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Q56Y85 (AMP2B_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionine aminopeptidase 2B

Short name=MAP 2B
Short name=MetAP 2B
EC=3.4.11.18
Alternative name(s):
Peptidase M 2B
Gene names
Name:MAP2B
Ordered Locus Names:At3g59990
ORF Names:F24G16.26
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Removes the amino-terminal methionine from nascent proteins By similarity.

Catalytic activity

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.

Cofactor

Binds 2 cobalt ions per subunit. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions By similarity.

Subcellular location

Cytoplasm Ref.1.

Tissue specificity

Ubiquitous. Preferentially expressed in roots. Ref.1

Sequence similarities

Belongs to the peptidase M24A family.

Sequence caution

The sequence BAD94472.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAB75818.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 439439Methionine aminopeptidase 2B
PRO_0000148971

Regions

Compositional bias61 – 7313Lys-rich

Sites

Metal binding2121Cobalt 1 By similarity
Metal binding2231Cobalt 1 By similarity
Metal binding2231Cobalt 2 By similarity
Metal binding2921Cobalt 2 By similarity
Metal binding3251Cobalt 2 By similarity
Metal binding4201Cobalt 1 By similarity
Metal binding4201Cobalt 2 By similarity
Binding site1921Substrate By similarity
Binding site3001Substrate By similarity

Experimental info

Sequence conflict2701E → K in AAL38337. Ref.4
Sequence conflict2701E → K in AAN15382. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q56Y85 [UniParc].

Last modified January 24, 2006. Version 2.
Checksum: EC1C79EA1B49D3BF

FASTA43949,060
        10         20         30         40         50         60 
MASESPDVAV VAPVVENGGA ESSNGKEEQL ESELSKKLEI AEDGQEENDG EEGSKAETST 

        70         80         90        100        110        120 
KKKKKKNKSK KKKELPQQTD PPSIPVVELF PSGEFPEGEI QEYKDDNLWR TTSEEKRELE 

       130        140        150        160        170        180 
RFEKPIYNSV RRAAEVHRQV RKYVRSIVKP GMLMTDICET LENTVRKLIS ENGLQAGIAF 

       190        200        210        220        230        240 
PTGCSLNWVA AHWTPNSGDK TVLQYDDVMK LDFGTHIDGH IIDCAFTVAF NPMFDPLLAA 

       250        260        270        280        290        300 
SREATYTGIK EAGIDVRLCD IGAAIQEVME SYEVEINGKV FQVKSIRNLN GHSIGPYQIH 

       310        320        330        340        350        360 
AGKSVPIVKG GEQTKMEEGE FYAIETFGST GKGYVREDLE CSHYMKNFDA GHVPLRLPRA 

       370        380        390        400        410        420 
KQLLATINKN FSTLAFCRRY LDRIGETKYL MALKNLCDSG IVQPYPPLCD VKGSYVSQFE 

       430 
HTILLRPTCK EVLSKGDDY 

« Hide

References

« Hide 'large scale' references
[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: 11060042] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[2]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed: 11130713] [Abstract]
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. expand/collapse author list , 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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 263-439.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF300880 mRNA. Translation: AAG34551.1.
AL138647 Genomic DNA. Translation: CAB75818.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE79996.1.
CP002686 Genomic DNA. Translation: AEE79997.1.
CP002686 Genomic DNA. Translation: AEE79998.1.
CP002686 Genomic DNA. Translation: AEE79999.1.
AY065161 mRNA. Translation: AAL38337.1.
BT000063 mRNA. Translation: AAN15382.1.
AY084710 mRNA. Translation: AAM61284.1.
AK221438 mRNA. Translation: BAD94472.1. Different initiation.
IPIIPI00536551.
PIRT47823.
RefSeqNP_001030898.1. NM_001035821.1.
NP_001190139.1. NM_001203210.1.
NP_567089.1. NM_115862.3.
NP_850725.1. NM_180394.1.
UniGeneAt.16912.

3D structure databases

ProteinModelPortalQ56Y85.
SMRQ56Y85. Positions 78-439.
ModBaseSearch...

Protein family/group databases

MEROPSM24.002.

Proteomic databases

PRIDEQ56Y85.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G59990.1; AT3G59990.1; AT3G59990.
AT3G59990.2; AT3G59990.2; AT3G59990.
AT3G59990.3; AT3G59990.3; AT3G59990.
AT3G59990.4; AT3G59990.4; AT3G59990.
GeneID825169.
GenomeReviewsGene locus AT3G59990 in contig BA000014_GR.
KEGGath:AT3G59990.
NMPDRfig|3702.1.peg.17359.

Organism-specific databases

GeneFarm1944. 191.
TAIRAt3g59990.

Phylogenomic databases

eggNOGKOG2775.
GeneTreeEPGT00070000029106.
HOGENOMHBG318153.
InParanoidQ56Y85.
OMAVKGCYTA.
PhylomeDBQ56Y85.
ProtClustDBCLSN2688923.

Gene expression databases

GenevestigatorQ56Y85.
GermOnlineAT3G59990. Arabidopsis thaliana.

Family and domain databases

InterProIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002468. Pept_M24A_MAP2.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]
Gene3DG3DSA:3.90.230.10. Peptidase_M24_cat_core. 2 hits.
G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KOK01265.
PANTHERPTHR10804:SF9. Pept_M24A_MAP2. 1 hit.
PfamPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSPR00599. MAPEPTIDASE.
SUPFAMSSF55920. Peptidase_M24_cat_core. 1 hit.
TIGRFAMsTIGR00501. Met_pdase_II. 1 hit.
PROSITEPS01202. MAP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMP2B_ARATH
AccessionPrimary (citable) accession number: Q56Y85
Secondary accession number(s): Q8VZ89, Q9FPV8, Q9M1X7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 24, 2006
Last modified: November 16, 2011
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families