Family Search for PF13680 (DUF4152)
PF13680 hits 7 sequences in PaperBLAST's database above the trusted cutoff. Showing all hits. Or show only hits to curated sequences or try another family.
Q8TZE9 exodeoxyribonuclease I (EC 3.1.11.1); poly(A)-specific ribonuclease (EC 3.1.13.4) from Pyrococcus furiosus (see 2 papers)
PF2046 hypothetical protein from Pyrococcus furiosus DSM 3638
Aligns to 1:225 / 229 (98.3%), covers 100.0% of PF13680, 478.4 bits
- Processing of A-form ssDNA by cryptic RNase H fold exonuclease PF2046
Kim, Archives of biochemistry and biophysics 2016 (PubMed)- “...RNase H fold exonuclease PF2046 Archives of Biochemistry and Biophysics Journal 00039861 606 143 150 143-150 text/plain 2016-09-15 15 September 2016 ...”
- “...Lee, Woo Cheol Abstract RNase H fold protein PF2046 of Pyrococcus furiosus is a 3 -5 ssDNA exonuclease that cleaves after the second nucleotide from...”
- A novel single-strand specific 3'-5' exonuclease found in the hyperthermophilic archaeon, Pyrococcus furiosus
Tori, PloS one 2013 - “...Pyrococcus furiosus, and identified a protein with the target activity. The purified protein, encoded by PF2046, is composed of 229 amino acids with a molecular weight of 25,596, and displayed single-strand specific 35 exonuclease activity. The protein, designated as PfuExo I, forms a stable trimeric complex...”
- “...As shown in Fig. 1C , the heat extract of the E. coli transformant containing PF2046 clearly expressed the nuclease activity. 10.1371/journal.pone.0058497.g001 Figure 1 Screening and identification of the gene responsible for the DNA cleavage activity. (A) The E. coli cells, transformed with pUC118 containing each...”
- Crystal structure of a novel non-Pfam protein PF2046 solved using low resolution B-factor sharpening and multi-crystal averaging methods
Su, Protein & cell 2010 - “...a novel non-Pfam protein PF2046 solved using low resolution B-factor sharpening and multi-crystal averaging methods Jing Su1*, Yang Li1*, Neil Shaw1*, Weihong...”
- “...Crystals of a 25.6 kDa non-Pfam, hypothetical protein, PF2046, diffracted X-rays to 3.38 A resolution. A combination of SeMet derived heavy atom positions with...”
5chiA / Q8TZE9 Crystal structure of pf2046 in complex with ssdna
Aligns to 2:226 / 230 (97.8%), covers 100.0% of PF13680, 478.4 bits
- Ligands: dna; magnesium ion (5chiA)
TK1646 hypothetical protein from Thermococcus kodakaraensis KOD1
Aligns to 1:224 / 227 (98.7%), covers 100.0% of PF13680, 477.2 bits
- Effect of Y50H and S187G substitutions on thermostability and exonuclease activity of TK1646 from Thermococcus kodakarensis
Saeed, Protein expression and purification 2021 (PubMed)- “...thermostability and exonuclease activity of TK1646 from Thermococcus kodakarensis Protein Expression and Purification Journal fla 10465928 179 105799 105799...”
- “...Muhammad Sulaiman Siddiqui, Masood Ahmed Rashid, Naeem TK1646 is a highly thermostable single strand specific 3 -5 exonuclease. Exonucleases play...”
- Characterization of TK1646, a highly thermostable 3'-5' single strand specific exonuclease from Thermococcus kodakarensis
Saeed, International journal of biological macromolecules 2019 (PubMed)- “...TK1646, a highly thermostable 3 5 single strand specific exonuclease from Thermococcus kodakarensis International Journal of Biological Macromolecules Journal fla 01418130 140 1194 1201...”
- “...exonucleases. Here we report molecular cloning of TK1646, a putative exonuclease from the hyperthermophilic archaeon Thermococcus kodakarensis, and expression...”
- A novel single-strand specific 3'-5' exonuclease found in the hyperthermophilic archaeon, Pyrococcus furiosus
Tori, PloS one 2013 - “...we could make a deletion mutant of the homolog of PfuExo I in T. kodakarensis (TK1646) and characterize it. This experiment is now underway. P. furiosus cells with high transformation efficiency have been described recently [42] , [43] , and therefore, the creation of PF2046-disrupted cells...”
- “...The other sequences were picked up from the database as follows. PF2046; NP_5797751, PAB2293; NP_125767.1, TK1646; YP_184059.1. The authors thank Dr. T. Yamagami at Kyushu University for the technical assistance and helpful discussions. References 1 Lindahl T , Wood RD ( 1999 ) Quality control by...”
4yorA / A0A060P168 Crystal structure of a trimeric exonuclease phoexo i from pyrococcus horikoshii ot3 at 1.52a resolution. (see paper)
Aligns to 1:225 / 227 (99.1%), covers 100.0% of PF13680, 426.3 bits
- Ligand: magnesium ion (4yorA)
PAB2293 hypothetical protein from Pyrococcus abyssi GE5
Aligns to 1:227 / 231 (98.3%), covers 100.0% of PF13680, 405.1 bits
4youB / A0A060P168 Crystal structure of a trimeric exonuclease phoexo i from pyrococcus horikoshii ot3 at 2.20a resolution. (see paper)
2 alignments in 1:196 / 199 (98.5%), covering up to 51.1% of PF13680, 324.0 bits
- Ligand: magnesium ion (4youB)
PH0067 hypothetical protein from Pyrococcus horikoshii OT3
Aligns to 11:192 / 192 (94.8%), covers 79.6% of PF13680, 323.3 bits
Or search for genetic data about PF13680 in the Fitness Browser
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory