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Conserved domains on  [gi|1477952101|ref|WP_119206936|]
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CpsB/CapC family capsule biosynthesis tyrosine phosphatase [Blautia sp. TF12-12AT]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YwqE super family cl47349
Tyrosine-protein phosphatase YwqE [Signal transduction mechanisms];
2-160 1.27e-52

Tyrosine-protein phosphatase YwqE [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG4464:

Pssm-ID: 443561 [Multi-domain]  Cd Length: 239  Bit Score: 167.64  E-value: 1.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477952101   2 EIMSIGPLEKKIRERKLIPLHESRYYLIEVPFDMAPDGIRKRLLEFPAMGKIPVLAHPERYFCVQDTPELLYEFREMGAV 81
Cdd:COG4464    80 EVRLDPDLLELLESGELLTLGGSRYLLVELPYNSIPPYLEELIFELQLKGYTPIIAHPERYPYLQEDPERLYELVERGAL 159

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1477952101  82 LQINKGSVFGRFGEEAERTARFLLENRLAGCVASDAHGADYRTTDMRPVRQFLEERYGEAYAQLLVKVNPRRILEDRQI 160
Cdd:COG4464   160 FQVNAGSLTGYFGKKVKKTAEKLLEEGLVHFLASDAHNLRHRPPRLAEALEALEKLFGSEKADRLLEENPRALLEGEPI 238
 
Name Accession Description Interval E-value
YwqE COG4464
Tyrosine-protein phosphatase YwqE [Signal transduction mechanisms];
2-160 1.27e-52

Tyrosine-protein phosphatase YwqE [Signal transduction mechanisms];


Pssm-ID: 443561 [Multi-domain]  Cd Length: 239  Bit Score: 167.64  E-value: 1.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477952101   2 EIMSIGPLEKKIRERKLIPLHESRYYLIEVPFDMAPDGIRKRLLEFPAMGKIPVLAHPERYFCVQDTPELLYEFREMGAV 81
Cdd:COG4464    80 EVRLDPDLLELLESGELLTLGGSRYLLVELPYNSIPPYLEELIFELQLKGYTPIIAHPERYPYLQEDPERLYELVERGAL 159

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1477952101  82 LQINKGSVFGRFGEEAERTARFLLENRLAGCVASDAHGADYRTTDMRPVRQFLEERYGEAYAQLLVKVNPRRILEDRQI 160
Cdd:COG4464   160 FQVNAGSLTGYFGKKVKKTAEKLLEEGLVHFLASDAHNLRHRPPRLAEALEALEKLFGSEKADRLLEENPRALLEGEPI 238
CpsB_CapC pfam19567
Capsular polysaccharide synthesis, CpsB/CapC;
1-156 9.53e-35

Capsular polysaccharide synthesis, CpsB/CapC;


Pssm-ID: 437399  Cd Length: 234  Bit Score: 121.85  E-value: 9.53e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477952101   1 MEIMSIGPLEKKIRERKLIPLHESRYYLIEV-PFDMApDGIRKRLLEFPAMGKIPVLAHPERYFCVQDTPELLYEFREMG 79
Cdd:pfam19567  79 NEIYYSEDTLELLEEGKILTLAGSRYVLVEFsPTDEY-SYIRNALYELLSAGYRPILAHVERYECLVKDIERVEELKDMG 157

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1477952101  80 AVLQINKGSVFGRFGEEAERTARFLLENRLAGCVASDAHGADYRTTDMRPVRQFLEERYGEAYAQLLVKVNPRRILE 156
Cdd:pfam19567 158 AYIQVNASSITGDYGFGVKRFVKKLLKEDLVHFVATDAHDTGSRAPRMQECARYVEKKYGEDYADKIFYDNPEKILR 234
PHP_HisPPase cd07432
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase ...
 53-118 8.43e-03

Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to produce histidinol. HisPPase can be classified into two types: the bifunctional HisPPase found in proteobacteria that belongs to the DDDD superfamily and the monofunctional Bacillus subtilis type that is a member of the PHP family. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.


