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Conserved domains on  [gi|15596969|ref|NP_250463|]
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ribonuclease activity regulator protein RraA [Pseudomonas aeruginosa PAO1]

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;
1-159 7.43e-112

ribonuclease E inhibitor RraA;


:

Pssm-ID: 236487  Cd Length: 159  Bit Score: 314.38  E-value: 7.43e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969    1 MHYVTPDLCDAYPELVQVVEPMFSNFGGRDSFGGEIVTIKCFEDNSLVKEQVDKDGKGKVLVVDGGGSLRRALLGDMLAE 80
Cdd:PRK09372   1 MEYDTSDLCDIYPDDVRVVEPLFSSFGGRSSFGGPITTVKCFEDNGLVKELLEEPGEGRVLVVDGGGSLRRALVGDNLAE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596969   81 KAAKNGWEGIVVYGCIRDVDVIAQTDLGVQALASHPLKTDKRGIGDLNVAVTFGGVTFRPGEFVYADNNGIIVSPQALK 159
Cdd:PRK09372  81 LAVDNGWEGIVVYGCVRDVDELAELDIGIQALAAIPVKSDKEGIGERDVPVNFGGVTFFPGDYLYADNDGIIVSPEPLD 159
 
Name Accession Description Interval E-value
PRK09372 PRK09372
ribonuclease E inhibitor RraA;
1-159 7.43e-112

ribonuclease E inhibitor RraA;


Pssm-ID: 236487  Cd Length: 159  Bit Score: 314.38  E-value: 7.43e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969    1 MHYVTPDLCDAYPELVQVVEPMFSNFGGRDSFGGEIVTIKCFEDNSLVKEQVDKDGKGKVLVVDGGGSLRRALLGDMLAE 80
Cdd:PRK09372   1 MEYDTSDLCDIYPDDVRVVEPLFSSFGGRSSFGGPITTVKCFEDNGLVKELLEEPGEGRVLVVDGGGSLRRALVGDNLAE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596969   81 KAAKNGWEGIVVYGCIRDVDVIAQTDLGVQALASHPLKTDKRGIGDLNVAVTFGGVTFRPGEFVYADNNGIIVSPQALK 159
Cdd:PRK09372  81 LAVDNGWEGIVVYGCVRDVDELAELDIGIQALAAIPVKSDKEGIGERDVPVNFGGVTFFPGDYLYADNDGIIVSPEPLD 159
NOT-MenG TIGR01935
RraA famliy; The E. coli member of this family has been characterized as a regulator of RNase ...
 5-154 1.91e-92

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: 264.96  E-value: 1.91e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969     5 TPDLCDAYPELVQVVEPMFSNFGGRDSFGGEIVTIKCFEDNSLVKEQVDKDGKGKVLVVDGGGSLRRALLGDMLAEKAAK 84
Cdd:TIGR01935   1 TPDLCDAYPDKVRVLEPMFRNFGGRAAFAGPIVTVKCFEDNSLVREVLEQPGAGRVLVVDGGGSLRCALLGDNLAVLAEE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969    85 NGWEGIVVYGCIRDVDVIAQTDLGVQALASHPLKTDKRGIGDLNVAVTFGGVTFRPGEFVYADNNGIIVS 154
Cdd:TIGR01935  81 NGWEGVIVNGCVRDVAELAGMDLGVKALAAHPRKTEKRGAGEVDVPVTFAGVTFVPGDYLYADEDGILVS 150
RraA_family cd16841
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator ...
 6-154 1.56e-62

