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P49040

- SUSY1_ARATH

UniProt

P49040 - SUSY1_ARATH

Protein

Sucrose synthase 1

Gene

SUS1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 3 (14 Apr 2009)
      Previous versions | rss
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    Functioni

    Sucrose-cleaving enzyme that provides UDP-glucose and fructose for various metabolic pathways.1 Publication

    Catalytic activityi

    NDP-glucose + D-fructose = NDP + sucrose.

    Kineticsi

    1. KM=4.37 mM for D-fructose (synthetic reaction) at pH 9.42 Publications
    2. KM=0.04 mM for UDP-glucose (synthetic reaction) at pH 9.42 Publications
    3. KM=31.58 mM for sucrose (degradative reaction) at pH 62 Publications
    4. KM=53 mM for sucrose (degradative reaction) at pH 72 Publications
    5. KM=0.08 mM for UDP (degradative reaction) at pH 62 Publications
    6. KM=0.39 mM for UDP (degradative reaction) at pH 72 Publications
    7. KM=0.17 mM for ADP (degradative reaction) at pH 72 Publications

    Vmax=11.14 µmol/min/mg enzyme for synthetic reaction at pH 9.42 Publications

    Vmax=4.68 µmol/min/mg enzyme for degradative reaction at pH 62 Publications

    Vmax=585 µmol/min/mg enzyme for degradative reaction at pH 72 Publications

    pH dependencei

    Optimum pH is 6.0-7.0 for degradative reaction and 7.0 (PubMed:22184213) or 9.0-9.5 (PubMed:17257168) for synthetic reaction.2 Publications

    GO - Molecular functioni

    1. sucrose synthase activity Source: UniProtKB

    GO - Biological processi

    1. biosynthetic process Source: InterPro
    2. response to cadmium ion Source: TAIR
    3. response to cold Source: UniProtKB
    4. response to flooding Source: TAIR
    5. response to glucose Source: UniProtKB
    6. response to hypoxia Source: UniProtKB
    7. response to mannitol Source: UniProtKB
    8. response to osmotic stress Source: TAIR
    9. response to sorbitol Source: UniProtKB
    10. response to sucrose Source: UniProtKB
    11. response to water deprivation Source: UniProtKB
    12. sucrose metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    BioCyciARA:AT5G20830-MONOMER.
    ARA:GQT-1272-MONOMER.
    MetaCyc:AT5G20830-MONOMER.

    Protein family/group databases

    CAZyiGT4. Glycosyltransferase Family 4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sucrose synthase 1 (EC:2.4.1.13)
    Short name:
    AtSUS1
    Alternative name(s):
    Sucrose-UDP glucosyltransferase 1
    Gene namesi
    Name:SUS1
    Ordered Locus Names:At5g20830
    ORF Names:T1M15.230
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G20830.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: TAIR
    2. plasmodesma Source: TAIR

    Pathology & Biotechi

    Biotechnological usei

    A one-pot system for efficient enzymatic production of a wide range of glucosides couples the activities of two recombinant enzymes, UDP-glucose: curcumin glucosyltransferase from Catharanthus roseus (CaUGT2) and sucrose synthase from Arabidopsis thaliana (AtSUS1). UDP, a product inhibitor of UDP-glucosyltransferase, was removed from the system and used for regeneration of UDP-glucose by the second enzyme, AtSUS1. The productivity was increased several-fold and UDP-glucose initially added to the reaction mixture could be reduced to one-tenth of the normal level.1 Publication

    Disruption phenotypei

    No visible phenotype.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 808808Sucrose synthase 1PRO_0000204644Add
    BLAST

    Proteomic databases

    PaxDbiP49040.
    PRIDEiP49040.

    Expressioni

    Tissue specificityi

    Expressed in the phloem of leaves and in roots. Detected in the whole plant but more precisely confined to the vasculature in cotyledons, mature leaves and siliques.4 Publications

    Inductioni

    By cold, drought and anaerobic stress. By sugar or osmoticum. By anoxia in the roots (at protein level). Up-regulated by NUC/IDD8.5 Publications

    Gene expression databases

    GenevestigatoriP49040.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi17481. 3 interactions.
    STRINGi3702.AT5G20830.1-P.

