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Conserved domains on  [gi|497383334|ref|WP_009697547|]
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MULTISPECIES: glutathione-regulated potassium-efflux system ancillary protein KefG [Vibrio]

Protein Classification

glutathione-regulated potassium-efflux system ancillary protein KefG( domain architecture ID 10012228)

glutathione-regulated potassium-efflux system ancillary protein KefG, a regulatory subunit that is required for full KefB activity, is part of a potassium efflux system that confers protection against electrophiles

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 4-183 3.34e-134

glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional


:

Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 373.18  E-value: 3.34e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334   4 ATPIPPRVLVIYAHPEPQNSIANQVMIKKIESLGHVTVHDLYGAYPDFFIDVNYEHDLLMTHDVIVFHHPLYMYSCPALL 83
Cdd:PRK04930   1 MMSQPPKVLLLYAHPESQDSVANRVLLKPAQQLEHVTVHDLYAHYPDFFIDIPHEQALLREHDVIVFQHPLYTYSCPALL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334  84 KEWMDRVLGKGFAFG-DGSALAGKYWRSVITTGGKEDAFSPMGYNKYPLEQILQPFELTAALCQMHWIEPLVLYWSRNVS 162
Cdd:PRK04930  81 KEWLDRVLSRGFASGpGGNALAGKYWRSVITTGEPESAYRYDGYNRYPMSDILRPFELTAAMCRMHWLSPIIIYWARRQS 160

                        170       180
                 ....*....|....*....|.
gi 497383334 163 DIERYQHAEQYRQWLNNPLRE 183
Cdd:PRK04930 161 PEELASHARAYGDWLANPLSA 181
 
Name Accession Description Interval E-value
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 4-183 3.34e-134

glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 373.18  E-value: 3.34e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334   4 ATPIPPRVLVIYAHPEPQNSIANQVMIKKIESLGHVTVHDLYGAYPDFFIDVNYEHDLLMTHDVIVFHHPLYMYSCPALL 83
Cdd:PRK04930   1 MMSQPPKVLLLYAHPESQDSVANRVLLKPAQQLEHVTVHDLYAHYPDFFIDIPHEQALLREHDVIVFQHPLYTYSCPALL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334  84 KEWMDRVLGKGFAFG-DGSALAGKYWRSVITTGGKEDAFSPMGYNKYPLEQILQPFELTAALCQMHWIEPLVLYWSRNVS 162
Cdd:PRK04930  81 KEWLDRVLSRGFASGpGGNALAGKYWRSVITTGEPESAYRYDGYNRYPMSDILRPFELTAAMCRMHWLSPIIIYWARRQS 160

                        170       180
                 ....*....|....*....|.
gi 497383334 163 DIERYQHAEQYRQWLNNPLRE 183
Cdd:PRK04930 161 PEELASHARAYGDWLANPLSA 181
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 10-181 4.41e-58

Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction only];


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 180.81  E-value: 4.41e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334  10 RVLVIYAHPEPQ---NSIANQVmIKKIESLGH-VTVHDLYG-AYP------DFF------IDVNYEHDLLMTHDVIVFHH 72
Cdd:COG2249    1 KILIIYAHPDPSsfnAALAEAA-AEGLEAAGHeVTVHDLYAeGFDpvlsaaDFYrdgplpIDVAAEQELLLWADHLVFQF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334  73 PLYMYSCPALLKEWMDRVLGKGFAFGDGS-----ALAGKYWRSVITTGGKEDAFSPMGYNKyPLEQILqpFELTAALCQM 147
Cdd:COG2249   80 PLWWYSMPALLKGWIDRVLTPGFAYGYGGgypggLLKGKKALLVVTTGGPEEAYSRLGYGG-PIEELL--FRGTLGYCGM 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 497383334 148 HWIEPLVLYWSRNVSDIERYQHAEQYRQWLNNPL 181
Cdd:COG2249  157 KVLPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 10-177 6.96e-51

Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyze the NAD(P)H-dependent two-electron reductions of quinones and protect cells against damage by free radicals and reactive oxygen species. This enzyme uses a FAD co-factor. The equation for this reaction is:- NAD(P)H + acceptor <=> NAD(P)(+) + reduced acceptor. This enzyme is also involved in the bioactivation of prodrugs used in chemotherapy. The family also includes acyl carrier protein phosphodiesterase EC:3.1.4.14. This enzyme converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine residue from ACP. This family is related to pfam03358 and pfam00258.


