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Conserved domains on  [gi|493447272|ref|WP_006402610|]
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MULTISPECIES: ribonuclease E activity regulator RraA [Burkholderia]

Protein Classification

RraA family protein( domain architecture ID 10013207)

RraA family protein such as regulator of ribonuclease activity A (RraA), which globally modulates RNA abundance by binding to RNase E and regulating its endonucleolytic activity, and 4-hydroxy-4-methyl-2-oxoglutarate (HMG) aldolase, which catalyzes the aldol cleavage of HMG into 2 molecules of pyruvate

Gene Ontology:  GO:0008428|GO:0019899

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09372 PRK09372
ribonuclease E inhibitor RraA;
1-164 2.36e-93

ribonuclease E inhibitor RraA;


:

Pssm-ID: 236487  Cd Length: 159  Bit Score: 267.39  E-value: 2.36e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272   1 MTFATTDLCDAHEDklaagTLRVLQPALRPYGGAARFAGPAATLKVFEDNTLVRAALEQDGGGRVLVVDGGASLRCALVG 80
Cdd:PRK09372   1 MEYDTSDLCDIYPD-----DVRVVEPLFSSFGGRSSFGGPITTVKCFEDNGLVKELLEEPGEGRVLVVDGGGSLRRALVG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272  81 GNLGALAEKNGWAGIVVHGCVRDAAELRECKVGVLALATHPRKSDKRGAGERDVPVTVLGTRIAPGEWIYADDDGVLVSA 160
Cdd:PRK09372  76 DNLAELAVDNGWEGIVVYGCVRDVDELAELDIGIQALAAIPVKSDKEGIGERDVPVNFGGVTFFPGDYLYADNDGIIVSP 155


                 ....
gi 493447272 161 TSLT 164
Cdd:PRK09372 156 EPLD 159
 
Name Accession Description Interval E-value
PRK09372 PRK09372
ribonuclease E inhibitor RraA;
1-164 2.36e-93

ribonuclease E inhibitor RraA;


Pssm-ID: 236487  Cd Length: 159  Bit Score: 267.39  E-value: 2.36e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272   1 MTFATTDLCDAHEDklaagTLRVLQPALRPYGGAARFAGPAATLKVFEDNTLVRAALEQDGGGRVLVVDGGASLRCALVG 80
Cdd:PRK09372   1 MEYDTSDLCDIYPD-----DVRVVEPLFSSFGGRSSFGGPITTVKCFEDNGLVKELLEEPGEGRVLVVDGGGSLRRALVG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272  81 GNLGALAEKNGWAGIVVHGCVRDAAELRECKVGVLALATHPRKSDKRGAGERDVPVTVLGTRIAPGEWIYADDDGVLVSA 160
Cdd:PRK09372  76 DNLAELAVDNGWEGIVVYGCVRDVDELAELDIGIQALAAIPVKSDKEGIGERDVPVNFGGVTFFPGDYLYADNDGIIVSP 155


                 ....
gi 493447272 161 TSLT 164
Cdd:PRK09372 156 EPLD 159
NOT-MenG TIGR01935
RraA famliy; The E. coli member of this family has been characterized as a regulator of RNase ...
 5-159 4.27e-81

RraA famliy; The E. coli member of this family has been characterized as a regulator of RNase E and its crystal structure has been analyzed. This model was initially classified as a "hypothetical equivalog" expressing the tentative hypothesis that all members might have the same function as the E. coli enzyme. Considering the second clade of enterobacterial sequences within this family, that appears to be less tenable. The function of these sequences outside of the narrow RraA equivalog model (TIGR02998) remains obscure. All of these were initially annotated as MenG, AKA S-adenosylmethionine: 2-demethylmenaquinone methyltransferase (EC 2.1.-.-). See the references characterizing this as a case of transitive annotation error in the case of the E. coli protein. [Unknown function, General]


