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Conserved domains on  [gi|1092311309|gb|OHV23233|]
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tellurium resistance protein [Frankia sp. NRRL B-16219]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
terB cd07176
tellurite resistance protein terB; This family contains uncharacterized bacterial proteins ...
232-346 1.63e-25

tellurite resistance protein terB; This family contains uncharacterized bacterial proteins involved in tellurium resistance. The prototype of this CD is the Kp-terB protein from Klebsiella pneumoniae, whose 3D structure was recently determined. The biological function of terB and the mechanism responsible for tellurium resistance are unknown.


:

Pssm-ID: 143580  Cd Length: 111  Bit Score: 98.83  E-value: 1.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092311309 232 FRDAAVAMCALVAAADGHVDPAERDAMAASIQAEDVLADYPRADLELLFDLHVARLRSDlaaGRRAAMREIGKVRGDPVR 311
Cdd:cd07176     1 FAEALVALAALVAAADGDIDDAELQAIEALLRSLPVLSGFDRERLIALLDKLLALLRPE---GLAALLKAAAKLLPPELR 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1092311309 312 sWAVLRIGAVIGRADGYFDPAERRVVQDAADTLGL 346
Cdd:cd07176    78 -ETAFAVAVDIAAADGEVDPEERAVLEKLYRALGL 111
Nudix_Hydrolase super family cl00447
Nudix hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it ...
14-78 3.02e-04

Nudix hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes 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. Members of this family are recognized by a highly conserved 23-residue nudix motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of nudix hydrolase 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 and "house-cleaning" enzymes. Substrate specificity is used to define child 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. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase.


The actual alignment was detected with superfamily member cd04688:

Pssm-ID: 351096 [Multi-domain]  Cd Length: 126  Bit Score: 39.97  E-value: 3.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092311309  14 LIEVDGGLLV-RADDTAGPRFPGGSARLGESSLDAAERILRAALSAAGRPV-FAGCVEHSEAWRPAP 78
Cdd:cd04688     7 IIIHNGKLLVqKNPDETFYRPPGGGIEFGESSEEALIREFKEELGLKIEITrLLGVVENIFTYNGKP 73
AJAP1_PANP_C super family cl21145
AJAP1/PANP C-terminus; This family includes the C-terminus of adherens junction-associated ...
102-177 1.96e-03

AJAP1/PANP C-terminus; This family includes the C-terminus of adherens junction-associated protein 1 (AJAP1) and of PILR-associating neural protein (PANP). AJAP1 inhibits cell adhesion and migration. PANP is a ligand for the immune inhibitory receptor paired immunoglobulin-like type 2 receptor alpha.


The actual alignment was detected with superfamily member pfam15298:

Pssm-ID: 317671  Cd Length: 200  Bit Score: 38.73  E-value: 1.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092311309 102 DTTPADRTPCDTPADRTPAETAATTDGTTSAHTLTVLYAVTLEPAGLAGGHALPRGLTLVrpyESDSGPALTIQPP 177
Cdd:pfam15298  10 DSLESSTFPGIYGSTRVSTTTTTATTTTTTTRTTTRTTTVTTQPPGLGPGRNEPGRLSTT---EPSAGHGKTAKPP 82
 
Name Accession Description Interval E-value
terB cd07176
tellurite resistance protein terB; This family contains uncharacterized bacterial proteins ...
232-346 1.63e-25

tellurite resistance protein terB; This family contains uncharacterized bacterial proteins involved in tellurium resistance. The prototype of this CD is the Kp-terB protein from Klebsiella pneumoniae, whose 3D structure was recently determined. The biological function of terB and the mechanism responsible for tellurium resistance are unknown.


