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Protein

DNA-directed DNA polymerase

Gene

43

Organism
Enterobacteria phage RB69 (Bacteriophage RB69)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Replicates the viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction for proofreading purpose.UniRule annotation4 Publications

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).UniRule annotation5 Publications

Cofactori

Mg2+UniRule annotation13 Publications2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi114 – 1141Magnesium 1; catalytic; for 3'-5' exonuclease activityUniRule annotation
Metal bindingi116 – 1161Magnesium 1; catalytic; for 3'-5' exonuclease activityUniRule annotation
Metal bindingi222 – 2221Magnesium 2; catalytic; for 3'-5' exonuclease activityUniRule annotation1 Publication
Metal bindingi327 – 3271Magnesium 1; catalytic; for 3'-5' exonuclease activityUniRule annotation1 Publication
Metal bindingi327 – 3271Magnesium 2; catalytic; for 3'-5' exonuclease activityUniRule annotation1 Publication
Metal bindingi411 – 4111Magnesium 3; catalytic; for polymerase activityUniRule annotationCombined sources9 Publications5 Publications
Metal bindingi411 – 4111Magnesium 4; catalytic; for polymerase activityUniRule annotationCombined sources9 Publications5 Publications
Metal bindingi412 – 4121Magnesium 4; catalytic; via carbonyl oxygen; for polymerase activityUniRule annotationCombined sources3 Publications3 Publications
Binding sitei482 – 4821SubstrateUniRule annotationCombined sources
Binding sitei560 – 5601SubstrateUniRule annotationCombined sources
Sitei621 – 6211Optimization of metal coordination by the polymerase active siteUniRule annotation4 Publications
Metal bindingi623 – 6231Magnesium 3; catalytic; for polymerase activityUniRule annotationCombined sources8 Publications7 Publications
Metal bindingi623 – 6231Magnesium 4; catalytic; for polymerase activityUniRule annotationCombined sources8 Publications7 Publications
Sitei706 – 7061Optimization of metal coordination by the polymerase active siteUniRule annotation2 Publications
Sitei714 – 7141Essential for viral replicationUniRule annotation1 Publication

GO - Molecular functioni

  • 3'-5' exonuclease activity Source: UniProtKB
  • DNA binding Source: UniProtKB-KW
  • DNA-directed DNA polymerase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • nucleotide binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

DNA replication, Viral DNA replication

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding

Enzyme and pathway databases

SABIO-RKQ38087.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed DNA polymeraseUniRule annotation (EC:2.7.7.7UniRule annotation5 Publications, EC:3.1.11.-UniRule annotation3 Publications)
Alternative name(s):
Gp43
Gene namesi
Name:43
OrganismiEnterobacteria phage RB69 (Bacteriophage RB69)
Taxonomic identifieri12353 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostiEscherichia coli [TaxID: 562]
Proteomesi
  • UP000000876 Componenti: Genome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi222 – 2221D → A: Complete loss of 3'-5' exonuclease activity. 1 Publication
Mutagenesisi327 – 3271D → A: Complete loss of 3'-5' exonuclease activity. 1 Publication
Mutagenesisi415 – 4151L → A or G: Decreases base selectivity by several hundred fold. 1 Publication
Mutagenesisi415 – 4151L → G or F: Increased misinsertion, increased mismatch extension and inefficient proofreading. 1 Publication
Mutagenesisi415 – 4151L → M: No effect on base selectivity. 1 Publication
Mutagenesisi561 – 5611L → A: No effect on the ability to recognize damaged DNA. Increase in probability of nucleotide incorporation. 1 Publication
Mutagenesisi565 – 5651S → G: Increased incorporation efficiency of correct dNMPs; when associated with A-567. 1 Publication
Mutagenesisi567 – 5671Y → A: Inserts both dCMP and dAMP opposite 8-oxoG rapidly and with equal efficiency. 100-fold increase of dAMP and dGMP when situated opposite guanidinohydantoin. Increased incorporation efficiency of correct dNMPs; when associated with G-565. 3 Publications
Mutagenesisi621 – 6211D → A: Drastic decrease in the efficiency of incorporation of dGMP. 1 Publication
Mutagenesisi706 – 7061K → A: Almost complete loss of polymerase activity. 1 Publication
Mutagenesisi714 – 7141D → A: Complete loss of viral replication. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 903903DNA-directed DNA polymerasePRO_0000046547Add
BLAST

