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B0CRL4

- MAP2_LACBS

UniProt

B0CRL4 - MAP2_LACBS

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Protein
Methionine aminopeptidase 2
Gene
LACBIDRAFT_242662
Organism
Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver) (Laccaria laccata var. bicolor)
Status
Reviewed - Annotation score: 2 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 sitei111 – 1111Substrate By similarity
Metal bindingi131 – 1311Divalent metal cation 1 By similarity
Metal bindingi142 – 1421Divalent metal cation 1 By similarity
Metal bindingi142 – 1421Divalent metal cation 2; catalytic By similarity
Metal bindingi211 – 2111Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei219 – 2191Substrate By similarity
Metal bindingi244 – 2441Divalent metal cation 2; catalytic By similarity
Metal bindingi339 – 3391Divalent metal cation 1 By similarity
Metal bindingi339 – 3391Divalent 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:LACBIDRAFT_242662
OrganismiLaccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver) (Laccaria laccata var. bicolor)
Taxonomic identifieri486041 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesTricholomataceaeLaccaria
ProteomesiUP000001194: 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 – 358358Methionine aminopeptidase 2UniRule annotation
PRO_0000407653Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi29883.JGI242662.

Structurei

3D structure databases

ProteinModelPortaliB0CRL4.
SMRiB0CRL4. Positions 23-358.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
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.

B0CRL4-1 [UniParc]FASTAAdd to Basket

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MSACTSFLRV AGDKVNLSFS SNSWRTTSEE KRYDERMANE DPEKTYQSIR    50
RAAEVHRQVR QHARRHIRPG MTMTEIANNI EDGTRALVEE DGLLSGVGFP 100
TGLSLNNCAA HYTPNAGDTT VLQKGDVLKV DIGVHVKGRI ADSAFTLTWE 150
PTYNKLLEAV KAATDTGIRE SGIDARLGEI AGAIQETMES YEVEVNGTVY 200
PVKPIENLSG HSINPYQIHG GKSILLVKND DQTKMEEGEY FAIETFGSTG 250
RGRIVESGEV SHYARRMDAP HVPLRLTSAK TLLKSINKNF GTLPFCRRYL 300
DRAGESKYLL ALNHLVGQGI VQDYPPLCDQ RGSMTAQFEH TILLRPTVKE 350
VVTRGDDY 358
Length:358
Mass (Da):39,747
Last modified:February 26, 2008 - v1
Checksum:i4EE375B300D588AF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS547091 Genomic DNA. Translation: EDR15225.1.
RefSeqiXP_001873433.1. XM_001873398.1.

Genome annotation databases

GeneIDi6069222.
KEGGilbc:LACBIDRAFT_242662.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS547091 Genomic DNA. Translation: EDR15225.1 .
RefSeqi XP_001873433.1. XM_001873398.1.

3D structure databases

ProteinModelPortali B0CRL4.
SMRi B0CRL4. Positions 23-358.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 29883.JGI242662.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 6069222.
KEGGi lbc:LACBIDRAFT_242662.

Phylogenomic databases

eggNOGi COG0024.
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. "The genome of Laccaria bicolor provides insights into mycorrhizal symbiosis."
    Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F., Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J., Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.
    , Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A., DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P., Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P., Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R., Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H., Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M., Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U., Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J., Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A., Tuskan G., Grigoriev I.V.
    Nature 452:88-92(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: S238N-H82 / ATCC MYA-4686.

Entry informationi

Entry nameiMAP2_LACBS
AccessioniPrimary (citable) accession number: B0CRL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: February 26, 2008
Last modified: May 14, 2014
This is version 40 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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