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D1ZEN1

- MAP2_SORMK

UniProt

D1ZEN1 - MAP2_SORMK

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Protein

Methionine aminopeptidase 2

Gene
SMAC_05580
Organism
Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell)
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 sitei191 – 1911Substrate By similarity
Metal bindingi211 – 2111Divalent metal cation 1 By similarity
Metal bindingi222 – 2221Divalent metal cation 1 By similarity
Metal bindingi222 – 2221Divalent metal cation 2; catalytic By similarity
Metal bindingi291 – 2911Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei299 – 2991Substrate By similarity
Metal bindingi324 – 3241Divalent metal cation 2; catalytic By similarity
Metal bindingi419 – 4191Divalent metal cation 1 By similarity
Metal bindingi419 – 4191Divalent 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:SMAC_05580
OrganismiSordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell)
Taxonomic identifieri771870 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeSordaria
ProteomesiUP000001881: 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 – 438438Methionine aminopeptidase 2UniRule annotationPRO_0000407669Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliD1ZEN1.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi52 – 587Poly-LysUniRule annotation
Compositional biasi61 – 644Poly-LysUniRule annotation

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.
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.

D1ZEN1-1 [UniParc]FASTAAdd to Basket

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MAAQAAPAEE LSKLSVEETK PVSAAANGND SNAESGDEEG EEGTTPAAGA    50
AKKKKKRKPR KKKKAPTSQS EPPRVLVSQL FPNKQYPKGE EVEYVNDNLS 100
RVTNEEKRHL DSLASNQEFL TDYRHAAEVH RQVRQWAQKS IKPGQTLTEI 150
AENIEDSVRA LTGHTGLEEG DALVAGMGFP TGLSINHCAA HYTPNAGNKM 200
VLQEDDVMKV DFGVHVNGRI VDSAFTVAFN PRYDPLLEAV KAATNAGIKE 250
AGIDVRVGDI GAAIQEVMES YEVEINGQML PVKSIRNLNG HTISHYSIHG 300
TKSVPIVKSN DQTKMEEGDV FAIETFGSTG NGYVHEEGEV SHYAKRGDAA 350
KVDLRLSSAK SLLKVIDKNF GTLPFCRRYI DRLGQDKYLL GLNNLVSQGI 400
VEAYPPLVDK KGSYTAQYEH TILLRPTVKE VISRGDDF 438
Length:438
Mass (Da):47,884
Last modified:February 9, 2010 - v1
Checksum:i10EECDB67085ABD2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CABT02000026 Genomic DNA. Translation: CCC12403.1.
RefSeqiXP_003349297.1. XM_003349249.1.

Genome annotation databases

GeneIDi10806780.
KEGGismp:SMAC_05580.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CABT02000026 Genomic DNA. Translation: CCC12403.1 .
RefSeqi XP_003349297.1. XM_003349249.1.

3D structure databases

ProteinModelPortali D1ZEN1.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 10806780.
KEGGi smp:SMAC_05580.

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.
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

  1. "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads: Sordaria macrospora, a model organism for fungal morphogenesis."
    Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K., Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S., Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.
    PLoS Genet. 6:E1000891-E1000891(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-333 / DSM 997 / K(L3346) / K-hell.

Entry informationi

Entry nameiMAP2_SORMK
AccessioniPrimary (citable) accession number: D1ZEN1
Secondary accession number(s): F7W449
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: February 9, 2010
Last modified: May 14, 2014
This is version 32 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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