Interactioni

Subunit structurei

Part of the replicase complex that includes the DNA polymerase, the polymerase clamp, the clamp loader complex, the single-stranded DNA binding protein, and the primase/helicase (By similarity). Interacts with the polymerase clamp; this interaction constitutes the polymerase holoenzyme (PubMed:10535734).UniRule annotation1 Publication

Structurei

Secondary structure

1
903
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 118Combined sources
Beta strandi14 – 207Combined sources
Beta strandi22 – 243Combined sources
Beta strandi26 – 316Combined sources
Beta strandi36 – 405Combined sources
Beta strandi43 – 453Combined sources
Beta strandi48 – 514Combined sources
Beta strandi56 – 616Combined sources
Helixi65 – 7814Combined sources
Beta strandi82 – 843Combined sources
Helixi88 – 969Combined sources
Helixi105 – 1073Combined sources
Beta strandi110 – 1167Combined sources
Beta strandi120 – 1234Combined sources
Turni126 – 1283Combined sources
Beta strandi135 – 1406Combined sources
Turni141 – 1444Combined sources
Beta strandi145 – 1517Combined sources
Beta strandi152 – 1565Combined sources
Helixi164 – 1685Combined sources
Helixi171 – 1733Combined sources
Turni176 – 1794Combined sources
Helixi180 – 1834Combined sources
Beta strandi186 – 1938Combined sources
Helixi194 – 20714Combined sources
Beta strandi211 – 2144Combined sources
Turni218 – 2214Combined sources
Helixi222 – 23413Combined sources
Helixi236 – 2394Combined sources
Helixi240 – 2423Combined sources
Beta strandi248 – 2558Combined sources
Beta strandi258 – 2658Combined sources
Beta strandi269 – 2724Combined sources
Helixi273 – 2808Combined sources
Helixi290 – 2989Combined sources
Helixi309 – 3113Combined sources
Helixi312 – 33827Combined sources
Helixi340 – 35112Combined sources
Helixi355 – 3595Combined sources
Helixi361 – 37414Combined sources
Turni375 – 3773Combined sources
Beta strandi402 – 4043Combined sources
Beta strandi405 – 4128Combined sources
Helixi415 – 4239Combined sources
Helixi427 – 4293Combined sources
Beta strandi430 – 4334Combined sources
Helixi439 – 4435Combined sources
Beta strandi452 – 4565Combined sources
Beta strandi460 – 4634Combined sources
Beta strandi465 – 4673Combined sources
Helixi470 – 50233Combined sources
Beta strandi503 – 5053Combined sources
Beta strandi507 – 5093Combined sources
Beta strandi518 – 5203Combined sources
Helixi524 – 5307Combined sources
Beta strandi531 – 5333Combined sources
Helixi535 – 56935Combined sources
Helixi580 – 60930Combined sources
Beta strandi617 – 6215Combined sources
Beta strandi624 – 6285Combined sources
Helixi630 – 6367Combined sources
Helixi638 – 6403Combined sources
Helixi644 – 65714Combined sources
Helixi659 – 67315Combined sources
Beta strandi683 – 6897Combined sources
Beta strandi693 – 6953Combined sources
Beta strandi700 – 7045Combined sources
Beta strandi707 – 7159Combined sources
Beta strandi718 – 73013Combined sources
Helixi731 – 7333Combined sources
Helixi739 – 75416Combined sources
Helixi757 – 77014Combined sources
Helixi771 – 7733Combined sources
Helixi776 – 7794Combined sources
Beta strandi781 – 7844Combined sources
Helixi789 – 7913Combined sources
Beta strandi792 – 7976Combined sources
Helixi803 – 81412Combined sources
Turni815 – 8173Combined sources
Beta strandi819 – 8213Combined sources
Beta strandi828 – 8358Combined sources
Beta strandi837 – 8393Combined sources
Beta strandi842 – 8498Combined sources
Helixi856 – 86510Combined sources
Helixi868 – 8758Combined sources
Helixi877 – 88711Combined sources
Beta strandi891 – 8944Combined sources
