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E5R3Z8

- MAP22_ARTGP

UniProt

E5R3Z8 - MAP22_ARTGP

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Protein

Methionine aminopeptidase 2-2

Gene
MGYG_01859
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 sitei199 – 1991Substrate By similarity
Metal bindingi219 – 2191Divalent metal cation 1 By similarity
Metal bindingi230 – 2301Divalent metal cation 1 By similarity
Metal bindingi230 – 2301Divalent metal cation 2; catalytic By similarity
Metal bindingi299 – 2991Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei307 – 3071Substrate By similarity
Metal bindingi335 – 3351Divalent metal cation 2; catalytic By similarity
Metal bindingi430 – 4301Divalent metal cation 1 By similarity
Metal bindingi430 – 4301Divalent 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 2-2 (EC:3.4.11.18)
Short name:
MAP 2-2
Short name:
MetAP 2-2
Alternative name(s):
Peptidase M
Gene namesi
ORF Names:MGYG_01859
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 – 449449Methionine aminopeptidase 2-2UniRule annotationPRO_0000407596Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliE5R3Z8.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi61 – 7616Lys-richUniRule annotationAdd
BLAST

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]
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.

E5R3Z8-1 [UniParc]FASTAAdd to Basket

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MAAQAAPELA KLDLNKNTGS AEASTVPASG SDKDDAENEG DSDDDRDDEQ    50
TGGSAEVNAE KKKKKKRPKK KKKTAKVQSV PPRIPLTTLF PNNSFPEGEI 100
VEYLNENSYR TTNEEKRHLD RMNNDFLAEY RQAAEIHRQV RQYAQKELIK 150
PGATLTDIAE GIEDGVRHLT GHLGLEEGDS LVAGMGFPTG LNINHCAAHY 200
SPNAGNKVVL QHGDVMKVDF GVHVNGRIVD SAFTVAFDPV FDPLLTAVKE 250
ATNTGIKEAG IDVRMSDIGA AIQETMESYE LELNGTSYPI KAIRNLNGHT 300
IGQYEIHGGV NGKSVPIVKG GDQTKMEEGE TYAIETFGST GKGYVRDDME 350
TSHYAKVPSA PSVPLRLTSA KNLYSLINKN FGTLPFCRRY LDRLGQEKYL 400
LGLNNLVSSG LVDAYPPLCD VKGSYTAQFE HTILLRPNVK EVISRGDDY 449
Length:449
Mass (Da):49,131
Last modified:February 8, 2011 - v1
Checksum:iA846835A274F41C4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS989822 Genomic DNA. Translation: EFQ98844.1.
RefSeqiXP_003177796.1. XM_003177748.1.

Genome annotation databases

GeneIDi10033131.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DS989822 Genomic DNA. Translation: EFQ98844.1 .
RefSeqi XP_003177796.1. XM_003177748.1.

3D structure databases

ProteinModelPortali E5R3Z8.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 10033131.

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

Entry informationi

Entry nameiMAP22_ARTGP
AccessioniPrimary (citable) accession number: E5R3Z8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: February 8, 2011
Last modified: May 14, 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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