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Conserved domains on  [gi|1232914644|gb|OZB20182.1|]
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metal-binding protein [Rhodobacterales bacterium 34-62-10]

Protein Classification

DUF411 domain-containing protein( domain architecture ID 10006855)

DUF411 domain-containing protein similar to Xanthomonas citri CopG may be involved in conferring resistance to cations

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3019 COG3019
Uncharacterized metal-binding protein, DUF411 family [Function unknown];
2-150 5.23e-79

Uncharacterized metal-binding protein, DUF411 family [Function unknown];


:

Pssm-ID: 442256  Cd Length: 152  Bit Score: 230.48  E-value: 5.23e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914644   2 NRREFIVAGGAAAGLPGVVHTQSLA--PRVEVYKSPTCGCCSAWIEHMERAGFVVDARNVDqdALYAFKAQSGITPNLAS 79
Cdd:COG3019     3 SRRTLLAAALALALLAALAGAAAAAaaPAITVYKSPTCGCCGAWVDHLEANGFEVTVVDTD--DLAAVKQRLGVPPELAS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1232914644  80 CHTALVDGYVIEGHVPAADVERLLAERPEAIGLSVPGMPIGSPGMEMGNQRDAFETLLLLKDSSTEIFERH 150
Cdd:COG3019    81 CHTAVVGGYVIEGHVPAADIKRLLAERPDAIGLAVPGMPVGSPGMEMGDRKDPYDVLLFGKDGSTSVFARY 151
 
Name Accession Description Interval E-value
COG3019 COG3019
Uncharacterized metal-binding protein, DUF411 family [Function unknown];
2-150 5.23e-79

Uncharacterized metal-binding protein, DUF411 family [Function unknown];


Pssm-ID: 442256  Cd Length: 152  Bit Score: 230.48  E-value: 5.23e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914644   2 NRREFIVAGGAAAGLPGVVHTQSLA--PRVEVYKSPTCGCCSAWIEHMERAGFVVDARNVDqdALYAFKAQSGITPNLAS 79
Cdd:COG3019     3 SRRTLLAAALALALLAALAGAAAAAaaPAITVYKSPTCGCCGAWVDHLEANGFEVTVVDTD--DLAAVKQRLGVPPELAS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1232914644  80 CHTALVDGYVIEGHVPAADVERLLAERPEAIGLSVPGMPIGSPGMEMGNQRDAFETLLLLKDSSTEIFERH 150
Cdd:COG3019    81 CHTAVVGGYVIEGHVPAADIKRLLAERPDAIGLAVPGMPVGSPGMEMGDRKDPYDVLLFGKDGSTSVFARY 151
DUF411 pfam04214
Protein of unknown function, DUF; The function of the members of this bacterial protein family ...
 57-124 1.12e-42

Protein of unknown function, DUF; The function of the members of this bacterial protein family is unknown. Some members may be involved in conferring cation resistance.


Pssm-ID: 427791  Cd Length: 69  Bit Score: 135.70  E-value: 1.12e-42
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1232914644  57 RNVDQDALYAFKAQSGITPNLASCHTALVDGYVIEGHVPAADVERLLAERPEAIGLSVPGMPIGSPGM 124
Cdd:pfam04214   2 TVVDTDDLAAVKRRLGVPAELASCHTAVVGGYVIEGHVPAADIKRLLAEKPDARGLAVPGMPVGSPGM 69
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 28-66 6.23e-03

NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein.


Pssm-ID: 239274 [Multi-domain]  Cd Length: 73  Bit Score: 33.74  E-value: 6.23e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1232914644  28 RVEVYKSPTCGCCSAWIEHMERAGFVVDARNVDQDALYA 66
Cdd:cd02976     1 EVTVYTKPDCPYCKATKRFLDERGIPFEEVDVDEDPEAL 39
 
Name Accession Description Interval E-value
COG3019 COG3019
Uncharacterized metal-binding protein, DUF411 family [Function unknown];
2-150 5.23e-79

Uncharacterized metal-binding protein, DUF411 family [Function unknown];


Pssm-ID: 442256  Cd Length: 152  Bit Score: 230.48  E-value: 5.23e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914644   2 NRREFIVAGGAAAGLPGVVHTQSLA--PRVEVYKSPTCGCCSAWIEHMERAGFVVDARNVDqdALYAFKAQSGITPNLAS 79
Cdd:COG3019     3 SRRTLLAAALALALLAALAGAAAAAaaPAITVYKSPTCGCCGAWVDHLEANGFEVTVVDTD--DLAAVKQRLGVPPELAS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1232914644  80 CHTALVDGYVIEGHVPAADVERLLAERPEAIGLSVPGMPIGSPGMEMGNQRDAFETLLLLKDSSTEIFERH 150
Cdd:COG3019    81 CHTAVVGGYVIEGHVPAADIKRLLAERPDAIGLAVPGMPVGSPGMEMGDRKDPYDVLLFGKDGSTSVFARY 151
DUF411 pfam04214
Protein of unknown function, DUF; The function of the members of this bacterial protein family ...
 57-124 1.12e-42

Protein of unknown function, DUF; The function of the members of this bacterial protein family is unknown. Some members may be involved in conferring cation resistance.


Pssm-ID: 427791  Cd Length: 69  Bit Score: 135.70  E-value: 1.12e-42
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1232914644  57 RNVDQDALYAFKAQSGITPNLASCHTALVDGYVIEGHVPAADVERLLAERPEAIGLSVPGMPIGSPGM 124
Cdd:pfam04214   2 TVVDTDDLAAVKRRLGVPAELASCHTAVVGGYVIEGHVPAADIKRLLAEKPDARGLAVPGMPVGSPGM 69
NrdH cd02976
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ...
 28-66 6.23e-03

NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein.


Pssm-ID: 239274 [Multi-domain]  Cd Length: 73  Bit Score: 33.74  E-value: 6.23e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1232914644  28 RVEVYKSPTCGCCSAWIEHMERAGFVVDARNVDQDALYA 66
Cdd:cd02976     1 EVTVYTKPDCPYCKATKRFLDERGIPFEEVDVDEDPEAL 39
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
28-74 6.63e-03

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 33.63  E-value: 6.63e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1232914644  28 RVEVYKSPTCGCCSAWIEHMERAGFVVDARNVDQD--ALYAFKAQSGIT 74
Cdd:COG0695     1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDEDpeAREELRERSGRR 49
 
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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