DNA polymerase III subunit gamma/tau;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108536075  54 IVAQPPAQAPSSDVPETAASAPYLATSAPAEAADAPTTPVAAAPPPAEPAVLTPPPAQEPIAQTRAASPAIsEVEAAAQE 133
Cdd:PRK12323  360 MLAFRPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAP-EALAAARQ 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108536075 134 ALASIRAAEAERVSGMAPVPSAAATTGAQSDSTYAAIRSyTLQTLAGGIPLPSAQLADPSSLEPVRRECAGDPPTIVIDL 213
Cdd:PRK12323  439 ASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAA-AAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAA 517

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1108536075 214 DPAGDLAPISGPIAVNTGLGRVLAEMRARGVTIAWVTNRGAMDARAIRDRLVASGLDP 271
Cdd:PRK12323  518 PAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPD 575

molecular class C acid phosphatases, similar to Haemophilus influenzae e (P4) acid phosphatase; belongs to the haloacid dehalogenase-like hydrolase superfamily; Molecular class C acid phosphatases (CAPs) are nonspecific acid phosphatases with generally broad substrate specificity and optimum activity at neutral to acidic pH. Members include Haemophilus influenzae lipoprotein e (P4), Elizabethkingia meningosepticum OlpA, Helicobacter pylori HppA, Enterobacter sp. 4 acid phosphatase PhoI, and Streptococcus pyogenes M1 GAS LppC. Lipoprotein e (P4) exhibits phosphomonoesterase activity with aryl phosphate substrates including nicotinamide mononucleotide (NMN), tyrosine phosphate, phenyl phosphate, p-nitrophenyl phosphate, and 4-methylumbelliferyl phosphate. The role of P4 in NAD+ uptake appears to be the dephosphorylation of NMN to nicotinamide riboside, which is then taken up by the organism. Elizabethkingia meningosepticum OlpA is a broad-spectrum nucleotidase with preference for 5'-nucleotides, it efficiently hydrolyzes nucleotide monophosphates, with a strong preference for 5'-nucleotides and for 3'-AMP; OlpA can also hydrolyze sugar phosphates and beta-glycerol phosphate, although with a lower efficiency. Helicobacter pylori HppA is also a 5' nucleotidase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108536075 241 ARGVTIAWVTNRGAMDARAIRDRLVASGLdPEARDVVYVERYPGESKQSRRDTLAQNHCIIAMAGDERSDFDDLYNY 317
Cdd:cd07534    88 AKGVTIFYVSNRDQKLKAATLKNLKRLGF-PQASDDHLLLKTDKSSKESRRQLVKEKYNIVLLFGDNLGDFGDFTYK 163

5'-nucleotidase, lipoprotein e(P4) family; This model represents a set of bacterial lipoproteins belonging to a larger acid phosphatase family (pfam03767), which in turn belongs to the haloacid dehalogenase (HAD) superfamily of aspartate-dependent hydrolases. Members are found on the outer membrane of Gram-negative bacteria and the cytoplasmic membrane of Gram-positive bacteria. Most members have classic lipoprotein signal sequences. A critical role of this 5'-nucleotidase in Haemophilus influenzae is the degradation of external riboside in order to allow transport into the cell. An earlier suggested role in hemin transport is no longer current. This enzyme may also have other physiologically significant roles. [Transport and binding proteins, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108536075 242 RGVTIAWVTNRGAMDARAIRDRLVASGLDPEARDVVYVERyPGESKQSRRDTLAQNHCIIAMAGDERSDFDDLYNYlRDE 321
Cdd:TIGR01533 133 KGVKIFYVSNRSEKEKAATLKNLKRFGFPQADEEHLLLKK-DKSSKESRRQKVQKDYEIVLLFGDNLLDFDDFFYK-DKE 210

