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E5R278

- MAP21_ARTGP

UniProt

E5R278 - MAP21_ARTGP

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Protein
Methionine aminopeptidase 2-1
Gene
MGYG_01664
Organism
Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum gypseum)
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 sitei219 – 2191Substrate By similarity
Metal bindingi240 – 2401Divalent metal cation 1 By similarity
Metal bindingi251 – 2511Divalent metal cation 1 By similarity
Metal bindingi251 – 2511Divalent metal cation 2; catalytic By similarity
Metal bindingi320 – 3201Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei328 – 3281Substrate By similarity
Metal bindingi353 – 3531Divalent metal cation 2; catalytic By similarity
Metal bindingi448 – 4481Divalent metal cation 1 By similarity
Metal bindingi448 – 4481Divalent metal cation 2; catalytic By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-HAMAP
  2. metalloaminopeptidase activity Source: UniProtKB-HAMAP
Complete GO annotation...

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 2-1 (EC:3.4.11.18)
Short name:
MAP 2-1
Short name:
MetAP 2-1
Alternative name(s):
Peptidase M
Gene namesi
ORF Names:MGYG_01664
OrganismiArthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum gypseum)
Taxonomic identifieri535722 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaeArthroderma
ProteomesiUP000002669: 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 – 467467Methionine aminopeptidase 2-1UniRule annotation
PRO_0000407618Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliE5R278.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi83 – 886Poly-LysUniRule annotation

Sequence similaritiesi

Phylogenomic databases

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]
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.

E5R278-1 [UniParc]FASTAAdd to Basket

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MGSKSPDGHR QGPNAESPSS SVAATTNPPK PAAASGLVQG MLDGDDEDED    50
GDDDGDNQRI GADLKSGVLP NNDGKKRKRK SNKKKKKKTS KGQQTTPPRV 100
SLPSIFHDQR YPEGEIVEYA ARNDNLQRTT AEELRHQAAI HNMDDEFLTD 150
YRQAAEVHRQ VRQYVQSIAK PGILMSELAE EIETGVRALT GHQGIETGDA 200
LKAGLAFPTG LCLNNVAAHW TPNPGAKEVI LKHDDVLKID FGVHVNGRIV 250
DSAFTVASNP VYDNLLTAVK AATNTGLKEA GIDARIDHIS GEIQEVMESY 300
EVEINGKAIP VKALRSLTGH NILRYKIHGE KQVPFVKSKT TQRMEEGDVF 350
AIETFGSTGK GYTRDEVGVY GYGLNEHAST AGLHHASAKS LLKTIRENFG 400
TLVFSRRYLE HMGVKNYHLG MRSLISNDIV ECYAPLVDVP GSYVAQFEHT 450
VLLRPNCKEI ISRGDDY 467
Length:467
Mass (Da):51,146
Last modified:February 8, 2011 - v1
Checksum:iFF54B66A7F399579
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS989822 Genomic DNA. Translation: EFQ98642.1.
RefSeqiXP_003177594.1. XM_003177546.1.

Genome annotation databases

GeneIDi10032929.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS989822 Genomic DNA. Translation: EFQ98642.1 .
RefSeqi XP_003177594.1. XM_003177546.1.

3D structure databases

ProteinModelPortali E5R278.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 10032929.

Phylogenomic databases

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 ]
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4604 / CBS 118893.

Entry informationi

Entry nameiMAP21_ARTGP
AccessioniPrimary (citable) accession number: E5R278
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: February 8, 2011
Last modified: June 11, 2014
This is version 22 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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