Searching in Clostridium tyrobutyricum FAM22553 (GCF_000816635.1)
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 Clostridium tyrobutyricum FAM22553, or try another query
| trpD PN53_RS11035 WP_017895263.1: anthranilate phosphoribosyltransferase is similar to: | PaperBLAST |
TRPD_THET8 / Q5SH88: Anthranilate phosphoribosyltransferase; EC 2.4.2.18 from Thermus thermophilus | 42% id, 99% cov |
TRPD_XANCP / Q8PD71: Anthranilate phosphoribosyltransferase; EC 2.4.2.18 from Xanthomonas campestris | 41% id, 97% cov |
Q9YGB4: anthranilate phosphoribosyltransferase (EC 2.4.2.18) from Thermococcus kodakarensis | 39% id, 99% cov |
| PN53_RS11040 WP_017751595.1: 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 | 38% id, 35% cov |
TRPGD_SALTY / P00905: Bifunctional protein TrpGD; EC 4.1.3.27; EC 2.4.2.18 from Salmonella typhimurium | 38% id, 35% cov |
| guaA PN53_RS02840 WP_017751932.1: glutamine-hydrolyzing GMP synthase is similar to: | PaperBLAST |
TRPGD_ECOLI / P00904: Bifunctional protein TrpGD; EC 4.1.3.27; EC 2.4.2.18 from Escherichia coli | 25% id, 35% cov |
TRPGD_SALTY / P00905: Bifunctional protein TrpGD; EC 4.1.3.27; EC 2.4.2.18 from Salmonella typhimurium | 25% id, 35% cov |
| PN53_RS06635 WP_017751023.1: carbamoyl phosphate synthase small subunit is similar to: | PaperBLAST |
TRPGD_ECOLI / P00904: Bifunctional protein TrpGD; EC 4.1.3.27; EC 2.4.2.18 from Escherichia coli | 28% id, 28% cov |
TRPGD_SALTY / P00905: Bifunctional protein TrpGD; EC 4.1.3.27; EC 2.4.2.18 from Salmonella typhimurium | 27% id, 28% 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 3 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory