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A5E5I9

- MAP2_LODEL

UniProt

A5E5I9 - MAP2_LODEL

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Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus)
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).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 Fe(2+)-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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei224 – 2241SubstrateUniRule annotation
Metal bindingi244 – 2441Divalent metal cation 1UniRule annotation
Metal bindingi255 – 2551Divalent metal cation 1UniRule annotation
Metal bindingi255 – 2551Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi326 – 3261Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei334 – 3341SubstrateUniRule annotation
Metal bindingi359 – 3591Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi454 – 4541Divalent metal cation 1UniRule annotation
Metal bindingi454 – 4541Divalent metal cation 2; catalyticUniRule annotation

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 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
Name:MAP2UniRule annotation
ORF Names:LELG_04878
OrganismiLodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus)
Taxonomic identifieri379508 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeLodderomyces
ProteomesiUP000001996: Unassembled WGS sequence

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Methionine aminopeptidase 2PRO_0000407655Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi36914.A5E5I9.

Structurei

3D structure databases

ProteinModelPortaliA5E5I9.
SMRiA5E5I9. Positions 112-473.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi97 – 11216Lys-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
InParanoidiA5E5I9.
KOiK01265.
OMAiIQICEEL.
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.

A5E5I9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTDTSIKAG IDSIRAKADD LHLAEDSSNG TQANLDKHQI KATTAVGQDN
60 70 80 90 100
GNNAGVADHK NDKNNKNNKN NNDDDDDDED DDVAAAAAAV GDAGSDKKKK
110 120 130 140 150
KKKSSNKKKK KKLVSIDQSY PDGVFPEGEW QEYGLDSNKY RTTSEEMRYL
160 170 180 190 200
DRQQNNKWED FRKGAEIHRR VRAKAKSSIR PGMTMIEIAD LIENSVRAYA
210 220 230 240 250
SADHTLKAGI GFPTGLSLNH VAAHYTPNTG DKLTLGKDDL MKVDIGVHVN
260 270 280 290 300
GRICDSAFTM TFNEDGKYDS IMQAVKEATN TGVKEAGIDV RLNDIGAAVQ
310 320 330 340 350
EVMESYEMEL DGKTYPIKCI KNLNGHNIGD FIIHSGKTVP IVANGDMTKM
360 370 380 390 400
EEGETFAIET FGSTGNGYVL PEGECSHYAL NSGVESIKPP SDKAKHLLNT
410 420 430 440 450
IQSNFGTLPW CRRYLERTGE EKYLFALNQL VKAGIVEDYP PIVDKRGSYT
460 470
AQFEHTILLH PHKKEVVTRG DDY
Length:473
Mass (Da):52,168
Last modified:June 12, 2007 - v1
Checksum:i276295946A163975
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH981530 Genomic DNA. Translation: EDK46697.1.
RefSeqiXP_001524065.1. XM_001524015.1.

Genome annotation databases

GeneIDi5231111.
KEGGilel:LELG_04878.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH981530 Genomic DNA. Translation: EDK46697.1 .
RefSeqi XP_001524065.1. XM_001524015.1.

3D structure databases

ProteinModelPortali A5E5I9.
SMRi A5E5I9. Positions 112-473.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 36914.A5E5I9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5231111.
KEGGi lel:LELG_04878.

Phylogenomic databases

eggNOGi COG0024.
InParanoidi A5E5I9.
KOi K01265.
OMAi IQICEEL.
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 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239.

Entry informationi

Entry nameiMAP2_LODEL
AccessioniPrimary (citable) accession number: A5E5I9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: June 12, 2007
Last modified: November 26, 2014
This is version 51 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

External Data

Dasty 3