Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9LJL3

- PREP1_ARATH

UniProt

Q9LJL3 - PREP1_ARATH

Protein

Presequence protease 1, chloroplastic/mitochondrial

Gene

PREP1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (19 Sep 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    ATP-independent protease that degrades both mitochondrial and chloroplastic transit peptides after their cleavage. Also degrades other unstructured peptides. Specific for peptides in the range of 10 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, with a bias for positively charged amino acid residues.1 Publication

    Cofactori

    Binds 1 zinc ion per subunit.
    Binds 2 Magnesium ions per subunit.

    Enzyme regulationi

    Inactive in the absence of MgCl2 and CaCl2 and full activation at 10 mM concentrations of either ion. Completely inhibited by the metal chelator orthophenanthroline, but not affected by phenylmethylsulfonyl fluoride (PMSF) or N-ethylmaleimide (NEM).

    pH dependencei

    Active from pH 4 to 10.

    Temperature dependencei

    Optimum temperature is 28 degrees Celsius. Active from 4 to 40 degrees Celsius.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi162 – 1621Zinc; catalytic
    Active sitei165 – 1651Proton acceptor
    Metal bindingi166 – 1661Zinc; catalytic
    Metal bindingi262 – 2621Zinc; catalytic

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. metalloendopeptidase activity Source: TAIR
    3. protein binding Source: IntAct

    GO - Biological processi

    1. protein processing Source: TAIR
    2. response to cadmium ion Source: TAIR

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Magnesium, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciARA:GQT-1641-MONOMER.
    ARA:GQT-1642-MONOMER.

    Protein family/group databases

    MEROPSiM16.012.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Presequence protease 1, chloroplastic/mitochondrial (EC:3.4.24.-)
    Short name:
    AtPreP1
    Short name:
    PreP 1
    Alternative name(s):
    Zinc metalloprotease 1
    Short name:
    AtZnMP1
    Gene namesi
    Name:PREP1
    Synonyms:ZNMP1
    Ordered Locus Names:At3g19170
    ORF Names:MVI11.6, MVI11.7, MVI11_8
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G19170.

    Subcellular locationi

    GO - Cellular componenti

    1. apoplast Source: TAIR
    2. chloroplast Source: TAIR
    3. chloroplast envelope Source: TAIR
    4. chloroplast stroma Source: TAIR
    5. mitochondrial matrix Source: UniProtKB-SubCell
    6. mitochondrion Source: TAIR

    Keywords - Cellular componenti

    Chloroplast, Mitochondrion, Plastid

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi162 – 1621H → L: Loss of activity. 1 Publication
    Mutagenesisi165 – 1651E → Q: Loss of activity. 1 Publication
    Mutagenesisi166 – 1661H → L: Loss of activity. 1 Publication
    Mutagenesisi179 – 1791E → Q: Decreased activity toward some substrates. 1 Publication
    Mutagenesisi194 – 1941N → A: Reduced activity. 1 Publication
    Mutagenesisi240 – 2401E → Q: Decreased activity toward some substrates. 1 Publication
    Mutagenesisi245 – 2451E → Q: No loss of activity. 1 Publication
    Mutagenesisi256 – 2561K → C: Inactive under oxidizing conditions and fully active under reducing conditions; when associated with C-937. 1 Publication
    Mutagenesisi262 – 2621E → Q: Loss of activity. 1 Publication
    Mutagenesisi264 – 2641K → C: Inactive under oxidizing conditions and fully active under reducing conditions; when associated with C-895. 1 Publication
    Mutagenesisi416 – 4161A → C: Little or no effect; when associated with C-700. 1 Publication
    Mutagenesisi430 – 4301E → C: Inactive under oxidizing conditions and fully active under reducing conditions; when associated with C-767. 1 Publication
    Mutagenesisi700 – 7001N → C: Little or no effect; when associated with C-416. 1 Publication
    Mutagenesisi767 – 7671S → C: Inactive under oxidizing conditions and fully active under reducing conditions; when associated with C-430. 1 Publication
    Mutagenesisi895 – 8951Q → C: Inactive under oxidizing conditions and fully active under reducing conditions; when associated with C-264. 1 Publication
    Mutagenesisi933 – 9331R → A or K: Loss of activity. 1 Publication
    Mutagenesisi937 – 9371G → C: Inactive under oxidizing conditions and fully active under reducing conditions; when associated with C-256. 1 Publication
    Mutagenesisi939 – 9391Y → F: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 8484Chloroplast and mitochondrionSequence AnalysisAdd
    BLAST
    Chaini85 – 1080996Presequence protease 1, chloroplastic/mitochondrialPRO_0000249938Add
    BLAST

    Proteomic databases

    PaxDbiQ9LJL3.
    PRIDEiQ9LJL3.