Pssm-ID: 130990  Cd Length: 150  Bit Score: 236.46  E-value: 4.27e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272    5 TTDLCDAHEDKLaagtlRVLQPALRPYGGAARFAGPAATLKVFEDNTLVRAALEQDGGGRVLVVDGGASLRCALVGGNLG 84
Cdd:TIGR01935   1 TPDLCDAYPDKV-----RVLEPMFRNFGGRAAFAGPIVTVKCFEDNSLVREVLEQPGAGRVLVVDGGGSLRCALLGDNLA 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493447272   85 ALAEKNGWAGIVVHGCVRDAAELRECKVGVLALATHPRKSDKRGAGERDVPVTVLGTRIAPGEWIYADDDGVLVS 159
Cdd:TIGR01935  76 VLAEENGWEGVIVNGCVRDVAELAGMDLGVKALAAHPRKTEKRGAGEVDVPVTFAGVTFVPGDYLYADEDGILVS 150
RraA_family cd16841
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator ...
 6-159 3.15e-60

ribonuclease activity regulator RraA family; RraA protein family is named after the regulator of ribonuclease activity A (RraA), a protein that binds to RNase E and inhibits RNase E endonucleolytic cleavages. Members also include proteins with other functions, like a 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate (HMG/CHA) aldolase from Pseudomonas putida, which catalyzes the last step of the bacterial protocatechuate 4,5-cleavage pathway and the uncharacterized YER010Cp protein from yeast, an organism lacking RNAse E.


Pssm-ID: 319245 [Multi-domain]  Cd Length: 150  Bit Score: 183.43  E-value: 3.15e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272   6 TDLCDAHEDKLAagtlrVLQPALRPYGGAARFAGPAATLKVFE-DNTLVRAALEQDGGGRVLVVDGGASLRCALVGGNLG 84
Cdd:cd16841    1 ADLSDALDRLGG-----VLPGIIRPLGGGARFVGPAVTVKCFPdDNLLVREALDEAGPGDVLVVDGGGSLRCALWGDLLA 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493447272  85 ALAEKNGWAGIVVHGCVRDAAELRECKVGVLALATHPRKSDKRGAGERDVPVTVLGTRIAPGEWIYADDDGVLVS 159
Cdd:cd16841   76 TLAKARGWAGIVIDGAVRDVDEIRELDFPVFARGTTPRGSKKVGPGEVNVPVTIGGVTVNPGDIIVADEDGVVVI 150
RraA-like pfam03737
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
 6-157 7.21e-51

Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) and 4-hydroxy-4-methyl-2-oxoglutarate (HMG)/4-carboxy- 4-hydroxy-2-oxoadipate (CHA) aldolase, also known as RraA-like protein. RraA acts as a trans-acting modulator of RNA turnover, binding essential endonuclease RNase E and inhibiting RNA processing. RraA-like proteins seem to contain aldolase and/or decarboxylase activity either in place of or in addition to the RNase E inhibitor functions.


Pssm-ID: 427475 [Multi-domain]  Cd Length: 148  Bit Score: 159.60  E-value: 7.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272    6 TDLCDAHEDKlaaGTLRVLQPALRPYGGAArFAGPAATLKVF-EDNTLVRAALEQDGGGRVLVVDGGASLRCALvGGNLG 84
Cdd:pfam03737   1 ADLSDALGSY---GGRLGAMPGIRPLNPGP-FVGPAVTVKCFpEDNLLVHEALDEAGPGDVLVVDGGGGSRAAL-GDLLA 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493447272   85 ALAEKNGWAGIVVHGCVRDAAELRECKVGVLALATHPRKSDKRGAGERDVPVTVLGTRIAPGEWIYADDDGVL 157
Cdd:pfam03737  76 TLAKANGWAGIVIDGAVRDVDELRELDFPVFARGTTPRGSVKRGPGEVNVPVTIGGVTVRPGDIIVADEDGVV 148
RraA COG0684
RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal ...
 3-158 3.24e-38

RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 129.13  E-value: 3.24e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272   3 FATTDLCDAHEDKLAagtlRVLQPALRPYGGAARFAGPAATLKVFE-DNTLVRAALEQDGGGRVLVVDGGASLRCALVGG 81
Cdd:COG0684   14 VSTATVSDALDRLLR----GALDPGIRPLHPGARLVGPAVTVRYRPgDNLMLHEAIDLAPPGDVLVIDAGGDTDAALWGE 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493447272  82 NLGALAEKNGWAGIVVHGCVRDAAELRECKVGVLALATHPRKSDKR-GAGERDVPVTVLGTRIAPGEWIYADDDGVLV 158
Cdd:COG0684   90 LLATAAKARGVAGVVIDGAVRDVAEIRELGFPVFARGVTPRGTKKRvGPGEINVPVSIGGVTVRPGDLVVADDDGVVV 167
 
Name Accession Description Interval E-value
PRK09372 PRK09372
ribonuclease E inhibitor RraA;
1-164 2.36e-93

ribonuclease E inhibitor RraA;


Pssm-ID: 236487  Cd Length: 159  Bit Score: 267.39  E-value: 2.36e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272   1 MTFATTDLCDAHEDklaagTLRVLQPALRPYGGAARFAGPAATLKVFEDNTLVRAALEQDGGGRVLVVDGGASLRCALVG 80
Cdd:PRK09372   1 MEYDTSDLCDIYPD-----DVRVVEPLFSSFGGRSSFGGPITTVKCFEDNGLVKELLEEPGEGRVLVVDGGGSLRRALVG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272  81 GNLGALAEKNGWAGIVVHGCVRDAAELRECKVGVLALATHPRKSDKRGAGERDVPVTVLGTRIAPGEWIYADDDGVLVSA 160
Cdd:PRK09372  76 DNLAELAVDNGWEGIVVYGCVRDVDELAELDIGIQALAAIPVKSDKEGIGERDVPVNFGGVTFFPGDYLYADNDGIIVSP 155


                 ....
gi 493447272 161 TSLT 164
Cdd:PRK09372 156 EPLD 159
NOT-MenG TIGR01935
RraA famliy; The E. coli member of this family has been characterized as a regulator of RNase ...
 5-159 4.27e-81

RraA famliy; The E. coli member of this family has been characterized as a regulator of RNase E and its crystal structure has been analyzed. This model was initially classified as a "hypothetical equivalog" expressing the tentative hypothesis that all members might have the same function as the E. coli enzyme. Considering the second clade of enterobacterial sequences within this family, that appears to be less tenable. The function of these sequences outside of the narrow RraA equivalog model (TIGR02998) remains obscure. All of these were initially annotated as MenG, AKA S-adenosylmethionine: 2-demethylmenaquinone methyltransferase (EC 2.1.-.-). See the references characterizing this as a case of transitive annotation error in the case of the E. coli protein. [Unknown function, General]


Pssm-ID: 130990  Cd Length: 150  Bit Score: 236.46  E-value: 4.27e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272    5 TTDLCDAHEDKLaagtlRVLQPALRPYGGAARFAGPAATLKVFEDNTLVRAALEQDGGGRVLVVDGGASLRCALVGGNLG 84
Cdd:TIGR01935   1 TPDLCDAYPDKV-----RVLEPMFRNFGGRAAFAGPIVTVKCFEDNSLVREVLEQPGAGRVLVVDGGGSLRCALLGDNLA 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493447272   85 ALAEKNGWAGIVVHGCVRDAAELRECKVGVLALATHPRKSDKRGAGERDVPVTVLGTRIAPGEWIYADDDGVLVS 159
Cdd:TIGR01935  76 VLAEENGWEGVIVNGCVRDVAELAGMDLGVKALAAHPRKTEKRGAGEVDVPVTFAGVTFVPGDYLYADEDGILVS 150
RraA_family cd16841
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator ...
 6-159 3.15e-60

ribonuclease activity regulator RraA family; RraA protein family is named after the regulator of ribonuclease activity A (RraA), a protein that binds to RNase E and inhibits RNase E endonucleolytic cleavages. Members also include proteins with other functions, like a 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate (HMG/CHA) aldolase from Pseudomonas putida, which catalyzes the last step of the bacterial protocatechuate 4,5-cleavage pathway and the uncharacterized YER010Cp protein from yeast, an organism lacking RNAse E.


