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Conserved domains on  [gi|612981947|gb|EZV92280|]
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hypothetical protein U896_00109 [Staphylococcus aureus 22835]

Protein Classification

FMN-binding negative transcriptional regulator( domain architecture ID 10006642)

FMN-binding negative transcriptional regulator is involved in the negative control of sporulation and degradative enzyme production

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PaiB COG2808
Predicted FMN-binding regulatory protein PaiB [Signal transduction mechanisms];
2-196 5.08e-79

Predicted FMN-binding regulatory protein PaiB [Signal transduction mechanisms];


:

Pssm-ID: 442058  Cd Length: 200  Bit Score: 234.71  E-value: 5.08e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612981947   2 HVPKYFQVDDFKEIEKFIQSNSFGMIVTVDQGKPIATHVPLVLDK-KGDDYYISGHLAKTNPQCNTLKDNQNVLIVYQGA 80
Cdd:COG2808    1 YIPPHFRETDPEELRALIRAHPFATLVTAGDGGPLATHLPLLLDEdAGEGGVLIGHVARANPQWRALAAGGEVLVIFQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612981947  81 HSYVSSAWYE-KENVPTWNYQAVHLYGESSIL-SEEETIDDLKSLLVKYERHREDPVLWDNISEN-TKMQAKGIVGFKVK 157
Cdd:COG2808   81 HAYISPSWYPsKRVVPTWNYVAVHAYGRLEVIdDPEELRALLERLTARFEAGRPEPWSVDDAPEDyIDRLLRGIVGFEIE 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 612981947 158 IHKIEAAYKMSQNRNEKDYNNIIEKLEDESNASSVAVAE 196
Cdd:COG2808  161 ITRLEGKFKLSQNRPAADRAGVIAGLEASGDPAARALAA 199
 
Name Accession Description Interval E-value
PaiB COG2808
Predicted FMN-binding regulatory protein PaiB [Signal transduction mechanisms];
2-196 5.08e-79

Predicted FMN-binding regulatory protein PaiB [Signal transduction mechanisms];


Pssm-ID: 442058  Cd Length: 200  Bit Score: 234.71  E-value: 5.08e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612981947   2 HVPKYFQVDDFKEIEKFIQSNSFGMIVTVDQGKPIATHVPLVLDK-KGDDYYISGHLAKTNPQCNTLKDNQNVLIVYQGA 80
Cdd:COG2808    1 YIPPHFRETDPEELRALIRAHPFATLVTAGDGGPLATHLPLLLDEdAGEGGVLIGHVARANPQWRALAAGGEVLVIFQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612981947  81 HSYVSSAWYE-KENVPTWNYQAVHLYGESSIL-SEEETIDDLKSLLVKYERHREDPVLWDNISEN-TKMQAKGIVGFKVK 157
Cdd:COG2808   81 HAYISPSWYPsKRVVPTWNYVAVHAYGRLEVIdDPEELRALLERLTARFEAGRPEPWSVDDAPEDyIDRLLRGIVGFEIE 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 612981947 158 IHKIEAAYKMSQNRNEKDYNNIIEKLEDESNASSVAVAE 196
Cdd:COG2808  161 ITRLEGKFKLSQNRPAADRAGVIAGLEASGDPAARALAA 199
FMN_bind_2 pfam04299
Putative FMN-binding domain; In Bacillus subtilis, family member PAI 2/ORF-2 was found to be ...
 2-160 2.43e-59

Putative FMN-binding domain; In Bacillus subtilis, family member PAI 2/ORF-2 was found to be essential for growth. The SUPERFAMILY database finds that this domain is related to FMN-binding domains, suggesting this protein is also FMN-binding.


