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Conserved domains on  [gi|2308572997|ref|WP_261262103|]
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glutathione-regulated potassium-efflux system ancillary protein KefG [Serratia fonticola]

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
 1-183 3.34e-149

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


:

Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 410.55  E-value: 3.34e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308572997   1 MSQPPKVLLLYAHPESQDSVANRVLLQPAQQLEHVTVHDLYAHYPDFFIDIHHEQQLLRDHQVIVFQHPLYTYSCPALLK 80
Cdd:PRK04930    2 MSQPPKVLLLYAHPESQDSVANRVLLKPAQQLEHVTVHDLYAHYPDFFIDIPHEQALLREHDVIVFQHPLYTYSCPALLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308572997  81 EWLDRVLSRGFASGMGGNALAGKYWRSVITTGEPEGAYRTGGYNRYPIEDILRPFELTAAMCHMHWMTPILVYWARRQKP 160
Cdd:PRK04930   82 EWLDRVLSRGFASGPGGNALAGKYWRSVITTGEPESAYRYDGYNRYPMSDILRPFELTAAMCRMHWLSPIIIYWARRQSP 161

                         170       180
                  ....*....|....*....|...
gi 2308572997 161 EVLSSHASAYGDWLRNPLPHTGR 183
Cdd:PRK04930  162 EELASHARAYGDWLANPLSAGGR 184
 
Name Accession Description Interval E-value
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 1-183 3.34e-149

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


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 410.55  E-value: 3.34e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308572997   1 MSQPPKVLLLYAHPESQDSVANRVLLQPAQQLEHVTVHDLYAHYPDFFIDIHHEQQLLRDHQVIVFQHPLYTYSCPALLK 80
Cdd:PRK04930    2 MSQPPKVLLLYAHPESQDSVANRVLLKPAQQLEHVTVHDLYAHYPDFFIDIPHEQALLREHDVIVFQHPLYTYSCPALLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308572997  81 EWLDRVLSRGFASGMGGNALAGKYWRSVITTGEPEGAYRTGGYNRYPIEDILRPFELTAAMCHMHWMTPILVYWARRQKP 160
Cdd:PRK04930   82 EWLDRVLSRGFASGPGGNALAGKYWRSVITTGEPESAYRYDGYNRYPMSDILRPFELTAAMCRMHWLSPIIIYWARRQSP 161

                         170       180
                  ....*....|....*....|...
gi 2308572997 161 EVLSSHASAYGDWLRNPLPHTGR 183
Cdd:PRK04930  162 EELASHARAYGDWLANPLSAGGR 184
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 6-178 6.39e-58

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 179.65  E-value: 6.39e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308572997   6 KVLLLYAHPESqdSVANRVLLQPAQQ-LE----HVTVHDLYA-HYP------DFF------IDIHHEQQLLRDHQVIVFQ 67
Cdd:COG2249     1 KILIIYAHPDP--SSFNAALAEAAAEgLEaaghEVTVHDLYAeGFDpvlsaaDFYrdgplpIDVAAEQELLLWADHLVFQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308572997  68 HPLYTYSCPALLKEWLDRVLSRGFA----SGMGGNALAGKYWRSVITTGEPEGAYRTGGYNRyPIEDILrpFELTAAMCH 143
Cdd:COG2249    79 FPLWWYSMPALLKGWIDRVLTPGFAygygGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGG-PIEELL--FRGTLGYCG 155

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2308572997 144 MHWMTPILVYWARRQKPEVLSSHASAYGDWLRNPL 178
Cdd:COG2249   156 MKVLPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 6-174 3.64e-50

