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)

O22265

- SR43C_ARATH

UniProt

O22265 - SR43C_ARATH

Protein

Signal recognition particle 43 kDa protein, chloroplastic

Gene

CAO

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 122 (01 Oct 2014)
      Sequence version 2 (01 Jun 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Component of the chloroplast signal recognition particle pathway. Required for post-translational targeting of proteins into the tylakoid membrane but seems to be dispensable for co-translational targeting with a translating ribosome present. May be able to function independently of cpFTSY and FFC/cpSRP54 in targeting LHCPs to the thylakoids. Acts as a highly specific chaperone for LHCPs, preventing aggregation and being able to dissolve aggregates.5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi232 – 2321Magnesium

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. protein import into chloroplast thylakoid membrane Source: TAIR
    2. response to high light intensity Source: TAIR

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Ligandi

    Metal-binding

    Protein family/group databases

    TCDBi3.A.5.1.2. the general secretory pathway (sec) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Signal recognition particle 43 kDa protein, chloroplastic
    Alternative name(s):
    Chromo protein SRP43
    Short name:
    CpSRP43
    Gene namesi
    Name:CAO
    Synonyms:CPSRP43
    Ordered Locus Names:At2g47450
    ORF Names:T30B22.25
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 2

    Organism-specific databases

    TAIRiAT2G47450.

    Subcellular locationi

    Plastidchloroplast stroma 1 Publication

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. chloroplast envelope Source: TAIR
    3. chloroplast stroma Source: UniProtKB-SubCell
    4. chloroplast thylakoid membrane Source: TAIR
    5. signal recognition particle, chloroplast targeting Source: TAIR
    6. signal recognition particle, endoplasmic reticulum targeting Source: UniProtKB-KW

    Keywords - Cellular componenti

    Chloroplast, Plastid, Signal recognition particle

    Pathology & Biotechi

    Disruption phenotypei

    Plants show a reduced level of the major light-harvesting chlorophyll a/b-binding proteins (LHCPs).1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi161 – 1611R → A: Decreased interaction with LHCP. 1 Publication
    Mutagenesisi192 – 1921R → A: Decreased interaction with LHCP. 1 Publication
    Mutagenesisi204 – 2041Y → A: Loss of interaction with LHCP. 1 Publication
    Mutagenesisi226 – 2261R → A: Decreased interaction with LHCP. 1 Publication
    Mutagenesisi269 – 2691Y → A: Decreased interaction with ALB3. 1 Publication
    Mutagenesisi291 – 2911W → A: Decreased interaction with ALB3. 1 Publication
    Mutagenesisi293 – 2931D → A: Decreased interaction with ALB3. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5656ChloroplastSequence AnalysisAdd
    BLAST
    Chaini57 – 373317Signal recognition particle 43 kDa protein, chloroplasticPRO_0000238461Add
    BLAST

    Proteomic databases

    PaxDbiO22265.
    PRIDEiO22265.

    Expressioni

    Tissue specificityi

    Expressed in leaves. Detected in roots.2 Publications

    Gene expression databases

    GenevestigatoriO22265.

    Interactioni

    Subunit structurei

    Homodimer. Component of the cpSRP complex, composed of a FFC/cpSRP54 monomer and a CAO/cpSRP43 dimer. Interacts (via chromo domains 2 and 3) with ALB3 (via C-terminus), but not with ALB3L1/ALB4. Can interact simultaneously with ALB3 and FFC/cpSRP54. Interacts with LHCP and LTD.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-780656,EBI-780656
    ALB3Q8LBP410EBI-780656,EBI-1806831
    CAB8P274904EBI-780656,EBI-8295162From a different organism.
    FFCP3710716EBI-780656,EBI-780642

    Protein-protein interaction databases

    BioGridi4693. 13 interactions.
    DIPiDIP-37639N.
    IntActiO22265. 19 interactions.
    MINTiMINT-126461.