    Structurei

    Secondary structure

    1
    808
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi30 – 4011
    Beta strandi43 – 475
    Helixi48 – 536
    Turni54 – 585
    Helixi61 – 633
    Turni64 – 685
    Helixi69 – 746
    Beta strandi76 – 816
    Beta strandi83 – 9311
    Beta strandi96 – 1038
    Beta strandi109 – 1124
    Helixi114 – 12613
    Beta strandi136 – 1383
    Helixi140 – 1434
    Helixi152 – 1543
    Helixi158 – 16912
    Turni170 – 1723
    Helixi174 – 18613
    Beta strandi192 – 1965
    Helixi203 – 21917
    Helixi226 – 23510
    Helixi246 – 26116
    Helixi265 – 27410
    Beta strandi280 – 2845
    Beta strandi292 – 2943
    Helixi303 – 32523
    Beta strandi333 – 3397
    Beta strandi346 – 3483
    Beta strandi351 – 3555
    Beta strandi360 – 3678
    Beta strandi369 – 3713
    Beta strandi374 – 3763
    Turni382 – 3843
    Helixi386 – 3883
    Helixi389 – 40315
    Beta strandi409 – 4146
    Helixi415 – 42915
    Beta strandi433 – 4364
    Helixi441 – 4444
    Turni446 – 4516
    Helixi452 – 4598
    Helixi461 – 47414
    Beta strandi475 – 4817
    Helixi483 – 4875
    Beta strandi490 – 4923
    Helixi497 – 4993
    Beta strandi500 – 5045
    Turni505 – 5073
    Beta strandi508 – 5136
    Beta strandi521 – 5233
    Turni530 – 5323
    Turni539 – 5413
    Helixi544 – 5463
    Helixi547 – 5559
    Beta strandi563 – 5653
    Beta strandi570 – 5723
    Beta strandi574 – 5785
    Turni583 – 5864
    Helixi587 – 59610
    Helixi598 – 6036
    Beta strandi605 – 6095
    Helixi620 – 63516
    Beta strandi639 – 6457
    Helixi651 – 66313
    Beta strandi667 – 6704
    Beta strandi675 – 6773
    Helixi679 – 6868
    Beta strandi691 – 6977
    Helixi699 – 7024
    Turni705 – 7073
    Beta strandi710 – 7123
    Helixi717 – 73317
    Helixi736 – 75116
    Helixi755 – 77622
    Turni777 – 7793
    Helixi780 – 79314
    Helixi795 – 8017

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3S27X-ray2.91A/B/C/D/E/F/G/H1-808[»]
    3S28X-ray2.80A/B/C/D/E/F/G/H1-808[»]
    3S29X-ray2.85A/B/C/D/E/F/G/H1-808[»]
    ProteinModelPortaliP49040.
    SMRiP49040. Positions 27-807.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49040.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni277 – 754478GT-B glycosyltransferaseAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0438.
    HOGENOMiHOG000240125.
    InParanoidiP49040.
    KOiK00695.
    OMAiYQNDKAS.
    PhylomeDBiP49040.

    Family and domain databases

    InterProiIPR001296. Glyco_trans_1.
    IPR000368. Sucrose_synth.
    IPR012820. Sucrose_synthase_pln/cyn.
    [Graphical view]
    PfamiPF00534. Glycos_transf_1. 1 hit.
    PF00862. Sucrose_synth. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02470. sucr_synth. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P49040-1 [UniParc]FASTAAdd to Basket