Helixi897 – 9004Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B1Fmodel-R387-892[»]
1B8HX-ray3.00D893-903[»]
1CLQX-ray2.70A1-903[»]
1IG9X-ray2.60A1-903[»]
1IH7X-ray2.21A1-903[»]
1Q9XX-ray2.69A/B/C/D1-903[»]
1Q9YX-ray2.80A1-903[»]
1QE4model-F1-903[»]
1WAFX-ray3.20A/B1-903[»]
1WAGmodel-R1-903[»]
1WAHmodel-R1-903[»]
1WAImodel-R1-903[»]
1WAJX-ray2.80A1-903[»]
2ATQX-ray3.20A1-903[»]
2DTUX-ray2.37A/B/C/D1-902[»]
2DY4X-ray2.65A/B/C/D1-903[»]
2OYQX-ray2.86A/B/C/D1-903[»]
2OZMX-ray2.86A1-903[»]
2OZSX-ray2.75A1-903[»]
2P5GX-ray2.80A/B/C/D1-903[»]
2P5OX-ray2.80A/B/C/D1-903[»]
3CFOX-ray2.60A1-903[»]
3CFPX-ray2.50A1-903[»]
3CFRX-ray2.40A1-903[»]
3CQ8X-ray2.50A1-903[»]
3KD1X-ray2.66E1-903[»]
3KD5X-ray2.69E1-903[»]
3L8BX-ray2.15A/B1-903[»]
3LDSX-ray3.00A1-903[»]
3LZIX-ray2.30A1-903[»]
3LZJX-ray2.05A1-903[»]
3NAEX-ray2.00A1-903[»]
3NCIX-ray1.79A1-903[»]
3NDKX-ray2.00A1-903[»]
3NE6X-ray2.00A1-903[»]
3NGIX-ray1.89A1-903[»]
3NHGX-ray2.50A1-903[»]
3QEIX-ray2.18A1-903[»]
3QEPX-ray1.80A1-903[»]
3QERX-ray1.96A1-903[»]
3QESX-ray1.98A1-903[»]
3QETX-ray2.08A1-903[»]
3QEVX-ray1.77A1-903[»]
3QEWX-ray1.84A1-903[»]
3QEXX-ray1.73A1-903[»]
3QNNX-ray1.92A1-901[»]
3QNOX-ray1.88A1-901[»]
3RMAX-ray2.84A/B/C/D1-903[»]
3RMBX-ray2.65A/B/C/D1-903[»]
3RMCX-ray3.00A/B/C/D1-903[»]
3RMDX-ray2.98A/B/C/D1-903[»]
3RWUX-ray2.33A1-901[»]
3S9HX-ray1.95A1-903[»]
3SCXX-ray2.35A1-901[»]
3SI6X-ray1.85A1-901[»]
3SJJX-ray2.38A1-901[»]
3SNNX-ray2.00A1-901[»]
3SPYX-ray2.14A1-901[»]
3SPZX-ray2.43A1-903[»]
3SQ0X-ray2.00A1-903[»]
3SQ1X-ray1.82A1-901[»]
3SQ2X-ray2.10A1-902[»]
3SQ4X-ray2.23A1-902[»]
3SUNX-ray2.42A1-895[»]
3SUOX-ray2.23A1-900[»]
3SUPX-ray2.32A1-903[»]
3SUQX-ray3.15A1-897[»]
3TABX-ray2.80A/B/C/D1-903[»]
3TAEX-ray2.71A/B/C/D1-903[»]
3TAFX-ray3.00A/B/C/D1-903[»]
3TAGX-ray2.95A/B/C/D1-903[»]
3UIQX-ray1.88A1-903[»]
4DTJX-ray1.90A1-901[»]
4DTMX-ray1.95A1-901[»]
4DTNX-ray1.96A1-903[»]
4DTOX-ray2.05A1-903[»]
4DTPX-ray2.05A1-903[»]
4DTRX-ray2.04A1-903[»]
4DTSX-ray1.96A1-903[»]
4DTUX-ray1.86A1-903[»]
4DTXX-ray1.84A1-903[»]
4DU1X-ray2.15A1-903[»]
4DU3X-ray2.02A1-903[»]
4DU4X-ray2.28A1-903[»]
4E3SX-ray2.04A1-903[»]
4FJ5X-ray2.05A1-903[»]
4FJ7X-ray1.90A1-903[»]
4FJ8X-ray2.19A1-903[»]
4FJ9X-ray1.97A1-903[»]
4FJGX-ray2.02A1-903[»]
4FJHX-ray2.11A1-903[»]
4FJIX-ray2.20A1-903[»]
4FJJX-ray1.99A1-903[»]
4FJKX-ray2.00A1-903[»]
4FJLX-ray1.87A1-903[»]
4FJMX-ray2.02A1-903[»]
4FJNX-ray1.98A1-903[»]
4FJXX-ray2.11A1-903[»]
4FK0X-ray2.18A1-903[»]
4FK2X-ray1.98A1-903[»]
4FK4X-ray1.90A1-903[»]
4I9LX-ray2.60A1-903[»]
4I9QX-ray2.30A/B1-903[»]
4J2AX-ray1.80A1-901[»]
4J2BX-ray2.04A1-901[»]
4J2DX-ray1.76A1-901[»]
4J2EX-ray2.02A1-901[»]
4KHNX-ray2.55A/B1-903[»]
4KHQX-ray2.19A1-903[»]
4KHSX-ray2.12A1-903[»]
4KHUX-ray2.05A1-903[»]
4KHWX-ray2.37A1-903[»]
4KHYX-ray2.25A1-903[»]
4KI4X-ray2.45A1-903[»]
4KI6X-ray2.55A1-903[»]
4M3RX-ray2.07A1-903[»]
4M3TX-ray1.90A1-903[»]
4M3UX-ray2.07A1-903[»]
4M3WX-ray2.10A1-903[»]
4M3XX-ray2.20A1-903[»]
4M3YX-ray1.86A1-903[»]
4M3ZX-ray1.84A1-903[»]
4M41X-ray2.15A1-903[»]
4M42X-ray2.04A1-903[»]
4M45X-ray1.89A1-903[»]
ProteinModelPortaliQ38087.
SMRiQ38087. Positions 1-903.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ38087.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni103 – 3402383'-5'exonucleaseUniRule annotation1 PublicationAdd
BLAST
Regioni248 – 26417Beta hairpinUniRule annotation1 PublicationAdd
BLAST
Regioni380 – 903524PolymeraseUniRule annotation1 PublicationAdd
BLAST
Regioni414 – 4163Substrate bindingUniRule annotationCombined sources
Regioni705 – 7084Binding of DNA in B-conformationUniRule annotation2 Publications
Regioni897 – 9037Interaction with the polymerase clampUniRule annotation

