Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P04053

- TDT_HUMAN

UniProt

P04053 - TDT_HUMAN

(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)

Protein

DNA nucleotidylexotransferase

Gene

DNTT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells.

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Cofactori

Magnesium.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi253 – 2531Sodium; via carbonyl oxygenBy similarity
Metal bindingi255 – 2551Sodium; via carbonyl oxygenBy similarity
Metal bindingi343 – 3431MagnesiumBy similarity
Metal bindingi345 – 3451MagnesiumBy similarity
Metal bindingi433 – 4331MagnesiumBy similarity

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. DNA-directed DNA polymerase activity Source: InterPro
  3. DNA nucleotidylexotransferase activity Source: ProtInc
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. DNA modification Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Terminal addition

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

SABIO-RKP04053.
SignaLinkiP04053.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA nucleotidylexotransferase (EC:2.7.7.31)
Alternative name(s):
Terminal addition enzyme
Terminal deoxynucleotidyltransferase
Short name:
Terminal transferase
Gene namesi
Name:DNTT
Synonyms:TDT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:2983. DNTT.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27449.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 509509DNA nucleotidylexotransferasePRO_0000218791Add
BLAST

Proteomic databases

MaxQBiP04053.
PaxDbiP04053.
PRIDEiP04053.

PTM databases

PhosphoSiteiP04053.

Expressioni

Gene expression databases

BgeeiP04053.
CleanExiHS_DNTT.
GenevestigatoriP04053.

Organism-specific databases

HPAiHPA044194.

Interactioni

Subunit structurei

Interacts with PRP19 and DNTTIP1. Forms a ternary complex with DNTTIP2 and core histone. Released from this complex by PCNA.3 Publications

Protein-protein interaction databases

BioGridi108127. 9 interactions.
IntActiP04053. 1 interaction.
STRINGi9606.ENSP00000360216.

Structurei

Secondary structure

1
509
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 253
Beta strandi36 – 405
Turni42 – 443
Helixi46 – 5813
Beta strandi73 – 786
Helixi81 – 9010
Beta strandi100 – 1034
Helixi104 – 1129
Beta strandi120 – 1245

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2COENMR-A19-125[»]
ProteinModelPortaliP04053.
SMRiP04053. Positions 21-125, 149-509.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04053.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 12498BRCTPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni151 – 509359Mediates interaction with DNTTIP2Add
BLAST
Regioni336 – 34510Involved in ssDNA bindingBy similarity

Sequence similaritiesi

Belongs to the DNA polymerase type-X family.Curated
Contains 1 BRCT domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1796.
GeneTreeiENSGT00530000063002.
HOGENOMiHOG000263600.
HOVERGENiHBG003670.
InParanoidiP04053.
KOiK00977.
OMAiRRTTLNN.
OrthoDBiEOG7BS4BH.
PhylomeDBiP04053.
TreeFamiTF103012.

Family and domain databases

Gene3Di1.10.150.110. 1 hit.
3.30.210.10. 1 hit.
3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR002054. DNA-dir_DNA_pol_X.
IPR019843. DNA_pol-X_BS.
IPR010996. DNA_pol_b-like_N.
IPR018944. DNA_pol_lambd_fingers_domain.
IPR022312. DNA_pol_X.
IPR027421. DNA_pol_X_lyase_dom.
IPR002934. Nucleotidyltransferase.
IPR029398. PolB_thumb.
IPR027292. TdT.
IPR001726. TdT/Mu.
[Graphical view]
PfamiPF00533. BRCT. 1 hit.
PF14791. DNA_pol_B_thumb. 1 hit.
PF10391. DNA_pol_lambd_f. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000817. DNA_NT. 1 hit.
PIRSF501175. TDT. 1 hit.
PRINTSiPR00869. DNAPOLX.
PR00871. DNAPOLXTDT.
SMARTiSM00292. BRCT. 1 hit.
SM00483. POLXc. 1 hit.
[Graphical view]
SUPFAMiSSF47802. SSF47802. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P04053-1) [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

        10         20         30         40         50
MDPPRASHLS PRKKRPRQTG ALMASSPQDI KFQDLVVFIL EKKMGTTRRA
60 70 80 90 100
FLMELARRKG FRVENELSDS VTHIVAENNS GSDVLEWLQA QKVQVSSQPE
110 120 130 140 150
LLDVSWLIEC IRAGKPVEMT GKHQLVVRRD YSDSTNPGPP KTPPIAVQKI
160 170 180 190 200
SQYACQRRTT LNNCNQIFTD AFDILAENCE FRENEDSCVT FMRAASVLKS
210 220 230 240 250
LPFTIISMKD TEGIPCLGSK VKGIIEEIIE DGESSEVKAV LNDERYQSFK
260 270 280 290 300
LFTSVFGVGL KTSEKWFRMG FRTLSKVRSD KSLKFTRMQK AGFLYYEDLV
310 320 330 340 350
SCVTRAEAEA VSVLVKEAVW AFLPDAFVTM TGGFRRGKKM GHDVDFLITS
360 370 380 390 400
PGSTEDEEQL LQKVMNLWEK KGLLLYYDLV ESTFEKLRLP SRKVDALDHF
410 420 430 440 450
QKCFLIFKLP RQRVDSDQSS WQEGKTWKAI RVDLVLCPYE RRAFALLGWT
460 470 480 490 500
GSRQFERDLR RYATHERKMI LDNHALYDKT KRIFLKAESE EEIFAHLGLD

