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A8QBZ2

- MAP2_MALGO

UniProt

A8QBZ2 - MAP2_MALGO

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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: 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) 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 sitei200 – 2001Substrate By similarity
Metal bindingi220 – 2201Divalent metal cation 1 By similarity
Metal bindingi231 – 2311Divalent metal cation 1 By similarity
Metal bindingi231 – 2311Divalent metal cation 2; catalytic By similarity
Metal bindingi300 – 3001Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei308 – 3081Substrate By similarity
Metal bindingi334 – 3341Divalent metal cation 2; catalytic By similarity
Metal bindingi429 – 4291Divalent metal cation 1 By similarity
Metal bindingi429 – 4291Divalent metal cation 2; catalytic By similarity

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

Subcellular locationi

Cytoplasm By similarity 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 2UniRule annotation
PRO_0000407657Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliA8QBZ2.
SMRiA8QBZ2. Positions 77-448.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi54 – 7320Lys-richUniRule annotation
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

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

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MPATAEAADA ATQATDAFST KLEENKLPEG QERGPEEEED DDDDETPAPG    50
DAEKKKKKKK KSGAKKKKSK TAKAVMEQTE PPSIGLTKMF PNGVFPVGEV 100
QQYDETKFDE SRKRVTGEEL RERERLIQEK DGFNYNFIRR AAEVHRQVRQ 150
YAQRTIKPGM SMTEIANMIE DGTRALVEVN GFESGIGFPT GLSLNEVAAH 200
YTPNAGDKRI LQSGDVLKVD FGVQVKGRIV DSAFTMNFEP TYDPLLAAVR 250
AATNTGVKEA GIDARLGEVG AAIQEVMESH EFEAEGKTHQ VKCIRNLQGH 300
DIAPYRIHGG KSVPIVAVPN LDVKMEEGET FAIETFGSTG RGYVVDSGEC 350
SHYARQANPP HVSLRINSAR QLLYTINKNF GSLPFCRRYL DRLGEQNYLL 400
GLRHLVSQGV VQDYPPLADV PGCMTAQFEH TILLRPTCKE VVSRGDDY 448
Length:448
Mass (Da):49,566
Last modified:January 15, 2008 - v1
Checksum:i12878A2062411469
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AAYY01000016 Genomic DNA. Translation: EDP41747.1 .
RefSeqi XP_001728961.1. XM_001728909.1.

3D structure databases

ProteinModelPortali A8QBZ2.
SMRi A8QBZ2. Positions 77-448.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5853267.
KEGGi mgl:MGL_3955.

Phylogenomic databases

KOi K01265.
OrthoDBi EOG7BGHW3.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPi MF_03175. MetAP_2_euk.
InterProi IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
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.
ProtoNeti Search...

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: May 14, 2014
This is version 44 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

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

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