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Protein

DNA polymerase I

Gene

polA

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

Functioni

In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' and 5' to 3' exonuclease activity. It is able to utilize nicked circular duplex DNA as a template and can unwind the parental DNA strand from its template.

Catalytic activityi

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

GO - Molecular functioni

  1. 3'-5' exonuclease activity Source: EcoCyc
  2. 5'-3' exonuclease activity Source: EcoCyc
  3. DNA binding Source: EcoCyc
  4. DNA-directed DNA polymerase activity Source: EcoCyc

GO - Biological processi

  1. base-excision repair Source: EcoCyc
  2. DNA biosynthetic process Source: GOC
  3. DNA-dependent DNA replication Source: EcoCyc
  4. DNA repair Source: EcoCyc
  5. DNA replication Source: EcoCyc
  6. nucleic acid phosphodiester bond hydrolysis Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Exonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA damage, DNA repair, DNA replication

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10746-MONOMER.
ECOL316407:JW3835-MONOMER.
MetaCyc:EG10746-MONOMER.
RETL1328306-WGS:GSTH-159-MONOMER.
BRENDAi2.7.7.7. 2026.
SABIO-RKP00582.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase I (EC:2.7.7.7)
Short name:
POL I
Gene namesi
Name:polA
Synonyms:resA
Ordered Locus Names:b3863, JW3835
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10746. polA.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 928928DNA polymerase IPRO_0000101239Add
BLAST

Proteomic databases

PaxDbiP00582.
PRIDEiP00582.

2D gel databases

SWISS-2DPAGEP00582.

Expressioni

Gene expression databases

GenevestigatoriP00582.

Interactioni

Subunit structurei

Single-chain monomer with multiple functions.

Protein-protein interaction databases

DIPiDIP-10524N.
IntActiP00582. 28 interactions.
MINTiMINT-1225247.
STRINGi511145.b3863.

Structurei

Secondary structure

1
928
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi327 – 3326Combined sources
Helixi336 – 34712Combined sources
Beta strandi349 – 35911Combined sources
Turni363 – 3653Combined sources
Beta strandi368 – 3769Combined sources
Beta strandi379 – 3846Combined sources
Helixi398 – 40912Combined sources
Beta strandi416 – 4205Combined sources
Helixi421 – 4299Combined sources
Turni430 – 4323Combined sources
Beta strandi438 – 4414Combined sources
Helixi442 – 4498Combined sources
Helixi451 – 4533Combined sources
Helixi458 – 4658Combined sources
Helixi473 – 4775Combined sources
Helixi480 – 4823Combined sources
Helixi486 – 4883Combined sources
Helixi491 – 51525Combined sources
Helixi520 – 5289Combined sources
Helixi530 – 54314Combined sources
Beta strandi545 – 5473Combined sources
Helixi549 – 57325Combined sources
Beta strandi574 – 5763Combined sources
Turni582 – 5854Combined sources
Helixi587 – 5904Combined sources
Turni591 – 5933Combined sources
Turni608 – 6103Combined sources
Helixi613 – 6175Combined sources
Turni618 – 6203Combined sources
Helixi623 – 63917Combined sources
Turni640 – 6434Combined sources
Helixi644 – 6474Combined sources
Turni650 – 6523Combined sources
Beta strandi653 – 6553Combined sources
Beta strandi658 – 6625Combined sources
Beta strandi665 – 6673Combined sources
Beta strandi670 – 6745Combined sources
Helixi676 – 6783Combined sources
Beta strandi681 – 6833Combined sources
Helixi684 – 6918Combined sources
Beta strandi699 – 7068Combined sources
Helixi709 – 7179Combined sources
Helixi721 – 7288Combined sources
Helixi733 – 7419Combined sources
Helixi746 – 7483Combined sources
Helixi751 – 76515Combined sources
Helixi772 – 7776Combined sources
Turni781 – 7833Combined sources
Helixi784 – 79411Combined sources
Helixi796 – 81217Combined sources
Beta strandi813 – 8164Combined sources
Beta strandi822 – 8243Combined sources
Turni826 – 8294Combined sources
Helixi833 – 87038Combined sources
Beta strandi873 – 8808Combined sources
Beta strandi883 – 8897Combined sources
Turni890 – 8923Combined sources
Helixi893 – 90614Combined sources
Beta strandi910 – 9123Combined sources
Beta strandi916 – 9238Combined sources
Helixi924 – 9274Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8YX-ray2.08A324-928[»]
1D9DX-ray2.18A324-928[»]
1D9FX-ray3.00A324-928[»]
1DPIX-ray2.80A324-928[»]
1KFDX-ray3.90A324-928[»]
1KFSX-ray2.10A324-928[»]
1KLNX-ray3.20A324-928[»]
1KRPX-ray2.20A324-928[»]
1KSPX-ray2.30A324-928[»]
1QSLX-ray2.20A324-928[»]
2KFNX-ray2.03A324-928[»]
2KFZX-ray2.03A324-928[»]
2KZMX-ray2.60A324-928[»]
2KZZX-ray2.25A324-928[»]
ProteinModelPortaliP00582.
SMRiP00582. Positions 5-284, 324-928.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00582.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 3233235'-3' exonucleaseAdd
BLAST
Domaini324 – 5171943'-5' exonucleaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni324 – 928605Klenow fragmentAdd
BLAST
Regioni521 – 928408PolymeraseAdd
BLAST

