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P10408

- SECA_ECOLI

UniProt

P10408 - SECA_ECOLI

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Protein

Protein translocase subunit SecA

Gene

secA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Required for protein export, interacts with the SecYEG preprotein conducting channel. SecA has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.1 Publication

Cofactori

Binds 1 zinc ion per subunit. Zinc is required for binding of the SecB chaperone to the extreme C-terminus of SecA.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi885 – 8851Zinc
Metal bindingi887 – 8871Zinc
Metal bindingi896 – 8961Zinc
Metal bindingi897 – 8971Zinc

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi102 – 1098ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. identical protein binding Source: IntAct
  3. metal ion binding Source: UniProtKB-KW
  4. protein-transmembrane transporting ATPase activity Source: EcoCyc

GO - Biological processi

  1. chaperone-mediated protein folding Source: EcoCyc
  2. intracellular protein transmembrane transport Source: EcoliWiki
  3. protein import Source: InterPro
  4. protein targeting Source: EcoliWiki
  5. protein transport Source: EcoliWiki
  6. protein transport by the Sec complex Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:SECA.
ECOL316407:JW0096-MONOMER.

Protein family/group databases

TCDBi3.A.5.1.1. the general secretory pathway (sec) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein translocase subunit SecA
Gene namesi
Name:secA
Synonyms:azi, pea, prlD
Ordered Locus Names:b0098, JW0096
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10936. secA.

Subcellular locationi

GO - Cellular componenti

  1. cell envelope Sec protein transport complex Source: EcoCyc
  2. cytoplasm Source: EcoliWiki
  3. cytosol Source: EcoCyc
  4. integral component of plasma membrane Source: EcoCyc
  5. plasma membrane Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

Essential. Leads to loss of translocation of lipoproteins Lpp and BRP.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 901901Protein translocase subunit SecAPRO_0000109585Add
BLAST

Proteomic databases

PaxDbiP10408.
PRIDEiP10408.

Expressioni

Inductioni

Repressed under conditions of excess protein secretion capacity and derepressed when protein secretion becomes limiting. This is regulated by SecM.

Gene expression databases

GenevestigatoriP10408.

Interactioni

Subunit structurei

Monomer and homodimer; probably dimeric in the cytoplasm. It is not yet clear whether the form that functions in protein insertion is monomeric or dimeric. Part of the essential protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF-YajC and YidC. Makes direct contact with SecY.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-543213,EBI-543213
lamBP029433EBI-543213,EBI-371309
secBP0AG864EBI-543213,EBI-555877
secGP0AG992EBI-543213,EBI-6404248
secYP0AGA24EBI-543213,EBI-761422
ybgCP0A8Z32EBI-543213,EBI-543276

Protein-protein interaction databases

BioGridi849222. 1 interaction.
DIPiDIP-10840N.
IntActiP10408. 77 interactions.
MINTiMINT-1224866.
STRINGi511145.b0098.

Structurei

Secondary structure

1
901
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 3017
Helixi32 – 376
Helixi40 – 5516
Helixi60 – 7920
Helixi85 – 9511
Beta strandi96 – 1016
Helixi108 – 12013
Beta strandi122 – 1243
Beta strandi127 – 1326
Helixi133 – 14917
Beta strandi154 – 1563
Helixi163 – 1719
Beta strandi172 – 1787
Helixi179 – 18911
Helixi195 – 1973
Beta strandi205 – 2095
Helixi211 – 2144
Turni215 – 2206
Beta strandi222 – 2276
Helixi234 – 2363
Helixi237 – 2404
Helixi241 – 2455
Beta strandi250 – 2523
Beta strandi278 – 2814
Helixi282 – 2843
Beta strandi286 – 2927
Helixi301 – 3033
Helixi304 – 31411
Turni315 – 3173
Beta strandi318 – 3203
Turni323 – 3253
Beta strandi326 – 3294
Beta strandi332 – 3365
Turni338 – 3403
Beta strandi343 – 3464
Turni350 – 3523
Helixi353 – 3608
Beta strandi370 – 3767
Helixi377 – 3815
Beta strandi384 – 3918
Helixi398 – 4058
Beta strandi408 – 4114
Beta strandi426 – 4305
Helixi431 – 44616
Turni447 – 4493
Beta strandi452 – 4587
Helixi459 – 47113
Beta strandi477 – 4793
Helixi484 – 4929
Turni493 – 4953
Beta strandi496 – 4983
Beta strandi500 – 5056
Helixi519 – 5257
Beta strandi526 – 5283
Helixi533 – 55018
Beta strandi553 – 5608
Helixi565 – 5728
Helixi577 – 5793
Beta strandi582 – 5898
Helixi590 – 5923
Helixi593 – 5964
Beta strandi597 – 5993
Helixi601 – 6044
Helixi605 – 6106
Helixi621 – 66848
Helixi673 – 68917
Helixi698 – 7003
Helixi703 – 71412
Helixi720 – 7267
Helixi728 – 7303
Helixi732 – 75423
Helixi756 – 78732
Turni788 – 7903
Beta strandi791 – 7933
Beta strandi795 – 7973
Turni799 – 8013
Helixi802 – 82827
Turni884 – 8874
Beta strandi889 – 8913
Helixi892 – 8965

