Skip Header

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

Methionine aminopeptidase

Gene

map

Organism
Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)
Status
Unreviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Binding sitei65SubstrateUniRule annotation1
Metal bindingi85Divalent metal cation 1UniRule annotation1
Metal bindingi96Divalent metal cation 1UniRule annotation1
Metal bindingi96Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi156Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei164SubstrateUniRule annotation1
Metal bindingi189Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi284Divalent metal cation 1UniRule annotation1
Metal bindingi284Divalent metal cation 2; catalyticUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAminopeptidaseUniRule annotationImported, Hydrolase, Protease
LigandMetal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciSISL429572:G1GUX-2241-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:LS215_2191Imported
OrganismiSulfolobus islandicus (strain L.S.2.15 / Lassen #1)Imported
Taxonomic identifieri429572 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
Proteomesi
  • UP000001747 Componenti: Chromosome

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliC3MJM5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 290Peptidase_M24InterPro annotationAdd BLAST280

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili243 – 263Sequence analysisAdd BLAST21

Sequence similaritiesi

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

Keywords - Domaini

Coiled coilSequence analysis

Phylogenomic databases

HOGENOMiHOG000226277
KOiK01265
OMAiHTVLLMP
OrthoDBiPOG093Z06FJ

Family and domain databases

CDDicd01088 MetAP2, 1 hit
Gene3Di1.10.10.10, 1 hit
HAMAPiMF_01975 MetAP_2_arc, 1 hit
InterProiView protein in InterPro
IPR036005 Creatinase/aminopeptidase-like
IPR028595 MetAP_archaeal
IPR000994 Pept_M24
IPR001714 Pept_M24_MAP
IPR002468 Pept_M24A_MAP2
IPR018349 Pept_M24A_MAP2_BS
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF00557 Peptidase_M24, 1 hit
PRINTSiPR00599 MAPEPTIDASE
SUPFAMiSSF46785 SSF46785, 1 hit
SSF55920 SSF55920, 2 hits
TIGRFAMsiTIGR00501 met_pdase_II, 1 hit
PROSITEiView protein in PROSITE
PS01202 MAP_2, 1 hit

Sequencei

Sequence statusi: Complete.

C3MJM5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEDELNKLL LAGKIAAKAR DEVSLNVKAN AKVLDICEEV ESIILENKAF
60 70 80 90 100
PSFPCNISIN SEAAHYSPVI NDEKRIPEGA VVKLDLGAHI DGYISDTATT
110 120 130 140 150
ISLDAKYQRL LDASKTALEA AIANFRAGLS VGEIGRVIEK MIRTQGYKPI
160 170 180 190 200
RNLGGHLIRR YELHAGVFIP NVYERGLGAI QSDSVYAIEP FATDGGGEVV
210 220 230 240 250
EGKDVTIYSL KNPNVKGLSA RESELLDFIY THFNYLPFSE RWLKEFSTNV
260 270 280 290 300
DELRNNIKNL IKKGALRGYP ILLEIKKGVV SQFEHTVIVK GNSIIVSTKS

L
Length:301
Mass (Da):33,205
Last modified:June 16, 2009 - v1
Checksum:i63AB3DF8AA7ABE33
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001399 Genomic DNA Translation: ACP36178.1
RefSeqiWP_012714142.1, NC_012589.1

Genome annotation databases

EnsemblBacteriaiACP36178; ACP36178; LS215_2191
GeneIDi7798169
KEGGisis:LS215_2191

Similar proteinsi

Entry informationi

Entry nameiC3MJM5_SULIL
AccessioniPrimary (citable) accession number: C3MJM5
Entry historyiIntegrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: March 28, 2018
This is version 69 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health