    Expressioni

    Tissue specificityi

    Expressed only in siliques and flowers.1 Publication

    Gene expression databases

    ArrayExpressiQ9LJL3.
    GenevestigatoriQ9LJL3.

    Interactioni

    Subunit structurei

    Homodimer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATPBP176146EBI-7143359,EBI-7143406From a different organism.

    Protein-protein interaction databases

    IntActiQ9LJL3. 4 interactions.
    MINTiMINT-7231907.

    Structurei

    Secondary structure

    1
    1080
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi101 – 1044
    Beta strandi107 – 1159
    Turni116 – 1194
    Beta strandi120 – 1278
    Turni128 – 1303
    Beta strandi133 – 1386
    Beta strandi142 – 15110
    Beta strandi155 – 1584
    Helixi160 – 1678
    Helixi180 – 1878
    Beta strandi190 – 1934
    Beta strandi199 – 21012
    Helixi211 – 22616
    Helixi229 – 2313
    Helixi235 – 2406
    Beta strandi243 – 2453
    Beta strandi254 – 2563
    Helixi258 – 2669
    Helixi270 – 28213
    Helixi287 – 2893
    Turni296 – 2983
    Helixi299 – 3013
    Helixi304 – 31411
    Helixi317 – 3193
    Beta strandi320 – 3289
    Helixi330 – 34112
    Helixi349 – 3524
    Beta strandi365 – 3728
    Beta strandi375 – 3773
    Helixi379 – 3813
    Beta strandi383 – 3908
    Helixi398 – 41215
    Helixi418 – 4258
    Beta strandi430 – 4323
    Beta strandi436 – 4383
    Beta strandi440 – 4434
    Beta strandi445 – 4539
    Helixi455 – 4573
    Helixi458 – 47518
    Helixi479 – 49517
    Helixi503 – 51513
    Turni516 – 5183
    Helixi523 – 5253
    Helixi528 – 54114
    Helixi543 – 55412
    Turni555 – 5573
    Beta strandi561 – 5699
    Helixi572 – 58918
    Helixi593 – 61018
    Helixi616 – 6194
    Helixi627 – 6293
    Beta strandi640 – 65314
    Beta strandi657 – 66711
    Turni673 – 6753
    Helixi676 – 6783
    Helixi679 – 68810
    Beta strandi692 – 6943
    Helixi696 – 70611
    Beta strandi707 – 71913
    Beta strandi722 – 73615
    Helixi737 – 7393
    Helixi740 – 75314
    Helixi759 – 77921
    Helixi781 – 79111
    Helixi795 – 80410
    Helixi806 – 82116
    Helixi823 – 83715
    Beta strandi844 – 8496
    Helixi851 – 86616
    Beta strandi888 – 8914
    Beta strandi895 – 90410
    Helixi905 – 9084
    Helixi915 – 92511
    Helixi927 – 9315
    Turni932 – 9365
    Beta strandi939 – 9468
    Turni947 – 9504
    Beta strandi951 – 96010
    Helixi963 – 9708
    Helixi972 – 9776
    Helixi983 – 99715
    Helixi1003 – 101513
    Helixi1020 – 103112
    Helixi1035 – 105117
    Beta strandi1053 – 10586
    Helixi1060 – 106910
    Turni1070 – 10723
    Beta strandi1074 – 10774

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FGEX-ray2.10A/B86-1080[»]
    ProteinModelPortaliQ9LJL3.
    SMRiQ9LJL3. Positions 100-1078.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9LJL3.

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili571 – 61242Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase M16 family. PreP subfamily.Curated

    Keywords - Domaini

    Coiled coil, Transit peptide

    Phylogenomic databases

    eggNOGiCOG1026.
    HOGENOMiHOG000008829.
    InParanoidiQ9LJL3.
    KOiK06972.
    OMAiANNERSN.
    PhylomeDBiQ9LJL3.

    Family and domain databases

    Gene3Di3.30.830.10. 2 hits.
    InterProiIPR011249. Metalloenz_LuxS/M16.
    IPR011237. Pept_M16_dom.
    IPR011765. Pept_M16_N.
    IPR007863. Peptidase_M16_C.
    IPR013578. Peptidase_M16C_assoc.
    [Graphical view]
    PfamiPF08367. M16C_assoc. 1 hit.
    PF00675. Peptidase_M16. 1 hit.
    PF05193. Peptidase_M16_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF63411. SSF63411. 4 hits.