Sequence similaritiesi

Belongs to the DNA polymerase type-A family.Curated
Contains 1 3'-5' exonuclease domain.Curated
Contains 1 5'-3' exonuclease domain.Curated

Phylogenomic databases

eggNOGiCOG0258.
HOGENOMiHOG000020998.
InParanoidiP00582.
KOiK02335.
OMAiKANRPPM.
OrthoDBiEOG6SJJH7.
PhylomeDBiP00582.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
3.40.50.1010. 1 hit.
InterProiIPR002562. 3'-5'_exonuclease_dom.
IPR020046. 5-3_exonucl_a-hlix_arch_N.
IPR020045. 5-3_exonuclease_C.
IPR002421. 5-3_exonuclease_N.
IPR019760. DNA-dir_DNA_pol_A_CS.
IPR001098. DNA-dir_DNA_pol_A_palm_dom.
IPR018320. DNA_polymerase_1.
IPR002298. DNA_polymerase_A.
IPR008918. HhH2.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR029060. PIN_domain-like.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF01367. 5_3_exonuc. 1 hit.
PF02739. 5_3_exonuc_N. 1 hit.
PF00476. DNA_pol_A. 1 hit.
PF01612. DNA_pol_A_exo1. 1 hit.
[Graphical view]
PRINTSiPR00868. DNAPOLI.
SMARTiSM00474. 35EXOc. 1 hit.
SM00475. 53EXOc. 1 hit.
SM00278. HhH1. 1 hit.
SM00279. HhH2. 1 hit.
SM00482. POLAc. 1 hit.
[Graphical view]
SUPFAMiSSF47807. SSF47807. 1 hit.
SSF53098. SSF53098. 1 hit.
SSF88723. SSF88723. 1 hit.
TIGRFAMsiTIGR00593. pola. 1 hit.
PROSITEiPS00447. DNA_POLYMERASE_A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00582-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQIPQNPLI LVDGSSYLYR AYHAFPPLTN SAGEPTGAMY GVLNMLRSLI
60 70 80 90 100
MQYKPTHAAV VFDAKGKTFR DELFEHYKSH RPPMPDDLRA QIEPLHAMVK
110 120 130 140 150
AMGLPLLAVS GVEADDVIGT LAREAEKAGR PVLISTGDKD MAQLVTPNIT
160 170 180 190 200
LINTMTNTIL GPEEVVNKYG VPPELIIDFL ALMGDSSDNI PGVPGVGEKT
210 220 230 240 250
AQALLQGLGG LDTLYAEPEK IAGLSFRGAK TMAAKLEQNK EVAYLSYQLA
260 270 280 290 300
TIKTDVELEL TCEQLEVQQP AAEELLGLFK KYEFKRWTAD VEAGKWLQAK
310 320 330 340 350
GAKPAAKPQE TSVADEAPEV TATVISYDNY VTILDEETLK AWIAKLEKAP
360 370 380 390 400
VFAFDTETDS LDNISANLVG LSFAIEPGVA AYIPVAHDYL DAPDQISRER
410 420 430 440 450
ALELLKPLLE DEKALKVGQN LKYDRGILAN YGIELRGIAF DTMLESYILN
460 470 480 490 500
SVAGRHDMDS LAERWLKHKT ITFEEIAGKG KNQLTFNQIA LEEAGRYAAE
510 520 530 540 550
DADVTLQLHL KMWPDLQKHK GPLNVFENIE MPLVPVLSRI ERNGVKIDPK
560 570 580 590 600
VLHNHSEELT LRLAELEKKA HEIAGEEFNL SSTKQLQTIL FEKQGIKPLK
610 620 630 640 650
KTPGGAPSTS EEVLEELALD YPLPKVILEY RGLAKLKSTY TDKLPLMINP
660 670 680 690 700
KTGRVHTSYH QAVTATGRLS STDPNLQNIP VRNEEGRRIR QAFIAPEDYV
710 720 730 740 750
IVSADYSQIE LRIMAHLSRD KGLLTAFAEG KDIHRATAAE VFGLPLETVT
760 770 780 790 800
SEQRRSAKAI NFGLIYGMSA FGLARQLNIP RKEAQKYMDL YFERYPGVLE
810 820 830 840 850
