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Conserved domains on  [gi|1233998078|ref|WP_094640575|]
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MULTISPECIES: PIG-L deacetylase family protein [unclassified Rhodococcus (in: high G+C Gram-positive bacteria)]

Protein Classification

PIG-L deacetylase family protein( domain architecture ID 10005328)

PIG-L (phosphatidylinositol glycan class L) deacetylase family protein may catalyze the removal of an acetyl group from a specific acetylated substrate

CATH:  3.40.50.10320
EC:  3.5.1.-
Gene Ontology:  GO:0019213
PubMed:  24970229
SCOP:  4001164

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LmbE COG2120
N-acetylglucosaminyl deacetylase, LmbE family [Carbohydrate transport and metabolism];
36-244 1.00e-42

N-acetylglucosaminyl deacetylase, LmbE family [Carbohydrate transport and metabolism];


:

Pssm-ID: 441723 [Multi-domain]  Cd Length: 201  Bit Score: 143.91  E-value: 1.00e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233998078  36 TMVVVAPHPDDEVLGVGGLLSLAAAAGVDVRVVAVTDGDGSHPGSPtVTAEDLRARRPVESERALAELGIDHsPTRLQIA 115
Cdd:COG2120     1 RVLVVAAHPDDEELGCGGTIARLAAAGHEVTVVTLTDGEAGSPGGP-PLREELAEIRRAEARAAAAILGVSD-VEFLGYP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233998078 116 DGAVEQHEGAVADALMPLLDATPGTWCLTPWRGDGHPDHEATARACLTAANAVGIPVVEYPiWMWHWATPnHPAVPWTrc 195
Cdd:COG2120    79 DGGLEGPLEELRRALARLIREVRPDVVLTPDPGDGHPDHRAVGRAVLAAARLAGLPKILGP-RLYLYEVP-SDTEPDV-- 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1233998078 196 rRVDLPAHtLDAKRASIEQFDSQIRPLsdhpadravLPPHILARYRRPF 244
Cdd:COG2120   155 -AVDITDV-LERKLAALAAHASQLDPL---------FAIRALARLRGAQ 192
 
Name Accession Description Interval E-value
LmbE COG2120
N-acetylglucosaminyl deacetylase, LmbE family [Carbohydrate transport and metabolism];
36-244 1.00e-42

N-acetylglucosaminyl deacetylase, LmbE family [Carbohydrate transport and metabolism];


Pssm-ID: 441723 [Multi-domain]  Cd Length: 201  Bit Score: 143.91  E-value: 1.00e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233998078  36 TMVVVAPHPDDEVLGVGGLLSLAAAAGVDVRVVAVTDGDGSHPGSPtVTAEDLRARRPVESERALAELGIDHsPTRLQIA 115
Cdd:COG2120     1 RVLVVAAHPDDEELGCGGTIARLAAAGHEVTVVTLTDGEAGSPGGP-PLREELAEIRRAEARAAAAILGVSD-VEFLGYP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233998078 116 DGAVEQHEGAVADALMPLLDATPGTWCLTPWRGDGHPDHEATARACLTAANAVGIPVVEYPiWMWHWATPnHPAVPWTrc 195
Cdd:COG2120    79 DGGLEGPLEELRRALARLIREVRPDVVLTPDPGDGHPDHRAVGRAVLAAARLAGLPKILGP-RLYLYEVP-SDTEPDV-- 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1233998078 196 rRVDLPAHtLDAKRASIEQFDSQIRPLsdhpadravLPPHILARYRRPF 244
Cdd:COG2120   155 -AVDITDV-LERKLAALAAHASQLDPL---------FAIRALARLRGAQ 192
PIG-L pfam02585
GlcNAc-PI de-N-acetylase; Members of this family are related to PIG-L an ...
 38-164 4.58e-25

GlcNAc-PI de-N-acetylase; Members of this family are related to PIG-L an N-acetylglucosaminylphosphatidylinositol de-N-acetylase (EC:3.5.1.89) that catalyzes the second step in GPI biosynthesis.