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: 189.21  E-value: 1.56e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969   6 PDLCDAYPELVQVVEPMFSNFGGRDSFGGEIVTIKCFEDNS-LVKEQVDKDGKGKVLVVDGGGSLRRALLGDMLAEKAAK 84
Cdd:cd16841   1 ADLSDALDRLGGVLPGIIRPLGGGARFVGPAVTVKCFPDDNlLVREALDEAGPGDVLVVDGGGSLRCALWGDLLATLAKA 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969  85 NGWEGIVVYGCIRDVDVIAQTDLGVQALASHPLKTDKRGIGDLNVAVTFGGVTFRPGEFVYADNNGIIVS 154
Cdd:cd16841  81 RGWAGIVIDGAVRDVDEIRELDFPVFARGTTPRGSKKVGPGEVNVPVTIGGVTVNPGDIIVADEDGVVVI 150
RraA-like pfam03737
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
 6-152 3.54e-52

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: 162.68  E-value: 3.54e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969     6 PDLCDAypelvqvvepmFSNFGGRDS------------FGGEIVTIKCF-EDNSLVKEQVDKDGKGKVLVVDGGGsLRRA 72
Cdd:pfam03737   1 ADLSDA-----------LGSYGGRLGampgirplnpgpFVGPAVTVKCFpEDNLLVHEALDEAGPGDVLVVDGGG-GSRA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969    73 LLGDMLAEKAAKNGWEGIVVYGCIRDVDVIAQTDLGVQALASHPLKTDKRGIGDLNVAVTFGGVTFRPGEFVYADNNGII 152
Cdd:pfam03737  69 ALGDLLATLAKANGWAGIVIDGAVRDVDELRELDFPVFARGTTPRGSVKRGPGEVNVPVTIGGVTVRPGDIIVADEDGVV 148
RraA COG0684
RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal ...
 5-158 4.33e-37

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


Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 126.44  E-value: 4.33e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969   5 TPDLCDAYPEL-VQVVEPMFSNFGGRDSFGGEIVTIKCFE-DNSLVKEQVDKDGKGKVLVVDGGGSLRRALLGDMLAEKA 82
Cdd:COG0684  16 TATVSDALDRLlRGALDPGIRPLHPGARLVGPAVTVRYRPgDNLMLHEAIDLAPPGDVLVIDAGGDTDAALWGELLATAA 95

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596969  83 AKNGWEGIVVYGCIRDVDVIAQTDLGVQALASHPLKTDKR-GIGDLNVAVTFGGVTFRPGEFVYADNNGIIVSPQAL 158
Cdd:COG0684  96 KARGVAGVVIDGAVRDVAEIRELGFPVFARGVTPRGTKKRvGPGEINVPVSIGGVTVRPGDLVVADDDGVVVIPAEL 172
 
Name Accession Description Interval E-value
PRK09372 PRK09372
ribonuclease E inhibitor RraA;
1-159 7.43e-112

ribonuclease E inhibitor RraA;


Pssm-ID: 236487  Cd Length: 159  Bit Score: 314.38  E-value: 7.43e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969    1 MHYVTPDLCDAYPELVQVVEPMFSNFGGRDSFGGEIVTIKCFEDNSLVKEQVDKDGKGKVLVVDGGGSLRRALLGDMLAE 80
Cdd:PRK09372   1 MEYDTSDLCDIYPDDVRVVEPLFSSFGGRSSFGGPITTVKCFEDNGLVKELLEEPGEGRVLVVDGGGSLRRALVGDNLAE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596969   81 KAAKNGWEGIVVYGCIRDVDVIAQTDLGVQALASHPLKTDKRGIGDLNVAVTFGGVTFRPGEFVYADNNGIIVSPQALK 159
Cdd:PRK09372  81 LAVDNGWEGIVVYGCVRDVDELAELDIGIQALAAIPVKSDKEGIGERDVPVNFGGVTFFPGDYLYADNDGIIVSPEPLD 159
NOT-MenG TIGR01935
RraA famliy; The E. coli member of this family has been characterized as a regulator of RNase ...
 5-154 1.91e-92