Domaini

The N-terminus contains the 3'-5' exonuclease activity (PubMed:9215631). The C-terminus contains the polymerase activity and is involved in binding to the polymerase clamp protein (PubMed:9215631). A beta hairpin structure is necessary for the proofreading function of the polymerase (By similarity).UniRule annotation1 Publication

Sequence similaritiesi

Belongs to the DNA polymerase type-B family.UniRule annotation

Phylogenomic databases

KOiK18942.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
3.90.1600.10. 2 hits.
HAMAPiMF_04100. DPOL_T4. 1 hit.
InterProiIPR006172. DNA-dir_DNA_pol_B.
IPR017964. DNA-dir_DNA_pol_B_CS.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR023211. DNA_pol_palm_dom.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
[Graphical view]
PRINTSiPR00106. DNAPOLB.
SMARTiSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q38087-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKEFYLTVEQ IGDSIFERYI DSNGRERTRE VEYKPSLFAH CPESQATKYF
60 70 80 90 100
DIYGKPCTRK LFANMRDASQ WIKRMEDIGL EALGMDDFKL AYLSDTYNYE
110 120 130 140 150
IKYDHTKIRV ANFDIEVTSP DGFPEPSQAK HPIDAITHYD SIDDRFYVFD
160 170 180 190 200
LLNSPYGNVE EWSIEIAAKL QEQGGDEVPS EIIDKIIYMP FDNEKELLME
210 220 230 240 250
YLNFWQQKTP VILTGWNVES FDIPYVYNRI KNIFGESTAK RLSPHRKTRV
260 270 280 290 300
KVIENMYGSR EIITLFGISV LDYIDLYKKF SFTNQPSYSL DYISEFELNV
310 320 330 340 350
GKLKYDGPIS KLRESNHQRY ISYNIIDVYR VLQIDAKRQF INLSLDMGYY
360 370 380 390 400
AKIQIQSVFS PIKTWDAIIF NSLKEQNKVI PQGRSHPVQP YPGAFVKEPI
410 420 430 440 450
PNRYKYVMSF DLTSLYPSII RQVNISPETI AGTFKVAPLH DYINAVAERP
460 470 480 490 500
SDVYSCSPNG MMYYKDRDGV VPTEITKVFN QRKEHKGYML AAQRNGEIIK
510 520 530 540 550
EALHNPNLSV DEPLDVDYRF DFSDEIKEKI KKLSAKSLNE MLFRAQRTEV
560 570 580 590 600
AGMTAQINRK LLINSLYGAL GNVWFRYYDL RNATAITTFG QMALQWIERK
610 620 630 640 650
VNEYLNEVCG TEGEAFVLYG DTDSIYVSAD KIIDKVGESK FRDTNHWVDF
660 670 680 690 700
LDKFARERME PAIDRGFREM CEYMNNKQHL MFMDREAIAG PPLGSKGIGG
710 720 730 740 750
FWTGKKRYAL NVWDMEGTRY AEPKLKIMGL ETQKSSTPKA VQKALKECIR
760 770 780 790 800
RMLQEGEESL QEYFKEFEKE FRQLNYISIA SVSSANNIAK YDVGGFPGPK
810 820 830 840 850
CPFHIRGILT YNRAIKGNID APQVVEGEKV YVLPLREGNP FGDKCIAWPS
860 870 880 890 900
GTEITDLIKD DVLHWMDYTV LLEKTFIKPL EGFTSAAKLD YEKKASLFDM

