Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195963416   27 KLSTFSAYLEDHSYNVEQIWRDIEDVIIKTlisahpIIRHNYHTCFPNHTLNSACFEILGFDILLDHKLKPWLLEVNHSP 106
Cdd:pfam03133 185 KWSLQNFWKYLEEKDKDEIWLEIESIIIKT------ILAAEVEASRLNVQPLPNCFELYGFDFMIDENLKPWLLEVNSSP 258

                          90       100       110
                  ....*....|....*....|....*....|.
gi 195963416  107 SFSTDSRLDKEVKDGLLYDTL---VLINLES 134
Cdd:pfam03133 259 SLHSTTKLDARLKEQLIDDVLnsvVPPDLEK 289

Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several post-translational modifications of which the reversible detyrosination/tyrosination of the carboxy-terminal end of most alpha-tubulins has been extensively analysed. This modification cycle involves a specific carboxypeptidase and the activity of the tubulin-tyrosine ligase (TTL). The true physiological function of TTL has so far not been established. Tubulin-tyrosine ligase (TTL) catalyzes the ATP-dependent post-translational addition of a tyrosine to the carboxy terminal end of detyrosinated alpha-tubulin. In normally cycling cells, the tyrosinated form of tubulin predominates. However, in breast cancer cells, the detyrosinated form frequently predominates, with a correlation to tumour aggressiveness. On the other hand, 3-nitrotyrosine has been shown to be incorporated, by TTL, into the carboxy terminal end of detyrosinated alpha-tubulin. This reaction is not reversible by the carboxypeptidase enzyme. Cells cultured in 3-nitrotyrosine rich medium showed evidence of altered microtubule structure and function, including altered cell morphology, epithelial barrier dysfunction, and apoptosis. Bacterial homologs of TTL are predicted to form peptide tags. Some of these are fused to a 2-oxoglutarate Fe(II)-dependent dioxygenase domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195963416   27 KLSTFSAYLEDHSYNVEQIWRDIEDVIIKTlisahpIIRHNYHTCFPNHTLNSACFEILGFDILLDHKLKPWLLEVNHSP 106
Cdd:pfam03133 185 KWSLQNFWKYLEEKDKDEIWLEIESIIIKT------ILAAEVEASRLNVQPLPNCFELYGFDFMIDENLKPWLLEVNSSP 258

                          90       100       110
                  ....*....|....*....|....*....|.
gi 195963416  107 SFSTDSRLDKEVKDGLLYDTL---VLINLES 134
Cdd:pfam03133 259 SLHSTTKLDARLKEQLIDDVLnsvVPPDLEK 289

Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several post-translational modifications of which the reversible detyrosination/tyrosination of the carboxy-terminal end of most alpha-tubulins has been extensively analysed. This modification cycle involves a specific carboxypeptidase and the activity of the tubulin-tyrosine ligase (TTL). The true physiological function of TTL has so far not been established. Tubulin-tyrosine ligase (TTL) catalyzes the ATP-dependent post-translational addition of a tyrosine to the carboxy terminal end of detyrosinated alpha-tubulin. In normally cycling cells, the tyrosinated form of tubulin predominates. However, in breast cancer cells, the detyrosinated form frequently predominates, with a correlation to tumour aggressiveness. On the other hand, 3-nitrotyrosine has been shown to be incorporated, by TTL, into the carboxy terminal end of detyrosinated alpha-tubulin. This reaction is not reversible by the carboxypeptidase enzyme. Cells cultured in 3-nitrotyrosine rich medium showed evidence of altered microtubule structure and function, including altered cell morphology, epithelial barrier dysfunction, and apoptosis. Bacterial homologs of TTL are predicted to form peptide tags. Some of these are fused to a 2-oxoglutarate Fe(II)-dependent dioxygenase domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195963416   27 KLSTFSAYLEDHSYNVEQIWRDIEDVIIKTlisahpIIRHNYHTCFPNHTLNSACFEILGFDILLDHKLKPWLLEVNHSP 106
Cdd:pfam03133 185 KWSLQNFWKYLEEKDKDEIWLEIESIIIKT------ILAAEVEASRLNVQPLPNCFELYGFDFMIDENLKPWLLEVNSSP 258

                          90       100       110
                  ....*....|....*....|....*....|.
gi 195963416  107 SFSTDSRLDKEVKDGLLYDTL---VLINLES 134
Cdd:pfam03133 259 SLHSTTKLDARLKEQLIDDVLnsvVPPDLEK 289

YheC/D like ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the modification/biosynthesis of spore-wall and capsular proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195963416   27 KLSTFSAYLED--HSYNVEQIWRDIEDVIIKtlISAHpiirhnYHTCFPnhtlnsACFEiLGFDILLDHKLKPWLLEVNH 104
Cdd:pfam14398 162 TAIPLEEALRRafGEERAEKILEKLEELALE--LARA------LEESFG------GLGE-LGLDLGIDKNGRVWLLEVNS 226

                          90
                  ....*....|.
gi 195963416  105 SPSFSTDSRLD 115
Cdd:pfam14398 227 KPGRSIFTHAG 237