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TM6NMR-A880-901[»]
2FSFX-ray2.00A/B9-861[»]
2FSGX-ray2.20A/B9-861[»]
2FSHX-ray2.00A/B9-861[»]
2FSIX-ray2.11A/B9-861[»]
2VDANMR-A9-836[»]
3BXZX-ray3.00A/B6-609[»]
ProteinModelPortaliP10408.
SMRiP10408. Positions 9-836.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10408.

Family & Domainsi

Sequence similaritiesi

Belongs to the SecA family.Curated

Phylogenomic databases

eggNOGiCOG0653.
HOGENOMiHOG000218168.
InParanoidiP10408.
KOiK03070.
OMAiEAYEFQQ.
OrthoDBiEOG654P48.
PhylomeDBiP10408.

Family and domain databases

Gene3Di1.10.3060.10. 1 hit.
3.40.50.300. 3 hits.
3.90.1440.10. 1 hit.
HAMAPiMF_01382. SecA.
InterProiIPR027417. P-loop_NTPase.
IPR004027. SEC_C_motif.
IPR000185. SecA.
IPR020937. SecA_CS.
IPR011115. SecA_DEAD.
IPR014018. SecA_motor_DEAD.
IPR011130. SecA_preprotein_X-link_dom.
IPR011116. SecA_Wing/Scaffold.
[Graphical view]
PfamiPF02810. SEC-C. 1 hit.
PF07517. SecA_DEAD. 1 hit.
PF01043. SecA_PP_bind. 1 hit.
PF07516. SecA_SW. 1 hit.
[Graphical view]
PRINTSiPR00906. SECA.
SMARTiSM00957. SecA_DEAD. 1 hit.
SM00958. SecA_PP_bind. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
SSF81767. SSF81767. 1 hit.
SSF81886. SSF81886. 2 hits.
TIGRFAMsiTIGR00963. secA. 1 hit.
PROSITEiPS01312. SECA. 1 hit.
PS51196. SECA_MOTOR_DEAD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10408-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLIKLLTKVF GSRNDRTLRR MRKVVNIINA MEPEMEKLSD EELKGKTAEF
60 70 80 90 100
RARLEKGEVL ENLIPEAFAV VREASKRVFG MRHFDVQLLG GMVLNERCIA
110 120 130 140 150
EMRTGEGKTL TATLPAYLNA LTGKGVHVVT VNDYLAQRDA ENNRPLFEFL
160 170 180 190 200
GLTVGINLPG MPAPAKREAY AADITYGTNN EYGFDYLRDN MAFSPEERVQ
210 220 230 240 250
RKLHYALVDE VDSILIDEAR TPLIISGPAE DSSEMYKRVN KIIPHLIRQE
260 270 280 290 300
KEDSETFQGE GHFSVDEKSR QVNLTERGLV LIEELLVKEG IMDEGESLYS
310 320 330 340 350
PANIMLMHHV TAALRAHALF TRDVDYIVKD GEVIIVDEHT GRTMQGRRWS
360 370 380 390 400
DGLHQAVEAK EGVQIQNENQ TLASITFQNY FRLYEKLAGM TGTADTEAFE
410 420 430 440 450
FSSIYKLDTV VVPTNRPMIR KDLPDLVYMT EAEKIQAIIE DIKERTAKGQ
460 470 480 490 500
PVLVGTISIE KSELVSNELT KAGIKHNVLN AKFHANEAAI VAQAGYPAAV
510 520 530 540 550
TIATNMAGRG TDIVLGGSWQ AEVAALENPT AEQIEKIKAD WQVRHDAVLE
560 570 580 590 600
AGGLHIIGTE RHESRRIDNQ LRGRSGRQGD AGSSRFYLSM EDALMRIFAS
610 620 630 640 650
DRVSGMMRKL GMKPGEAIEH PWVTKAIANA QRKVESRNFD IRKQLLEYDD
660 670 680 690 700
VANDQRRAIY SQRNELLDVS DVSETINSIR EDVFKATIDA YIPPQSLEEM
710 720 730 740 750
WDIPGLQERL KNDFDLDLPI AEWLDKEPEL HEETLRERIL AQSIEVYQRK
760 770 780 790 800
EEVVGAEMMR HFEKGVMLQT LDSLWKEHLA AMDYLRQGIH LRGYAQKDPK
810 820 830 840 850
QEYKRESFSM FAAMLESLKY EVISTLSKVQ VRMPEEVEEL EQQRRMEAER
860 870 880 890 900
LAQMQQLSHQ DDDSAAAAAL AAQTGERKVG RNDPCPCGSG KKYKQCHGRL