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: 160.19  E-value: 3.64e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308572997   6 KVLLLYAHPE--SQDSVANRVLLQPAQQLEH-VTVHDLYA--------------HYPDFFIDIHHEQQLLRDHQVIVFQH 68
Cdd:pfam02525   2 KILIINAHPRpgSFSSRLADALVEALKAAGHeVTVRDLYAlflpvldaedladlTYPQGAADVESEQEELLAADVIVFQF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308572997  69 PLYTYSCPALLKEWLDRVLSRGFA-----SGMGGNALAGKYWRSVITTGEPEGAYRTGGYNRYPIEDILRPFELTAAMCH 143
Cdd:pfam02525  82 PLYWFSVPALLKGWIDRVLRAGFAfkyeeGGPGGGGLLGKKVLVIVTTGGPEYAYGKGGYNGFSLDELLPYLRGILGFCG 161

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2308572997 144 MHWMTPILVYWARRQKPE-VLSSHASAYGDWL 174
Cdd:pfam02525 162 ITDLPPFAVEGTAGPEDEaALAEALERYEERL 193
 
Name Accession Description Interval E-value
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 1-183 3.34e-149

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


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 410.55  E-value: 3.34e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308572997   1 MSQPPKVLLLYAHPESQDSVANRVLLQPAQQLEHVTVHDLYAHYPDFFIDIHHEQQLLRDHQVIVFQHPLYTYSCPALLK 80
Cdd:PRK04930    2 MSQPPKVLLLYAHPESQDSVANRVLLKPAQQLEHVTVHDLYAHYPDFFIDIPHEQALLREHDVIVFQHPLYTYSCPALLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308572997  81 EWLDRVLSRGFASGMGGNALAGKYWRSVITTGEPEGAYRTGGYNRYPIEDILRPFELTAAMCHMHWMTPILVYWARRQKP 160
Cdd:PRK04930   82 EWLDRVLSRGFASGPGGNALAGKYWRSVITTGEPESAYRYDGYNRYPMSDILRPFELTAAMCRMHWLSPIIIYWARRQSP 161

                         170       180
                  ....*....|....*....|...
gi 2308572997 161 EVLSSHASAYGDWLRNPLPHTGR 183
Cdd:PRK04930  162 EELASHARAYGDWLANPLSAGGR 184
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 6-178 6.39e-58

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 179.65  E-value: 6.39e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308572997   6 KVLLLYAHPESqdSVANRVLLQPAQQ-LE----HVTVHDLYA-HYP------DFF------IDIHHEQQLLRDHQVIVFQ 67
Cdd:COG2249     1 KILIIYAHPDP--SSFNAALAEAAAEgLEaaghEVTVHDLYAeGFDpvlsaaDFYrdgplpIDVAAEQELLLWADHLVFQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308572997  68 HPLYTYSCPALLKEWLDRVLSRGFA----SGMGGNALAGKYWRSVITTGEPEGAYRTGGYNRyPIEDILrpFELTAAMCH 143
Cdd:COG2249    79 FPLWWYSMPALLKGWIDRVLTPGFAygygGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGG-PIEELL--FRGTLGYCG 155

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2308572997 144 MHWMTPILVYWARRQKPEVLSSHASAYGDWLRNPL 178
Cdd:COG2249   156 MKVLPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 6-174 3.64e-50

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: 160.19  E-value: 3.64e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308572997   6 KVLLLYAHPE--SQDSVANRVLLQPAQQLEH-VTVHDLYA--------------HYPDFFIDIHHEQQLLRDHQVIVFQH 68
Cdd:pfam02525   2 KILIINAHPRpgSFSSRLADALVEALKAAGHeVTVRDLYAlflpvldaedladlTYPQGAADVESEQEELLAADVIVFQF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308572997  69 PLYTYSCPALLKEWLDRVLSRGFA-----SGMGGNALAGKYWRSVITTGEPEGAYRTGGYNRYPIEDILRPFELTAAMCH 143
Cdd:pfam02525  82 PLYWFSVPALLKGWIDRVLRAGFAfkyeeGGPGGGGLLGKKVLVIVTTGGPEYAYGKGGYNGFSLDELLPYLRGILGFCG 161

