300
DELRNNIKNL VKKGALRGYP ILIEIKKGVV SQFEHTVIVK GDSIIVSTKS

L
Length:301
Mass (Da):33,252
Last modified:May 1, 1997 - v1
Checksum:i3E156B383EF516F0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08257 Genomic DNA. Translation: CAA69553.1.
AE006641 Genomic DNA. Translation: AAK40454.1.
PIRiS75391.
RefSeqiNP_341664.1. NC_002754.1.
WP_009988912.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK40454; AAK40454; SSO0098.
GeneIDi1453282.
KEGGisso:SSO0098.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08257 Genomic DNA. Translation: CAA69553.1.
AE006641 Genomic DNA. Translation: AAK40454.1.
PIRiS75391.
RefSeqiNP_341664.1. NC_002754.1.
WP_009988912.1. NC_002754.1.

3D structure databases

ProteinModelPortaliP95963.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273057.SSO0098.

Protein family/group databases

MEROPSiM24.035.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK40454; AAK40454; SSO0098.
GeneIDi1453282.
KEGGisso:SSO0098.

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226277.
InParanoidiP95963.
KOiK01265.
OMAiRTIDENF.

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-93-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Organizational characteristics and information content of an archaeal genome: 156 kb of sequence from Sulfolobus solfataricus P2."
    Sensen C.W., Klenk H.-P., Singh R.K., Allard G., Chan C.C.-Y., Liu Q.Y., Penny S.L., Young F., Schenk M.E., Gaasterland T., Doolittle W.F., Ragan M.A., Charlebois R.L.
    Mol. Microbiol. 22:175-191(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.

Entry informationi

Entry nameiMAP2_SULSO
AccessioniPrimary (citable) accession number: P95963
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: February 4, 2015
This is version 107 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. 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.