SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9UYT4

- MAP2_PYRAB

UniProt

Q9UYT4 - MAP2_PYRAB

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Methionine aminopeptidase
Gene
map, PYRAB14230, PAB1434
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) By similarity.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 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei62 – 621Substrate By similarity
Metal bindingi82 – 821Divalent metal cation 1 By similarity
Metal bindingi93 – 931Divalent metal cation 1 By similarity
Metal bindingi93 – 931Divalent metal cation 2; catalytic By similarity
Metal bindingi153 – 1531Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei161 – 1611Substrate By similarity
Metal bindingi187 – 1871Divalent metal cation 2; catalytic By similarity
Metal bindingi280 – 2801Divalent metal cation 1 By similarity
Metal bindingi280 – 2801Divalent metal cation 2; catalytic By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-HAMAP
  2. metalloaminopeptidase activity Source: UniProtKB-HAMAP
Complete GO annotation...

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 aminopeptidase (EC:3.4.11.18)
Short name:
MAP
Short name:
MetAP
Alternative name(s):
Peptidase M
Gene namesi
Name:map
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 aminopeptidaseUniRule annotation
PRO_0000148977Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi272844.PAB1434.

Structurei

3D structure databases

ProteinModelPortaliQ9UYT4.
SMRiQ9UYT4. Positions 1-295.

Family & Domainsi

Sequence similaritiesi

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

MDVDKLIEAG KIAKKVREEA VKLAKPGVSL LELAEKIEGR IIELGAKPAF    50
PVNLSLNEIA AHYTPYKGDE TTLKEGDYLK IDIGVHIDGY IADTAVTVRV 100
GMEEDDLMEA AREALESAIS VARAGVEIKE LGRAIEDEIR KRGFNPIVNL 150
SGHKIERYKL HAGISIPNIY RPHDNYKLRE GDVFAIEPFA TTGAGQVIEV 200
PPTLIYMYVR DAPVRMVQAR FLLAKIKREY KTLPFAYRWL QGEMPEGQLK 250
LALRTLEKSG ALYGYPVLRE IRNGLVTQFE HTIIVEKDSV IVTTE 295
Length:295
Mass (Da):33,027
Last modified:May 1, 2000 - v1
Checksum:i2670D3E7DE6BF7B3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ248287 Genomic DNA. Translation: CAB50328.1.
HE613800 Genomic DNA. Translation: CCE70868.1.
PIRiC75054.
RefSeqiNP_127098.1. NC_000868.1.
WP_010868538.1. NC_000868.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ248287 Genomic DNA. Translation: CAB50328.1 .
HE613800 Genomic DNA. Translation: CCE70868.1 .
PIRi C75054.
RefSeqi NP_127098.1. NC_000868.1.
WP_010868538.1. NC_000868.1.

3D structure databases

ProteinModelPortali Q9UYT4.
SMRi Q9UYT4. Positions 1-295.
ModBasei 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: September 3, 2014
This is version 99 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

Similar proteinsi