Pssm-ID: 461254  Cd Length: 166  Bit Score: 183.51  E-value: 2.43e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612981947    2 HVPKYFQVDDFKEIEKFIQSNSFGMIVTVDQGKPIATHVPLVLDKKGDDY-YISGHLAKTNPQCNTLKDNQNVLIVYQGA 80
Cdd:pfam04299   1 YIPPHFAEEDPEELRALIRENPFGTLVTAGAGGLQATHLPFLLDPEEGGGgVLRGHLARANPQWKALAEGEEVLVIFQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612981947   81 HSYVSSAWYEKEN----VPTWNYQAVHLYGESSILSEEETIDD-LKSLLVKYERHREDPVLWDNISEN-TKMQAKGIVGF 154
Cdd:pfam04299  81 HAYISPSWYPSKKetgvVPTWNYAAVHAYGRARIIDDPEELRAqLERLTDRFEAGRPSPWKVDDAPEDyIERLLKAIVGF 160


                  ....*.
gi 612981947  155 KVKIHK 160
Cdd:pfam04299 161 EIEITR 166
PBP1_mGluR cd06362
ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of ...
 161-192 8.12e-03

ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of the metabotropic glutamate receptors (mGluR), which are members of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into cellular responses. mGluRs bind to glutamate and function as an excitatory neurotransmitter; they are involved in learning, memory, anxiety, and the perception of pain. Eight subtypes of mGluRs have been cloned so far, and are classified into three groups according to their sequence similarities, transduction mechanisms, and pharmacological profiles. Group I is composed of mGlu1R and mGlu5R that both stimulate PLC hydrolysis. Group II includes mGlu2R and mGlu3R, which inhibit adenylyl cyclase, as do mGlu4R, mGlu6R, mGlu7R, and mGlu8R, which form group III.


Pssm-ID: 380585 [Multi-domain]  Cd Length: 460  Bit Score: 36.50  E-value: 8.12e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 612981947 161 IEAAYKMSQNRNEKDYNNIIEKLEDESNASSV 192
Cdd:cd06362  207 IAESERISQDSDEKDYDDVIQKLLQKKNARVV 238
 
Name Accession Description Interval E-value
PaiB COG2808
Predicted FMN-binding regulatory protein PaiB [Signal transduction mechanisms];
2-196 5.08e-79

Predicted FMN-binding regulatory protein PaiB [Signal transduction mechanisms];


Pssm-ID: 442058  Cd Length: 200  Bit Score: 234.71  E-value: 5.08e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612981947   2 HVPKYFQVDDFKEIEKFIQSNSFGMIVTVDQGKPIATHVPLVLDK-KGDDYYISGHLAKTNPQCNTLKDNQNVLIVYQGA 80
Cdd:COG2808    1 YIPPHFRETDPEELRALIRAHPFATLVTAGDGGPLATHLPLLLDEdAGEGGVLIGHVARANPQWRALAAGGEVLVIFQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612981947  81 HSYVSSAWYE-KENVPTWNYQAVHLYGESSIL-SEEETIDDLKSLLVKYERHREDPVLWDNISEN-TKMQAKGIVGFKVK 157
Cdd:COG2808   81 HAYISPSWYPsKRVVPTWNYVAVHAYGRLEVIdDPEELRALLERLTARFEAGRPEPWSVDDAPEDyIDRLLRGIVGFEIE 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 612981947 158 IHKIEAAYKMSQNRNEKDYNNIIEKLEDESNASSVAVAE 196
Cdd:COG2808  161 ITRLEGKFKLSQNRPAADRAGVIAGLEASGDPAARALAA 199
FMN_bind_2 pfam04299
Putative FMN-binding domain; In Bacillus subtilis, family member PAI 2/ORF-2 was found to be ...
 2-160 2.43e-59

Putative FMN-binding domain; In Bacillus subtilis, family member PAI 2/ORF-2 was found to be essential for growth. The SUPERFAMILY database finds that this domain is related to FMN-binding domains, suggesting this protein is also FMN-binding.


Pssm-ID: 461254  Cd Length: 166  Bit Score: 183.51  E-value: 2.43e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612981947    2 HVPKYFQVDDFKEIEKFIQSNSFGMIVTVDQGKPIATHVPLVLDKKGDDY-YISGHLAKTNPQCNTLKDNQNVLIVYQGA 80
Cdd:pfam04299   1 YIPPHFAEEDPEELRALIRENPFGTLVTAGAGGLQATHLPFLLDPEEGGGgVLRGHLARANPQWKALAEGEEVLVIFQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612981947   81 HSYVSSAWYEKEN----VPTWNYQAVHLYGESSILSEEETIDD-LKSLLVKYERHREDPVLWDNISEN-TKMQAKGIVGF 154
Cdd:pfam04299  81 HAYISPSWYPSKKetgvVPTWNYAAVHAYGRARIIDDPEELRAqLERLTDRFEAGRPSPWKVDDAPEDyIERLLKAIVGF 160


                  ....*.
gi 612981947  155 KVKIHK 160
Cdd:pfam04299 161 EIEITR 166
Putative_PNPOx pfam01243
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ...
 13-115 1.23e-04

Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family members were predicted to encode pyridoxamine 5'-phosphate oxidase, based on sequence similarity. However, there is no experimental data to validate the predicted activity and purified proteins, such as Swiss:Q06199 and its paralogs, do not possess this activity, nor do they bind to flavin mononucleotide (FMN). To date, the only time functional oxidase activity has been experimentally demonstrated is when the sequences contain both pfam01243 and pfam10590. Moreover, some of the family members that contain both domains have been shown to be involved in phenazine biosynthesis. While some molecular function has been experimentally validated for the proteins containing both domains, the role performed by each domain on its own is unknown.


Pssm-ID: 426149 [Multi-domain]  Cd Length: 88  Bit Score: 39.54  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612981947   13 KEIEKFIQSNSFGMIVTVD-QGKPIATHVPLVL--DKKGDDYYISGHLAKTnpqcntlkdnQNVLivyqgAHSYVSSAWY 89
Cdd:pfam01243   3 EEIREFLAEPNAVVLATVDkDGRPNVRPVGLKYgfDTVGILFATNTDSRKA----------RNLE-----ENPRVALLFG 67

                          90       100
                  ....*....|....*....|....*.
gi 612981947   90 EKEnvptwNYQAVHLYGESSILSEEE 115
Cdd:pfam01243  68 DPE-----LRRGVRIEGTAEIVTDGE 88
YzzA COG3871
General stress protein 26 (function unknown) [Function unknown];
8-134 5.36e-03

General stress protein 26 (function unknown) [Function unknown];


Pssm-ID: 443080 [Multi-domain]  Cd Length: 132  Bit Score: 35.68  E-value: 5.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612981947   8 QVDDFKEIEKFIQSNSFGMIVTVD-QGKPIATHVPLVLDKKGDDYYIS--------GHLAKtNPQCntlkdnqNVLIVYQ 78
Cdd:COG3871    4 DEELEEKLWELLEDIRTAMLATVDaDGRPHSRPMWFQVDVDDGTLWFFtsrdsakvRNIRR-DPRV-------SLSFADP 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 612981947  79 GAHSYVSsawyekenvptwnyqavhLYGESSILSEEETIDDLKSLLVK--YERHREDP 134
Cdd:COG3871   76 GDDRYVS------------------VEGTAEIVDDRAKIDELWNPLAEawFPDGPDDP 115
PBP1_mGluR cd06362
ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of ...
 161-192 8.12e-03

ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of the metabotropic glutamate receptors (mGluR), which are members of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into cellular responses. mGluRs bind to glutamate and function as an excitatory neurotransmitter; they are involved in learning, memory, anxiety, and the perception of pain. Eight subtypes of mGluRs have been cloned so far, and are classified into three groups according to their sequence similarities, transduction mechanisms, and pharmacological profiles. Group I is composed of mGlu1R and mGlu5R that both stimulate PLC hydrolysis. Group II includes mGlu2R and mGlu3R, which inhibit adenylyl cyclase, as do mGlu4R, mGlu6R, mGlu7R, and mGlu8R, which form group III.


Pssm-ID: 380585 [Multi-domain]  Cd Length: 460  Bit Score: 36.50  E-value: 8.12e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 612981947 161 IEAAYKMSQNRNEKDYNNIIEKLEDESNASSV 192
Cdd:cd06362  207 IAESERISQDSDEKDYDDVIQKLLQKKNARVV 238
 
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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