    « Hide

    MANAERMITR VHSQRERLNE TLVSERNEVL ALLSRVEAKG KGILQQNQII    50
    AEFEALPEQT RKKLEGGPFF DLLKSTQEAI VLPPWVALAV RPRPGVWEYL 100
    RVNLHALVVE ELQPAEFLHF KEELVDGVKN GNFTLELDFE PFNASIPRPT 150
    LHKYIGNGVD FLNRHLSAKL FHDKESLLPL LKFLRLHSHQ GKNLMLSEKI 200
    QNLNTLQHTL RKAEEYLAEL KSETLYEEFE AKFEEIGLER GWGDNAERVL 250
    DMIRLLLDLL EAPDPCTLET FLGRVPMVFN VVILSPHGYF AQDNVLGYPD 300
    TGGQVVYILD QVRALEIEML QRIKQQGLNI KPRILILTRL LPDAVGTTCG 350
    ERLERVYDSE YCDILRVPFR TEKGIVRKWI SRFEVWPYLE TYTEDAAVEL 400
    SKELNGKPDL IIGNYSDGNL VASLLAHKLG VTQCTIAHAL EKTKYPDSDI 450
    YWKKLDDKYH FSCQFTADIF AMNHTDFIIT STFQEIAGSK ETVGQYESHT 500
    AFTLPGLYRV VHGIDVFDPK FNIVSPGADM SIYFPYTEEK RRLTKFHSEI 550
    EELLYSDVEN KEHLCVLKDK KKPILFTMAR LDRVKNLSGL VEWYGKNTRL 600
    RELANLVVVG GDRRKESKDN EEKAEMKKMY DLIEEYKLNG QFRWISSQMD 650
    RVRNGELYRY ICDTKGAFVQ PALYEAFGLT VVEAMTCGLP TFATCKGGPA 700
    EIIVHGKSGF HIDPYHGDQA ADTLADFFTK CKEDPSHWDE ISKGGLQRIE 750
    EKYTWQIYSQ RLLTLTGVYG FWKHVSNLDR LEARRYLEMF YALKYRPLAQ 800
    AVPLAQDD 808
    Length:808
    Mass (Da):92,998
    Last modified:April 14, 2009 - v3
    Checksum:iCDB56C6A57BD852E
    GO

    Sequence cautioni

    The sequence BAD94975.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 611R → Q in CAA50317. (PubMed:8220487)Curated
    Sequence conflicti108 – 1081V → L in CAA50317. (PubMed:8220487)Curated
    Sequence conflicti222 – 2221S → P in CAA50317. (PubMed:8220487)Curated
    Sequence conflicti405 – 4051N → D in CAA50317. (PubMed:8220487)Curated
    Sequence conflicti434 – 4341C → QC in CAA50317. (PubMed:8220487)Curated
    Sequence conflicti609 – 6091V → I in CAA50317. (PubMed:8220487)Curated
    Sequence conflicti751 – 7522EK → DE in CAA50317. (PubMed:8220487)Curated
    Sequence conflicti799 – 8002Missing in CAA50317. (PubMed:8220487)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70990 Genomic DNA. Translation: CAA50317.1.
    AF296832 Genomic DNA. No translation available.
    CP002688 Genomic DNA. Translation: AED92894.1.
    CP002688 Genomic DNA. Translation: AED92895.1.
    AK316826 mRNA. Translation: BAH19538.1.
    AK222090 mRNA. Translation: BAD94975.1. Different initiation.
    RefSeqiNP_001031915.1. NM_001036838.1.
    NP_197583.1. NM_122090.3.
    UniGeneiAt.21918.

    Genome annotation databases

    EnsemblPlantsiAT5G20830.1; AT5G20830.1; AT5G20830.
    AT5G20830.2; AT5G20830.2; AT5G20830.
    GeneIDi832206.
    KEGGiath:AT5G20830.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70990 Genomic DNA. Translation: CAA50317.1 .
    AF296832 Genomic DNA. No translation available.
    CP002688 Genomic DNA. Translation: AED92894.1 .
    CP002688 Genomic DNA. Translation: AED92895.1 .
    AK316826 mRNA. Translation: BAH19538.1 .
    AK222090 mRNA. Translation: BAD94975.1 . Different initiation.
    RefSeqi NP_001031915.1. NM_001036838.1.
    NP_197583.1. NM_122090.3.
    UniGenei At.21918.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3S27 X-ray 2.91 A/B/C/D/E/F/G/H 1-808 [» ]
    3S28 X-ray 2.80 A/B/C/D/E/F/G/H 1-808 [» ]
    3S29 X-ray 2.85 A/B/C/D/E/F/G/H 1-808 [» ]
    ProteinModelPortali P49040.
    SMRi P49040. Positions 27-807.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 17481. 3 interactions.
    STRINGi 3702.AT5G20830.1-P.