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2308572997 144 MHWMTPILVYWARRQKPE-VLSSHASAYGDWL 174
Cdd:pfam02525 162 ITDLPPFAVEGTAGPEDEaALAEALERYEERL 193
PRK00871 PRK00871
glutathione-regulated potassium-efflux system oxidoreductase KefF;
7-174 1.07e-36

glutathione-regulated potassium-efflux system oxidoreductase KefF;


Pssm-ID: 234852  Cd Length: 176  Bit Score: 125.28  E-value: 1.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308572997   7 VLLLYAHPESQDSVANRVLLQPAQQLEHVTVHDLYAHYPDFFIDIHHEQQLLRDHQVIVFQHPLYTYSCPALLKEWLDRV 86
Cdd:PRK00871    2 ILIIYAHPYPHHSHANKRMLEQARTLEGVEIRSLYQLYPDFNIDIAAEQEALSRADLIVWQHPMQWYSIPPLLKLWIDKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308572997  87 LSRGFASGMGGNALAGKYWRSVITTGEPEGAYRTGGYNRYPIedILRPFELTAAMCHMHWMTPILVYWARRQKPEVLSSH 166
Cdd:PRK00871   82 LSHGWAYGHGGTALHGKHLLWAVTTGGGESHFEIGAHPGFDV--LSQPLQATALYCGLNWLPPFAMHCTFICDDETLEGQ 159


                  ....*...
gi 2308572997 167 ASAYGDWL 174
Cdd:PRK00871  160 ARHYKQRL 167
PRK09739 PRK09739
NAD(P)H oxidoreductase;
3-132 1.39e-11

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 60.49  E-value: 1.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308572997   3 QPPKVLLLYAHPEsQDS----VANRVLLQPAQQLEHVTVHDLYAHY----------PD-------FFIDIHHEQQLLRDH 61
Cdd:PRK09739    2 QSMRIYLVWAHPR-HDSltakVAEAIHQRAQERGHQVEELDLYRSGfdpvltpedePDwknpdkrYSPEVHQLYSELLEH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2308572997  62 QVIVFQHPLYTYSCPALLKEWLDRVLSRGFASGmGGNALAGKYWRSVITTGEPEGAYRTGGYNRYpIEDIL 132
Cdd:PRK09739   81 DALVFVFPLWWYSFPAMLKGYIDRVWNNGLAYG-DGHKLPFNKVRWVALVGGSKESFVKRGWEKN-MSDYL 149
PRK00170 PRK00170
azoreductase; Reviewed
 1-116 1.02e-04

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 41.03  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308572997   1 MSqppKVLLLYAHPESQDSVANRV---LLQPAQQLE---HVTVHDLYAHY-PDFFIDI------------HHEQQLL--- 58
Cdd:PRK00170    1 MS---KVLVIKSSILGDYSQSMQLgdaFIEAYKEAHpddEVTVRDLAAEPiPVLDGEVvgalgksaetltPRQQEAVals 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2308572997  59 -------RDHQVIVFQHPLYTYSCPALLKEWLDRVlsrgfasgmggnALAGKYWRsvITTGEPEG 116
Cdd:PRK00170   78 delleefLAADKIVIAAPMYNFSIPTQLKAYIDLI------------ARAGKTFR--YTENGPVG 128
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 56-161 1.35e-03

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 37.60  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308572997  56 QLLRDHQVIVFQHPLYTYSCPALLKEWLDRVlsrgFASGMGGNALAGKYWRSVITTGEPEGayrtggynrypiEDILRPF 135
Cdd:COG0655    66 EKLLEADGIIFGSPTYFGNMSAQLKAFIDRL----YALWAKGKLLKGKVGAVFTTGGHGGA------------EATLLSL 129

                          90       100
                  ....*....|....*....|....*.
gi 2308572997 136 ELTAAMCHMHWMTPILVYWARRQKPE 161
Cdd:COG0655   130 NTFLLHHGMIVVGLPPYGAVGGGGPG 155
 
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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