Pssm-ID: 319245 [Multi-domain]  Cd Length: 150  Bit Score: 183.43  E-value: 3.15e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272   6 TDLCDAHEDKLAagtlrVLQPALRPYGGAARFAGPAATLKVFE-DNTLVRAALEQDGGGRVLVVDGGASLRCALVGGNLG 84
Cdd:cd16841    1 ADLSDALDRLGG-----VLPGIIRPLGGGARFVGPAVTVKCFPdDNLLVREALDEAGPGDVLVVDGGGSLRCALWGDLLA 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493447272  85 ALAEKNGWAGIVVHGCVRDAAELRECKVGVLALATHPRKSDKRGAGERDVPVTVLGTRIAPGEWIYADDDGVLVS 159
Cdd:cd16841   76 TLAKARGWAGIVIDGAVRDVDEIRELDFPVFARGTTPRGSKKVGPGEVNVPVTIGGVTVNPGDIIVADEDGVVVI 150
PRK12487 PRK12487
putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase;
1-163 3.67e-60

putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase;


Pssm-ID: 183553  Cd Length: 163  Bit Score: 183.62  E-value: 3.67e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272   1 MTFATTDLCDAHEDKLaagtlRVLQPALRPYGGAARFAGPAATLKVFEDNTLVRAALEQDGGGRVLVVDGGASLRCALVG 80
Cdd:PRK12487   1 MLDLLPDLFDHYEDKL-----TLLNLPFKNFGGKRIFWGEIVTVRCFEDNSKVKEVLAQDGKGKVLVVDGGGSCRRALLG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272  81 GNLGALAEKNGWAGIVVHGCVRDAAELRECKVGVLALATHPRKSDKRGAGERDVPVTVLGTRIAPGEWIYADDDGVLVSA 160
Cdd:PRK12487  76 DQIAQSALDNGWEGIVINGCVRDVGALSTMDLGVKALGASPIKTEKRGQGEVNVTLTMGNVIIEPGDMLYADENGIAVSK 155


                 ...
gi 493447272 161 TSL 163
Cdd:PRK12487 156 EAL 158
RraA-like pfam03737
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
 6-157 7.21e-51

Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) and 4-hydroxy-4-methyl-2-oxoglutarate (HMG)/4-carboxy- 4-hydroxy-2-oxoadipate (CHA) aldolase, also known as RraA-like protein. RraA acts as a trans-acting modulator of RNA turnover, binding essential endonuclease RNase E and inhibiting RNA processing. RraA-like proteins seem to contain aldolase and/or decarboxylase activity either in place of or in addition to the RNase E inhibitor functions.


Pssm-ID: 427475 [Multi-domain]  Cd Length: 148  Bit Score: 159.60  E-value: 7.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272    6 TDLCDAHEDKlaaGTLRVLQPALRPYGGAArFAGPAATLKVF-EDNTLVRAALEQDGGGRVLVVDGGASLRCALvGGNLG 84
Cdd:pfam03737   1 ADLSDALGSY---GGRLGAMPGIRPLNPGP-FVGPAVTVKCFpEDNLLVHEALDEAGPGDVLVVDGGGGSRAAL-GDLLA 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493447272   85 ALAEKNGWAGIVVHGCVRDAAELRECKVGVLALATHPRKSDKRGAGERDVPVTVLGTRIAPGEWIYADDDGVL 157
Cdd:pfam03737  76 TLAKANGWAGIVIDGAVRDVDELRELDFPVFARGTTPRGSVKRGPGEVNVPVTIGGVTVRPGDIIVADEDGVV 148
RraA_entero TIGR02998
regulator of ribonuclease activity A; This family includes a number of closely related ...
 1-163 2.18e-43