FDF
Length:903
Mass (Da):104,613
Last modified:November 1, 1996 - v1
Checksum:iA3983FC16D4C0509
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34036 Genomic DNA. Translation: AAA93077.1.
AY303349 Genomic DNA. Translation: AAP75958.1.
RefSeqiNP_861746.1. NC_004928.1.

Genome annotation databases

GeneIDi1494172.
KEGGivg:1494172.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34036 Genomic DNA. Translation: AAA93077.1.
AY303349 Genomic DNA. Translation: AAP75958.1.
RefSeqiNP_861746.1. NC_004928.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B1Fmodel-R387-892[»]
1B8HX-ray3.00D893-903[»]
1CLQX-ray2.70A1-903[»]
1IG9X-ray2.60A1-903[»]
1IH7X-ray2.21A1-903[»]
1Q9XX-ray2.69A/B/C/D1-903[»]
1Q9YX-ray2.80A1-903[»]
1QE4model-F1-903[»]
1WAFX-ray3.20A/B1-903[»]
1WAGmodel-R1-903[»]
1WAHmodel-R1-903[»]
1WAImodel-R1-903[»]
1WAJX-ray2.80A1-903[»]
2ATQX-ray3.20A1-903[»]
2DTUX-ray2.37A/B/C/D1-902[»]
2DY4X-ray2.65A/B/C/D1-903[»]
2OYQX-ray2.86A/B/C/D1-903[»]
2OZMX-ray2.86A1-903[»]
2OZSX-ray2.75A1-903[»]
2P5GX-ray2.80A/B/C/D1-903[»]
2P5OX-ray2.80A/B/C/D1-903[»]
3CFOX-ray2.60A1-903[»]
3CFPX-ray2.50A1-903[»]
3CFRX-ray2.40A1-903[»]
3CQ8X-ray2.50A1-903[»]
3KD1X-ray2.66E1-903[»]
3KD5X-ray2.69E1-903[»]
3L8BX-ray2.15A/B1-903[»]
3LDSX-ray3.00A1-903[»]
3LZIX-ray2.30A1-903[»]
3LZJX-ray2.05A1-903[»]
3NAEX-ray2.00A1-903[»]
3NCIX-ray1.79A1-903[»]
3NDKX-ray2.00A1-903[»]
3NE6X-ray2.00A1-903[»]
3NGIX-ray1.89A1-903[»]
3NHGX-ray2.50A1-903[»]
3QEIX-ray2.18A1-903[»]
3QEPX-ray1.80A1-903[»]
3QERX-ray1.96A1-903[»]
3QESX-ray1.98A1-903[»]
3QETX-ray2.08A1-903[»]
3QEVX-ray1.77A1-903[»]
3QEWX-ray1.84A1-903[»]
3QEXX-ray1.73A1-903[»]
3QNNX-ray1.92A1-901[»]
3QNOX-ray1.88A1-901[»]
3RMAX-ray2.84A/B/C/D1-903[»]
3RMBX-ray2.65A/B/C/D1-903[»]
3RMCX-ray3.00A/B/C/D1-903[»]
3RMDX-ray2.98A/B/C/D1-903[»]
3RWUX-ray2.33A1-901[»]
3S9HX-ray1.95A1-903[»]
3SCXX-ray2.35A1-901[»]
3SI6X-ray1.85A1-901[»]
3SJJX-ray2.38A1-901[»]
3SNNX-ray2.00A1-901[»]
3SPYX-ray2.14A1-901[»]
3SPZX-ray2.43A1-903[»]
3SQ0X-ray2.00A1-903[»]
3SQ1X-ray1.82A1-901[»]
3SQ2X-ray2.10A1-902[»]
3SQ4X-ray2.23A1-902[»]
3SUNX-ray2.42A1-895[»]
3SUOX-ray2.23A1-900[»]
3SUPX-ray2.32A1-903[»]
3SUQX-ray3.15A1-897[»]
3TABX-ray2.80A/B/C/D1-903[»]