Pssm-ID: 213987 [Multi-domain]  Cd Length: 129  Bit Score: 34.91  E-value: 8.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1477952101  53 IPVLAHPERYFCVQDTPELLYEFREMGAVLQINKGSVfgRFGEEAERTARFLLENRLAGCVASDAH 118
Cdd:cd07432    65 LVVLAHPDRPSRYGLSDLILKPLIKNGDAIEVNNSRL--RYGLNNLAAKRYAELGGLPITGGSDAH 128
 
Name Accession Description Interval E-value
YwqE COG4464
Tyrosine-protein phosphatase YwqE [Signal transduction mechanisms];
2-160 1.27e-52

Tyrosine-protein phosphatase YwqE [Signal transduction mechanisms];


Pssm-ID: 443561 [Multi-domain]  Cd Length: 239  Bit Score: 167.64  E-value: 1.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477952101   2 EIMSIGPLEKKIRERKLIPLHESRYYLIEVPFDMAPDGIRKRLLEFPAMGKIPVLAHPERYFCVQDTPELLYEFREMGAV 81
Cdd:COG4464    80 EVRLDPDLLELLESGELLTLGGSRYLLVELPYNSIPPYLEELIFELQLKGYTPIIAHPERYPYLQEDPERLYELVERGAL 159

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1477952101  82 LQINKGSVFGRFGEEAERTARFLLENRLAGCVASDAHGADYRTTDMRPVRQFLEERYGEAYAQLLVKVNPRRILEDRQI 160
Cdd:COG4464   160 FQVNAGSLTGYFGKKVKKTAEKLLEEGLVHFLASDAHNLRHRPPRLAEALEALEKLFGSEKADRLLEENPRALLEGEPI 238
CpsB_CapC pfam19567
Capsular polysaccharide synthesis, CpsB/CapC;
1-156 9.53e-35

Capsular polysaccharide synthesis, CpsB/CapC;


Pssm-ID: 437399  Cd Length: 234  Bit Score: 121.85  E-value: 9.53e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477952101   1 MEIMSIGPLEKKIRERKLIPLHESRYYLIEV-PFDMApDGIRKRLLEFPAMGKIPVLAHPERYFCVQDTPELLYEFREMG 79
Cdd:pfam19567  79 NEIYYSEDTLELLEEGKILTLAGSRYVLVEFsPTDEY-SYIRNALYELLSAGYRPILAHVERYECLVKDIERVEELKDMG 157

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1477952101  80 AVLQINKGSVFGRFGEEAERTARFLLENRLAGCVASDAHGADYRTTDMRPVRQFLEERYGEAYAQLLVKVNPRRILE 156
Cdd:pfam19567 158 AYIQVNASSITGDYGFGVKRFVKKLLKEDLVHFVATDAHDTGSRAPRMQECARYVEKKYGEDYADKIFYDNPEKILR 234
YciV COG0613
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and ...
 49-121 4.60e-05

5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and metabolism];


Pssm-ID: 440378 [Multi-domain]  Cd Length: 188  Bit Score: 41.82  E-value: 4.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1477952101  49 AMGKIPVLAHPERYFCVQDTPELLYEFREMG--AVlqinkgSVF--GRFGEEAERTARFLLENRLAGCVASDAHGAD 121
Cdd:COG0613   115 EAGGVAVLAHPFRYKRGRWLDDLLEELADAGldGI------EVYngRHSPEDNERAAELAEEYGLLATGGSDAHGPE 185
CutA1 COG1324
Divalent cation tolerance protein CutA [Inorganic ion transport and metabolism];
95-113 7.26e-03

Divalent cation tolerance protein CutA [Inorganic ion transport and metabolism];


Pssm-ID: 440935  Cd Length: 104  Bit Score: 34.39  E-value: 7.26e-03
                          10
                  ....*....|....*....
gi 1477952101  95 EEAERTARFLLENRLAGCV 113
Cdd:COG1324    14 EEAERIARALVEERLAACV 32
PHP_HisPPase cd07432
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase ...
 53-118 8.43e-03

Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to produce histidinol. HisPPase can be classified into two types: the bifunctional HisPPase found in proteobacteria that belongs to the DDDD superfamily and the monofunctional Bacillus subtilis type that is a member of the PHP family. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.


Pssm-ID: 213987 [Multi-domain]  Cd Length: 129  Bit Score: 34.91  E-value: 8.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1477952101  53 IPVLAHPERYFCVQDTPELLYEFREMGAVLQINKGSVfgRFGEEAERTARFLLENRLAGCVASDAH 118
Cdd:cd07432    65 LVVLAHPDRPSRYGLSDLILKPLIKNGDAIEVNNSRL--RYGLNNLAAKRYAELGGLPITGGSDAH 128
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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