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Conserved domains on  [gi|818289202|gb|KKP74398|]
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MAG: hypothetical protein UR65_C0001G0015 [Candidatus Moranbacteria bacterium GW2011_GWE2_35_164]

Protein Classification

SixA phosphatase family protein; histidine phosphatase family protein( domain architecture ID 1904218)

SixA phosphatase family protein belongs to the histidine phosphatase superfamily, members of which contain a conserved His residue that is transiently phosphorylated during the catalytic cycle| histidine phosphatase family protein catalyzes the dephosphorylation of a phosphorylated substrate involving a conserved catalytic histidine residue which becomes phosphorylated during the reaction

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SixA super family cl41878
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
3-96 3.26e-06

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG2062:

Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 43.71  E-value: 3.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818289202   3 LSEEGRTRGEELMSALsylfRRKRENYNQIVHAPAVRCKETAYMVSAALPfasvnLEECLNWSPAIADSNNNAVKEMIAR 82
Cdd:COG2062   23 LTERGRRQARAMARWL----AALGLKPDRILSSPALRARQTAEILAEALG-----LPPKVEVEDELYDADPEDLLDLLRE 93

                         90
                 ....*....|....
gi 818289202  83 YEKSGVtlLIIVSH 96
Cdd:COG2062   94 LDDGET--VLLVGH 105
 
Name Accession Description Interval E-value
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
3-96 3.26e-06

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 43.71  E-value: 3.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818289202   3 LSEEGRTRGEELMSALsylfRRKRENYNQIVHAPAVRCKETAYMVSAALPfasvnLEECLNWSPAIADSNNNAVKEMIAR 82
Cdd:COG2062   23 LTERGRRQARAMARWL----AALGLKPDRILSSPALRARQTAEILAEALG-----LPPKVEVEDELYDADPEDLLDLLRE 93

                         90
                 ....*....|....
gi 818289202  83 YEKSGVtlLIIVSH 96
Cdd:COG2062   94 LDDGET--VLLVGH 105
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 3-96 7.26e-04

Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.


Pssm-ID: 132718 [Multi-domain]  Cd Length: 153  Bit Score: 37.30  E-value: 7.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818289202   3 LSEEGRTRgeelMSALSYLFRRKRENYNQIVHAPAVRCKETAYMVSAALPFASVNLEECLNwspaiADSNNNAVKEMIAR 82
Cdd:cd07067   26 LTEKGREQ----ARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPGLPVEVDPRLR-----EARVLPALEELIAP 96

                         90
                 ....*....|....
gi 818289202  83 YEKSGVtllIIVSH 96
Cdd:cd07067   97 HDGKNV---LIVSH 107
 
Name Accession Description Interval E-value
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
3-96 3.26e-06

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 43.71  E-value: 3.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818289202   3 LSEEGRTRGEELMSALsylfRRKRENYNQIVHAPAVRCKETAYMVSAALPfasvnLEECLNWSPAIADSNNNAVKEMIAR 82
Cdd:COG2062   23 LTERGRRQARAMARWL----AALGLKPDRILSSPALRARQTAEILAEALG-----LPPKVEVEDELYDADPEDLLDLLRE 93

                         90
                 ....*....|....
gi 818289202  83 YEKSGVtlLIIVSH 96
Cdd:COG2062   94 LDDGET--VLLVGH 105
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 3-96 7.26e-04

Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.


Pssm-ID: 132718 [Multi-domain]  Cd Length: 153  Bit Score: 37.30  E-value: 7.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818289202   3 LSEEGRTRgeelMSALSYLFRRKRENYNQIVHAPAVRCKETAYMVSAALPFASVNLEECLNwspaiADSNNNAVKEMIAR 82
Cdd:cd07067   26 LTEKGREQ----ARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPGLPVEVDPRLR-----EARVLPALEELIAP 96

                         90
                 ....*....|....
gi 818289202  83 YEKSGVtllIIVSH 96
Cdd:cd07067   97 HDGKNV---LIVSH 107
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 3-98 3.79e-03

Histidine phosphatase domain found in a functionally diverse set of proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This set of proteins includes cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, histidine acid phosphatases, phytases, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system; phytases scavenge phosphate from extracellular sources. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG. Clinical applications include the use of prostatic acid phosphatase (PAP) as a serum marker for prostate cancer. Agricultural applications include the addition of phytases to animal feed.


Pssm-ID: 132716 [Multi-domain]  Cd Length: 153  Bit Score: 35.47  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818289202   3 LSEEGRtrgeELMSALSYLFRRKRENYNQIVHAPAVRCKETAYMVsaalpfasvnLEECLNWSPAIADSNN---NAVKEM 79
Cdd:cd07040   26 LTEKGR----QQARELGKALRERYIKFDRIYSSPLKRAIQTAEII----------LEGLFEGLPVEVDPRArvlNALLEL 91

                         90
                 ....*....|....*....
gi 818289202  80 IARYEKSGVTLLiIVSHDA 98
Cdd:cd07040   92 LARHLLDGKNVL-IVSHGG 109
 
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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