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Q9UYT4

- MAP2_PYRAB

UniProt

Q9UYT4 - MAP2_PYRAB

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Protein

Methionine aminopeptidase

Gene

map

Organism
Pyrococcus abyssi (strain GE5 / Orsay)
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 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

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:PYRAB14230
ORF Names:PAB1434
OrganismiPyrococcus abyssi (strain GE5 / Orsay)
Taxonomic identifieri272844 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000000810: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Methionine aminopeptidasePRO_0000148977Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi272844.PAB1434.

Structurei

3D structure databases

ProteinModelPortaliQ9UYT4.
SMRiQ9UYT4. 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.

Q9UYT4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDVDKLIEAG KIAKKVREEA VKLAKPGVSL LELAEKIEGR IIELGAKPAF
60 70 80 90 100
PVNLSLNEIA AHYTPYKGDE TTLKEGDYLK IDIGVHIDGY IADTAVTVRV
110 120 130 140 150
GMEEDDLMEA AREALESAIS VARAGVEIKE LGRAIEDEIR KRGFNPIVNL
160 170 180 190 200
SGHKIERYKL HAGISIPNIY RPHDNYKLRE GDVFAIEPFA TTGAGQVIEV
210 220 230 240 250
PPTLIYMYVR DAPVRMVQAR FLLAKIKREY KTLPFAYRWL QGEMPEGQLK
260 270 280 290
LALRTLEKSG ALYGYPVLRE IRNGLVTQFE HTIIVEKDSV IVTTE
Length:295
Mass (Da):33,027
Last modified:May 1, 2000 - v1
Checksum:i2670D3E7DE6BF7B3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ248287 Genomic DNA. Translation: CAB50328.1.
HE613800 Genomic DNA. Translation: CCE70868.1.
PIRiC75054.
RefSeqiNP_127098.1. NC_000868.1.

Genome annotation databases

EnsemblBacteriaiCAB50328; CAB50328; PAB1434.
GeneIDi1496814.
KEGGipab:PAB1434.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ248287 Genomic DNA. Translation: CAB50328.1 .
HE613800 Genomic DNA. Translation: CCE70868.1 .
PIRi C75054.
RefSeqi NP_127098.1. NC_000868.1.

3D structure databases

ProteinModelPortali Q9UYT4.
SMRi Q9UYT4. Positions 1-295.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272844.PAB1434.

Protein family/group databases

MEROPSi M24.035.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB50328 ; CAB50328 ; PAB1434 .
GeneIDi 1496814.
KEGGi pab:PAB1434.

Phylogenomic databases

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

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: GE5 / Orsay.
  2. "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
    Gao J., Wang J.
    Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: GE5 / Orsay.

Entry informationi

Entry nameiMAP2_PYRAB
AccessioniPrimary (citable) accession number: Q9UYT4
Secondary accession number(s): G8ZHN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: November 26, 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