Pssm-ID: 143580  Cd Length: 111  Bit Score: 98.83  E-value: 1.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092311309 232 FRDAAVAMCALVAAADGHVDPAERDAMAASIQAEDVLADYPRADLELLFDLHVARLRSDlaaGRRAAMREIGKVRGDPVR 311
Cdd:cd07176     1 FAEALVALAALVAAADGDIDDAELQAIEALLRSLPVLSGFDRERLIALLDKLLALLRPE---GLAALLKAAAKLLPPELR 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1092311309 312 sWAVLRIGAVIGRADGYFDPAERRVVQDAADTLGL 346
Cdd:cd07176    78 -ETAFAVAVDIAAADGEVDPEERAVLEKLYRALGL 111
TerB COG3793
Tellurite resistance protein [Inorganic ion transport and metabolism];
232-348 1.55e-17

Tellurite resistance protein [Inorganic ion transport and metabolism];


Pssm-ID: 226316  Cd Length: 144  Bit Score: 78.21  E-value: 1.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092311309 232 FRDAAVAMCALVAAADGHVDPAERDAMAASIQAEDVLADYPRADLELLFDLHVARLRSDLAAGRRAAMREIGKVRGDPVR 311
Cdd:COG3793    23 FLQAVVAACALIARADGEVDSEEKQKMVQFLRSSAALSVFDSNEINEIFETLVGSFDTDFEIGKREAMKEIEDLKHDTEA 102
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1092311309 312 SWAVLRIGAVIGRADGYFDPAERRVVQDAADTLGLRS 348
Cdd:COG3793   103 AEDVLRVAVAVAEADGEFEAEERAVLREIAGALGLSP 139
TerB pfam05099
Tellurite resistance protein TerB; This family contains the TerB tellurite resistance proteins ...
217-346 6.41e-13

Tellurite resistance protein TerB; This family contains the TerB tellurite resistance proteins from a a number of bacteria.


Pssm-ID: 309991  Cd Length: 142  Bit Score: 65.33  E-value: 6.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092311309 217 RAQLTARREDVRGEVFRDAAVAMCALVAAADGHVDPAERDAMAASIQAEDVLADYPRADLELLFDLHVARlrsdlAAGRR 296
Cdd:pfam05099   9 LLAAAAGALATDDARFALALAALLAEVARADGQVSESERQAFRRLLASRFGLSPEEADALIELAEAAVEE-----AVDLY 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1092311309 297 AAMREIGKVRGDPVRSwAVLRIGAVIGRADGYFDPAERRVVQDAADTLGL 346
Cdd:pfam05099  84 QFTRALKRHFDPEQRR-ALIEALWEIAYADGELDPYEDAVIRRVADLLGL 132
Nudix_Hydrolase_29 cd04688
Members of the Nudix hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates ...
14-78 3.02e-04

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.


Pssm-ID: 240044 [Multi-domain]  Cd Length: 126  Bit Score: 39.97  E-value: 3.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092311309  14 LIEVDGGLLV-RADDTAGPRFPGGSARLGESSLDAAERILRAALSAAGRPV-FAGCVEHSEAWRPAP 78
Cdd:cd04688     7 IIIHNGKLLVqKNPDETFYRPPGGGIEFGESSEEALIREFKEELGLKIEITrLLGVVENIFTYNGKP 73
AJAP1_PANP_C pfam15298
AJAP1/PANP C-terminus; This family includes the C-terminus of adherens junction-associated ...
102-177 1.96e-03

AJAP1/PANP C-terminus; This family includes the C-terminus of adherens junction-associated protein 1 (AJAP1) and of PILR-associating neural protein (PANP). AJAP1 inhibits cell adhesion and migration. PANP is a ligand for the immune inhibitory receptor paired immunoglobulin-like type 2 receptor alpha.


Pssm-ID: 317671  Cd Length: 200  Bit Score: 38.73  E-value: 1.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092311309 102 DTTPADRTPCDTPADRTPAETAATTDGTTSAHTLTVLYAVTLEPAGLAGGHALPRGLTLVrpyESDSGPALTIQPP 177
Cdd:pfam15298  10 DSLESSTFPGIYGSTRVSTTTTTATTTTTTTRTTTRTTTVTTQPPGLGPGRNEPGRLSTT---EPSAGHGKTAKPP 82
 
Name Accession Description Interval E-value
terB cd07176
tellurite resistance protein terB; This family contains uncharacterized bacterial proteins ...
232-346 1.63e-25

tellurite resistance protein terB; This family contains uncharacterized bacterial proteins involved in tellurium resistance. The prototype of this CD is the Kp-terB protein from Klebsiella pneumoniae, whose 3D structure was recently determined. The biological function of terB and the mechanism responsible for tellurium resistance are unknown.


