Protein : Qrob_P0542660.2 Q. robur
Protein Identifier  ? Qrob_P0542660.2 Organism . Name  Quercus robur
Score  94.0 Score Type  egn
Protein Description  (M=1) PF03121 - Herpesviridae UL52/UL70 DNA primase Gene Prediction Quality  validated
Protein length 

Sequence

Length: 619  
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0 Synonyms

2 GO Terms

Identifier Name Description
GO:0006260 DNA replication The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by initiation proteins, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.
GO:0003896 DNA primase activity Catalysis of the synthesis of a short RNA primer on a DNA template, providing a free 3'-OH that can be extended by DNA-directed DNA polymerases. Catalyzed by a DNA-directed RNA polymerase that forms a complex with alpha DNA polymerase.

15 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pmum:103333714 1 615 + 615 Gaps:32 100.00 587 75.30 0.0 DNA-directed primase/polymerase protein
blastp_kegg lcl|pper:PRUPE_ppa003300mg 1 615 + 615 Gaps:32 100.00 587 74.96 0.0 hypothetical protein
blastp_kegg lcl|tcc:TCM_015263 1 615 + 615 Gaps:4 98.55 620 68.90 0.0 Coiled-coil domain-containing protein 111 isoform 1
blastp_kegg lcl|vvi:100257712 1 615 + 615 Gaps:20 99.53 632 68.68 0.0 coiled-coil domain-containing protein 111 homolog
blastp_kegg lcl|cic:CICLE_v10006841mg 1 611 + 611 Gaps:8 99.34 607 73.30 0.0 hypothetical protein
blastp_kegg lcl|cit:102625684 1 611 + 611 Gaps:8 99.34 607 73.30 0.0 coiled-coil domain-containing protein 111-like
blastp_kegg lcl|rcu:RCOM_1582000 1 614 + 614 Gaps:14 99.83 601 71.17 0.0 hypothetical protein
blastp_kegg lcl|pxb:103966166 1 615 + 615 Gaps:31 100.00 588 71.26 0.0 DNA-directed primase/polymerase protein-like
blastp_kegg lcl|pxb:103966147 1 615 + 615 Gaps:31 100.00 588 71.26 0.0 DNA-directed primase/polymerase protein-like
blastp_kegg lcl|mdm:103426489 1 615 + 615 Gaps:31 100.00 588 71.43 0.0 DNA-directed primase/polymerase protein-like
blastp_uniprot_sprot sp|Q32PL8|PRIPO_DANRE 129 522 + 394 Gaps:60 78.01 523 37.25 5e-67 DNA-directed primase/polymerase protein OS Danio rerio GN primpol PE 2 SV 2
blastp_uniprot_sprot sp|Q6P1E7|PRIPO_MOUSE 129 528 + 400 Gaps:71 78.77 537 37.59 4e-61 DNA-directed primase/polymerase protein OS Mus musculus GN Primpol PE 2 SV 1
blastp_uniprot_sprot sp|Q96LW4|PRIPO_HUMAN 129 511 + 383 Gaps:90 76.25 560 35.83 2e-59 DNA-directed primase/polymerase protein OS Homo sapiens GN PRIMPOL PE 1 SV 2
blastp_uniprot_sprot sp|Q08DZ8|PRIPO_BOVIN 129 511 + 383 Gaps:99 76.76 555 33.57 6e-49 DNA-directed primase/polymerase protein OS Bos taurus GN PRIMPOL PE 2 SV 1
rpsblast_cdd gnl|CDD|202543 448 508 + 61 Gaps:12 98.65 74 36.99 2e-09 pfam03121 Herpes_UL52 Herpesviridae UL52/UL70 DNA primase. Herpes simplex virus type 1 DNA replication in host cells is known to be mediated by seven viral-encoded proteins three of which form a heterotrimeric DNA helicase-primase complex. This complex consists of UL5 UL8 and UL52 subunits. Heterodimers consisting of UL5 and UL52 have been shown to retain both helicase and primase activities. Nevertheless UL8 is still essential for replication: though it lacks any DNA binding or catalytic activities it is involved in the transport of UL5-UL52 and it also interacts with other replication proteins. The molecular mechanisms of the UL5-UL52 catalytic activities are not known. While UL5 is associated with DNA helicase activity and UL52 with DNA primase activity the helicase activity requires the interaction of UL5 and UL52. It is not known if the primase activity can be maintained by UL52 alone. The region encompassed by residues 610-636 of HSV1 UL52 is thought to contain a divalent metal cation binding motif. Indeed this region contains several aspartate and glutamate residues that might be involved in divalent cation binding. The biological significance of UL52-UL8 interaction is not known. Yeast two-hybrid analysis together with immunoprecipitation experiments have shown that the HSV1 UL52 region between residues 366-914 is essential for this interaction while the first 349 N-terminal residues are dispensable. This family also includes protein UL70 from cytomegalovirus (CMV a subgroup of the Herpesviridae) strains which by analogy with UL52 is thought to have DNA primase activity. Indeed CMV strains also possess a DNA helicase-primase complex the other subunits being protein UL105 (with known similarity to HSV1 UL5) and protein UL102.

4 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Pfam 448 504 57 PF03121 none Herpesviridae UL52/UL70 DNA primase IPR004340
Coils 577 598 22 Coil none none none
PANTHER 105 601 497 PTHR31399:SF0 none none none
PANTHER 105 601 497 PTHR31399 none none none

0 Localization

7 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran1_2004_QTL4_peak_Bud_burst_A4 Qrob_Chr09 9 s_1BY6BQ_440 s_1AOIKO_756 16,45 0 27,45 lod 4,5 10,6
Bourran_2000_2002_QTL7_Delta.F Qrob_Chr09 9 v_5944_442 s_1BA1PC_866 23.51 10,96 35,74 lod 4.1466 0.041
Bourran2_2003_QTL11_peak_Bud_burst_3P Qrob_Chr09 9 s_1CGP2H_273 v_15801_330 27,16 4,16 48,16 lod 2,3 5,1
Bourran2_2003_QTL13_peak_Bud_burst_A4 Qrob_Chr09 9 s_1AP8MN_635 s_1A3QQ_692 18,18 10,88 25,88 lod 3,4 7,2
Bourran2_2004_QTL14_peak_Bud_burst_A4 Qrob_Chr09 9 s_1BY6BQ_440 s_1AOIKO_756 16,83 10,33 22,33 lod 3,8 9
Bourran2_2015_nEpis_A4 Qrob_Chr09 9 v_15847_485 v_8329_369 34,94 34,88 37,45 lod 3.1 7
Bourran2_2015_nSecLBD_A4 Qrob_Chr09 9 v_15847_485 v_8329_369 35,81 34,88 37,45 lod 4.4 10.4

0 Targeting