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Q9QZX7

- SRR_MOUSE

UniProt

Q9QZX7 - SRR_MOUSE

Protein

Serine racemase

Gene

Srr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine.5 Publications

    Catalytic activityi

    L-serine = D-serine.
    L-serine = pyruvate + NH3.
    D-serine = pyruvate + NH3.

    Cofactori

    Pyridoxal phosphate.2 Publications

    Enzyme regulationi

    Allosterically activated by magnesium, and possibly also other divalent metal cations. Allosterically activated by ATP, ADP or GTP.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei51 – 511ATPCurated
    Active sitei56 – 561Proton acceptorBy similarity
    Active sitei84 – 841Proton acceptorBy similarity
    Binding sitei121 – 1211ATPBy similarity
    Binding sitei135 – 1351SubstrateBy similarity
    Metal bindingi210 – 2101MagnesiumBy similarity
    Metal bindingi214 – 2141Magnesium; via carbonyl oxygenBy similarity
    Metal bindingi216 – 2161MagnesiumBy similarity

    GO - Molecular functioni

    1. ATP binding Source: MGI
    2. calcium ion binding Source: MGI
    3. D-serine ammonia-lyase activity Source: UniProtKB-EC
    4. glycine binding Source: MGI
    5. L-serine ammonia-lyase activity Source: UniProtKB-EC
    6. magnesium ion binding Source: Ensembl
    7. protein binding Source: MGI
    8. protein homodimerization activity Source: MGI
    9. pyridoxal phosphate binding Source: MGI
    10. serine racemase activity Source: MGI
    11. threonine racemase activity Source: MGI

    GO - Biological processi

    1. aging Source: Ensembl
    2. brain development Source: Ensembl
    3. D-serine biosynthetic process Source: MGI
    4. L-serine metabolic process Source: MGI
    5. protein homotetramerization Source: MGI
    6. pyruvate biosynthetic process Source: Ensembl
    7. response to drug Source: Ensembl
    8. response to lipopolysaccharide Source: Ensembl
    9. response to morphine Source: Ensembl
    10. serine family amino acid metabolic process Source: MGI

    Keywords - Molecular functioni

    Isomerase, Lyase

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Pyridoxal phosphate

    Enzyme and pathway databases

    BRENDAi5.1.1.18. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine racemase (EC:4.3.1.17, EC:4.3.1.18, EC:5.1.1.18)
    Alternative name(s):
    D-serine ammonia-lyase
    D-serine dehydratase
    L-serine ammonia-lyase
    L-serine dehydratase
    Gene namesi
    Name:Srr
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1351636. Srr.

    Subcellular locationi

    GO - Cellular componenti

    1. apical part of cell Source: Ensembl
    2. cytoplasm Source: Ensembl
    3. neuronal cell body Source: Ensembl
    4. plasma membrane Source: Ensembl

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi51 – 511K → A: Impairs ATP-binding inducing a 80% decrease in enzyme activity.
    Mutagenesisi113 – 1131C → S: Abolishes S-nitrosylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 339339Serine racemasePRO_0000185651Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei56 – 561N6-(pyridoxal phosphate)lysineBy similarity
    Modified residuei113 – 1131S-nitrosocysteine1 Publication

    Post-translational modificationi

    S-nitrosylated, leading to decrease the enzyme activity.1 Publication

    Keywords - PTMi

    S-nitrosylation

    Proteomic databases

    MaxQBiQ9QZX7.
    PaxDbiQ9QZX7.
    PRIDEiQ9QZX7.

    PTM databases

    PhosphoSiteiQ9QZX7.

    Expressioni

    Tissue specificityi

    Detected in brain (at protein level). Brain.

    Gene expression databases

    ArrayExpressiQ9QZX7.
    BgeeiQ9QZX7.
    CleanExiMM_SRR.
    GenevestigatoriQ9QZX7.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi205172. 3 interactions.
    IntActiQ9QZX7. 2 interactions.
    MINTiMINT-5202279.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9QZX7.
    SMRiQ9QZX7. Positions 3-324.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni238 – 2392Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1171.
    GeneTreeiENSGT00550000075026.
    HOVERGENiHBG023167.
    InParanoidiQ9QZX7.
    KOiK12235.
    OMAiVEHYEAP.
    OrthoDBiEOG7HB5B2.
    PhylomeDBiQ9QZX7.
    TreeFamiTF313346.