YMERTRAQAK EQGYVETLDG RRLYLPDIKS SNGARRAAAE RAAINAPMQG
860 870 880 890 900
TAADIIKRAM IAVDAWLQAE QPRVRMIMQV HDELVFEVHK DDVDAVAKQI
910 920
HQLMENCTRL DVPLLVEVGS GENWDQAH
Length:928
Mass (Da):103,118
Last modified:July 21, 1986 - v1
Checksum:iDAAE1C448A59030C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00317 Genomic DNA. Translation: CAA23607.1.
L19201 Genomic DNA. Translation: AAB02998.1.
U00096 Genomic DNA. Translation: AAC76861.1.
AP009048 Genomic DNA. Translation: BAE77445.1.
J01663 Genomic DNA. Translation: AAA24402.1.
J01664 Genomic DNA. Translation: AAA24404.1.
PIRiA92360. DJECI.
RefSeqiNP_418300.1. NC_000913.3.
YP_491586.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76861; AAC76861; b3863.
BAE77445; BAE77445; BAE77445.
GeneIDi12933188.
948356.
KEGGiecj:Y75_p3322.
eco:b3863.
PATRICi32123225. VBIEscCol129921_3973.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00317 Genomic DNA. Translation: CAA23607.1.
L19201 Genomic DNA. Translation: AAB02998.1.
U00096 Genomic DNA. Translation: AAC76861.1.
AP009048 Genomic DNA. Translation: BAE77445.1.
J01663 Genomic DNA. Translation: AAA24402.1.
J01664 Genomic DNA. Translation: AAA24404.1.
PIRiA92360. DJECI.
RefSeqiNP_418300.1. NC_000913.3.
YP_491586.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8YX-ray2.08A324-928[»]
1D9DX-ray2.18A324-928[»]
1D9FX-ray3.00A324-928[»]
1DPIX-ray2.80A324-928[»]
1KFDX-ray3.90A324-928[»]
1KFSX-ray2.10A324-928[»]
1KLNX-ray3.20A324-928[»]
1KRPX-ray2.20A324-928[»]
1KSPX-ray2.30A324-928[»]
1QSLX-ray2.20A324-928[»]
2KFNX-ray2.03A324-928[»]
2KFZX-ray2.03A324-928[»]
2KZMX-ray2.60A324-928[»]
2KZZX-ray2.25A324-928[»]
ProteinModelPortaliP00582.
SMRiP00582. Positions 5-284, 324-928.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10524N.
IntActiP00582. 28 interactions.
MINTiMINT-1225247.
STRINGi511145.b3863.

Chemistry

BindingDBiP00582.
ChEMBLiCHEMBL4298.
DrugBankiDB00548. Azelaic Acid.

2D gel databases

SWISS-2DPAGEP00582.

Proteomic databases

PaxDbiP00582.
PRIDEiP00582.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76861; AAC76861; b3863.
BAE77445; BAE77445; BAE77445.
GeneIDi12933188.
948356.
KEGGiecj:Y75_p3322.
eco:b3863.
PATRICi32123225. VBIEscCol129921_3973.

Organism-specific databases

EchoBASEiEB0739.
EcoGeneiEG10746. polA.

Phylogenomic databases

eggNOGiCOG0258.
HOGENOMiHOG000020998.
InParanoidiP00582.
KOiK02335.
OMAiKANRPPM.
OrthoDBiEOG6SJJH7.
PhylomeDBiP00582.

Enzyme and pathway databases

BioCyciEcoCyc:EG10746-MONOMER.
ECOL316407:JW3835-MONOMER.
MetaCyc:EG10746-MONOMER.
RETL1328306-WGS:GSTH-159-MONOMER.
BRENDAi2.7.7.7. 2026.
SABIO-RKP00582.