                          90       100
                  ....*....|....*....|....*
gi 1108536075 322 SGAQS-----LEPMLGAGWFLIDNP 341
Cdd:TIGR01533 211 SQDRQalvlqNQEKFGKKFIILPNP 235

molecular class C acid phosphatases, similar to Haemophilus influenzae e (P4) acid phosphatase; belongs to the haloacid dehalogenase-like hydrolase superfamily; Molecular class C acid phosphatases (CAPs) are nonspecific acid phosphatases with generally broad substrate specificity and optimum activity at neutral to acidic pH. Members include Haemophilus influenzae lipoprotein e (P4), Elizabethkingia meningosepticum OlpA, Helicobacter pylori HppA, Enterobacter sp. 4 acid phosphatase PhoI, and Streptococcus pyogenes M1 GAS LppC. Lipoprotein e (P4) exhibits phosphomonoesterase activity with aryl phosphate substrates including nicotinamide mononucleotide (NMN), tyrosine phosphate, phenyl phosphate, p-nitrophenyl phosphate, and 4-methylumbelliferyl phosphate. The role of P4 in NAD+ uptake appears to be the dephosphorylation of NMN to nicotinamide riboside, which is then taken up by the organism. Elizabethkingia meningosepticum OlpA is a broad-spectrum nucleotidase with preference for 5'-nucleotides, it efficiently hydrolyzes nucleotide monophosphates, with a strong preference for 5'-nucleotides and for 3'-AMP; OlpA can also hydrolyze sugar phosphates and beta-glycerol phosphate, although with a lower efficiency. Helicobacter pylori HppA is also a 5' nucleotidase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108536075 241 ARGVTIAWVTNRGAMDARAIRDRLVASGLdPEARDVVYVERYPGESKQSRRDTLAQNHCIIAMAGDERSDFDDLYNY 317
Cdd:cd07534    88 AKGVTIFYVSNRDQKLKAATLKNLKRLGF-PQASDDHLLLKTDKSSKESRRQLVKEKYNIVLLFGDNLGDFGDFTYK 163

5'-nucleotidase, lipoprotein e(P4) family; This model represents a set of bacterial lipoproteins belonging to a larger acid phosphatase family (pfam03767), which in turn belongs to the haloacid dehalogenase (HAD) superfamily of aspartate-dependent hydrolases. Members are found on the outer membrane of Gram-negative bacteria and the cytoplasmic membrane of Gram-positive bacteria. Most members have classic lipoprotein signal sequences. A critical role of this 5'-nucleotidase in Haemophilus influenzae is the degradation of external riboside in order to allow transport into the cell. An earlier suggested role in hemin transport is no longer current. This enzyme may also have other physiologically significant roles. [Transport and binding proteins, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108536075 242 RGVTIAWVTNRGAMDARAIRDRLVASGLDPEARDVVYVERyPGESKQSRRDTLAQNHCIIAMAGDERSDFDDLYNYlRDE 321
Cdd:TIGR01533 133 KGVKIFYVSNRSEKEKAATLKNLKRFGFPQADEEHLLLKK-DKSSKESRRQKVQKDYEIVLLFGDNLLDFDDFFYK-DKE 210

                          90       100
                  ....*....|....*....|....*
gi 1108536075 322 SGAQS-----LEPMLGAGWFLIDNP 341
Cdd:TIGR01533 211 SQDRQalvlqNQEKFGKKFIILPNP 235

DNA polymerase III subunit gamma/tau;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108536075  56 AQPPAQAPSSDVPETAASAPYLATSAPAEAADAPTTPVAAAPPPAEPAVLTPPPAQEPIAQTRAASPAISEVEAAAQEAL 135
Cdd:PRK07003  374 ARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKA 453

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108536075 136 ASIRAAEAERVSGMAPVPSAAATTGAQSDSTYAAIRSYTLQTLAGGIPLPSAQLADPSSLEPVRRECAGDPP 207
Cdd:PRK07003  454 NARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAA 525

DNA polymerase III subunits gamma and tau; Validated

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108536075  44 DEAQAPEGTVIVAQPPAQAPSSDVPETAASAPYLATSAPAEAADAPTTPVAAAPPPAEPAVLTPPPAQEPIAQTRAASPA 123
Cdd:PRK07764  613 ARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAA 692

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108536075 124 ISEVEAAAQEALASIRAAEAERVSGMAPVPSAAATTGAQSDSTYAAIRSYTLQTLAGGIPLPSAQLADPSSLEPVRRECA 203
Cdd:PRK07764  693 PAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAA 772

                  ....*
gi 1108536075 204 GDPPT 208
Cdd:PRK07764  773 APPPS 777