    Family and domain databases

    InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view]
    PfamiPF00291. PALP. 1 hit.
    [Graphical view]
    SUPFAMiSSF53686. SSF53686. 1 hit.
    PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9QZX7-1) [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

    MCAQYCISFA DVEKAHINIQ DSIHLTPVLT SSILNQIAGR NLFFKCELFQ    50
    KTGSFKIRGA LNAIRGLIPD TPEEKPKAVV THSSGNHGQA LTYAAKLEGI 100
    PAYIVVPQTA PNCKKLAIQA YGASIVYCDP SDESREKVTQ RIMQETEGIL 150
    VHPNQEPAVI AGQGTIALEV LNQVPLVDAL VVPVGGGGMV AGIAITIKAL 200
    KPSVKVYAAE PSNADDCYQS KLKGELTPNL HPPETIADGV KSSIGLNTWP 250
    IIRDLVDDVF TVTEDEIKYA TQLVWGRMKL LIEPTAGVAL AAVLSQHFQT 300
    VSPEVKNVCI VLSGGNVDLT SLNWVGQAER PAPYQTVSV 339
    Length:339
    Mass (Da):36,359
    Last modified:May 1, 2000 - v1
    Checksum:iB9AE9A9336358728
    GO
    Isoform 2 (identifier: Q9QZX7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         174-198: Missing.

    Show »
    Length:314
    Mass (Da):34,030
    Checksum:i0BB6492649FF8491
    GO
    Isoform 3 (identifier: Q9QZX7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         183-339: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:182
    Mass (Da):19,694
    Checksum:i23075946C01AF288
    GO

    Sequence cautioni

    The sequence CAI24255.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti111 – 1111P → T in BAC25712. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei174 – 19825Missing in isoform 2. 1 PublicationVSP_025013Add
    BLAST
    Alternative sequencei183 – 339157Missing in isoform 3. CuratedVSP_025014Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF148321 mRNA. Translation: AAF08701.1.
    AK031687 mRNA. Translation: BAC27514.1.
    AK028034 mRNA. Translation: BAC25712.1.
    AK043738 mRNA. Translation: BAC31637.1.
    AK157122 mRNA. Translation: BAE33968.1.
    AK170096 mRNA. Translation: BAE41561.1.
    AL604066 Genomic DNA. Translation: CAI24252.1.
    AL604066 Genomic DNA. Translation: CAI24253.1.
    AL604066 Genomic DNA. Translation: CAI24254.1.
    AL604066 Genomic DNA. Translation: CAI24255.1. Sequence problems.
    BC011164 mRNA. Translation: AAH11164.1.
    AB232340 mRNA. Translation: BAE19920.1.
    AB232341 mRNA. Translation: BAE19921.1.
    AB232342 mRNA. Translation: BAE19922.1.
    AB232343 mRNA. Translation: BAE19923.1.
    AB235396 mRNA. Translation: BAE44529.1.
    CCDSiCCDS25038.1. [Q9QZX7-1]
    RefSeqiNP_001156783.1. NM_001163311.1. [Q9QZX7-1]
    NP_038789.1. NM_013761.4. [Q9QZX7-1]
    XP_006533520.1. XM_006533457.1. [Q9QZX7-1]
    XP_006533521.1. XM_006533458.1. [Q9QZX7-1]
    UniGeneiMm.131443.
    Mm.220843.
    Mm.412219.

    Genome annotation databases

    EnsembliENSMUST00000065211; ENSMUSP00000067552; ENSMUSG00000001323. [Q9QZX7-1]
    ENSMUST00000108447; ENSMUSP00000104086; ENSMUSG00000001323. [Q9QZX7-2]
    ENSMUST00000108448; ENSMUSP00000104087; ENSMUSG00000001323. [Q9QZX7-1]
    ENSMUST00000121738; ENSMUSP00000113372; ENSMUSG00000001323. [Q9QZX7-1]
    ENSMUST00000128556; ENSMUSP00000120012; ENSMUSG00000001323. [Q9QZX7-3]
    GeneIDi27364.
    KEGGimmu:27364.
    UCSCiuc007kcr.2. mouse. [Q9QZX7-1]
    uc007kcu.2. mouse. [Q9QZX7-3]
    uc011xzd.1. mouse. [Q9QZX7-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF148321 mRNA. Translation: AAF08701.1 .
    AK031687 mRNA. Translation: BAC27514.1 .
    AK028034 mRNA. Translation: BAC25712.1 .
    AK043738 mRNA. Translation: BAC31637.1 .
    AK157122 mRNA. Translation: BAE33968.1 .
    AK170096 mRNA. Translation: BAE41561.1 .
    AL604066 Genomic DNA. Translation: CAI24252.1 .
    AL604066 Genomic DNA. Translation: CAI24253.1 .
    AL604066 Genomic DNA. Translation: CAI24254.1 .
    AL604066 Genomic DNA. Translation: CAI24255.1 . Sequence problems.
    BC011164 mRNA. Translation: AAH11164.1 .
    AB232340 mRNA. Translation: BAE19920.1 .
    AB232341 mRNA. Translation: BAE19921.1 .
    AB232342 mRNA. Translation: BAE19922.1 .
    AB232343 mRNA. Translation: BAE19923.1 .
    AB235396 mRNA. Translation: BAE44529.1 .
    CCDSi CCDS25038.1. [Q9QZX7-1 ]
    RefSeqi NP_001156783.1. NM_001163311.1. [Q9QZX7-1 ]
    NP_038789.1. NM_013761.4. [Q9QZX7-1 ]
    XP_006533520.1. XM_006533457.1. [Q9QZX7-1 ]
    XP_006533521.1. XM_006533458.1. [Q9QZX7-1 ]
    UniGenei Mm.131443.
    Mm.220843.
    Mm.412219.

