UniProtKB - P03680 (DPOL_BPPH2)
DNA polymerase
2
Functioni
Polymerase responsible for protein-primed viral DNA replication by strand displacement with high processivity and fidelity (PubMed:3863101) (PubMed:2498321).
To start replication, the DNA polymerase forms a heterodimer with a free primer terminal protein (TP), recognizes the replication origins at both 5' ends of the linear chromosome, and initiates replication using as primer the OH-group of Ser-232 of the TP (PubMed:22210885).
This polymerase possesses three enzymatic activities: DNA synthesis (polymerase), primer terminal protein (TP) deoxynucleotidylation, which is the formation of a covalent linkage (phosphoester) between the hydroxyl group of a specific serine residue in TP and 5'-dAMP, a reaction directed by the second T at the 3' end, and 3' to 5' exonuclease activity (PubMed:2790959).
Exonuclease activity has a proofreading purpose (PubMed:2790959).
DNA polymerase edits the polymerization errors using an intramolecular pathway as the primer terminus travels from one active site to the other without dissociation from the DNA (PubMed:10493855).
DNA polymerization catalyzed by the DNA polymerase is a highly accurate process, but the protein-primed initiation is a quite inaccurate reaction (PubMed:8428945).
Since the polymerase initiates the replication on the second thymine, the TP-dAMP initiation product translocates backwards to recover the template information of the first nucleotide (sliding back-mechanism) (PubMed:19011105).
9 PublicationsMiscellaneous
Catalytic activityi
- EC:2.7.7.71 Publication
Cofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 12 | Essential for 3'-5' exonucleolysis2 Publications | 1 | |
Sitei | 14 | Essential for 3'-5' exonucleolysis2 Publications | 1 | |
Sitei | 15 | Involved in proofreading function by stabilization of the frayed primer-terminus at the 3'-5' exonuclease active site1 Publication | 1 | |
Sitei | 62 | Involved in proofreading function by stabilization of the frayed primer-terminus at the 3'-5' exonuclease active site1 Publication | 1 | |
Sitei | 65 | Binds ssDNA; Essential for 3'-5' exonucleolysis1 Publication | 1 | |
Sitei | 66 | Essential for 3'-5' exonucleolysis2 Publications | 1 | |
Sitei | 93 | Involved in binding template-primer structures1 Publication | 1 | |
Sitei | 122 | Binds ssDNA; Essential for 3'-5' exonucleolysis1 Publication | 1 | |
Sitei | 123 | Binds ssDNA; Essential for 3'-5' exonucleolysis1 Publication | 1 | |
Metal bindingi | 145 | Magnesium 1Combined sources | 1 | |
Sitei | 148 | Involved in the stabilization of the frayed 3' terminus at the exonuclease active site1 Publication | 1 | |
Metal bindingi | 169 | Magnesium 1Combined sources | 1 | |
Metal bindingi | 249 | Magnesium 2; catalyticCombined sources1 Publication | 1 | |
Metal bindingi | 250 | Magnesium 2; via carbonyl oxygen; catalyticCombined sources1 Publication | 1 | |
Sitei | 252 | Probably involved in binding template-primer structures1 Publication | 1 | |
Binding sitei | 254 | TTP; via amide nitrogenCombined sources | 1 | |
Sitei | 254 | Probably involved in nucleotide binding selection1 Publication | 1 | |
Sitei | 356 | Binds ssDNA; Essential for 3'-5' exonucleolysis1 Publication | 1 | |
Sitei | 364 | Involved in the binding of DNA and dNTP1 Publication | 1 | |
Sitei | 366 | Stabilization of the incoming nucleotide1 Publication | 1 | |
Binding sitei | 371 | TTPCombined sources | 1 | |
Sitei | 371 | Interacts with the phosphate groups of the incoming nucleotide1 Publication | 1 | |
Sitei | 379 | Stabilization of the incoming nucleotide1 Publication | 1 | |
Binding sitei | 383 | TTPCombined sources | 1 | |