YIEPWERNA
Length:509
Mass (Da):58,536
Last modified:November 2, 2010 - v3
Checksum:i0EC01E380FA7E5A2
GO
Isoform 2 (identifier: P04053-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     454-454: Missing.

Show »
Length:508
Mass (Da):58,408
Checksum:iC72DABE3ACAEADD1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511F → L in BAD97037. 1 PublicationCurated
Sequence conflicti299 – 2991L → P in BAD97037. 1 PublicationCurated
Sequence conflicti329 – 3291T → A in BAD97037. 1 PublicationCurated
Sequence conflicti383 – 3831T → A in BAD97037. 1 PublicationCurated
Sequence conflicti389 – 3891L → M in BAD97037. 1 PublicationCurated
Sequence conflicti452 – 4521S → SP in AAA53100. (PubMed:2833741)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti112 – 1121R → G.5 Publications
Corresponds to variant rs6584066 [ dbSNP | Ensembl ].
VAR_058200

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei454 – 4541Missing in isoform 2. 2 PublicationsVSP_038397

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11722 mRNA. Translation: AAA36726.1.
M20703
, M22968, M20694, M20695, M20696, M20697, M20698, M20699, M20700, M20701, M20702 mRNA. Translation: AAA53100.1.
AB046378 mRNA. Translation: BAB72001.1.
AK223317 mRNA. Translation: BAD97037.1.
AL136181 Genomic DNA. Translation: CAH72984.1.
BC012920 mRNA. Translation: AAH12920.1.
M21195 Genomic DNA. Translation: AAA61137.1.
K01919 mRNA. Translation: AAA61136.1.
CCDSiCCDS7447.1. [P04053-1]
PIRiA23924. WXHU.
RefSeqiNP_001017520.1. NM_001017520.1. [P04053-2]
NP_004079.3. NM_004088.3. [P04053-1]
UniGeneiHs.534206.

Genome annotation databases

EnsembliENST00000371174; ENSP00000360216; ENSG00000107447. [P04053-1]
GeneIDi1791.
KEGGihsa:1791.
UCSCiuc001kmf.3. human. [P04053-1]
uc001kmg.3. human. [P04053-2]

Polymorphism databases

DMDMi311033533.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11722 mRNA. Translation: AAA36726.1 .
M20703
, M22968 , M20694 , M20695 , M20696 , M20697 , M20698 , M20699 , M20700 , M20701 , M20702 mRNA. Translation: AAA53100.1 .
AB046378 mRNA. Translation: BAB72001.1 .
AK223317 mRNA. Translation: BAD97037.1 .
AL136181 Genomic DNA. Translation: CAH72984.1 .
BC012920 mRNA. Translation: AAH12920.1 .
M21195 Genomic DNA. Translation: AAA61137.1 .
K01919 mRNA. Translation: AAA61136.1 .
CCDSi CCDS7447.1. [P04053-1 ]
PIRi A23924. WXHU.
RefSeqi NP_001017520.1. NM_001017520.1. [P04053-2 ]
NP_004079.3. NM_004088.3. [P04053-1 ]
UniGenei Hs.534206.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2COE NMR - A 19-125 [» ]
ProteinModelPortali P04053.
SMRi P04053. Positions 21-125, 149-509.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108127. 9 interactions.
IntActi P04053. 1 interaction.
STRINGi 9606.ENSP00000360216.

Chemistry

BindingDBi P04053.
ChEMBLi CHEMBL4810.

PTM databases

PhosphoSitei P04053.

Polymorphism databases

DMDMi 311033533.

Proteomic databases

MaxQBi P04053.
PaxDbi P04053.
PRIDEi P04053.

Protocols and materials databases

DNASUi 1791.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371174 ; ENSP00000360216 ; ENSG00000107447 . [P04053-1 ]
GeneIDi 1791.
KEGGi hsa:1791.
UCSCi uc001kmf.3. human. [P04053-1 ]
uc001kmg.3. human. [P04053-2 ]

Organism-specific databases

CTDi 1791.
GeneCardsi GC10P098072.
H-InvDB HIX0009072.
HGNCi HGNC:2983. DNTT.
HPAi HPA044194.
MIMi 187410. gene.
neXtProti NX_P04053.
PharmGKBi PA27449.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1796.
GeneTreei ENSGT00530000063002.
HOGENOMi HOG000263600.
HOVERGENi HBG003670.
InParanoidi P04053.
KOi K00977.
OMAi RRTTLNN.
OrthoDBi EOG7BS4BH.
PhylomeDBi P04053.
TreeFami TF103012.

