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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)DescriptionActionsGraphical viewLength
Metal bindingi114Magnesium 1; catalytic; for 3'-5' exonuclease activityUniRule annotation1
Metal bindingi116Magnesium 1; catalytic; for 3'-5' exonuclease activityUniRule annotation1
Metal bindingi222Magnesium 2; catalytic; for 3'-5' exonuclease activityUniRule annotation1 Publication1
Metal bindingi327Magnesium 1; catalytic; for 3'-5' exonuclease activityUniRule annotation1 Publication1
Metal bindingi327Magnesium 2; catalytic; for 3'-5' exonuclease activityUniRule annotation1 Publication1
Metal bindingi411Magnesium 3; catalytic; for polymerase activityUniRule annotationCombined sources9 Publications5 Publications1
Metal bindingi411Magnesium 4; catalytic; for polymerase activityUniRule annotationCombined sources9 Publications5 Publications1
Metal bindingi412Magnesium 4; catalytic; via carbonyl oxygen; for polymerase activityUniRule annotationCombined sources3 Publications3 Publications1
Binding sitei482SubstrateUniRule annotationCombined sources1
Binding sitei560SubstrateUniRule annotationCombined sources1
Sitei621Optimization of metal coordination by the polymerase active siteUniRule annotation4 Publications1
Metal bindingi623Magnesium 3; catalytic; for polymerase activityUniRule annotationCombined sources8 Publications7 Publications1
Metal bindingi623Magnesium 4; catalytic; for polymerase activityUniRule annotationCombined sources8 Publications7 Publications1
Sitei706Optimization of metal coordination by the polymerase active siteUniRule annotation2 Publications1
Sitei714Essential for viral replicationUniRule annotation1 Publication1

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)DescriptionActionsGraphical viewLength
Mutagenesisi222D → A: Complete loss of 3'-5' exonuclease activity. 1 Publication1
Mutagenesisi327D → A: Complete loss of 3'-5' exonuclease activity. 1 Publication1
Mutagenesisi415L → A or G: Decreases base selectivity by several hundred fold. 1 Publication1
Mutagenesisi415L → G or F: Increased misinsertion, increased mismatch extension and inefficient proofreading. 1 Publication1
Mutagenesisi415L → M: No effect on base selectivity. 1 Publication1
Mutagenesisi561L → A: No effect on the ability to recognize damaged DNA. Increase in probability of nucleotide incorporation. 1 Publication1
Mutagenesisi565S → G: Increased incorporation efficiency of correct dNMPs; when associated with A-567. 1 Publication1
Mutagenesisi567Y → 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 Publications1
Mutagenesisi621D → A: Drastic decrease in the efficiency of incorporation of dGMP. 1 Publication1
Mutagenesisi706K → A: Almost complete loss of polymerase activity. 1 Publication1
Mutagenesisi714D → A: Complete loss of viral replication. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000465471 – 903DNA-directed DNA polymeraseAdd BLAST903

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

1903
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 11Combined sources8
Beta strandi14 – 20Combined sources7
Beta strandi22 – 24Combined sources3
Beta strandi26 – 31Combined sources6
Beta strandi36 – 40Combined sources5
Beta strandi43 – 45Combined sources3
Beta strandi48 – 51Combined sources4
Beta strandi56 – 61Combined sources6
Helixi65 – 78Combined sources14
Beta strandi82 – 84Combined sources3
Helixi88 – 96Combined sources9
Helixi105 – 107Combined sources3
Beta strandi110 – 116Combined sources7
Beta strandi120 – 123Combined sources4
Turni126 – 128Combined sources3
Beta strandi135 – 140Combined sources6
Turni141 – 144Combined sources4
Beta strandi145 – 151Combined sources7
Beta strandi152 – 156Combined sources5
Helixi164 – 168Combined sources5
Helixi171 – 173Combined sources3
Turni176 – 179Combined sources4
Helixi180 – 183Combined sources4
Beta strandi186 – 193Combined sources8
Helixi194 – 207Combined sources14
Beta strandi211 – 214Combined sources4
Turni218 – 221Combined sources4
Helixi222 – 234Combined sources13
Helixi236 – 239Combined sources4
Helixi240 – 242Combined sources3
Beta strandi248 – 255Combined sources8
Beta strandi258 – 265Combined sources8
Beta strandi269 – 272Combined sources4
Helixi273 – 280Combined sources8
Helixi290 – 298Combined sources9
Helixi309 – 311Combined sources3
Helixi312 – 338Combined sources27
Helixi340 – 351Combined sources12
Helixi355 – 359Combined sources5
Helixi361 – 374Combined sources14
Turni375 – 377Combined sources3
Beta strandi402 – 404Combined sources3
Beta strandi405 – 412Combined sources8
Helixi415 – 423Combined sources9
Helixi427 – 429Combined sources3
Beta strandi430 – 433Combined sources4
Helixi439 – 443Combined sources5
Beta strandi452 – 456Combined sources5
Beta strandi460 – 463Combined sources4
Beta strandi465 – 467Combined sources3
Helixi470 – 502Combined sources33
Beta strandi503 – 505Combined sources3
Beta strandi507 – 509Combined sources3
Beta strandi518 – 520Combined sources3
Helixi524 – 530Combined sources7
Beta strandi531 – 533Combined sources3
Helixi535 – 569Combined sources35
Helixi580 – 609Combined sources30
Beta strandi617 – 621Combined sources5
Beta strandi624 – 628Combined sources5
Helixi630 – 636Combined sources7
Helixi638 – 640Combined sources3
Helixi644 – 657Combined sources14
Helixi659 – 673Combined sources15
Beta strandi683 – 689Combined sources7
Beta strandi693 – 695Combined sources3
Beta strandi700 – 704Combined sources5
Beta strandi707 – 715Combined sources9
Beta strandi718 – 730Combined sources13
Helixi731 – 733Combined sources3
Helixi739 – 754Combined sources16
Helixi757 – 770Combined sources14
Helixi771 – 773Combined sources3
Helixi776 – 779Combined sources4
Beta strandi781 – 784Combined sources4
Helixi789 – 791Combined sources3
Beta strandi792 – 797Combined sources6
Helixi803 – 814Combined sources12
Turni815 – 817Combined sources3
Beta strandi819 – 821Combined sources3
Beta strandi828 – 835Combined sources8
Beta strandi837 – 839Combined sources3
Beta strandi842 – 849Combined sources8
Helixi856 – 865Combined sources10
Helixi868 – 875Combined sources8
Helixi877 – 887Combined sources11
Beta strandi891 – 894Combined sources4
Helixi897 – 900Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ38087.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni103 – 3403'-5'exonucleaseUniRule annotation1 PublicationAdd BLAST238
Regioni248 – 264Beta hairpinUniRule annotation1 PublicationAdd BLAST17
Regioni380 – 903PolymeraseUniRule annotation1 PublicationAdd BLAST524
Regioni414 – 416Substrate bindingUniRule annotationCombined sources3
Regioni705 – 708Binding of DNA in B-conformationUniRule annotation2 Publications4
Regioni897 – 903Interaction with the polymerase clampUniRule annotation7

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
PDB 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.
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: November 30, 2016
This is version 122 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, Reference proteome

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.