    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: Q9LJL3-1) [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

    MLRTVSCLAS RSSSSLFFRF FRQFPRSYMS LTSSTAALRV PSRNLRRISS     50
    PSVAGRRLLL RRGLRIPSAA VRSVNGQFSR LSVRAVATQP APLYPDVGQD 100
    EAEKLGFEKV SEEFISECKS KAILFKHKKT GCEVMSVSNE DENKVFGVVF 150
    RTPPKDSTGI PHILEHSVLC GSRKYPVKEP FVELLKGSLH TFLNAFTYPD 200
    RTCYPVASTN TKDFYNLVDV YLDAVFFPKC VDDAHTFQQE GWHYELNDPS 250
    EDISYKGVVF NEMKGVYSQP DNILGRIAQQ ALSPENTYGV DSGGDPKDIP 300
    NLTFEEFKEF HRQYYHPSNA RIWFYGDDDP VHRLRVLSEY LDMFEASPSP 350
    NSSKIKFQKL FSEPVRLVEK YPAGRDGDLK KKHMLCVNWL LSEKPLDLQT 400
    QLALGFLDHL MLGTPASPLR KILLESGLGE ALVSSGLSDE LLQPQFGIGL 450
    KGVSEENVQK VEELIMDTLK KLAEEGFDND AVEASMNTIE FSLRENNTGS 500
    FPRGLSLMLQ SISKWIYDMD PFEPLKYTEP LKALKTRIAE EGSKAVFSPL 550
    IEKLILNNSH RVTIEMQPDP EKATQEEVEE KNILEKVKAA MTEEDLAELA 600
    RATEELKLKQ ETPDPPEALR CVPSLNLGDI PKEPTYVPTE VGDINGVKVL 650
    RHDLFTNDII YTEVVFDIGS LKHELLPLVP LFCQSLLEMG TKDLTFVQLN 700
    QLIGRKTGGI SVYPLTSSVR GKDEPCSKII VRGKSMAGRA DDLFNLMNCL 750
    LQEVQFTDQQ RFKQFVSQSR ARMENRLRGS GHGIAAARMD AMLNIAGWMS 800
    EQMGGLSYLE FLHTLEKKVD EDWEGISSSL EEIRRSLLAR NGCIVNMTAD 850
    GKSLTNVEKS VAKFLDLLPE NPSGGLVTWD GRLPLRNEAI VIPTQVNYVG 900
    KAGNIYSTGY ELDGSAYVIS KHISNTWLWD RVRVSGGAYG GFCDFDSHSG 950
    VFSYLSYRDP NLLKTLDIYD GTGDFLRGLD VDQETLTKAI IGTIGDVDSY 1000
    QLPDAKGYSS LLRHLLGVTD EERQRKREEI LTTSLKDFKD FAQAIDVVRD 1050
    KGVAVAVASA EDIDAANNER SNFFEVKKAL 1080
    Length:1,080
    Mass (Da):121,015
    Last modified:September 19, 2006 - v2
    Checksum:i9FD259970195B9FC
    GO

    Sequence cautioni

    The sequence BAB02957.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP000419 Genomic DNA. Translation: BAB02957.1. Different initiation.
    CP002686 Genomic DNA. Translation: AEE76201.1.
    AY090240 mRNA. Translation: AAL90904.1.
    AY091051 mRNA. Translation: AAM13872.1.
    BT006362 mRNA. Translation: AAP21170.1.
    BT002372 mRNA. Translation: AAN86205.1.
    RefSeqiNP_188548.2. NM_112804.4. [Q9LJL3-1]
    UniGeneiAt.27915.

    Genome annotation databases

    EnsemblPlantsiAT3G19170.1; AT3G19170.1; AT3G19170. [Q9LJL3-1]
    GeneIDi821451.
    KEGGiath:AT3G19170.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP000419 Genomic DNA. Translation: BAB02957.1 . Different initiation.
    CP002686 Genomic DNA. Translation: AEE76201.1 .
    AY090240 mRNA. Translation: AAL90904.1 .
    AY091051 mRNA. Translation: AAM13872.1 .
    BT006362 mRNA. Translation: AAP21170.1 .
    BT002372 mRNA. Translation: AAN86205.1 .
    RefSeqi NP_188548.2. NM_112804.4. [Q9LJL3-1 ]
    UniGenei At.27915.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FGE X-ray 2.10 A/B 86-1080 [» ]
    ProteinModelPortali Q9LJL3.
    SMRi Q9LJL3. Positions 100-1078.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9LJL3. 4 interactions.
    MINTi MINT-7231907.