    Structurei

    Secondary structure

    1
    373
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi86 – 9510
    Turni96 – 983
    Beta strandi99 – 1068
    Turni107 – 1104
    Beta strandi113 – 1164
    Helixi117 – 1193
    Helixi122 – 13716
    Helixi141 – 1477
    Turni148 – 1503
    Helixi163 – 1708
    Helixi173 – 1819
    Beta strandi191 – 1944
    Helixi197 – 2037
    Helixi207 – 21610
    Helixi230 – 23910
    Helixi246 – 26318
    Beta strandi267 – 28014
    Beta strandi281 – 2833
    Beta strandi286 – 29510
    Beta strandi297 – 3026
    Helixi307 – 31711
    Beta strandi328 – 3303
    Beta strandi332 – 3343
    Beta strandi344 – 3485
    Beta strandi357 – 3615
    Helixi362 – 3654

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X32NMR-A84-128[»]
    1X3PNMR-A320-373[»]
    1X3QNMR-A265-319[»]
    2HUGNMR-A265-319[»]
    3DEOX-ray1.50A85-267[»]
    3DEPX-ray2.70A85-267[»]
    3UI2X-ray3.18A84-327[»]
    ProteinModelPortaliO22265.
    SMRiO22265. Positions 31-318, 320-373.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO22265.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini84 – 13552Chromo 1PROSITE-ProRule annotationAdd
    BLAST
    Repeati136 – 15823ANK 1Add
    BLAST
    Repeati159 – 18830ANK 2Add
    BLAST
    Repeati193 – 22230ANK 3Add
    BLAST
    Repeati242 – 26928ANK 4Add
    BLAST
    Domaini270 – 32051Chromo 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini321 – 37353Chromo 3PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili57 – 7923Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi79 – 824Poly-Ser
    Compositional biasi366 – 3694Poly-Gln

    Domaini

    The binding to LHCP occurs through the first ankyrin repeat and the L18 domain of LHCP.
    Homodimerization occurs through both the third and the fourth ankyrin repeats.
    Chromo domain 1 may act as a negative regulator of GTP hydrolysis by FFC/cpSRP54. It is unnecessary for targeting complex formation but is required for integration into the thylakoid membrane.
    Chromo domain 2 is involved in binding to the M domain of FFC/cpSRP54.

    Sequence similaritiesi

    Contains 4 ANK repeats.PROSITE-ProRule annotation
    Contains 3 chromo domains.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Coiled coil, Repeat, Transit peptide

    Phylogenomic databases

    eggNOGiNOG268128.
    HOGENOMiHOG000239692.
    InParanoidiO22265.
    KOiK12271.
    OMAiMEYLIEW.
    PhylomeDBiO22265.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR023780. Chromo_domain.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    [Graphical view]
    PfamiPF00023. Ank. 2 hits.
    PF00385. Chromo. 1 hit.
    [Graphical view]
    SMARTiSM00248. ANK. 3 hits.
    SM00298. CHROMO. 3 hits.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    SSF54160. SSF54160. 3 hits.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 2 hits.
    PS50013. CHROMO_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O22265-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQKVFLAMDT CALVIHQSLS RIKLSPPKSS SSSSSAFSPE SLPIRRIELC    50
    FRGAICAAVQ RNYEETTSSV EEAEEDDESS SSYGEVNKII GSRTAGEGAM 100
    EYLIEWKDGH SPSWVPSSYI AADVVSEYET PWWTAARKAD EQALSQLLED 150
    RDVDAVDENG RTALLFVAGL GSDKCVRLLA EAGADLDHRD MRGGLTALHM 200
    AAGYVRPEVV EALVELGADI EVEDERGLTA LELAREILKT TPKGNPMQFG 250
    RRIGLEKVIN VLEGQVFEYA EVDEIVEKRG KGKDVEYLVR WKDGGDCEWV 300
    KGVHVAEDVA KDYEDGLEYA VAESVIGKRV GDDGKTIEYL VKWTDMSDAT 350
    WEPQDNVDST LVLLYQQQQP MNE 373
    Length:373
    Mass (Da):41,279
    Last modified:June 1, 2002 - v2
    Checksum:iF75ED9C7046A1441
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti35 – 351S → SSSS in AAD01509. (PubMed:9878634)Curated
    Sequence conflicti73 – 731A → V in AAK96775. (PubMed:14593172)Curated
    Sequence conflicti73 – 731A → V in AAN72202. (PubMed:14593172)Curated
    Sequence conflicti137 – 1371R → K in AAD01509. (PubMed:9878634)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF013115 Genomic DNA. Translation: AAD01509.1.
    AC002535 Genomic DNA. Translation: AAC62865.2.
    CP002685 Genomic DNA. Translation: AEC10842.1.
    AY050442 mRNA. Translation: AAK91457.1.
    AY054584 mRNA. Translation: AAK96775.1.
    AY057532 mRNA. Translation: AAL09772.1.
    AY133540 mRNA. Translation: AAM91370.1.
    BT002191 mRNA. Translation: AAN72202.1.
    PIRiT00439.
    RefSeqiNP_566101.1. NM_130313.2.
    UniGeneiAt.19748.
    At.72297.