Q
Length:901
Mass (Da):102,023
Last modified:November 1, 1997 - v2
Checksum:i683D66DD4305DBC2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191R → G AA sequence (PubMed:2841285)Curated
Sequence conflicti737 – 7382ER → DG in AAA24619. (PubMed:2841285)Curated
Sequence conflicti737 – 7382ER → DG in CAA38875. (PubMed:1630901)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M20791 Genomic DNA. Translation: AAA24619.1.
M19211 Genomic DNA. Translation: AAA83851.1.
X55034 Genomic DNA. Translation: CAA38875.1.
U00096 Genomic DNA. Translation: AAC73209.1.
AP009048 Genomic DNA. Translation: BAB96666.2.
PIRiB64732. BVECCA.
RefSeqiNP_414640.1. NC_000913.3.
YP_488403.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73209; AAC73209; b0098.
BAB96666; BAB96666; BAB96666.
GeneIDi12932123.
944821.
KEGGiecj:Y75_p0097.
eco:b0098.
PATRICi32115301. VBIEscCol129921_0102.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M20791 Genomic DNA. Translation: AAA24619.1 .
M19211 Genomic DNA. Translation: AAA83851.1 .
X55034 Genomic DNA. Translation: CAA38875.1 .
U00096 Genomic DNA. Translation: AAC73209.1 .
AP009048 Genomic DNA. Translation: BAB96666.2 .
PIRi B64732. BVECCA.
RefSeqi NP_414640.1. NC_000913.3.
YP_488403.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TM6 NMR - A 880-901 [» ]
2FSF X-ray 2.00 A/B 9-861 [» ]
2FSG X-ray 2.20 A/B 9-861 [» ]
2FSH X-ray 2.00 A/B 9-861 [» ]
2FSI X-ray 2.11 A/B 9-861 [» ]
2VDA NMR - A 9-836 [» ]
3BXZ X-ray 3.00 A/B 6-609 [» ]
ProteinModelPortali P10408.
SMRi P10408. Positions 9-836.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 849222. 1 interaction.
DIPi DIP-10840N.
IntActi P10408. 77 interactions.
MINTi MINT-1224866.
STRINGi 511145.b0098.

Protein family/group databases

TCDBi 3.A.5.1.1. the general secretory pathway (sec) family.

Proteomic databases

PaxDbi P10408.
PRIDEi P10408.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73209 ; AAC73209 ; b0098 .
BAB96666 ; BAB96666 ; BAB96666 .
GeneIDi 12932123.
944821.
KEGGi ecj:Y75_p0097.
eco:b0098.
PATRICi 32115301. VBIEscCol129921_0102.

Organism-specific databases

EchoBASEi EB0929.
EcoGenei EG10936. secA.

Phylogenomic databases

eggNOGi COG0653.
HOGENOMi HOG000218168.
InParanoidi P10408.
KOi K03070.
OMAi EAYEFQQ.
OrthoDBi EOG654P48.
PhylomeDBi P10408.

Enzyme and pathway databases

BioCyci EcoCyc:SECA.
ECOL316407:JW0096-MONOMER.

Miscellaneous databases

EvolutionaryTracei P10408.
PROi P10408.

Gene expression databases

Genevestigatori P10408.