3TAEX-ray2.71A/B/C/D1-903[»]
3TAFX-ray3.00A/B/C/D1-903[»]
3TAGX-ray2.95A/B/C/D1-903[»]
3UIQX-ray1.88A1-903[»]
4DTJX-ray1.90A1-901[»]
4DTMX-ray1.95A1-901[»]
4DTNX-ray1.96A1-903[»]
4DTOX-ray2.05A1-903[»]
4DTPX-ray2.05A1-903[»]
4DTRX-ray2.04A1-903[»]
4DTSX-ray1.96A1-903[»]
4DTUX-ray1.86A1-903[»]
4DTXX-ray1.84A1-903[»]
4DU1X-ray2.15A1-903[»]
4DU3X-ray2.02A1-903[»]
4DU4X-ray2.28A1-903[»]
4E3SX-ray2.04A1-903[»]
4FJ5X-ray2.05A1-903[»]
4FJ7X-ray1.90A1-903[»]
4FJ8X-ray2.19A1-903[»]
4FJ9X-ray1.97A1-903[»]
4FJGX-ray2.02A1-903[»]
4FJHX-ray2.11A1-903[»]
4FJIX-ray2.20A1-903[»]
4FJJX-ray1.99A1-903[»]
4FJKX-ray2.00A1-903[»]
4FJLX-ray1.87A1-903[»]
4FJMX-ray2.02A1-903[»]
4FJNX-ray1.98A1-903[»]
4FJXX-ray2.11A1-903[»]
4FK0X-ray2.18A1-903[»]
4FK2X-ray1.98A1-903[»]
4FK4X-ray1.90A1-903[»]
4I9LX-ray2.60A1-903[»]
4I9QX-ray2.30A/B1-903[»]
4J2AX-ray1.80A1-901[»]
4J2BX-ray2.04A1-901[»]
4J2DX-ray1.76A1-901[»]
4J2EX-ray2.02A1-901[»]
4KHNX-ray2.55A/B1-903[»]
4KHQX-ray2.19A1-903[»]
4KHSX-ray2.12A1-903[»]
4KHUX-ray2.05A1-903[»]
4KHWX-ray2.37A1-903[»]
4KHYX-ray2.25A1-903[»]
4KI4X-ray2.45A1-903[»]
4KI6X-ray2.55A1-903[»]
4M3RX-ray2.07A1-903[»]
4M3TX-ray1.90A1-903[»]
4M3UX-ray2.07A1-903[»]
4M3WX-ray2.10A1-903[»]
4M3XX-ray2.20A1-903[»]
4M3YX-ray1.86A1-903[»]
4M3ZX-ray1.84A1-903[»]
4M41X-ray2.15A1-903[»]
4M42X-ray2.04A1-903[»]
4M45X-ray1.89A1-903[»]
ProteinModelPortaliQ38087.
SMRiQ38087. Positions 1-903.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1494172.
KEGGivg:1494172.

Phylogenomic databases

KOiK18942.

Enzyme and pathway databases

SABIO-RKQ38087.

Miscellaneous databases

EvolutionaryTraceiQ38087.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
3.90.1600.10. 2 hits.
HAMAPiMF_04100. DPOL_T4. 1 hit.
InterProiIPR006172. DNA-dir_DNA_pol_B.
IPR017964. DNA-dir_DNA_pol_B_CS.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR023211. DNA_pol_palm_dom.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
[Graphical view]
PRINTSiPR00106. DNAPOLB.
SMARTiSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDPOL_BPR69
AccessioniPrimary (citable) accession number: Q38087
Secondary accession number(s): Q76XX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.