Sitei | 383 | Probably involved in nucleotide binding selection1 Publication | 1 | |
Sitei | 384 | Probably involved in positioning the templating nucleotide at the polymerization active site and in controlling nucleotide insertion fidelity1 Publication | 1 | |
Sitei | 387 | Probably involved in binding template-primer structures1 Publication | 1 | |
Sitei | 390 | Probably involved in nucleotide binding selection1 Publication | 1 | |
Sitei | 391 | Probably involved in binding template-primer structures1 Publication | 1 | |
Sitei | 420 | Binds ssDNA; Essential for 3'-5' exonucleolysis1 Publication | 1 | |
Sitei | 434 | Probably involved in binding template-primer structures1 Publication | 1 | |
Sitei | 438 | Probably involved in binding template-primer structures1 Publication | 1 | |
Metal bindingi | 456 | Magnesium 2; catalytic1 Publication | 1 | |
Metal bindingi | 458 | Magnesium 2; catalyticCombined sources | 1 | |
Binding sitei | 458 | TTPCombined sources | 1 | |
Sitei | 498 | Probably involved in binding template-primer structures1 Publication | 1 | |
Sitei | 500 | Probably involved in binding template-primer structures1 Publication | 1 | |
Sitei | 529 | Stabilizes the primer-terminus at the polymerization active site and contributes to the coordination between the exonuclease and polymerazation activities1 Publication | 1 |
GO - Molecular functioni
- DNA binding Source: UniProtKB-KW
- DNA-directed DNA polymerase activity Source: UniProtKB-KW
- exonuclease activity Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
- nucleoside binding Source: InterPro
- nucleotide binding Source: UniProtKB-KW
GO - Biological processi
- DNA replication Source: UniProtKB-KW
- viral DNA genome replication Source: UniProtKB
Keywordsi
Molecular function | DNA-binding, DNA-directed DNA polymerase, Exonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Transferase |
Biological process | DNA replication, Viral DNA replication |
Ligand | Magnesium, Metal-binding, Nucleotide-binding |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:2 |
Organismi | Bacillus phage phi29 (Bacteriophage phi-29) |
Taxonomic identifieri | 10756 [NCBI] |
Taxonomic lineagei | Viruses › Duplodnaviria › Heunggongvirae › Uroviricota › Caudoviricetes › Caudovirales › Salasmaviridae › Picovirinae › Salasvirus |
Virus hosti | Bacillus subtilis [TaxID: 1423] |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 12 | D → A: Strong loss of 3'-5' exonucleolysis. 2 Publications | 1 | |
Mutagenesisi | 14 | E → A: Strong loss of 3'-5' exonucleolysis. 2 Publications | 1 | |
Mutagenesisi | 15 | T → I: 95% loss of ssDNA-binding. Decreased in fidelity of DNA replication. 1 Publication | 1 | |
Mutagenesisi | 59 | Y → F: Almost no effect on replication activity. About 20% loss of TP-DNA initiation, 20% loss of TP-DNA replication and 10% loss of TP-DNA amplification. Complete loss of interaction with TP. 1 Publication | 1 | |
Mutagenesisi | 59 | Y → L: 3 fold decrease in replication activity. About 80% loss of TP-DNA initiation, 70% loss of TP-DNA replication and 97% loss of TP-DNA amplification. Complete loss of interaction with TP. 1 Publication | 1 | |
Mutagenesisi | 59 | Y → R: 3 fold decrease in replication activity. About 75% loss of TP-DNA initiation, complete loss of TP-DNA replication and complete loss of TP-DNA amplification. 1 Publication | 1 | |
Mutagenesisi | 61 | H → L: 5 fold decrease in replication activity. About 85% loss of TP-DNA initiation, 80% loss of TP-DNA replication and complete loss of TP-DNA amplification. Complete loss of interaction with TP. 1 Publication | 1 | |