Miscellaneous databases

EvolutionaryTraceiP00582.
PROiP00582.

Gene expression databases

GenevestigatoriP00582.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
3.40.50.1010. 1 hit.
InterProiIPR002562. 3'-5'_exonuclease_dom.
IPR020046. 5-3_exonucl_a-hlix_arch_N.
IPR020045. 5-3_exonuclease_C.
IPR002421. 5-3_exonuclease_N.
IPR019760. DNA-dir_DNA_pol_A_CS.
IPR001098. DNA-dir_DNA_pol_A_palm_dom.
IPR018320. DNA_polymerase_1.
IPR002298. DNA_polymerase_A.
IPR008918. HhH2.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR029060. PIN_domain-like.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF01367. 5_3_exonuc. 1 hit.
PF02739. 5_3_exonuc_N. 1 hit.
PF00476. DNA_pol_A. 1 hit.
PF01612. DNA_pol_A_exo1. 1 hit.
[Graphical view]
PRINTSiPR00868. DNAPOLI.
SMARTiSM00474. 35EXOc. 1 hit.
SM00475. 53EXOc. 1 hit.
SM00278. HhH1. 1 hit.
SM00279. HhH2. 1 hit.
SM00482. POLAc. 1 hit.
[Graphical view]
SUPFAMiSSF47807. SSF47807. 1 hit.
SSF53098. SSF53098. 1 hit.
SSF88723. SSF88723. 1 hit.
TIGRFAMsiTIGR00593. pola. 1 hit.
PROSITEiPS00447. DNA_POLYMERASE_A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the Escherichia coli polA gene and primary structure of DNA polymerase I."
    Joyce C.M., Kelley W.S., Grindley N.D.F.
    J. Biol. Chem. 257:1958-1964(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
    Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 21:3391-3398(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Identification of two genes immediately downstream from the polA gene of Escherichia coli."
    Joyce C.M., Grindley N.D.
    J. Bacteriol. 152:1211-1219(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 918-928.
    Strain: K12.
  6. "Genetic characterization of early amber mutations in the Escherichia coli polA gene and purification of the amber peptides."
    Kelley W.S., Joyce C.M.
    J. Mol. Biol. 164:529-560(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 284-350.
  7. "Escherichia coli DNA polymerase I. Sequence characterization and secondary structure prediction."
    Brown W.E., Stump K.H., Kelley W.S.
    J. Biol. Chem. 257:1965-1972(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: AMINO-ACID COMPOSITION, PARTIAL PROTEIN SEQUENCE.
  8. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  9. "Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP."
    Ollis D.L., Brick P., Hamlin R., Xuong N.G., Steitz T.A.
    Nature 313:762-766(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF KLENOW FRAGMENT.
  10. "Structural basis for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism."
    Beese L.S., Steitz T.A.
    EMBO J. 10:25-33(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF KLENOW FRAGMENT.
  11. "Structure of DNA polymerase I Klenow fragment bound to duplex DNA."
    Beese L.S., Derbyshire V., Steitz T.A.
    Science 260:352-355(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF KLENOW FRAGMENT.
  12. "Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and pyrophosphate."
    Beese L.S., Friedman J.M., Steitz T.A.
    Biochemistry 32:14095-14101(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.9 ANGSTROMS) OF KLENOW FRAGMENT.
  13. "Structural principles for the inhibition of the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I by phosphorothioates."
    Brautigam C.A., Steitz T.A.
    J. Mol. Biol. 277:363-377(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF KLENOW FRAGMENT.
  14. "Structures of normal single-stranded DNA and deoxyribo-3'-S-phosphorothiolates bound to the 3'-5' exonucleolytic active site of DNA polymerase I from Escherichia coli."
    Brautigam C.A., Sun S., Piccirilli J.A., Steitz T.A.
    Biochemistry 38:696-704(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF KLENOW FRAGMENT.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF KLENOW FRAGMENT.
  16. "Sequential proton NMR resonance assignments, circular dichroism, and structural properties of a 50-residue substrate-binding peptide from DNA polymerase I."
    Mullen G.P., Vaughn J.B. Jr., Mildvan A.S.
    Arch. Biochem. Biophys. 301:174-183(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 728-777.

Entry informationi

Entry nameiDPO1_ECOLI
AccessioniPrimary (citable) accession number: P00582
Secondary accession number(s): Q2M8G1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 1, 2015
This is version 167 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.