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Q9FV52

- MAP1B_ARATH

UniProt

Q9FV52 - MAP1B_ARATH

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Protein
Methionine aminopeptidase 1B, chloroplastic
Gene
MAP1B, At1g13270, T6J4.3
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

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 bindingi216 – 2161Divalent metal cation 1 By similarity
Metal bindingi227 – 2271Divalent metal cation 1 By similarity
Metal bindingi227 – 2271Divalent metal cation 2; catalytic By similarity
Metal bindingi290 – 2901Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei297 – 2971Substrate By similarity
Metal bindingi322 – 3221Divalent metal cation 2; catalytic By similarity
Metal bindingi353 – 3531Divalent metal cation 1 By similarity
Metal bindingi353 – 3531Divalent 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. 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:AT1G13270-MONOMER.
ARA:GQT-2392-MONOMER.

Protein family/group databases

MEROPSiM24.A05.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 1B, chloroplastic (EC:3.4.11.18)
Short name:
MAP 1B
Short name:
MetAP 1B
Alternative name(s):
Peptidase M 1B
Gene namesi
Name:MAP1B
Ordered Locus Names:At1g13270
ORF Names:T6J4.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G13270.

Subcellular locationi

Plastidchloroplast 1 Publication

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5555Chloroplast Reviewed prediction
Add
BLAST
Chaini56 – 369314Methionine aminopeptidase 1B, chloroplasticUniRule annotation
PRO_0000045805Add
BLAST

Proteomic databases

PaxDbiQ9FV52.
PRIDEiQ9FV52.

Expressioni

Tissue specificityi

Ubiquitous. Preferentially expressed in green tissues.1 Publication

Gene expression databases

ArrayExpressiQ9FV52.
GenevestigatoriQ9FV52.

Interactioni

Protein-protein interaction databases

BioGridi23127. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9FV52.
SMRiQ9FV52. Positions 91-367.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
InParanoidiQ9FV52.
KOiK01265.
OMAiATTYEAM.
PhylomeDBiQ9FV52.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 1 hit.
TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
PROSITEiPS00680. MAP_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9FV52-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MASSVFLSSF SSSSSLQLCS SFHGEYLAPS RCFLGAPVTS SSLSLSGKKN    50
SYSPRQFHVS AKKVSGLEEA IRIRKMRELE TKSKVRRNPP LRRGRVSPRL 100
LVPDHIPRPP YVESGVLPDI SSEFQIPGPE GIAKMRAACE LAARVLNYAG 150
TLVKPSVTTN EIDKAVHDMI IEAGAYPSPL GYGGFPKSVC TSVNECMCHG 200
IPDSRQLQSG DIINIDVTVY LDGYHGDTSR TFFCGEVDEG FKRLVKVTEE 250
CLERGIAVCK DGASFKKIGK RISEHAEKFG YNVVERFVGH GVGPVFHSEP 300
LIYHYRNDEP GLMVEGQTFT IEPILTIGTT ECVTWPDNWT TLTADGGVAA 350
QFEHTILITR TGSEILTKC 369
Length:369
Mass (Da):40,424
Last modified:January 24, 2006 - v2
Checksum:i0D28974852F33747
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341L → I in AAG33975. 1 Publication
Sequence conflicti243 – 2431R → Q in AAG33975. 1 Publication
Sequence conflicti254 – 2541R → K in AAG33975. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF250961 mRNA. Translation: AAG33975.1.
AC011810 Genomic DNA. Translation: AAG09564.1.
CP002684 Genomic DNA. Translation: AEE28993.1.
BT000449 mRNA. Translation: AAN17426.1.
BT001213 mRNA. Translation: AAN65100.1.
PIRiC86267.
RefSeqiNP_172785.1. NM_101198.3. [Q9FV52-1]
UniGeneiAt.21097.

Genome annotation databases

EnsemblPlantsiAT1G13270.1; AT1G13270.1; AT1G13270. [Q9FV52-1]
GeneIDi837887.
KEGGiath:AT1G13270.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF250961 mRNA. Translation: AAG33975.1 .
AC011810 Genomic DNA. Translation: AAG09564.1 .
CP002684 Genomic DNA. Translation: AEE28993.1 .
BT000449 mRNA. Translation: AAN17426.1 .
BT001213 mRNA. Translation: AAN65100.1 .
PIRi C86267.
RefSeqi NP_172785.1. NM_101198.3. [Q9FV52-1 ]
UniGenei At.21097.

3D structure databases

ProteinModelPortali Q9FV52.
SMRi Q9FV52. Positions 91-367.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 23127. 1 interaction.

Protein family/group databases

MEROPSi M24.A05.

Proteomic databases

PaxDbi Q9FV52.
PRIDEi Q9FV52.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G13270.1 ; AT1G13270.1 ; AT1G13270 . [Q9FV52-1 ]
GeneIDi 837887.
KEGGi ath:AT1G13270.

Organism-specific databases

GeneFarmi 2345. 184.
TAIRi AT1G13270.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000030427.
InParanoidi Q9FV52.
KOi K01265.
OMAi ATTYEAM.
PhylomeDBi Q9FV52.

Enzyme and pathway databases

BioCyci ARA:AT1G13270-MONOMER.
ARA:GQT-2392-MONOMER.

Gene expression databases

ArrayExpressi Q9FV52.
Genevestigatori Q9FV52.

Family and domain databases

Gene3Di 3.90.230.10. 1 hit.
HAMAPi MF_01974. MetAP_1.
InterProi IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view ]
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SUPFAMi SSF55920. SSF55920. 1 hit.
TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
PROSITEi PS00680. MAP_1. 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. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [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.
    , 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 nameiMAP1B_ARATH
AccessioniPrimary (citable) accession number: Q9FV52
Secondary accession number(s): Q9FX70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 24, 2006
Last modified: June 11, 2014
This is version 95 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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