Searching in Salinicoccus carnicancri Crm (GCF_000330705.1)
Found 17 curated entries in PaperBLAST's database that match '2.4.2.18' as complete word(s).
These curated entries have 11 distinct sequences.
Running ublast with E ≤ 0.01
Found 4 relevant proteins in Salinicoccus carnicancri Crm, or try another query
trpD C792_RS0103170 WP_026090203.1: anthranilate phosphoribosyltransferase is similar to: | PaperBLAST |
TRPD_THET8 / Q5SH88: Anthranilate phosphoribosyltransferase; EC 2.4.2.18 from Thermus thermophilus | 43% id, 96% cov |
TRPD2_NOSS1 / Q8YXQ9: Anthranilate phosphoribosyltransferase 2; EC 2.4.2.18 from Nostoc sp. | 41% id, 94% cov |
Q9YGB4: anthranilate phosphoribosyltransferase (EC 2.4.2.18) from Thermococcus kodakarensis | 39% id, 98% cov |
C792_RS0109535 WP_017549241.1: aminodeoxychorismate/anthranilate synthase component II is similar to: | PaperBLAST |
TRPGD_ECOLI / P00904: Bifunctional protein TrpGD; EC 4.1.3.27; EC 2.4.2.18 from Escherichia coli | 39% id, 36% cov |
TRPGD_SALTY / P00905: Bifunctional protein TrpGD; EC 4.1.3.27; EC 2.4.2.18 from Salmonella typhimurium | 37% id, 36% cov |
C792_RS14125 WP_017547846.1: aminodeoxychorismate/anthranilate synthase component II is similar to: | PaperBLAST |
TRPGD_ECOLI / P00904: Bifunctional protein TrpGD; EC 4.1.3.27; EC 2.4.2.18 from Escherichia coli | 37% id, 35% cov |
TRPGD_SALTY / P00905: Bifunctional protein TrpGD; EC 4.1.3.27; EC 2.4.2.18 from Salmonella typhimurium | 36% id, 35% cov |
carA C792_RS0105600 WP_017548471.1: glutamine-hydrolyzing carbamoyl-phosphate synthase small subunit is similar to: | PaperBLAST |
TRPGD_SALTY / P00905: Bifunctional protein TrpGD; EC 4.1.3.27; EC 2.4.2.18 from Salmonella typhimurium | 31% id, 30% cov |
TRPGD_ECOLI / P00904: Bifunctional protein TrpGD; EC 4.1.3.27; EC 2.4.2.18 from Escherichia coli | 28% id, 30% cov |
The hits are sorted by %identity * %coverage (highest first)
Running ublast against the 6-frame translation. All reading frames of at least 30 codons are included.
Found hits to 4 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory