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Q9FV49

- MAP21_ARATH

UniProt

Q9FV49 - MAP21_ARATH

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Protein
Methionine aminopeptidase 2A
Gene
MAP2A, At2g44180, F6E13.31
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

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 sitei194 – 1941Substrate By similarity
Metal bindingi214 – 2141Divalent metal cation 1 By similarity
Metal bindingi225 – 2251Divalent metal cation 1 By similarity
Metal bindingi225 – 2251Divalent metal cation 2; catalytic By similarity
Metal bindingi294 – 2941Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei302 – 3021Substrate By similarity
Metal bindingi327 – 3271Divalent metal cation 2; catalytic By similarity
Metal bindingi422 – 4221Divalent metal cation 1 By similarity
Metal bindingi422 – 4221Divalent 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. N-terminal protein amino acid modification Source: TAIR
  2. protein initiator methionine removal Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciARA:AT2G44180-MONOMER.

Protein family/group databases

MEROPSiM24.A02.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2A (EC:3.4.11.18)
Short name:
MAP 2A
Short name:
MetAP 2A
Alternative name(s):
Peptidase M
Gene namesi
Name:MAP2A
Ordered Locus Names:At2g44180
ORF Names:F6E13.31
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 2

Organism-specific databases

TAIRiAT2G44180.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Methionine aminopeptidase 2AUniRule annotation
PRO_0000148970Add
BLAST

Proteomic databases

PaxDbiQ9FV49.
PRIDEiQ9FV49.

Expressioni

Tissue specificityi

Ubiquitous. Preferentially expressed in roots.1 Publication

Gene expression databases

ArrayExpressiQ9FV49.
GenevestigatoriQ9FV49.

Structurei

3D structure databases

ProteinModelPortaliQ9FV49.
SMRiQ9FV49. Positions 80-441.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi63 – 7513Lys-richUniRule annotation
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000226278.
InParanoidiQ9FV49.
KOiK01265.
OMAiERYKLHA.
PhylomeDBiQ9FV49.

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.

Q9FV49-1 [UniParc]FASTAAdd to Basket

« Hide

MAIGNPEVAT MGKENTEAES SNGNESQLSS DLTKSLDLAE VKEDEKDNNQ    50
EEEDGLKAEA STKKKKKKSK SKKKKSSLQQ TDPPSIPVLE LFPSGDFPQG 100
EIQQYNDDNL WRTTSEEKRE MERLQKPIYN SLRQAAEVHR QVRKYMRSIL 150
KPGMLMIDLC ETLENTVRKL ISENGLQAGI AFPTGCSLNN VAAHWTPNSG 200
DKTVLQYDDV MKLDFGTHID GHIVDSAFTV AFNPMFDPLL AASRDATYTG 250
IKEAGVDVRL CDVGAAVQEV MESYEVEING KVYQVKSIRN LNGHSIGRYQ 300
IHAEKSVPNV RGGEQTKMEE GELYAIETFG STGKGYVRED LECSHYMKNY 350
DVGHVPLRLP RAKQLLATIN KNFSTLAFCR RYLDRLGETK YLMALKNLCD 400
SGIIEPCPPV CDVKGSYISQ FEHTILLRPT CKEIISKGDD Y 441
Length:441
Mass (Da):49,395
Last modified:January 24, 2006 - v2
Checksum:iFEC98F6679F0D573
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121G → E in AAG33978. 1 Publication
Sequence conflicti51 – 511Missing in AAG33978. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF250964 mRNA. Translation: AAG33978.1.
AC004005 Genomic DNA. Translation: AAC23422.2.
CP002685 Genomic DNA. Translation: AEC10386.1.
BT006476 mRNA. Translation: AAP21284.1.
PIRiT00698.
RefSeqiNP_566013.1. NM_129981.4.
UniGeneiAt.19509.

Genome annotation databases

EnsemblPlantsiAT2G44180.1; AT2G44180.1; AT2G44180.
GeneIDi819025.
KEGGiath:AT2G44180.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF250964 mRNA. Translation: AAG33978.1 .
AC004005 Genomic DNA. Translation: AAC23422.2 .
CP002685 Genomic DNA. Translation: AEC10386.1 .
BT006476 mRNA. Translation: AAP21284.1 .
PIRi T00698.
RefSeqi NP_566013.1. NM_129981.4.
UniGenei At.19509.

3D structure databases

ProteinModelPortali Q9FV49.
SMRi Q9FV49. Positions 80-441.
ModBasei Search...

Protein family/group databases

MEROPSi M24.A02.

Proteomic databases

PaxDbi Q9FV49.
PRIDEi Q9FV49.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT2G44180.1 ; AT2G44180.1 ; AT2G44180 .
GeneIDi 819025.
KEGGi ath:AT2G44180.

Organism-specific databases

GeneFarmi 1935. 191.
TAIRi AT2G44180.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000226278.
InParanoidi Q9FV49.
KOi K01265.
OMAi ERYKLHA.
PhylomeDBi Q9FV49.

Enzyme and pathway databases

BioCyci ARA:AT2G44180-MONOMER.

Gene expression databases

ArrayExpressi Q9FV49.
Genevestigatori Q9FV49.

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

« Hide 'large scale' publications
  1. "Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms."
    Giglione C., Serero A., Pierre M., Boisson B., Meinnel T.
    EMBO J. 19:5916-5929(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.

Entry informationi

Entry nameiMAP21_ARATH
AccessioniPrimary (citable) accession number: Q9FV49
Secondary accession number(s): O80587
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 24, 2006
Last modified: May 14, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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