Family and domain databases

Gene3Di 1.10.3060.10. 1 hit.
3.40.50.300. 3 hits.
3.90.1440.10. 1 hit.
HAMAPi MF_01382. SecA.
InterProi IPR027417. P-loop_NTPase.
IPR004027. SEC_C_motif.
IPR000185. SecA.
IPR020937. SecA_CS.
IPR011115. SecA_DEAD.
IPR014018. SecA_motor_DEAD.
IPR011130. SecA_preprotein_X-link_dom.
IPR011116. SecA_Wing/Scaffold.
[Graphical view ]
Pfami PF02810. SEC-C. 1 hit.
PF07517. SecA_DEAD. 1 hit.
PF01043. SecA_PP_bind. 1 hit.
PF07516. SecA_SW. 1 hit.
[Graphical view ]
PRINTSi PR00906. SECA.
SMARTi SM00957. SecA_DEAD. 1 hit.
SM00958. SecA_PP_bind. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 3 hits.
SSF81767. SSF81767. 1 hit.
SSF81886. SSF81886. 2 hits.
TIGRFAMsi TIGR00963. secA. 1 hit.
PROSITEi PS01312. SECA. 1 hit.
PS51196. SECA_MOTOR_DEAD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli."
    Schmidt M., Rollo E., Grodberg J., Oliver D.
    J. Bacteriol. 170:3404-3414(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
    Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
    Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 737-738.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Sequence analysis, transcriptional organization, and insertional mutagenesis of the envA gene of Escherichia coli."
    Beall B., Lutkenhaus J.
    J. Bacteriol. 169:5408-5415(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67.
    Strain: K12.
  6. "SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli."
    Lill R., Cunningham K., Brundage L.A., Ito K., Oliver D., Wickner W.
    EMBO J. 8:961-966(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: ATP HYDROLYSIS.
  7. Cited for: COFACTOR.
  8. "Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane."
    Or E., Navon A., Rapoport T.
    EMBO J. 21:4470-4479(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DIMER DISSOCIATION IN THE PRESENCE OF ACIDIC PHOSPHOLIPIDS, DETERGENTS, SYNTHETIC SIGNAL PEPTIDES.
  9. "Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase."
    Duong F.
    EMBO J. 22:4375-4384(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION OF MONOMER WITH SECYEG TRANSLOCATION COMPLEX.
  10. "Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA."
    Benach J., Chou Y.T., Fak J.J., Itkin A., Nicolae D.D., Smith P.C., Wittrock G., Floyd D.L., Golsaz C.M., Gierasch L.M., Hunt J.F.
    J. Biol. Chem. 278:3628-3638(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACIDIC PHOSPHOLIPIDS, SYNTHETIC SIGNAL PEPTIDES, OLIGOMERIZATION STATE OF SECA.
  11. "Nucleotide binding induces changes in the oligomeric state and conformation of Sec A in a lipid environment: a small-angle neutron-scattering study."
    Bu Z., Wang L., Kendall D.A.
    J. Mol. Biol. 332:23-30(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE TURNOVER, OLIGOMERIZATION STATE OF SECA.
  12. "Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway."
    Froderberg L., Houben E.N., Baars L., Luirink J., de Gier J.W.
    J. Biol. Chem. 279:31026-31032(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LIPOPROTEIN EXPORT, DISRUPTION PHENOTYPE.
  13. "Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel."
    Osborne A.R., Rapoport T.A.
    Cell 129:97-110(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SECY.
  14. Cited for: CONTROL OF ATPASE ACTIVITY.
  15. "NMR structure of the C-terminal domain of SecA in the free state."
    Matousek W.M., Alexandrescu A.T.
    Biochim. Biophys. Acta 1702:163-171(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 880-901.
  16. "Structure of dimeric SecA, the Escherichia coli preprotein translocase motor."
    Papanikolau Y., Papadovasilaki M., Ravelli R.B.G., McCarthy A.A., Cusack S., Economou A., Petratos K.
    J. Mol. Biol. 366:1545-1557(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 9-861 AS A DIMERIC APOPROTEIN, AS A NUCLEOTIDE-BOUND DIMER.
  17. "Control of SecA and SecM translation by protein secretion."
    Nakatogawa H., Murakami A., Ito K.
    Curr. Opin. Microbiol. 7:145-150(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW OF PROTEIN SECRETION CONTROL OF SECA EXPRESSION.
  18. "Bacterial protein secretion through the translocase nanomachine."
    Papanikou E., Karamanou S., Economou A.
    Nat. Rev. Microbiol. 5:839-851(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW OF PROTEIN SECRETION.

Entry informationi

Entry nameiSECA_ECOLI
AccessioniPrimary (citable) accession number: P10408
Secondary accession number(s): P75642
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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