Mutagenesisi | 61 | H → R: 100 fold decrease in replication activity. Complete loss of interaction with TP. 1 Publication | 1 | |
Mutagenesisi | 62 | N → D or H: 88% loss of ssDNA-binding. Decreased in fidelity of DNA replication. 1 Publication | 1 | |
Mutagenesisi | 65 | F → S: Loss of capacity to interact with a DNA primer/template structure. 1 Publication | 1 | |
Mutagenesisi | 66 | D → A: Strong loss of 3'-5' exonucleolysis. 2 Publications | 1 | |
Mutagenesisi | 69 | F → S: 2 fold decrease in replication activity. About 50% loss of TP-DNA initiation, 40% loss of TP-DNA replication and 60% loss of TP-DNA amplification. Complete loss of interaction with TP. 1 Publication | 1 | |
Mutagenesisi | 69 | F → Y: 2 fold decrease in replication activity. About 80% loss of TP-DNA initiation, 50% loss of TP-DNA replication and almost 95% loss of TP-DNA. Complete loss of interaction with TP amplification. 1 Publication | 1 | |
Mutagenesisi | 122 | S → T: Loss of capacity to interact with a DNA primer/template structure. 1 Publication | 1 | |
Mutagenesisi | 123 | L → N: Loss of capacity to interact with a DNA primer/template structure. 1 Publication | 1 | |
Mutagenesisi | 128 | F → A: Slight loss of interaction with TP. 1 Publication | 1 | |
Mutagenesisi | 128 | F → Y: Almost complete loss of interaction with TP. 1 Publication | 1 | |
Mutagenesisi | 143 | K → I or R: Strong loss of 3'-5' exonuclease, proofreading and strand-displacement activities. 1 Publication | 1 | |
Mutagenesisi | 148 | Y → A: Reduced capacity to stabilize the binding of the primer terminus at the 3'-5' exonuclease active site. 1 Publication | 1 | |
Mutagenesisi | 169 | D → A: Strong loss of 3'-5' exonucleolysis. 1 Publication | 1 | |
Mutagenesisi | 187 | R → K: No effect on DNA-binding, TP binding and replication/amplification. 1 Publication | 1 | |
Mutagenesisi | 189 | T → A: No effect on DNA-binding, TP binding and replication/amplification. 1 Publication | 1 | |
Mutagenesisi | 192 | S → I: Loss of DNA-binding. Reduced TP binding. 25% loss of replication and almost complete loss of amplification. 1 Publication | 1 | |
Mutagenesisi | 192 | S → N: Loss of DNA-binding. No effect on TP binding. 50% loss of replication/amplification. 1 Publication | 1 | |
Mutagenesisi | 196 | K → I: Loss of DNA-binding. Reduced TP binding. 25% loss of replication and almost complete loss of amplification. 6-fold reduced 3'-5' exonucleolysis. 1 Publication | 1 | |
Mutagenesisi | 196 | K → R: Slight loss of DNA-binding. No loss of replication and amplification. 1 Publication | 1 | |
Mutagenesisi | 198 | F → V: Loss of DNA-binding. Reduced TP binding. 25% loss of replication and almost complete loss of amplification. 6-fold reduced 3'-5' exonucleolysis. 1 Publication | 1 | |
Mutagenesisi | 206 | K → I: No effect on DNA-binding. Reduced TP binding. 70% loss of replication and 20% loss of amplification. 1 Publication | 1 | |
Mutagenesisi | 223 | R → I: Favored exonucleolysis (low pol/exo ratio). 2 Publications | 1 | |
Mutagenesisi | 226 | Y → F: Favored polymerization (high pol/exo ratio). decrease in forward and reverse rates of translocation. Increased affinity for dNTP and for pyrophosphate in the pre-translocation state. 3 Publications | 1 | |
Mutagenesisi | 226 | Y → S: Favored exonucleolysis. Complete loss of polymerization. 2 Publications | 1 | |
Mutagenesisi | 227 | R → I: Favored exonucleolysis (low pol/exo ratio). 2 Publications | 1 | |
Mutagenesisi | 227 | R → K: No effect on the pol/exo ratio. 1 Publication | 1 | |
Mutagenesisi | 228 | G → A: Favored polymerization (high pol/exo ratio). 2 Publications | 1 | |
Mutagenesisi | 229 | G → A: Favored exonucleolysis (low pol/exo ratio). 2 Publications | 1 | |