    Genome annotation databases

    EnsemblPlantsiAT2G47450.1; AT2G47450.1; AT2G47450.
    GeneIDi819358.
    KEGGiath:AT2G47450.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF013115 Genomic DNA. Translation: AAD01509.1 .
    AC002535 Genomic DNA. Translation: AAC62865.2 .
    CP002685 Genomic DNA. Translation: AEC10842.1 .
    AY050442 mRNA. Translation: AAK91457.1 .
    AY054584 mRNA. Translation: AAK96775.1 .
    AY057532 mRNA. Translation: AAL09772.1 .
    AY133540 mRNA. Translation: AAM91370.1 .
    BT002191 mRNA. Translation: AAN72202.1 .
    PIRi T00439.
    RefSeqi NP_566101.1. NM_130313.2.
    UniGenei At.19748.
    At.72297.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X32 NMR - A 84-128 [» ]
    1X3P NMR - A 320-373 [» ]
    1X3Q NMR - A 265-319 [» ]
    2HUG NMR - A 265-319 [» ]
    3DEO X-ray 1.50 A 85-267 [» ]
    3DEP X-ray 2.70 A 85-267 [» ]
    3UI2 X-ray 3.18 A 84-327 [» ]
    ProteinModelPortali O22265.
    SMRi O22265. Positions 31-318, 320-373.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 4693. 13 interactions.
    DIPi DIP-37639N.
    IntActi O22265. 19 interactions.
    MINTi MINT-126461.

    Protein family/group databases

    TCDBi 3.A.5.1.2. the general secretory pathway (sec) family.

    Proteomic databases

    PaxDbi O22265.
    PRIDEi O22265.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT2G47450.1 ; AT2G47450.1 ; AT2G47450 .
    GeneIDi 819358.
    KEGGi ath:AT2G47450.

    Organism-specific databases

    GeneFarmi 2589. 230.
    TAIRi AT2G47450.

    Phylogenomic databases

    eggNOGi NOG268128.
    HOGENOMi HOG000239692.
    InParanoidi O22265.
    KOi K12271.
    OMAi MEYLIEW.
    PhylomeDBi O22265.

    Miscellaneous databases

    EvolutionaryTracei O22265.

