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Protein

Methionine aminopeptidase 2

Gene

SCHCODRAFT_64644

Organism
Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill 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)DescriptionActionsGraphical viewLength
Binding sitei176SubstrateUniRule annotation1
Metal bindingi196Divalent metal cation 1UniRule annotation1
Metal bindingi207Divalent metal cation 1UniRule annotation1
Metal bindingi207Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi276Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei284SubstrateUniRule annotation1
Metal bindingi309Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi404Divalent metal cation 1UniRule annotation1
Metal bindingi404Divalent metal cation 2; catalyticUniRule annotation1

GO - Molecular functioni

GO - Biological processi

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:SCHCODRAFT_64644
OrganismiSchizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus)
Taxonomic identifieri578458 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesSchizophyllaceaeSchizophyllum
Proteomesi
  • UP000007431 Componenti: Unassembled WGS sequence

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004076671 – 423Methionine aminopeptidase 2Add BLAST423

Interactioni

Protein-protein interaction databases

STRINGi578458.XP_003038710.1.

Structurei

3D structure databases

ProteinModelPortaliD8PR70.
SMRiD8PR70.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi41 – 54Lys-richAdd BLAST14

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2775. Eukaryota.
COG0024. LUCA.
InParanoidiD8PR70.
KOiK01265.
OrthoDBiEOG092C3NQP.

Family and domain databases

CDDicd01088. MetAP2. 1 hit.
Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_03175. MetAP_2_euk. 1 hit.
InterProiIPR000994. Pept_M24.
IPR001714. Pept_M24_MAP.
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.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.

Sequencei

Sequence statusi: Complete.

D8PR70-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDVIDAKPE EAKKVPPEVE DEDSGDESAP EASAAGGEAT KKKKKKKKPK
60 70 80 90 100
KKKKAAEQSE PPRVGLSKLF PNGIYPEGEI QPYKDDNAYR TTSEEKRYLE
110 120 130 140 150
RITCEDPDET YQNIRKGAEV HRQVRQYAQR TIKPGMTMTE IANLIEDGTR
160 170 180 190 200
ALVEENGLEA GIGFPTGLSL NNCAAHYTPN AGDTIVLQQG DVMKVDIGVQ
210 220 230 240 250
VKGRIVDSAF TMTFEPTYDK LLEAVRAATN TGIREAGIDA RLGEIAGAIQ
260 270 280 290 300
ETMESYEVEV NGKLIPVKPI ANLSGHSIDR YTIHAGKSVC LVKNDDQTKM
310 320 330 340 350
EEGEYFAIET FGSTGRGRVV DGGECSHYAR KVDAPHVPLR LTTAKSLLKS
360 370 380 390 400
INKNFGTIPF CRRYLDRIGE SKYLLALNHL VQQGIVEDYP PLYDQQGSMT
410 420
AQFEHTILLR PTVKEVVSRG DDY
Length:423
Mass (Da):46,783
Last modified:October 5, 2010 - v1
Checksum:i3680863E582C4A34
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GL377302 Genomic DNA. Translation: EFJ03808.1.
RefSeqiXP_003038710.1. XM_003038664.1.

Genome annotation databases

EnsemblFungiiEFJ03808; EFJ03808; SCHCODRAFT_64644.
GeneIDi9592388.
KEGGiscm:SCHCODRAFT_64644.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GL377302 Genomic DNA. Translation: EFJ03808.1.
RefSeqiXP_003038710.1. XM_003038664.1.

3D structure databases

ProteinModelPortaliD8PR70.
SMRiD8PR70.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi578458.XP_003038710.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFJ03808; EFJ03808; SCHCODRAFT_64644.
GeneIDi9592388.
KEGGiscm:SCHCODRAFT_64644.

Phylogenomic databases

eggNOGiKOG2775. Eukaryota.
COG0024. LUCA.
InParanoidiD8PR70.
KOiK01265.
OrthoDBiEOG092C3NQP.

Family and domain databases

CDDicd01088. MetAP2. 1 hit.
Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
HAMAPiMF_03175. MetAP_2_euk. 1 hit.
InterProiIPR000994. Pept_M24.
IPR001714. Pept_M24_MAP.
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.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMAP2_SCHCM
AccessioniPrimary (citable) accession number: D8PR70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: October 5, 2010
Last modified: November 30, 2016
This is version 37 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

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 one 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.