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O58362

- MAP2_PYRHO

UniProt

O58362 - MAP2_PYRHO

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Protein

Methionine aminopeptidase

Gene

map

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
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

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 sitei62 – 621SubstrateUniRule annotation
Metal bindingi82 – 821Divalent metal cation 1UniRule annotation
Metal bindingi93 – 931Divalent metal cation 1UniRule annotation
Metal bindingi93 – 931Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi153 – 1531Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei161 – 1611SubstrateUniRule annotation
Metal bindingi187 – 1871Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi280 – 2801Divalent metal cation 1UniRule annotation
Metal bindingi280 – 2801Divalent 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

BioCyciPHOR70601:GJWR-623-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:PH0628
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000000752: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Methionine aminopeptidasePRO_0000148979Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi70601.PH0628.

Structurei

3D structure databases

ProteinModelPortaliO58362.
SMRiO58362. Positions 1-295.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226277.
KOiK01265.
OMAiERYKLHA.

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.

O58362 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDVDKLIEAG KIAKKVREEA VKLAKPGVSL LELAEKIESR IVELGGKPAF
60 70 80 90 100
PANLSLNEVA AHYTPYKGDQ TVLKEGDYLK IDLGVHIDGY IADTAVTVRV
110 120 130 140 150
GMDFDELMEA AKEALESAIS VARAGVEVKE LGKAIENEIR KRGFNPIVNL
160 170 180 190 200
SGHKIERYKL HAGVSIPNIY RPHDNYVLQE GDVFAIEPFA TTGAGQVIEV
210 220 230 240 250
PPTLIYMYVR DAPVRMAQAR FLLAKIKREY KTLPFAYRWL QGEMPEGQLK
260 270 280 290
LALRSLERSG ALYGYPVLRE IRGGMVTQFE HTIIVEKDSV TVTTE
Length:295
Mass (Da):32,795
Last modified:August 1, 1998 - v1
Checksum:iD228F4377CEB2AAC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000001 Genomic DNA. Translation: BAA29717.1.
PIRiC71107.
RefSeqiNP_142587.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA29717; BAA29717; BAA29717.
GeneIDi1442960.
KEGGipho:PH0628.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000001 Genomic DNA. Translation: BAA29717.1 .
PIRi C71107.
RefSeqi NP_142587.1. NC_000961.1.

3D structure databases

ProteinModelPortali O58362.
SMRi O58362. Positions 1-295.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 70601.PH0628.

Protein family/group databases

MEROPSi M24.035.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAA29717 ; BAA29717 ; BAA29717 .
GeneIDi 1442960.
KEGGi pho:PH0628.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000226277.
KOi K01265.
OMAi ERYKLHA.

Enzyme and pathway databases

BioCyci PHOR70601:GJWR-623-MONOMER.

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 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Entry informationi

Entry nameiMAP2_PYRHO
AccessioniPrimary (citable) accession number: O58362
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: October 1, 2014
This is version 101 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

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