Pssm-ID: 143580  Cd Length: 111  Bit Score: 98.83  E-value: 1.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092311309 232 FRDAAVAMCALVAAADGHVDPAERDAMAASIQAEDVLADYPRADLELLFDLHVARLRSDlaaGRRAAMREIGKVRGDPVR 311
Cdd:cd07176     1 FAEALVALAALVAAADGDIDDAELQAIEALLRSLPVLSGFDRERLIALLDKLLALLRPE---GLAALLKAAAKLLPPELR 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1092311309 312 sWAVLRIGAVIGRADGYFDPAERRVVQDAADTLGL 346
Cdd:cd07176    78 -ETAFAVAVDIAAADGEVDPEERAVLEKLYRALGL 111
TerB COG3793
Tellurite resistance protein [Inorganic ion transport and metabolism];
232-348 1.55e-17

Tellurite resistance protein [Inorganic ion transport and metabolism];


Pssm-ID: 226316  Cd Length: 144  Bit Score: 78.21  E-value: 1.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092311309 232 FRDAAVAMCALVAAADGHVDPAERDAMAASIQAEDVLADYPRADLELLFDLHVARLRSDLAAGRRAAMREIGKVRGDPVR 311
Cdd:COG3793    23 FLQAVVAACALIARADGEVDSEEKQKMVQFLRSSAALSVFDSNEINEIFETLVGSFDTDFEIGKREAMKEIEDLKHDTEA 102
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1092311309 312 SWAVLRIGAVIGRADGYFDPAERRVVQDAADTLGLRS 348
Cdd:COG3793   103 AEDVLRVAVAVAEADGEFEAEERAVLREIAGALGLSP 139
TerB pfam05099
Tellurite resistance protein TerB; This family contains the TerB tellurite resistance proteins ...
217-346 6.41e-13

Tellurite resistance protein TerB; This family contains the TerB tellurite resistance proteins from a a number of bacteria.


Pssm-ID: 309991  Cd Length: 142  Bit Score: 65.33  E-value: 6.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092311309 217 RAQLTARREDVRGEVFRDAAVAMCALVAAADGHVDPAERDAMAASIQAEDVLADYPRADLELLFDLHVARlrsdlAAGRR 296
Cdd:pfam05099   9 LLAAAAGALATDDARFALALAALLAEVARADGQVSESERQAFRRLLASRFGLSPEEADALIELAEAAVEE-----AVDLY 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1092311309 297 AAMREIGKVRGDPVRSwAVLRIGAVIGRADGYFDPAERRVVQDAADTLGL 346
Cdd:pfam05099  84 QFTRALKRHFDPEQRR-ALIEALWEIAYADGELDPYEDAVIRRVADLLGL 132
terB_like cd07177
tellurium resistance terB-like protein; This family consists of tellurium resistance terB ...
235-344 1.27e-12

tellurium resistance terB-like protein; This family consists of tellurium resistance terB proteins, N-terminal domain of heat shock DnaJ-like proteins, N-terminal domain of Mo-dependent nitrogenase-like proteins, C-terminal domain of ABC transporter ATP-binding proteins, C-terminal domain of serine/threonine protein kinase, and many hypothetical bacterial proteins. The function of this family is unknown.


Pssm-ID: 143581  Cd Length: 104  Bit Score: 63.15  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092311309 235 AAVAMCALVAAADGHVDPAERDAMAASIQAEDVLADYPRADLELLFDLHVARLRSDlaagrrAAMREIGKVRGDPVRSWA 314
Cdd:cd07177     1 ALAALLLAAAKADGRVDEEEIAAIEALLRRLPLLDAEERAELIALLEEPLAEAGDL------AALAALLKELPDAELREA 74
                          90       100       110
                  ....*....|....*....|....*....|
gi 1092311309 315 VLRIGAVIGRADGYFDPAERRVVQDAADTL 344
Cdd:cd07177    75 LLAALWEVALADGELDPEERALLRRLADAL 104
Nudix_Hydrolase_29 cd04688
Members of the Nudix hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates ...
14-78 3.02e-04

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.