Mutagenesisi | 229 | G → D: Favored exonucleolysis. Complete loss of polymerization. 2 Publications | 1 | |
Mutagenesisi | 230 | F → A: Favored polymerization (high pol/exo ratio). 2 Publications | 1 | |
Mutagenesisi | 230 | F → S: Favored exonucleolysis (low pol/exo ratio). 2 Publications | 1 | |
Mutagenesisi | 230 | F → Y: No effect on the pol/exo ratio. 1 Publication | 1 | |
Mutagenesisi | 249 | D → E: Complete loss of DNA polymerase activity. Slight decrease in template-primer binding. No effect on 3' to 5' exonucleolysis. 1 Publication | 1 | |
Mutagenesisi | 250 | V → A: No effect on TP-DNA replication. 1 Publication | 1 | |
Mutagenesisi | 250 | V → F: Complete loss of TP-DNA replication. 1 Publication | 1 | |
Mutagenesisi | 251 | N → D: No effect on TP-DNA replication. 1 Publication | 1 | |
Mutagenesisi | 252 | S → G: 40% loss of DNA polymerase activity. No effect on translocation or stabilization of the incorporated nucIeotide. No effect on 3' to 5' exonucleolysis. 1 Publication | 1 | |
Mutagenesisi | 252 | S → R: Complete loss of DNA polymerase activity. Drastic loss of template-primer binding. No effect on 3' to 5' exonucleolysis and interaction with the TP primer. 1 Publication | 1 | |
Mutagenesisi | 253 | L → V: 30% loss of DNA polymerase activity. No effect on translocation or stabilization of the incorporated nucIeotide. No effect on 3' to 5' exonucleolysis. 1 Publication | 1 | |
Mutagenesisi | 254 | Y → F: Decreased dNTP binding affinity. 10-fold reduced affinity for the correct nucleotide. 1 Publication | 1 | |
Mutagenesisi | 254 | Y → V: Loss of discrimination for rNTPs over dNTPs. 1 Publication | 1 | |
Mutagenesisi | 255 | P → S: 30% loss of DNA polymerase activity. No effect on translocation or stabilization of the incorporated nucIeotide. No effect on 3' to 5' exonucleolysis. 1 Publication | 1 | |
Mutagenesisi | 364 | I → Q: Partial loss of hability to stably bind the DNA substrate. 1 Publication | 1 | |
Mutagenesisi | 364 | I → R: Complete loss of hability to stably bind the DNA substrate. 1 Publication | 1 | |
Mutagenesisi | 366 | K → T: Slight decrease in DNA-binding capacity. No effect on polymerisation activity, except that it is reduced in the absence of a DNA template. Reduced affinity for the initiating nucleotide. 3 fold reduction of the initiation activity in the presence of p6. 1 Publication | 1 | |
Mutagenesisi | 371 | K → T: Strong decrease in the affinity for dNTPs and pyrophosphorolytic activity. No effect on exonucleolysis. 1 Publication | 1 | |
Mutagenesisi | 379 | K → T: Slight increase in DNA-binding capacity. Reduced affinity for the initiating nucleotide. 1 Publication | 1 | |
Mutagenesisi | 383 | K → P: Complete loss of incorporation of dNTP substrates using either DNA or TP as primer. No effect on 3' to 5' exonucleolysis. 1 Publication | 1 | |
Mutagenesisi | 383 | K → R: Strong loss of ability to use dNTPs in both processive and non-processive DNA synthesis. Impaired progression from protein-primed initiation to DNA elongation. No effect on 3' to 5' exonucleolysis. 1 Publication | 1 | |
Mutagenesisi | 384 | L → R: Reduced nucleotide insertion fidelity during DNA-primed polymerization and protein-primed initiation. No effect on the affinity for the different dNTPs. 1 Publication | 1 | |
Mutagenesisi | 387 | N → Y: 3-fold higher Km value for dATP and more than 11-fold lower Vmax value than the wild-type enzyme in the initiation reaction. Impaired in enzyme-DNA translocation. 1 Publication | 1 | |
Mutagenesisi | 388 | S → G: No effect on initiation and polymerization activities. Increased efficiency of dNTP incorporation in non-templated reactions. 1 Publication | 1 | |
