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Conserved domains on  [gi|489738842|ref|WP_003642935|]
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MULTISPECIES: Rrf2 family transcriptional regulator [Lactobacillaceae]

Protein Classification

Rrf2 family transcriptional regulator( domain architecture ID 10489162)

Rrf2 family transcriptional regulator similar to nitric oxide-responsive regulator NsrR

Gene Ontology:  GO:0003700|GO:0003677
PubMed:  15808743

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rrf2 pfam02082
Iron-dependent Transcriptional regulator; Several proteins in this family form iron-sulfur ...
 3-133 5.07e-36

Iron-dependent Transcriptional regulator; Several proteins in this family form iron-sulfur clusters enabling iron dependent DNA transcription regulation. The iron binding is mediated by three conserved cysteine residues. Members of this family can also bind O-acetyl-L-serine, [Fe-S] and nitric oxide (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


:

Pssm-ID: 396591 [Multi-domain]  Cd Length: 131  Bit Score: 120.35  E-value: 5.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738842    3 NTQLSDATHIMAYIALHTDDQ-LKSEHIASSLNTDPTMVRRMMSKLRKAGLLTSVRGV-ARPTLACSPNDITLKDIYVAV 80
Cdd:pfam02082   2 STKTDYALHALLYLALHPGGEpVTSEEIAERQNISPVYLEKILAKLRKAGLVESVRGAgGGYRLARPPEEITLLDVVRAV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489738842   81 VAKRNFLnvdHNTSETCPVGSVIPRVMEKYYCDIQNSAEARMSRVTLQDIIDD 133
Cdd:pfam02082  82 EGPLALF---ECNNPKCPCGIEIQCALREAWEEAQDAMEDVLDSVTLADLVAD 131
 
Name Accession Description Interval E-value
Rrf2 pfam02082
Iron-dependent Transcriptional regulator; Several proteins in this family form iron-sulfur ...
 3-133 5.07e-36

Iron-dependent Transcriptional regulator; Several proteins in this family form iron-sulfur clusters enabling iron dependent DNA transcription regulation. The iron binding is mediated by three conserved cysteine residues. Members of this family can also bind O-acetyl-L-serine, [Fe-S] and nitric oxide (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 396591 [Multi-domain]  Cd Length: 131  Bit Score: 120.35  E-value: 5.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738842    3 NTQLSDATHIMAYIALHTDDQ-LKSEHIASSLNTDPTMVRRMMSKLRKAGLLTSVRGV-ARPTLACSPNDITLKDIYVAV 80
Cdd:pfam02082   2 STKTDYALHALLYLALHPGGEpVTSEEIAERQNISPVYLEKILAKLRKAGLVESVRGAgGGYRLARPPEEITLLDVVRAV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489738842   81 VAKRNFLnvdHNTSETCPVGSVIPRVMEKYYCDIQNSAEARMSRVTLQDIIDD 133
Cdd:pfam02082  82 EGPLALF---ECNNPKCPCGIEIQCALREAWEEAQDAMEDVLDSVTLADLVAD 131
IscR COG1959
DNA-binding transcriptional regulator, IscR family [Transcription];
3-141 1.00e-25

DNA-binding transcriptional regulator, IscR family [Transcription];


Pssm-ID: 441562  Cd Length: 141  Bit Score: 94.52  E-value: 1.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738842   3 NTQLSDATHIMAYIALHTDDQ-LKSEHIASSLNTDPTMVRRMMSKLRKAGLLTSVRGVA---RptLACSPNDITLKDIYV 78
Cdd:COG1959    3 STKTDYALRALLYLALHPGGEpVTSKEIAERQGISPSYLEKILQKLRKAGLVESVRGPGggyR--LARPPEEITLGDVVR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489738842  79 AVVAKRnFLNVDHNTSETCPVGSviPRVMEKYYCDIQNSAEARMSRVTLQDIIDDISAVQQQA 141
Cdd:COG1959   81 AVEGPL-ALVECVSGPPDCPVEE--ACALHGVWEEAEDAILEVLDSVTLADLVEDAEAREVAE 140
rrf2_super TIGR00738
Rrf2 family protein; This model represents a superfamily of probable transcriptional ...
 9-132 3.01e-12

Rrf2 family protein; This model represents a superfamily of probable transcriptional regulators. One member, RRF2 of Desulfovibrio vulgaris is an apparent regulatory protein experimentally (MEDLINE:97293189). The N-terminal region appears related to the DNA-binding biotin repressor region of the BirA bifunctional according to results after three rounds of PSI-BLAST with a fairly high stringency. [Unknown function, General]


Pssm-ID: 273242  Cd Length: 132  Bit Score: 59.57  E-value: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738842    9 ATHIMAYIALHTDDQ-LKSEHIASSLNTDPTMVRRMMSKLRKAGLLTSVRGvarP----TLACSPNDITLKDIYVAV--- 80
Cdd:TIGR00738  10 ALRALLDLALNPDEGpVSVKEIAERQGISRSYLEKILRTLRKAGLVESVRG---PgggyRLARPPEEITVGDVVRAVegs 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489738842   81 --VAKRNFLNVDHNTSETCPVGSViprvmekyYCDIQNSAEARMSRVTLQDIID 132
Cdd:TIGR00738  87 laPVQCIGLNGCHPGEEVCLLHAV--------WRELEDAIEDFLREITLADLVK 132
 
Name Accession Description Interval E-value
Rrf2 pfam02082
Iron-dependent Transcriptional regulator; Several proteins in this family form iron-sulfur ...
 3-133 5.07e-36

Iron-dependent Transcriptional regulator; Several proteins in this family form iron-sulfur clusters enabling iron dependent DNA transcription regulation. The iron binding is mediated by three conserved cysteine residues. Members of this family can also bind O-acetyl-L-serine, [Fe-S] and nitric oxide (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 396591 [Multi-domain]  Cd Length: 131  Bit Score: 120.35  E-value: 5.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738842    3 NTQLSDATHIMAYIALHTDDQ-LKSEHIASSLNTDPTMVRRMMSKLRKAGLLTSVRGV-ARPTLACSPNDITLKDIYVAV 80
Cdd:pfam02082   2 STKTDYALHALLYLALHPGGEpVTSEEIAERQNISPVYLEKILAKLRKAGLVESVRGAgGGYRLARPPEEITLLDVVRAV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489738842   81 VAKRNFLnvdHNTSETCPVGSVIPRVMEKYYCDIQNSAEARMSRVTLQDIIDD 133
Cdd:pfam02082  82 EGPLALF---ECNNPKCPCGIEIQCALREAWEEAQDAMEDVLDSVTLADLVAD 131
IscR COG1959
DNA-binding transcriptional regulator, IscR family [Transcription];
3-141 1.00e-25

DNA-binding transcriptional regulator, IscR family [Transcription];


Pssm-ID: 441562  Cd Length: 141  Bit Score: 94.52  E-value: 1.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738842   3 NTQLSDATHIMAYIALHTDDQ-LKSEHIASSLNTDPTMVRRMMSKLRKAGLLTSVRGVA---RptLACSPNDITLKDIYV 78
Cdd:COG1959    3 STKTDYALRALLYLALHPGGEpVTSKEIAERQGISPSYLEKILQKLRKAGLVESVRGPGggyR--LARPPEEITLGDVVR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489738842  79 AVVAKRnFLNVDHNTSETCPVGSviPRVMEKYYCDIQNSAEARMSRVTLQDIIDDISAVQQQA 141
Cdd:COG1959   81 AVEGPL-ALVECVSGPPDCPVEE--ACALHGVWEEAEDAILEVLDSVTLADLVEDAEAREVAE 140
rrf2_super TIGR00738
Rrf2 family protein; This model represents a superfamily of probable transcriptional ...
 9-132 3.01e-12

Rrf2 family protein; This model represents a superfamily of probable transcriptional regulators. One member, RRF2 of Desulfovibrio vulgaris is an apparent regulatory protein experimentally (MEDLINE:97293189). The N-terminal region appears related to the DNA-binding biotin repressor region of the BirA bifunctional according to results after three rounds of PSI-BLAST with a fairly high stringency. [Unknown function, General]


Pssm-ID: 273242  Cd Length: 132  Bit Score: 59.57  E-value: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489738842    9 ATHIMAYIALHTDDQ-LKSEHIASSLNTDPTMVRRMMSKLRKAGLLTSVRGvarP----TLACSPNDITLKDIYVAV--- 80
Cdd:TIGR00738  10 ALRALLDLALNPDEGpVSVKEIAERQGISRSYLEKILRTLRKAGLVESVRG---PgggyRLARPPEEITVGDVVRAVegs 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489738842   81 --VAKRNFLNVDHNTSETCPVGSViprvmekyYCDIQNSAEARMSRVTLQDIID 132
Cdd:TIGR00738  87 laPVQCIGLNGCHPGEEVCLLHAV--------WRELEDAIEDFLREITLADLVK 132
HrcA_DNA-bdg pfam03444
Winged helix-turn-helix transcription repressor, HrcA DNA-binding; This domain is always found ...
 25-64 2.88e-04

Winged helix-turn-helix transcription repressor, HrcA DNA-binding; This domain is always found with a pair of CBS domains pfam00571.


Pssm-ID: 281443 [Multi-domain]  Cd Length: 79  Bit Score: 37.31  E-value: 2.88e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 489738842   25 KSEHIASSLNTDPTMVRRMMSKLRKAGLLTSV---RGVARPTL 64
Cdd:pfam03444  25 KGEEIADIIGRNPGTVRNQMQSLKALGLVEGVpgpKGGYKPTS 67
 
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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