Pssm-ID: 240044 [Multi-domain]  Cd Length: 126  Bit Score: 39.97  E-value: 3.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092311309  14 LIEVDGGLLV-RADDTAGPRFPGGSARLGESSLDAAERILRAALSAAGRPV-FAGCVEHSEAWRPAP 78
Cdd:cd04688     7 IIIHNGKLLVqKNPDETFYRPPGGGIEFGESSEEALIREFKEELGLKIEITrLLGVVENIFTYNGKP 73
terB_like_DjlA cd07316
N-terminal tellurium resistance protein terB-like domain of heat shock DnaJ-like proteins; ...
235-345 3.03e-04

N-terminal tellurium resistance protein terB-like domain of heat shock DnaJ-like proteins; Tellurium resistance terB-like domain of the DnaJ-like DjlA proteins. This family represents the terB-like domain of DjlA-like proteins, a subgroup of heat shock DnaJ-like proteins. Escherichia coli DjlA is a type III membrane protein with a small N-terminal transmembrane region and DnaJ-like domain on the extreme C-terminus. Overproduction has been shown to activate the RcsC pathway, which regulates the production of the capsular exopolysaccharide colanic acid. The specific function of this domain is unknown.


Pssm-ID: 143585  Cd Length: 106  Bit Score: 39.43  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092311309 235 AAVAMCALVAAADGHVDPAERDAmaasiqAEDVLADYP-----RADLELLFDLHVARlrsdlAAGRRAAMREIGKV-RGD 308
Cdd:cd07316     1 ALFALMGKLAKADGRVSEAEIQA------ARALMDQMGldaeaRREAIRLFNEGKES-----DFGLEEYARQFRRAcGGR 69
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1092311309 309 PVRSWAVLRIGAVIGRADGYFDPAERRVVQDAADTLG 345
Cdd:cd07316    70 PELLLQLLEFLFQIAYADGELSEAERELLRRIARLLG 106
AJAP1_PANP_C pfam15298
AJAP1/PANP C-terminus; This family includes the C-terminus of adherens junction-associated ...
102-177 1.96e-03

AJAP1/PANP C-terminus; This family includes the C-terminus of adherens junction-associated protein 1 (AJAP1) and of PILR-associating neural protein (PANP). AJAP1 inhibits cell adhesion and migration. PANP is a ligand for the immune inhibitory receptor paired immunoglobulin-like type 2 receptor alpha.


Pssm-ID: 317671  Cd Length: 200  Bit Score: 38.73  E-value: 1.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092311309 102 DTTPADRTPCDTPADRTPAETAATTDGTTSAHTLTVLYAVTLEPAGLAGGHALPRGLTLVrpyESDSGPALTIQPP 177
Cdd:pfam15298  10 DSLESSTFPGIYGSTRVSTTTTTATTTTTTTRTTTRTTTVTTQPPGLGPGRNEPGRLSTT---EPSAGHGKTAKPP 82
TerB COG4103
Uncharacterized conserved protein, tellurite resistance protein B (TerB) family [Function ...
233-347 2.56e-03

Uncharacterized conserved protein, tellurite resistance protein B (TerB) family [Function unknown];


Pssm-ID: 226588  Cd Length: 148  Bit Score: 37.78  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092311309 233 RDAAVAMCALVAAADGHVDPAERDAMAASI---------QAEDVLADYPRADLELLfDLH--VARLRSDLAAGRRAAMre 301
Cdd:COG4103    28 RLAAAALLFHVMEADGTVSESEREAFRAILkenfgidgeELDALIEAGEEAGYEAI-DLYsfTSVLKRHLDEEQRLEL-- 104
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1092311309 302 igkvrgdpvrswavLRIGAVIGRADGYFDPAERRVVQDAADTLGLR 347
Cdd:COG4103   105 --------------IGLMWEIAYADGELDESEDHVIWRVAELLGVS 136
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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