    Gene expression databases

    Genevestigatori O22265.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR023780. Chromo_domain.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    [Graphical view ]
    Pfami PF00023. Ank. 2 hits.
    PF00385. Chromo. 1 hit.
    [Graphical view ]
    SMARTi SM00248. ANK. 3 hits.
    SM00298. CHROMO. 3 hits.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    SSF54160. SSF54160. 3 hits.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 2 hits.
    PS50013. CHROMO_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A chromodomain protein encoded by the arabidopsis CAO gene is a plant-specific component of the chloroplast signal recognition particle pathway that is involved in LHCP targeting."
      Klimyuk V.I., Persello-Cartieaux F., Havaux M., Contard-David P., Schuenemann D., Meiherhoff K., Gouet P., Jones J.D.G., Hoffman N.E., Nussaume L.
      Plant Cell 11:87-99(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Strain: cv. Landsberg erecta.
    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.
    5. "Chloroplast FtsY, chloroplast signal recognition particle, and GTP are required to reconstitute the soluble phase of light-harvesting chlorophyll protein transport into thylakoid membranes."
      Tu C.J., Schuenemann D., Hoffman N.E.
      J. Biol. Chem. 274:27219-27224(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, INTERACTION WITH FFC/CPSRP54.
    6. "Functional analysis of the protein-interacting domains of chloroplast SRP43."
      Jonas-Straube E., Hutin C., Hoffman N.E., Schuenemann D.
      J. Biol. Chem. 276:24654-24660(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, SUBUNIT, BINDING TO LIGHT-HARVESTING CHLOROPHYLL PROTEINS AND TO FFC/CPSRP54.
    7. "Regulation of the GTPase cycle in post-translational signal recognition particle-based protein targeting involves cpSRP43."
      Goforth R.L., Peterson E.C., Yuan J., Moore M.J., Kight A.D., Lohse M.B., Sakon J., Henry R.L.
      J. Biol. Chem. 279:43077-43084(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FFC/CPSRP54.
    8. "Arabidopsis cpFtsY mutants exhibit pleiotropic defects including an inability to increase iron deficiency-inducible root Fe(III) chelate reductase activity."
      Durrett T.P., Connolly E.L., Rogers E.E.
      Plant J. 47:467-479(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. "Canonical signal recognition particle components can be bypassed for posttranslational protein targeting in chloroplasts."
      Tzvetkova-Chevolleau T., Hutin C., Noel L.D., Goforth R., Carde J.P., Caffarri S., Sinning I., Groves M., Teulon J.M., Hoffman N.E., Henry R., Havaux M., Nussaume L.
      Plant Cell 19:1635-1648(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ALB3.
    10. "Interplay between the cpSRP pathway components, the substrate LHCP and the translocase Alb3: an in vivo and in vitro study."
      Bals T., Duenschede B., Funke S., Schuenemann D.
      FEBS Lett. 584:4138-4144(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ALB3; FFC/CPSRP54; CPFTSY AND LHCP.
    11. "The C terminus of the Alb3 membrane insertase recruits cpSRP43 to the thylakoid membrane."
      Falk S., Ravaud S., Koch J., Sinning I.
      J. Biol. Chem. 285:5954-5962(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ALB3 AND FFC/CPSRP54, MUTAGENESIS OF TYR-269; TRP-291 AND ASP-293.
    12. "cpSRP43 is a novel chaperone specific for light-harvesting chlorophyll a,b-binding proteins."
      Falk S., Sinning I.
      J. Biol. Chem. 285:21655-21661(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "LTD is a protein required for sorting light-harvesting chlorophyll-binding proteins to the chloroplast SRP pathway."
      Ouyang M., Li X., Ma J., Chi W., Xiao J., Zou M., Chen F., Lu C., Zhang L.
      Nat. Commun. 2:277-277(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LTD.
    14. Cited for: STRUCTURE BY NMR OF 84-128 AND 265-373, INTERACTION WITH FFC/CPSRP54.
    15. "Assembly of chloroplast signal recognition particle involves structural rearrangement in cpSRP43."
      Kathir K.M., Rajalingam D., Sivaraja V., Kight A., Goforth R.L., Yu C., Henry R., Kumar T.K.
      J. Mol. Biol. 381:49-60(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 265-319.
    16. "Structural basis for specific substrate recognition by the chloroplast signal recognition particle protein cpSRP43."
      Stengel K.F., Holdermann I., Cain P., Robinson C., Wild K., Sinning I.
      Science 321:253-256(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 85-267 IN COMPLEX WITH THE L18 DOMAIN OF LHCP, MUTAGENESIS OF ARG-161; ARG-192; TYR-204 AND ARG-226.

    Entry informationi

    Entry nameiSR43C_ARATH
    AccessioniPrimary (citable) accession number: O22265
    Secondary accession number(s): Q93V50, Q940I7, Q9SAU3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 122 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Unlike eukaryotic or prokaryotic signal recognition particle (SRP), the chloroplast SRP from higher plants lacks an SRP-RNA component. It targets both chloroplast-encoded and nucleus-encoded substrates to the thylakoid membrane, post-translationally for the nucleus-encoded proteins and co-translationally for the chloroplast-encoded proteins.

    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