    3D structure databases

    ProteinModelPortali Q9QZX7.
    SMRi Q9QZX7. Positions 3-324.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 205172. 3 interactions.
    IntActi Q9QZX7. 2 interactions.
    MINTi MINT-5202279.

    Chemistry

    ChEMBLi CHEMBL1075306.

    PTM databases

    PhosphoSitei Q9QZX7.

    Proteomic databases

    MaxQBi Q9QZX7.
    PaxDbi Q9QZX7.
    PRIDEi Q9QZX7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000065211 ; ENSMUSP00000067552 ; ENSMUSG00000001323 . [Q9QZX7-1 ]
    ENSMUST00000108447 ; ENSMUSP00000104086 ; ENSMUSG00000001323 . [Q9QZX7-2 ]
    ENSMUST00000108448 ; ENSMUSP00000104087 ; ENSMUSG00000001323 . [Q9QZX7-1 ]
    ENSMUST00000121738 ; ENSMUSP00000113372 ; ENSMUSG00000001323 . [Q9QZX7-1 ]
    ENSMUST00000128556 ; ENSMUSP00000120012 ; ENSMUSG00000001323 . [Q9QZX7-3 ]
    GeneIDi 27364.
    KEGGi mmu:27364.
    UCSCi uc007kcr.2. mouse. [Q9QZX7-1 ]
    uc007kcu.2. mouse. [Q9QZX7-3 ]
    uc011xzd.1. mouse. [Q9QZX7-2 ]

    Organism-specific databases

    CTDi 63826.
    MGIi MGI:1351636. Srr.

    Phylogenomic databases

    eggNOGi COG1171.
    GeneTreei ENSGT00550000075026.
    HOVERGENi HBG023167.
    InParanoidi Q9QZX7.
    KOi K12235.
    OMAi VEHYEAP.
    OrthoDBi EOG7HB5B2.
    PhylomeDBi Q9QZX7.
    TreeFami TF313346.

    Enzyme and pathway databases

    BRENDAi 5.1.1.18. 3474.

    Miscellaneous databases

    NextBioi 305244.
    PROi Q9QZX7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9QZX7.
    Bgeei Q9QZX7.
    CleanExi MM_SRR.
    Genevestigatori Q9QZX7.

    Family and domain databases

    InterProi IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view ]
    Pfami PF00291. PALP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53686. SSF53686. 1 hit.
    PROSITEi PS00165. DEHYDRATASE_SER_THR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Serine racemase: a glial enzyme synthesizing D-serine to regulate glutamate-N-methyl-D-aspartate neurotransmission."
      Wolosker H., Blackshaw S., Snyder S.H.
      Proc. Natl. Acad. Sci. U.S.A. 96:13409-13414(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
      Strain: BALB/c.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J and NOD.
      Tissue: Brain cortex, Spleen and Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Liver.
    5. "Multiple splice variants in 5'UTR of mouse serine racemase."
      Ohba H., Ohnishi T., Yoshikawa T.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-56 (ISOFORMS 1/2/3).
      Tissue: Brain.
    6. Lubec G., Klug S.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 15-40, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hippocampus.
    7. "Allosteric regulation of mouse brain serine racemase."
      Neidle A., Dunlop D.S.
      Neurochem. Res. 27:1719-1724(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ENZYME REGULATION.
    8. "Cofactors of serine racemase that physiologically stimulate the synthesis of the N-methyl-D-aspartate (NMDA) receptor coagonist D-serine."
      De Miranda J., Panizzutti R., Foltyn V.N., Wolosker H.
      Proc. Natl. Acad. Sci. U.S.A. 99:14542-14547(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
    9. "Serine racemase modulates intracellular D-serine levels through an alpha,beta-elimination activity."
      Foltyn V.N., Bendikov I., De Miranda J., Panizzutti R., Dumin E., Shleper M., Li P., Toney M.D., Kartvelishvily E., Wolosker H.
      J. Biol. Chem. 280:1754-1763(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    10. "Nitric oxide S-nitrosylates serine racemase, mediating feedback inhibition of D-serine formation."
      Mustafa A.K., Kumar M., Selvakumar B., Ho G.P., Ehmsen J.T., Barrow R.K., Amzel L.M., Snyder S.H.
      Proc. Natl. Acad. Sci. U.S.A. 104:2950-2955(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, S-NITROSYLATION AT CYS-113, ATP-BINDING, MUTAGENESIS OF CYS-113.

    Entry informationi

    Entry nameiSRR_MOUSE
    AccessioniPrimary (citable) accession number: Q9QZX7
    Secondary accession number(s): Q401M7
    , Q5SWE4, Q5SWE5, Q5SWE7, Q8BT19, Q8CD11
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 31, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3