Mutagenesisi | 390 | Y → F: Decreased dNTP binding affinity in the post-translocation state. 4.6-fold reduced affinity for the correct nucleotide. 2 Publications | 1 | |
Mutagenesisi | 390 | Y → S: Decreased dNTP binding affinity. 14-fold reduced affinity for the correct nucleotide. Loss of discrimination against dA insertion opposite 8oxodG. 2 Publications | 1 | |
Mutagenesisi | 391 | G → D: Complete loss of template-primer binding. 1 Publication | 1 | |
Mutagenesisi | 392 | K → Q: 50% loss of exonuclease activity. 80% loss of processivity. No effect on DNA polymerase/DNA complex formation. 1 Publication | 1 | |
Mutagenesisi | 392 | K → R: 90% loss of exonuclease activity. 80% loss of processivity. No effect on DNA polymerase/DNA complex formation. 1 Publication | 1 | |
Mutagenesisi | 393 | F → Y: Severe decrease in initial binding to template-primer DNA molecules. 1 Publication | 1 | |
Mutagenesisi | 434 | T → N: Complete loss of TP-dAMP formation. Almost complete loss of DNA polymerization. 1 Publication | 1 | |
Mutagenesisi | 437 | A → G: No effect on TP-dAMP formation. 20% loss of DNA polymerization. 1 Publication | 1 | |
Mutagenesisi | 438 | R → I: Complete loss of TP-dAMP formation. Almost complete loss of DNA polymerization. 1 Publication | 1 | |
Mutagenesisi | 438 | R → K: Complete loss of TP-dAMP formation. 30% loss of DNA polymerization. 1 Publication | 1 | |
Mutagenesisi | 454 | Y → F: No effect on the formation of the covalent complex between the TP and 5'-dAMP. Loss of replication of a p3-DNA complex or a primed M13 DNA. Increased 3'-5' exonucleolysis. 1 Publication | 1 | |
Mutagenesisi | 455 | C → G: 65% loss of formation of the covalent complex between the TP and 5'-dAMP. Increased 3'-5' exonucleolysis. 1 Publication | 1 | |
Mutagenesisi | 456 | D → G: 50% loss of synthetic activities, TP-primed initiation and DNA-primed polymerization. When polymerization requires an efficient translocation along the template, catalytic efficiency is strongly reduced. 90% loss of formation of the covalent complex between the TP and 5'-dAMP. Increased 3'-5' exonucleolysis. 2 Publications | 1 | |
Mutagenesisi | 457 | T → P: Complete loss of initiation and polymerization activities. Severe loss of protein-priming activity. Increased 3'-5' exonucleolysis. 1 Publication | 1 | |
Mutagenesisi | 458 | D → G: Complete loss of initiation and polymerization activities. Severe loss of protein-priming activity. Increased 3'-5' exonucleolysis. 1 Publication | 1 | |
Mutagenesisi | 498 | K → R: Strong decrease in DNA polymerization activity. Loss of binding to a primer-template DNA. Increased 3'-5' exonucleolysis. 1 Publication | 1 | |
Mutagenesisi | 498 | K → T: Strong decrease in initiation and DNA polymerization activities. Loss of binding to a primer-template DNA. Increased 3'-5' exonucleolysis. 1 Publication | 1 | |
Mutagenesisi | 500 | Y → S: Strong decrease in DNA polymerization activity and interaction with primer-template DNA. Increased 3'-5' exonucleolysis. 1 Publication | 1 | |
Mutagenesisi | 529 | K → A: Increased exonuclease activity and loss of primer elongation. Deficient in nucleotide incorporation. 1 Publication | 1 | |
Mutagenesisi | 529 | K → E: Increased exonuclease activity and complete loss of primer elongation. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000046542 | 1 – 575 | DNA polymeraseAdd BLAST | 575 |
Proteomic databases
PRIDEi | P03680 |
Interactioni
Subunit structurei
Interacts with the primer terminal protein; this interaction allows the initiation of TP-primed DNA replication at both viral DNA ends.