Pssm-ID: 426852  Cd Length: 128  Bit Score: 95.83  E-value: 4.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233998078  38 VVVAPHPDDEVLGVGGLLSLAAAAGVDVRVVAVTDGDGSHPGSPTVTAEDLRARRPVESERALAELGIDHsPTRLQIADG 117
Cdd:pfam02585   1 LVVSAHPDDEELGAGGTIARLAAAGVEVHVVCLTDGEAGSGGGSLEEGEELGEIRRAEARAAAEILGVDD-VEFLDYPDG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1233998078 118 -AVEQHEGAVADALMPLLDATPGTWCLTPWR-GDGHPDHEATARACLTA 164
Cdd:pfam02585  80 gLEYWDLEELLDALADLIRRYRPDVVVTPDPdGGGHPDHRATGRAVLAA 128
thiol_BshB2 TIGR04000
bacillithiol biosynthesis deacetylase BshB2; Members of this protein family are BshB2 (YojG), ...
 38-164 2.53e-12

bacillithiol biosynthesis deacetylase BshB2; Members of this protein family are BshB2 (YojG), an enzyme of bacillithiol biosynthesis; either BshB1 (YpjG) or BshB2 must be present, and often both are present. Bacillithiol is a low-molecular-weight thiol, an analog of glutathione and mycothiol, and is found largely in the Firmicutes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 188515  Cd Length: 217  Bit Score: 63.98  E-value: 2.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233998078  38 VVVAPHPDDEVLGVGGLLSLAAAAGVDVRVVAVTDGD-GSHPGSPT-VTAEDLRARRPVESERALAELGIdHSPTRLQIA 115
Cdd:TIGR04000   4 LVIFPHPDDEAFGVAGTIALYRQKGIPVTYACLTLGEmGRNMGNPPfATRESLPEIRKKELIEACKAMGI-TDLRMLGLR 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1233998078 116 DGAVE-QHEGAVADALMPLLDATPGTWCLTPWRGDG-HPDHEATARACLTA 164
Cdd:TIGR04000  83 DKTIEfEDDEELADMVKGIIEELNPSLIITFYPGYAvHPDHDATGRAVIRA 133
PBP2_SsuA_like_2 cd13558
Putative substrate binding domain of sulfonate binding protein, the type 2 periplasmic binding ...
 58-117 4.63e-03

Putative substrate binding domain of sulfonate binding protein, the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270276  Cd Length: 267  Bit Score: 37.65  E-value: 4.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1233998078  58 AAAAGVDVRVVAVTDGDGS------HPGSPTVTAEDLRARRPVESE---------RALAELGIDHS---PTRLQIADG 117
Cdd:cd13558    61 AAAAGAPIKIVAALRGDVNgqallvPKDSPIRSVADLKGKRVAYVRgsishylllKALEKAGLSPSdveLVFLTPADA 138
 
Name Accession Description Interval E-value
LmbE COG2120
N-acetylglucosaminyl deacetylase, LmbE family [Carbohydrate transport and metabolism];
36-244 1.00e-42

N-acetylglucosaminyl deacetylase, LmbE family [Carbohydrate transport and metabolism];