regulator of ribonuclease activity A; This family includes a number of closely related sequences from certain enterobacteria. The E. coli member of this family has been characterized as a regulator of RNase E and its crystal structure has been analyzed. The broader subfamily which includes this equivalog, TIGR01935, was initially classified as a "hypothetical equivalog" with the name "regulator of ribonuclease activity A" based on the same evidence for this model. It now appears that, considering the second group of enterobacterial sequences within TIGR01935, the functional assignment is unsupported. THIS PROTEIN IS _NOT_ MenG, AKA S-adenosylmethionine: 2-demethylmenaquinone methyltransferase (EC 2.1.-.-). See the references characterizing this as a case of transitive annotation error. [Transcription, Degradation of RNA, Regulatory functions, Protein interactions]


Pssm-ID: 132043  Cd Length: 161  Bit Score: 141.10  E-value: 2.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272    1 MTFATTDLCDAHEDKLaagtlRVLQPALRPYGGAARFAGPAATLKVFEDNTLVRAALEQDGGGRVLVVDGGASLRCALVG 80
Cdd:TIGR02998   1 MQYDTSELCDFYADLV-----DVVEPIFSNFGGRSSFGGKVVTVKCFEHNGLINELLEQNGTGRVLVIDGGGSTRRALID 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272   81 GNLGALAEKNGWAGIVVHGCVRDAAELRECKVGVLALATHPRKSDKRGAGERDVPVTVLGTRIAPGEWIYADDDGVLVSA 160
Cdd:TIGR02998  76 AELAQLAANNGWEGIVVYGAVRQVDALEELDIGIQALAAIPVGADEQGIGESDIAVNFAGVTFFPDDYIYADNTGIILSP 155


                  ...
gi 493447272  161 TSL 163
Cdd:TIGR02998 156 EPL 158
RraA COG0684
RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal ...
 3-158 3.24e-38

RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 129.13  E-value: 3.24e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272   3 FATTDLCDAHEDKLAagtlRVLQPALRPYGGAARFAGPAATLKVFE-DNTLVRAALEQDGGGRVLVVDGGASLRCALVGG 81
Cdd:COG0684   14 VSTATVSDALDRLLR----GALDPGIRPLHPGARLVGPAVTVRYRPgDNLMLHEAIDLAPPGDVLVIDAGGDTDAALWGE 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493447272  82 NLGALAEKNGWAGIVVHGCVRDAAELRECKVGVLALATHPRKSDKR-GAGERDVPVTVLGTRIAPGEWIYADDDGVLV 158
Cdd:COG0684   90 LLATAAKARGVAGVVIDGAVRDVAEIRELGFPVFARGVTPRGTKKRvGPGEINVPVSIGGVTVRPGDLVVADDDGVVV 167
PRK06201 PRK06201
hypothetical protein; Validated
 26-158 3.34e-29

hypothetical protein; Validated


Pssm-ID: 180465 [Multi-domain]  Cd Length: 221  Bit Score: 106.57  E-value: 3.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272  26 PALRPYGGAARFAGPAATLKVFE-DNTLVRAALEQDGGGRVLVVDGGASLRCALVGGNLGALAEKNGWAGIVVHGCVRDA 104
Cdd:PRK06201  42 AGLRPMHRGGRLAGTALTVRTRPgDNLMIHRALDLARPGDVIVVDGGGDLTNALVGEIMLAIAARRGVAGVVIDGAVRDV 121

