TPM domain; This family was first named TPM domain after its founding proteins: TLP18.3, Psb32 and MOLO-1. In Arabidopsis, this domain is called the thylakoid acid phosphatase -TAP - domain and has a Rossmann-like fold. In plants, the family resides in the thylakoid lumen attached to the outer membrane of the chloroplast/plastid. It is active in the photosystem II.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175388   31 VTDLTATLSGDQRQHLEQQLAALEAKSGAQLAVLLVPTTGDDSIEEYAVRTFEKWKLGQKKVDDGVLLLVAKNDRTLRIE 110
Cdd:pfam04536   1 VVDYAGLLSDEEEAELEQKLAALEKKTGVQIVVVTVPSLDGEDIEDYADDLFDKWGIGQKGKDNGVLLLVAMDDRKVRIE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 489175388  111 VGYGLEGAITDVQAGRIISEQITPQFRQGNFYGGIQAGVDSLVQL 155
Cdd:pfam04536  81 VGYGLEGALTDALADRIIDEYILPYFKDGDYYGGILAGVDAIAAV 125

NUDIX domain family NudE found in Escherichia coli, and similar proteins; The adenosine nucleotide hydrolase NudE protein in Escherichia coli is a NUDIX hydrolase family member active against ADP ribose, NADH, AP2A and AP3A33, and is classified as a hydrolase (E.C. 3.6.1.-) based on gene annotations. It is an ADPRase (EC 3.6.1.13) catalyzes the hydrolysis of ADP-ribose to AMP and ribose-5-P. Like other members of the NUDIX hydrolase superfamily of enzymes, it is thought to require a divalent cation, such as Mg2+, for its activity. It also contains a 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489175388  62 AVLLVPTTGDDS---IEEYAVRTfEKWKLGQKK--VDDGVLLLVAKNdRTLRIEVGYG 114
Cdd:cd24156    4 AVMIVPILDDDHlllIREYAAGT-ERYELGFPKglIDPGETPEEAAN-RELKEEIGFG 59

TPM domain; This family was first named TPM domain after its founding proteins: TLP18.3, Psb32 and MOLO-1. In Arabidopsis, this domain is called the thylakoid acid phosphatase -TAP - domain and has a Rossmann-like fold. In plants, the family resides in the thylakoid lumen attached to the outer membrane of the chloroplast/plastid. It is active in the photosystem II.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175388   31 VTDLTATLSGDQRQHLEQQLAALEAKSGAQLAVLLVPTTGDDSIEEYAVRTFEKWKLGQKKVDDGVLLLVAKNDRTLRIE 110
Cdd:pfam04536   1 VVDYAGLLSDEEEAELEQKLAALEKKTGVQIVVVTVPSLDGEDIEDYADDLFDKWGIGQKGKDNGVLLLVAMDDRKVRIE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 489175388  111 VGYGLEGAITDVQAGRIISEQITPQFRQGNFYGGIQAGVDSLVQL 155
Cdd:pfam04536  81 VGYGLEGALTDALADRIIDEYILPYFKDGDYYGGILAGVDAIAAV 125

Modulator of levamisole receptor-1; MOLO1 is a one-pass transmembrane protein that contains a single extracellular globular domain. It is a positive regulator of levamisole-sensitive acetylcholine receptors in Caenorhabditis elegans, UniProtKB:Q19280. These receptors are Cys-loop ligand-gated ion channels, and the MOLO1 domain is an auxiliary subunit of the gated channel. The proteins carry a Rossmann fold.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489175388   38 LSGDQRQHLEQQLAALEAKS---------------GAQLAVLLV---------PTTGDDSIEEYAVRTFEKWKLGQKKVD 93
Cdd:pfam17175  31 LTTEQRDRLNDNLKELRSRTscdkpfcddrsprpgGYVIGVAIVkrieshynqPSPLLEDAEQFARYLRERWKLDNESCG 110

                          90
                  ....*....|..
gi 489175388   94 DGVLLLVAKNDR 105
Cdd:pfam17175 111 DSVIIVYSKDDK 122