Searching in Methanosarcina acetivorans C2A (GCF_000007345.1)
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 Methanosarcina acetivorans C2A, or try another query
| trpD MA_RS15675 MA2989 WP_011022929.1: anthranilate phosphoribosyltransferase is similar to: | PaperBLAST |
TRPD_THET8 / Q5SH88: Anthranilate phosphoribosyltransferase; EC 2.4.2.18 from Thermus thermophilus | 44% id, 99% cov |
Q9YGB4: anthranilate phosphoribosyltransferase (EC 2.4.2.18) from Thermococcus kodakarensis | 44% id, 95% cov |
TRPD_XANCP / Q8PD71: Anthranilate phosphoribosyltransferase; EC 2.4.2.18 from Xanthomonas campestris | 42% id, 99% cov |
| MA_RS15660 MA2986 WP_011022926.1: 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 | 36% id, 37% cov |
TRPGD_SALTY / P00905: Bifunctional protein TrpGD; EC 4.1.3.27; EC 2.4.2.18 from Salmonella typhimurium | 37% id, 35% cov |
| MA_RS23955 MA4590 WP_011024463.1: GMP synthase subunit A is similar to: | PaperBLAST |
TRPGD_ECOLI / P00904: Bifunctional protein TrpGD; EC 4.1.3.27; EC 2.4.2.18 from Escherichia coli | 32% id, 34% cov |
TRPGD_SALTY / P00905: Bifunctional protein TrpGD; EC 4.1.3.27; EC 2.4.2.18 from Salmonella typhimurium | 31% id, 34% cov |
| carA MA_RS11135 MA2144 WP_011022130.1: 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 | 27% id, 30% cov |
TRPGD_ECOLI / P00904: Bifunctional protein TrpGD; EC 4.1.3.27; EC 2.4.2.18 from Escherichia coli | 27% 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