Pssm-ID: 426816 [Multi-domain]  Cd Length: 193  Bit Score: 162.50  E-value: 6.96e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334   10 RVLVIYAHPEPQ--NSIANQVMIKKIESLGH-VTVHDLY--------------GAYPDFFIDVNYEHDLLMTHDVIVFHH 72
Cdd:pfam02525   2 KILIINAHPRPGsfSSRLADALVEALKAAGHeVTVRDLYalflpvldaedladLTYPQGAADVESEQEELLAADVIVFQF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334   73 PLYMYSCPALLKEWMDRVLGKGFAF------GDGSALAGKYWRSVITTGGKEDAFSPMGYNKYPLEQILQPFELTAALCQ 146
Cdd:pfam02525  82 PLYWFSVPALLKGWIDRVLRAGFAFkyeeggPGGGGLLGKKVLVIVTTGGPEYAYGKGGYNGFSLDELLPYLRGILGFCG 161

                         170       180       190
                  ....*....|....*....|....*....|..
gi 497383334  147 MHWIEPLVLYWSRNVSDIE-RYQHAEQYRQWL 177
Cdd:pfam02525 162 ITDLPPFAVEGTAGPEDEAaLAEALERYEERL 193
 
Name Accession Description Interval E-value
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 4-183 3.34e-134

glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 373.18  E-value: 3.34e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334   4 ATPIPPRVLVIYAHPEPQNSIANQVMIKKIESLGHVTVHDLYGAYPDFFIDVNYEHDLLMTHDVIVFHHPLYMYSCPALL 83
Cdd:PRK04930   1 MMSQPPKVLLLYAHPESQDSVANRVLLKPAQQLEHVTVHDLYAHYPDFFIDIPHEQALLREHDVIVFQHPLYTYSCPALL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334  84 KEWMDRVLGKGFAFG-DGSALAGKYWRSVITTGGKEDAFSPMGYNKYPLEQILQPFELTAALCQMHWIEPLVLYWSRNVS 162
Cdd:PRK04930  81 KEWLDRVLSRGFASGpGGNALAGKYWRSVITTGEPESAYRYDGYNRYPMSDILRPFELTAAMCRMHWLSPIIIYWARRQS 160

                        170       180
                 ....*....|....*....|.
gi 497383334 163 DIERYQHAEQYRQWLNNPLRE 183
Cdd:PRK04930 161 PEELASHARAYGDWLANPLSA 181
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 10-181 4.41e-58

Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction only];


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 180.81  E-value: 4.41e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334  10 RVLVIYAHPEPQ---NSIANQVmIKKIESLGH-VTVHDLYG-AYP------DFF------IDVNYEHDLLMTHDVIVFHH 72
Cdd:COG2249    1 KILIIYAHPDPSsfnAALAEAA-AEGLEAAGHeVTVHDLYAeGFDpvlsaaDFYrdgplpIDVAAEQELLLWADHLVFQF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334  73 PLYMYSCPALLKEWMDRVLGKGFAFGDGS-----ALAGKYWRSVITTGGKEDAFSPMGYNKyPLEQILqpFELTAALCQM 147
Cdd:COG2249   80 PLWWYSMPALLKGWIDRVLTPGFAYGYGGgypggLLKGKKALLVVTTGGPEEAYSRLGYGG-PIEELL--FRGTLGYCGM 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 497383334 148 HWIEPLVLYWSRNVSDIERYQHAEQYRQWLNNPL 181
Cdd:COG2249  157 KVLPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 10-177 6.96e-51

Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyze the NAD(P)H-dependent two-electron reductions of quinones and protect cells against damage by free radicals and reactive oxygen species. This enzyme uses a FAD co-factor. The equation for this reaction is:- NAD(P)H + acceptor <=> NAD(P)(+) + reduced acceptor. This enzyme is also involved in the bioactivation of prodrugs used in chemotherapy. The family also includes acyl carrier protein phosphodiesterase EC:3.1.4.14. This enzyme converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine residue from ACP. This family is related to pfam03358 and pfam00258.


Pssm-ID: 426816 [Multi-domain]  Cd Length: 193  Bit Score: 162.50  E-value: 6.96e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334   10 RVLVIYAHPEPQ--NSIANQVMIKKIESLGH-VTVHDLY--------------GAYPDFFIDVNYEHDLLMTHDVIVFHH 72
Cdd:pfam02525   2 KILIINAHPRPGsfSSRLADALVEALKAAGHeVTVRDLYalflpvldaedladLTYPQGAADVESEQEELLAADVIVFQF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334   73 PLYMYSCPALLKEWMDRVLGKGFAF------GDGSALAGKYWRSVITTGGKEDAFSPMGYNKYPLEQILQPFELTAALCQ 146
Cdd:pfam02525  82 PLYWFSVPALLKGWIDRVLRAGFAFkyeeggPGGGGLLGKKVLVIVTTGGPEYAYGKGGYNGFSLDELLPYLRGILGFCG 161

                         170       180       190
                  ....*....|....*....|....*....|..
gi 497383334  147 MHWIEPLVLYWSRNVSDIE-RYQHAEQYRQWL 177
Cdd:pfam02525 162 ITDLPPFAVEGTAGPEDEAaLAEALERYEERL 193
PRK00871 PRK00871
glutathione-regulated potassium-efflux system oxidoreductase KefF;
11-192 3.26e-37

glutathione-regulated potassium-efflux system oxidoreductase KefF;