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493447272 105 AELRECKVGVLALATHPRKSDKRGAGERDVPVTVLGTRIAPGEWIYADDDGVLV 158
Cdd:PRK06201 122 AALREMGFPVFARGVTHRGPYKDGPGEINVPVAIGGMVIEPGDLIVGDDDGLVA 175
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 28-158 1.45e-13

bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 66.97  E-value: 1.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272  28 LRPYGGAARFAGPAATLKVFE-DNTLVRAALEQDGGGRVLVVDGGASLrcALVGGNLGALAEKN-GWAGIVVHGCVRDAA 105
Cdd:PRK07028 254 IKPLVRGTKMVGKAVTVQTFAgDWAKPVEAIDVAKPGDVIVIYNSSKD--IAPWGELATLSCLNkGIAGVVIDGAVRDVD 331

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493447272 106 ELRECKVGVLALATHPRKSDKRGAGERDVPVTVLGTRIAPGEWIYADDDGVLV 158
Cdd:PRK07028 332 EIRKLGFPVFARAIVPNAGEPKGFGEINAEIVCGGQTVRPGDWIIGDENGVVV 384
PRK09262 PRK09262
hypothetical protein; Provisional
 12-158 8.27e-13

hypothetical protein; Provisional


Pssm-ID: 181735  Cd Length: 225  Bit Score: 63.41  E-value: 8.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272  12 HEdklAAGTLRVLQPALRPYGGAARFAGPAATLKVFE-DNTLVRAALEQDGGGRVLVVDGGASLRCALVGGNLGALAEKN 90
Cdd:PRK09262  29 HE---AQGRVGLLKPYMRPIYQGARIAGTAVTVLVQPgDNWMMHVAVEQCQPGDVLVVAPTSPCTDGFFGDLLATSLQAR 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493447272  91 GWAGIVVHGCVRDAAELRECKVGVLALATHPRKSDKRGAGERDVPVTVLGTRIAPGEWIYADDDGVLV 158
Cdd:PRK09262 106 GVRGLVIDAGVRDVRTLTEMGFPVWSRAISAQGTVKATLGSVNVPVVCAGALVNPGDVVVADDDGVVV 173
PRK08245 PRK08245
hypothetical protein; Validated
 28-158 4.56e-11

hypothetical protein; Validated


Pssm-ID: 236200  Cd Length: 240  Bit Score: 59.14  E-value: 4.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272  28 LRPygGAARFAGPAATLK------------VFED-NTLVRAALEQDGGGRVLVVDGGASLRCALVGGNLGALAEKNGWAG 94
Cdd:PRK08245  42 LRP--GGPRMVGPAFTLRfvparedlntpeSFADpESPQRAAIETCPPGCVLVVDARGDARAGSFGDILCTRLKKRGVAG 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493447272  95 IVVHGCVRDAAELRECKVGV-LALATHPRKSDKRGAGERDVPVTVLGTRIAPGEWIYADDDGVLV 158
Cdd:PRK08245 120 LVTDGGVRDSPGIAALGLPVwCAGPSAPTNLTGLTAVDINVPIGCGGVAVFPGDIIVADDDGVVV 184
PRK12764 PRK12764
fumarylacetoacetate hydrolase family protein;
56-158 5.65e-08

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 237193 [Multi-domain]  Cd Length: 500  Bit Score: 50.91  E-value: 5.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493447272  56 ALEQDGGGRVLVVDGGASLRCALVGGNLGALAEKNGWAGIVVHGCVRDAAELRECKVGVLALATHPRKSDKRGAG-ERDV 134
Cdd:PRK12764 339 AFDSVNPGEVLVIEARGEKGTGTLGDILALRAQVRGAAGVVTDGGVRDYAAVAELGLPVFFAGPHPAVLGRRHVPwDVDI 418

                         90       100
                 ....*....|....*....|....
gi 493447272 135 PVTVLGTRIAPGEWIYADDDGVLV 158
Cdd:PRK12764 419 TVACGGATVQPGDVIVGDDDGVVV 442
 
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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