Enzyme and pathway databases

SABIO-RK P04053.
SignaLinki P04053.

Miscellaneous databases

EvolutionaryTracei P04053.
GeneWikii Terminal_deoxynucleotidyl_transferase.
GenomeRNAii 1791.
NextBioi 7299.
PROi P04053.
SOURCEi Search...

Gene expression databases

Bgeei P04053.
CleanExi HS_DNTT.
Genevestigatori P04053.

Family and domain databases

Gene3Di 1.10.150.110. 1 hit.
3.30.210.10. 1 hit.
3.40.50.10190. 1 hit.
InterProi IPR001357. BRCT_dom.
IPR002054. DNA-dir_DNA_pol_X.
IPR019843. DNA_pol-X_BS.
IPR010996. DNA_pol_b-like_N.
IPR018944. DNA_pol_lambd_fingers_domain.
IPR022312. DNA_pol_X.
IPR027421. DNA_pol_X_lyase_dom.
IPR002934. Nucleotidyltransferase.
IPR029398. PolB_thumb.
IPR027292. TdT.
IPR001726. TdT/Mu.
[Graphical view ]
Pfami PF00533. BRCT. 1 hit.
PF14791. DNA_pol_B_thumb. 1 hit.
PF10391. DNA_pol_lambd_f. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000817. DNA_NT. 1 hit.
PIRSF501175. TDT. 1 hit.
PRINTSi PR00869. DNAPOLX.
PR00871. DNAPOLXTDT.
SMARTi SM00292. BRCT. 1 hit.
SM00483. POLXc. 1 hit.
[Graphical view ]
SUPFAMi SSF47802. SSF47802. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEi PS50172. BRCT. 1 hit.
PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Expression of human terminal deoxynucleotidyl transferase in Escherichia coli."
    Peterson R.C., Cheung L.C., Mattaliano R.J., White S.T., Chang L.M.S., Bollum F.J.
    J. Biol. Chem. 260:10495-10502(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT GLY-112.
  2. "Human terminal deoxyribonucleotidyltransferase: molecular cloning and structural analysis of the gene and 5' flanking region."
    Riley L.K., Morrow J.K., Danton M.J., Coleman M.S.
    Proc. Natl. Acad. Sci. U.S.A. 85:2489-2493(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-112.
  3. "Terminal deoxynucleotidyltransferase is negatively regulated by direct interaction with proliferating cell nuclear antigen."
    Ibe S., Fujita K., Toyomoto T., Shimazaki N., Kaneko R., Tanabe A., Takebe I., Kuroda S., Kobayashi T., Toji S., Tamai K., Yamamoto H., Koiwai O.
    Genes Cells 6:815-824(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-112.
  4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLY-112.
    Tissue: Thymus.
  5. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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), VARIANT GLY-112.
    Tissue: Testis.
  7. "Isolation of putative promoter region for human terminal deoxynucleotidyltransferase gene."
    Koiwai O., Morita A.
    Biochem. Biophys. Res. Commun. 154:91-100(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67.
  8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 271-508 (ISOFORM 2).
  9. "Terminal deoxynucleotidyltransferase directly interacts with a novel nuclear protein that is homologous to p65."
    Yamashita N., Shimazaki N., Ibe S., Kaneko R., Tanabe A., Toyomoto T., Fujita K., Hasegawa T., Toji S., Tamai K., Yamamoto H., Koiwai O.
    Genes Cells 6:641-652(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNTTIP1.
    Tissue: Thymus.
  10. "Terminal deoxynucleotidyltransferase forms a ternary complex with a novel chromatin remodeling protein with 82 kDa and core histone."
    Fujita K., Shimazaki N., Ohta Y., Kubota T., Ibe S., Toji S., Tamai K., Fujisaki S., Hayano T., Koiwai O.
    Genes Cells 8:559-571(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNTTIP2 AND CORE HISTONE.
  11. "Role of human Pso4 in mammalian DNA repair and association with terminal deoxynucleotidyl transferase."
    Mahajan K.N., Mitchell B.S.
    Proc. Natl. Acad. Sci. U.S.A. 100:10746-10751(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRP19.
  12. "Mutational analysis of residues in the nucleotide binding domain of human terminal deoxynucleotidyl transferase."
    Yang B., Gathy K.N., Coleman M.S.
    J. Biol. Chem. 269:11859-11868(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  13. "Solution structure of BRCT domain of terminal deoxynucleotidyltransferase."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 19-125.

Entry informationi

Entry nameiTDT_HUMAN
AccessioniPrimary (citable) accession number: P04053
Secondary accession number(s): Q53FH1, Q5W103, Q96E50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 2, 2010
Last modified: October 29, 2014
This is version 163 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3