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Protein

Methionine aminopeptidase 2

Gene

MGL_3955

Organism
Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated fungus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Cotranslationally 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 sitei200 – 2001SubstrateUniRule annotation
Metal bindingi220 – 2201Divalent metal cation 1UniRule annotation
Metal bindingi231 – 2311Divalent metal cation 1UniRule annotation
Metal bindingi231 – 2311Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi300 – 3001Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei308 – 3081SubstrateUniRule annotation
Metal bindingi334 – 3341Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi429 – 4291Divalent metal cation 1UniRule annotation
Metal bindingi429 – 4291Divalent 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

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2UniRule annotation
Short name:
MetAP 2UniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
ORF Names:MGL_3955
OrganismiMalassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated fungus)
Taxonomic identifieri425265 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaMalasseziomycetesMalassezialesMalasseziaceaeMalassezia
ProteomesiUP000008837: Unassembled WGS sequence

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Methionine aminopeptidase 2PRO_0000407657Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliA8QBZ2.
SMRiA8QBZ2. Positions 77-448.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi54 – 7320Lys-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

InParanoidiA8QBZ2.
KOiK01265.
OrthoDBiEOG7BGHW3.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_03175. MetAP_2_euk.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
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.

Sequencei

Sequence statusi: Complete.

A8QBZ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPATAEAADA ATQATDAFST KLEENKLPEG QERGPEEEED DDDDETPAPG
60 70 80 90 100
DAEKKKKKKK KSGAKKKKSK TAKAVMEQTE PPSIGLTKMF PNGVFPVGEV
110 120 130 140 150
QQYDETKFDE SRKRVTGEEL RERERLIQEK DGFNYNFIRR AAEVHRQVRQ
160 170 180 190 200
YAQRTIKPGM SMTEIANMIE DGTRALVEVN GFESGIGFPT GLSLNEVAAH
210 220 230 240 250
YTPNAGDKRI LQSGDVLKVD FGVQVKGRIV DSAFTMNFEP TYDPLLAAVR
260 270 280 290 300
AATNTGVKEA GIDARLGEVG AAIQEVMESH EFEAEGKTHQ VKCIRNLQGH
310 320 330 340 350
DIAPYRIHGG KSVPIVAVPN LDVKMEEGET FAIETFGSTG RGYVVDSGEC
360 370 380 390 400
SHYARQANPP HVSLRINSAR QLLYTINKNF GSLPFCRRYL DRLGEQNYLL
410 420 430 440
GLRHLVSQGV VQDYPPLADV PGCMTAQFEH TILLRPTCKE VVSRGDDY
Length:448
Mass (Da):49,566
Last modified:January 15, 2008 - v1
Checksum:i12878A2062411469
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAYY01000016 Genomic DNA. Translation: EDP41747.1.
RefSeqiXP_001728961.1. XM_001728909.1.

Genome annotation databases

GeneIDi5853267.
KEGGimgl:MGL_3955.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAYY01000016 Genomic DNA. Translation: EDP41747.1.
RefSeqiXP_001728961.1. XM_001728909.1.

3D structure databases

ProteinModelPortaliA8QBZ2.
SMRiA8QBZ2. Positions 77-448.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5853267.
KEGGimgl:MGL_3955.

Phylogenomic databases

InParanoidiA8QBZ2.
KOiK01265.
OrthoDBiEOG7BGHW3.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_03175. MetAP_2_euk.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
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.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4612 / CBS 7966.

Entry informationi

Entry nameiMAP2_MALGO
AccessioniPrimary (citable) accession number: A8QBZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: January 15, 2008
Last modified: January 7, 2015
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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.