Pssm-ID: 441723 [Multi-domain]  Cd Length: 201  Bit Score: 143.91  E-value: 1.00e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233998078  36 TMVVVAPHPDDEVLGVGGLLSLAAAAGVDVRVVAVTDGDGSHPGSPtVTAEDLRARRPVESERALAELGIDHsPTRLQIA 115
Cdd:COG2120     1 RVLVVAAHPDDEELGCGGTIARLAAAGHEVTVVTLTDGEAGSPGGP-PLREELAEIRRAEARAAAAILGVSD-VEFLGYP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233998078 116 DGAVEQHEGAVADALMPLLDATPGTWCLTPWRGDGHPDHEATARACLTAANAVGIPVVEYPiWMWHWATPnHPAVPWTrc 195
Cdd:COG2120    79 DGGLEGPLEELRRALARLIREVRPDVVLTPDPGDGHPDHRAVGRAVLAAARLAGLPKILGP-RLYLYEVP-SDTEPDV-- 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1233998078 196 rRVDLPAHtLDAKRASIEQFDSQIRPLsdhpadravLPPHILARYRRPF 244
Cdd:COG2120   155 -AVDITDV-LERKLAALAAHASQLDPL---------FAIRALARLRGAQ 192
PIG-L pfam02585
GlcNAc-PI de-N-acetylase; Members of this family are related to PIG-L an ...
 38-164 4.58e-25

GlcNAc-PI de-N-acetylase; Members of this family are related to PIG-L an N-acetylglucosaminylphosphatidylinositol de-N-acetylase (EC:3.5.1.89) that catalyzes the second step in GPI biosynthesis.


Pssm-ID: 426852  Cd Length: 128  Bit Score: 95.83  E-value: 4.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233998078  38 VVVAPHPDDEVLGVGGLLSLAAAAGVDVRVVAVTDGDGSHPGSPTVTAEDLRARRPVESERALAELGIDHsPTRLQIADG 117
Cdd:pfam02585   1 LVVSAHPDDEELGAGGTIARLAAAGVEVHVVCLTDGEAGSGGGSLEEGEELGEIRRAEARAAAEILGVDD-VEFLDYPDG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1233998078 118 -AVEQHEGAVADALMPLLDATPGTWCLTPWR-GDGHPDHEATARACLTA 164
Cdd:pfam02585  80 gLEYWDLEELLDALADLIRRYRPDVVVTPDPdGGGHPDHRATGRAVLAA 128
thiol_BshB2 TIGR04000
bacillithiol biosynthesis deacetylase BshB2; Members of this protein family are BshB2 (YojG), ...
 38-164 2.53e-12

bacillithiol biosynthesis deacetylase BshB2; Members of this protein family are BshB2 (YojG), an enzyme of bacillithiol biosynthesis; either BshB1 (YpjG) or BshB2 must be present, and often both are present. Bacillithiol is a low-molecular-weight thiol, an analog of glutathione and mycothiol, and is found largely in the Firmicutes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 188515  Cd Length: 217  Bit Score: 63.98  E-value: 2.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233998078  38 VVVAPHPDDEVLGVGGLLSLAAAAGVDVRVVAVTDGD-GSHPGSPT-VTAEDLRARRPVESERALAELGIdHSPTRLQIA 115
Cdd:TIGR04000   4 LVIFPHPDDEAFGVAGTIALYRQKGIPVTYACLTLGEmGRNMGNPPfATRESLPEIRKKELIEACKAMGI-TDLRMLGLR 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1233998078 116 DGAVE-QHEGAVADALMPLLDATPGTWCLTPWRGDG-HPDHEATARACLTA 164
Cdd:TIGR04000  83 DKTIEfEDDEELADMVKGIIEELNPSLIITFYPGYAvHPDHDATGRAVIRA 133
PBP2_SsuA_like_2 cd13558
Putative substrate binding domain of sulfonate binding protein, the type 2 periplasmic binding ...
 58-117 4.63e-03

Putative substrate binding domain of sulfonate binding protein, the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270276  Cd Length: 267  Bit Score: 37.65  E-value: 4.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1233998078  58 AAAAGVDVRVVAVTDGDGS------HPGSPTVTAEDLRARRPVESE---------RALAELGIDHS---PTRLQIADG 117
Cdd:cd13558    61 AAAAGAPIKIVAALRGDVNgqallvPKDSPIRSVADLKGKRVAYVRgsishylllKALEKAGLSPSdveLVFLTPADA 138
 
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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