    Protein family/group databases

    CAZyi GT4. Glycosyltransferase Family 4.

    Proteomic databases

    PaxDbi P49040.
    PRIDEi P49040.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G20830.1 ; AT5G20830.1 ; AT5G20830 .
    AT5G20830.2 ; AT5G20830.2 ; AT5G20830 .
    GeneIDi 832206.
    KEGGi ath:AT5G20830.

    Organism-specific databases

    TAIRi AT5G20830.

    Phylogenomic databases

    eggNOGi COG0438.
    HOGENOMi HOG000240125.
    InParanoidi P49040.
    KOi K00695.
    OMAi YQNDKAS.
    PhylomeDBi P49040.

    Enzyme and pathway databases

    BioCyci ARA:AT5G20830-MONOMER.
    ARA:GQT-1272-MONOMER.
    MetaCyc:AT5G20830-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P49040.

    Gene expression databases

    Genevestigatori P49040.

    Family and domain databases

    InterProi IPR001296. Glyco_trans_1.
    IPR000368. Sucrose_synth.
    IPR012820. Sucrose_synthase_pln/cyn.
    [Graphical view ]
    Pfami PF00534. Glycos_transf_1. 1 hit.
    PF00862. Sucrose_synth. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02470. sucr_synth. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Expression of an Arabidopsis sucrose synthase gene indicates a role in metabolization of sucrose both during phloem loading and in sink organs."
      Martin T., Frommer W.B., Salanoubat M., Willmitzer L.
      Plant J. 4:367-377(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION.
      Strain: cv. C24.
    2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
      Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
      , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
      Nature 408:823-826(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. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
      Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
      DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "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.
      , 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 521-808.
      Strain: cv. Columbia.
    6. "Sugar/osmoticum levels modulate differential abscisic acid-independent expression of two stress-responsive sucrose synthase genes in Arabidopsis."
      Dejardin A., Sokolov L.N., Kleczkowski L.A.
      Biochem. J. 344:503-509(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    7. "Structure and expression profile of the sucrose synthase multigene family in Arabidopsis."
      Baud S., Vaultier M.N., Rochat C.
      J. Exp. Bot. 55:397-409(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, TISSUE SPECIFICITY, INDUCTION.
    8. "An efficient chemoenzymatic production of small molecule glucosides with in situ UDP-glucose recycling."
      Masada S., Kawase Y., Nagatoshi M., Oguchi Y., Terasaka K., Mizukami H.
      FEBS Lett. 581:2562-2566(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOTECHNOLOGY.
    9. Cited for: BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE.
    10. "Localization of sucrose synthase in developing seed and siliques of Arabidopsis thaliana reveals diverse roles for SUS during development."
      Fallahi H., Scofield G.N., Badger M.R., Chow W.S., Furbank R.T., Ruan Y.L.
      J. Exp. Bot. 59:3283-3295(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    11. "Modulation of sugar metabolism by an INDETERMINATE DOMAIN transcription factor contributes to photoperiodic flowering in Arabidopsis."
      Seo P.J., Ryu J., Kang S.K., Park C.M.
      Plant J. 65:418-429(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY NUC.
    12. "Sucrose synthase activity in the sus1/sus2/sus3/sus4 Arabidopsis mutant is sufficient to support normal cellulose and starch production."
      Baroja-Fernandez E., Munoz F.J., Li J., Bahaji A., Almagro G., Montero M., Etxeberria E., Hidalgo M., Sesma M.T., Pozueta-Romero J.
      Proc. Natl. Acad. Sci. U.S.A. 109:321-326(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    13. "The structure of sucrose synthase-1 from Arabidopsis thaliana and its functional implications."
      Zheng Y., Anderson S., Zhang Y., Garavito R.M.
      J. Biol. Chem. 286:36108-36118(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBUNIT, FUNCTION.

    Entry informationi

    Entry nameiSUSY1_ARATH
    AccessioniPrimary (citable) accession number: P49040
    Secondary accession number(s): B9DFM1, Q56WF2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: April 14, 2009
    Last modified: October 1, 2014
    This is version 106 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3