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Protein

Methionine aminopeptidase

Gene

map

Organism
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
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 sitei63 – 631SubstrateUniRule annotation
Metal bindingi83 – 831Divalent metal cation 1UniRule annotation
Metal bindingi94 – 941Divalent metal cation 1UniRule annotation
Metal bindingi94 – 941Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi154 – 1541Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei162 – 1621SubstrateUniRule annotation
Metal bindingi188 – 1881Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi281 – 2811Divalent metal cation 1UniRule annotation
Metal bindingi281 – 2811Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciTKOD69014:GH72-1198-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:TK1183
OrganismiThermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Taxonomic identifieri69014 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
ProteomesiUP000000536 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Methionine aminopeptidasePRO_0000148980Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi69014.TK1183.

Structurei

3D structure databases

ProteinModelPortaliQ5JGD1.
SMRiQ5JGD1. Positions 3-295.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226277.
InParanoidiQ5JGD1.
KOiK01265.
OMAiPNYPDKT.

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.

Q5JGD1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDEREALIKA GEIARQVKKE VVDLIKPGAK LYDIAEFVER RIVELGGKPA
60 70 80 90 100
FPCNLSINEI AAHYTPYKGD GTVLKEGDYL KLDIGVHVDG YIADTAVTFR
110 120 130 140 150
VGMEEDELME AAREALENAI ATVRAGVMIR DVARAIEETI RGKGFNPIVN
160 170 180 190 200
LSGHKVERYK LHAGVSVPNV YREADTYVLQ EGDVFAIEPF ATTGAGQVIE
210 220 230 240 250
VPPALIFMYL RDRPVRMLQA RRLLMHIKKN YKTLPFAYRW LQDFLPEGQL
260 270 280 290
KLALAQLEKA GAIYAYPILR EVRGGMVAQF EHTVIVEKEG AYITT
Length:295
Mass (Da):33,021
Last modified:February 15, 2005 - v1
Checksum:i4199B9ADA77AD173
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006878 Genomic DNA. Translation: BAD85372.1.
RefSeqiWP_011250134.1. NC_006624.1.
YP_183596.1. NC_006624.1.

Genome annotation databases

EnsemblBacteriaiBAD85372; BAD85372; TK1183.
GeneIDi3234128.
KEGGitko:TK1183.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006878 Genomic DNA. Translation: BAD85372.1.
RefSeqiWP_011250134.1. NC_006624.1.
YP_183596.1. NC_006624.1.

3D structure databases

ProteinModelPortaliQ5JGD1.
SMRiQ5JGD1. Positions 3-295.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi69014.TK1183.

Protein family/group databases

MEROPSiM24.035.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD85372; BAD85372; TK1183.
GeneIDi3234128.
KEGGitko:TK1183.

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226277.
InParanoidiQ5JGD1.
KOiK01265.
OMAiPNYPDKT.

Enzyme and pathway databases

BioCyciTKOD69014:GH72-1198-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

  1. "Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."
    Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.
    Genome Res. 15:352-363(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-918 / JCM 12380 / KOD1.

Entry informationi

Entry nameiMAP2_THEKO
AccessioniPrimary (citable) accession number: Q5JGD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: February 15, 2005
Last modified: June 24, 2015
This is version 79 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.