Interacts with DNA.
3 PublicationsSites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 59 | Interaction with the primer terminal protein1 Publication | 1 | |
Sitei | 61 | Interaction with the primer terminal protein1 Publication | 1 | |
Sitei | 69 | Interaction with the primer terminal protein1 Publication | 1 |
Structurei
Secondary structure
3D structure databases
SMRi | P03680 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P03680 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 191 | 3'-5' exonuclease and strand displacement activities1 PublicationAdd BLAST | 191 | |
Regioni | 192 – 229 | Involved in DNA-binding, coordination between DNA synthesis and degradation and TP interaction3 PublicationsAdd BLAST | 38 | |
Regioni | 230 – 562 | Initiation, polymerization and pyrophosphorolytic activities1 PublicationAdd BLAST | 333 | |
Regioni | 398 – 420 | TPR21 PublicationAdd BLAST | 23 | |
Regioni | 563 – 575 | Involved in DNA-binding and TP interaction1 PublicationAdd BLAST | 13 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 454 – 458 | YCDTD1 Publication | 5 |
Domaini
Sequence similaritiesi
Family and domain databases
Gene3Di | 3.30.420.10, 1 hit 3.90.1600.10, 1 hit |
InterProi | View protein in InterPro IPR006172, DNA-dir_DNA_pol_B IPR017964, DNA-dir_DNA_pol_B_CS IPR004868, DNA-dir_DNA_pol_B_mt/vir IPR014416, DNA-dir_DNA_polB_phi29_vir IPR043502, DNA/RNA_pol_sf IPR023211, DNA_pol_palm_dom_sf IPR012337, RNaseH-like_sf IPR036397, RNaseH_sf |
Pfami | View protein in Pfam PF03175, DNA_pol_B_2, 1 hit |
PIRSFi | PIRSF004178, Dpol_Bac_phage, 1 hit |
PRINTSi | PR00106, DNAPOLB |
SMARTi | View protein in SMART SM00486, POLBc, 1 hit |
SUPFAMi | SSF53098, SSF53098, 1 hit SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS00116, DNA_POLYMERASE_B, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MKHMPRKMYS CDFETTTKVE DCRVWAYGYM NIEDHSEYKI GNSLDEFMAW
60 70 80 90 100
VLKVQADLYF HNLKFDGAFI INWLERNGFK WSADGLPNTY NTIISRMGQW
110 120 130 140 150
YMIDICLGYK GKRKIHTVIY DSLKKLPFPV KKIAKDFKLT VLKGDIDYHK
160 170 180 190 200
ERPVGYKITP EEYAYIKNDI QIIAEALLIQ FKQGLDRMTA GSDSLKGFKD
210 220 230 240 250
IITTKKFKKV FPTLSLGLDK EVRYAYRGGF TWLNDRFKEK EIGEGMVFDV
260 270 280 290 300
NSLYPAQMYS RLLPYGEPIV FEGKYVWDED YPLHIQHIRC EFELKEGYIP
310 320 330 340 350
TIQIKRSRFY KGNEYLKSSG GEIADLWLSN VDLELMKEHY DLYNVEYISG
360 370 380 390 400
LKFKATTGLF KDFIDKWTYI KTTSEGAIKQ LAKLMLNSLY GKFASNPDVT
410 420 430 440 450
GKVPYLKENG ALGFRLGEEE TKDPVYTPMG VFITAWARYT TITAAQACYD
460 470 480 490 500
RIIYCDTDSI HLTGTEIPDV IKDIVDPKKL GYWAHESTFK RAKYLRQKTY
510 520 530 540 550
IQDIYMKEVD GKLVEGSPDD YTDIKFSVKC AGMTDKIKKE VTFENFKVGF