Pssm-ID: 234852  Cd Length: 176  Bit Score: 127.21  E-value: 3.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334  11 VLVIYAHPEPQNSIANQVMIKKIESLGHVTVHDLYGAYPDFFIDVNYEHDLLMTHDVIVFHHPLYMYSCPALLKEWMDRV 90
Cdd:PRK00871   2 ILIIYAHPYPHHSHANKRMLEQARTLEGVEIRSLYQLYPDFNIDIAAEQEALSRADLIVWQHPMQWYSIPPLLKLWIDKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334  91 LGKGFAFG-DGSALAGKYWRSVITTGGKEDAFSPMGYNKYPLeqILQPFELTAALCQMHWIEPLVLYWSRNVSDIERYQH 169
Cdd:PRK00871  82 LSHGWAYGhGGTALHGKHLLWAVTTGGGESHFEIGAHPGFDV--LSQPLQATALYCGLNWLPPFAMHCTFICDDETLEGQ 159

                        170       180
                 ....*....|....*....|...
gi 497383334 170 AEQYRQwlnnplREWDEQGGYHG 192
Cdd:PRK00871 160 ARHYKQ------RLLEWQEAHHG 176
PRK09739 PRK09739
NAD(P)H oxidoreductase;
9-129 3.39e-15

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 70.50  E-value: 3.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334   9 PRVLVIYAHPEPqNSIANQV---MIKKIESLGH-VTVHDLYGAY----------PD-------FFIDVNYEHDLLMTHDV 67
Cdd:PRK09739   4 MRIYLVWAHPRH-DSLTAKVaeaIHQRAQERGHqVEELDLYRSGfdpvltpedePDwknpdkrYSPEVHQLYSELLEHDA 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497383334  68 IVFHHPLYMYSCPALLKEWMDRVLGKGFAFGDGSALAGKYWRSVITTGGKEDAFSPMGYNKY 129
Cdd:PRK09739  83 LVFVFPLWWYSFPAMLKGYIDRVWNNGLAYGDGHKLPFNKVRWVALVGGSKESFVKRGWEKN 144
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 10-150 2.48e-07

Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and conversion];


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 48.77  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334  10 RVLVIYAHPEPQ-NS--IANQVmIKKIESLGH-VTVHDLYGAYPDFFIDVNYEH------------DLLMTHDVIVFHHP 73
Cdd:COG0655    1 KILVINGSPRKNgNTaaLAEAV-AEGAEEAGAeVELIRLADLDIKPCIGCGGTGkcvikddmnaiyEKLLEADGIIFGSP 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497383334  74 LYMYSCPALLKEWMDRVlgkGFAFGDGSALAGKYWrSVITTGGKEDAfspmgynkyplEQILQPFELTAALCQMHWI 150
Cdd:COG0655   80 TYFGNMSAQLKAFIDRL---YALWAKGKLLKGKVG-AVFTTGGHGGA-----------EATLLSLNTFLLHHGMIVV 141
PRK00170 PRK00170
azoreductase; Reviewed
 10-95 1.05e-04

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 41.42  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334  10 RVLVIYAHPEPQNSIANQVMIKKIESLG------HVTVHDLYGAY--------------PDFFIDVNYEHDL-------- 61
Cdd:PRK00170   3 KVLVIKSSILGDYSQSMQLGDAFIEAYKeahpddEVTVRDLAAEPipvldgevvgalgkSAETLTPRQQEAValsdelle 82

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 497383334  62 -LMTHDVIVFHHPLYMYSCPALLKEWMDRVL--GKGF 95
Cdd:PRK00170  83 eFLAADKIVIAAPMYNFSIPTQLKAYIDLIAraGKTF 119
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
9-106 1.61e-04

FMN-dependent NADH-azoreductase [Energy production and conversion];


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 40.88  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334   9 PRVLVIYAHPEPQNSIANQV------MIKKIESLGHVTVHDLYGAYPDFF----IDVNY----EH--------------- 59
Cdd:COG1182    2 MKLLHIDSSPRGEGSVSRRLadafvaALRAAHPDDEVTYRDLAAEPLPHLdgawLAAFFtpaeGRtpeqqaalalsdeli 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 497383334  60 DLLMTHDVIVFHHPLYMYSCPALLKEWMDRVL--GKGFAFGDGSA---LAGK 106
Cdd:COG1182   82 DELLAADVIVIGAPMYNFGIPSQLKAWIDHIAraGRTFRYTENGPvglLTGK 133
FMN_red pfam03358
NADPH-dependent FMN reductase;
9-106 3.42e-03

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 36.45  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497383334    9 PRVLVIYAHPEPQ--NSIANQVMIKKIESLGHVTVHDLYGAYPDFFI-----------DVNYEHDLLMTHDVIVFHHPLY 75
Cdd:pfam03358   1 MKILAISGSPRKGsnTRKLARWAAELLEEGAEVELIDLADLILPLCDedleeeqgdpdDVQELREKIAAADAIIIVTPEY 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 497383334   76 MYSCPALLKEWMDRVlgkgFAFGDGSALAGK 106
Cdd:pfam03358  81 NGSVSGLLKNAIDWL----SRLRGGKELRGK 107
 
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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