    Protein family/group databases

    MEROPSi M16.012.

    Proteomic databases

    PaxDbi Q9LJL3.
    PRIDEi Q9LJL3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G19170.1 ; AT3G19170.1 ; AT3G19170 . [Q9LJL3-1 ]
    GeneIDi 821451.
    KEGGi ath:AT3G19170.

    Organism-specific databases

    GeneFarmi 2137. 225.
    TAIRi AT3G19170.

    Phylogenomic databases

    eggNOGi COG1026.
    HOGENOMi HOG000008829.
    InParanoidi Q9LJL3.
    KOi K06972.
    OMAi ANNERSN.
    PhylomeDBi Q9LJL3.

    Enzyme and pathway databases

    BioCyci ARA:GQT-1641-MONOMER.
    ARA:GQT-1642-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q9LJL3.
    PROi Q9LJL3.

    Gene expression databases

    ArrayExpressi Q9LJL3.
    Genevestigatori Q9LJL3.

    Family and domain databases

    Gene3Di 3.30.830.10. 2 hits.
    InterProi IPR011249. Metalloenz_LuxS/M16.
    IPR011237. Pept_M16_dom.
    IPR011765. Pept_M16_N.
    IPR007863. Peptidase_M16_C.
    IPR013578. Peptidase_M16C_assoc.
    [Graphical view ]
    Pfami PF08367. M16C_assoc. 1 hit.
    PF00675. Peptidase_M16. 1 hit.
    PF05193. Peptidase_M16_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF63411. SSF63411. 4 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones."
      Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.
      DNA Res. 7:217-221(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "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.
    4. "Isolation and identification of a novel mitochondrial metalloprotease (PreP) that degrades targeting presequences in plants."
      Staahl A., Moberg P., Ytterberg J., Panfilov O., Brockenhuus Von Lowenhielm H., Nilsson F., Glaser E.
      J. Biol. Chem. 277:41931-41939(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
    5. "Characterization of a novel zinc metalloprotease involved in degrading targeting peptides in mitochondria and chloroplasts."
      Moberg P., Staahl A., Bhushan S., Wright S.J., Eriksson A., Bruce B.D., Glaser E.
      Plant J. 36:616-628(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MUTAGENESIS OF HIS-162; GLU-165; HIS-166; GLU-240 AND GLU-245, SUBCELLULAR LOCATION.
    6. "Catalysis, subcellular localization, expression and evolution of the targeting peptides degrading protease, AtPreP2."
      Bhushan S., Staahl A., Nilsson S., Lefebvre B., Seki M., Roth C., McWilliam D., Wright S.J., Liberles D.A., Shinozaki K., Bruce B.D., Boutry M., Glaser E.
      Plant Cell Physiol. 46:985-996(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    7. "Two novel targeting peptide degrading proteases, PrePs, in mitochondria and chloroplasts, so similar and still different."
      Staahl A., Nilsson S., Lundberg P., Bhushan S., Biverstaahl H., Moberg P., Morisset M., Vener A., Maeler L., Langel U., Glaser E.
      J. Mol. Biol. 349:847-860(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE SPECIFICITY.
    8. "The closed structure of presequence protease PreP forms a unique 10,000 Angstroms3 chamber for proteolysis."
      Johnson K.A., Bhushan S., Staahl A., Hallberg B.M., Frohn A., Glaser E., Eneqvist T.
      EMBO J. 25:1977-1986(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 86-1080, MUTAGENESIS OF GLU-179; ASN-194; LYS-256; GLU-262; LYS-264; ALA-416; GLU-430; ASN-700; SER-767; GLN-895; ARG-933; GLY-937 AND TYR-939.

    Entry informationi

    Entry nameiPREP1_ARATH
    AccessioniPrimary (citable) accession number: Q9LJL3
    Secondary accession number(s): Q8RUN6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2006
    Last sequence update: September 19, 2006
    Last modified: October 1, 2014
    This is version 93 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The 2 enzymes halves enclose a large proteolytic chamber spacious enough to hold peptide substrates, but sufficiently small to exclude larger, folded proteins. Since the active site includes residues from both the N- and C-terminal part of the protein, proteolysis can occur only when the chamber is closed. Covalently locking the 2 halves of the protease with disulfide bonds induces a loss of activity.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3