560 570
SRKMKPKPVQ VPGGVVLVDD TFTIK
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 492 | A → V in CAA37450 (PubMed:2118623).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 176 | A → R in mutant TS2(24). | 1 | |
Natural varianti | 355 | A → V in mutant TS2(24). | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V01155 Genomic DNA Translation: CAA24480.1 X53370 Genomic DNA Translation: CAA37450.1 EU771092 Genomic DNA Translation: ACE96023.1 Different initiation. X53371 Genomic DNA Translation: CAA37451.1 |
PIRi | A04282, ERBP29 |
RefSeqi | YP_002004529.1, NC_011048.1 |
Genome annotation databases
GeneIDi | 6446511 |
KEGGi | vg:6446511 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V01155 Genomic DNA Translation: CAA24480.1 X53370 Genomic DNA Translation: CAA37450.1 EU771092 Genomic DNA Translation: ACE96023.1 Different initiation. X53371 Genomic DNA Translation: CAA37451.1 |
PIRi | A04282, ERBP29 |
RefSeqi | YP_002004529.1, NC_011048.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1XHX | X-ray | 2.35 | A/B/C/D | 1-575 | [»] | |
1XHZ | X-ray | 2.70 | A/B/C/D | 1-575 | [»] | |
1XI1 | X-ray | 2.20 | A/B | 1-575 | [»] | |
2EX3 | X-ray | 3.00 | A/C/E/G/I/K | 1-575 | [»] | |
2PY5 | X-ray | 1.60 | A/B | 1-575 | [»] | |
2PYJ | X-ray | 2.03 | A/B | 1-575 | [»] | |
2PYL | X-ray | 2.20 | A | 1-575 | [»] | |
2PZS | X-ray | 2.60 | A/B/C/D | 1-575 | [»] | |
SMRi | P03680 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Proteomic databases
PRIDEi | P03680 |
Genome annotation databases
GeneIDi | 6446511 |
KEGGi | vg:6446511 |
Miscellaneous databases
EvolutionaryTracei | P03680 |
Family and domain databases
Gene3Di | 3.30.420.10, 1 hit 3.90.1600.10, 1 hit |
InterProi | View protein in InterPro IPR006172, DNA-dir_DNA_pol_B IPR017964, DNA-dir_DNA_pol_B_CS IPR004868, DNA-dir_DNA_pol_B_mt/vir IPR014416, DNA-dir_DNA_polB_phi29_vir IPR043502, DNA/RNA_pol_sf IPR023211, DNA_pol_palm_dom_sf IPR012337, RNaseH-like_sf IPR036397, RNaseH_sf |
Pfami | View protein in Pfam PF03175, DNA_pol_B_2, 1 hit |
PIRSFi | PIRSF004178, Dpol_Bac_phage, 1 hit |
PRINTSi | PR00106, DNAPOLB |
SMARTi | View protein in SMART SM00486, POLBc, 1 hit |
SUPFAMi | SSF53098, SSF53098, 1 hit SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS00116, DNA_POLYMERASE_B, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | DPOL_BPPH2 | |
Accessioni | P03680Primary (citable) accession number: P03680 Secondary accession number(s): B3VMN6, Q38545 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | July 21, 1986 | |
Last modified: | September 29, 2021 | |
This is version 134 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families