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: 264.96  E-value: 1.91e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969     5 TPDLCDAYPELVQVVEPMFSNFGGRDSFGGEIVTIKCFEDNSLVKEQVDKDGKGKVLVVDGGGSLRRALLGDMLAEKAAK 84
Cdd:TIGR01935   1 TPDLCDAYPDKVRVLEPMFRNFGGRAAFAGPIVTVKCFEDNSLVREVLEQPGAGRVLVVDGGGSLRCALLGDNLAVLAEE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969    85 NGWEGIVVYGCIRDVDVIAQTDLGVQALASHPLKTDKRGIGDLNVAVTFGGVTFRPGEFVYADNNGIIVS 154
Cdd:TIGR01935  81 NGWEGVIVNGCVRDVAELAGMDLGVKALAAHPRKTEKRGAGEVDVPVTFAGVTFVPGDYLYADEDGILVS 150
PRK12487 PRK12487
putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase;
1-158 1.55e-83

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


Pssm-ID: 183553  Cd Length: 163  Bit Score: 242.94  E-value: 1.55e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969    1 MHYVTPDLCDAYPELVQVVEPMFSNFGGRDSFGGEIVTIKCFEDNSLVKEQVDKDGKGKVLVVDGGGSLRRALLGDMLAE 80
Cdd:PRK12487   1 MLDLLPDLFDHYEDKLTLLNLPFKNFGGKRIFWGEIVTVRCFEDNSKVKEVLAQDGKGKVLVVDGGGSCRRALLGDQIAQ 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596969   81 KAAKNGWEGIVVYGCIRDVDVIAQTDLGVQALASHPLKTDKRGIGDLNVAVTFGGVTFRPGEFVYADNNGIIVSPQAL 158
Cdd:PRK12487  81 SALDNGWEGIVINGCVRDVGALSTMDLGVKALGASPIKTEKRGQGEVNVTLTMGNVIIEPGDMLYADENGIAVSKEAL 158
RraA_entero TIGR02998
regulator of ribonuclease activity A; This family includes a number of closely related ...
 1-160 3.17e-71

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: 211.59  E-value: 3.17e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969     1 MHYVTPDLCDAYPELVQVVEPMFSNFGGRDSFGGEIVTIKCFEDNSLVKEQVDKDGKGKVLVVDGGGSLRRALLGDMLAE 80
Cdd:TIGR02998   1 MQYDTSELCDFYADLVDVVEPIFSNFGGRSSFGGKVVTVKCFEHNGLINELLEQNGTGRVLVIDGGGSTRRALIDAELAQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969    81 KAAKNGWEGIVVYGCIRDVDVIAQTDLGVQALASHPLKTDKRGIGDLNVAVTFGGVTFRPGEFVYADNNGIIVSPQALKM 160
Cdd:TIGR02998  81 LAANNGWEGIVVYGAVRQVDALEELDIGIQALAAIPVGADEQGIGESDIAVNFAGVTFFPDDYIYADNTGIILSPEPLEI 160
RraA_family cd16841
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator ...
 6-154 1.56e-62

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: 189.21  E-value: 1.56e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969   6 PDLCDAYPELVQVVEPMFSNFGGRDSFGGEIVTIKCFEDNS-LVKEQVDKDGKGKVLVVDGGGSLRRALLGDMLAEKAAK 84
Cdd:cd16841   1 ADLSDALDRLGGVLPGIIRPLGGGARFVGPAVTVKCFPDDNlLVREALDEAGPGDVLVVDGGGSLRCALWGDLLATLAKA 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969  85 NGWEGIVVYGCIRDVDVIAQTDLGVQALASHPLKTDKRGIGDLNVAVTFGGVTFRPGEFVYADNNGIIVS 154
Cdd:cd16841  81 RGWAGIVIDGAVRDVDEIRELDFPVFARGTTPRGSKKVGPGEVNVPVTIGGVTVNPGDIIVADEDGVVVI 150
RraA-like pfam03737
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
 6-152 3.54e-52

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: 162.68  E-value: 3.54e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969     6 PDLCDAypelvqvvepmFSNFGGRDS------------FGGEIVTIKCF-EDNSLVKEQVDKDGKGKVLVVDGGGsLRRA 72
Cdd:pfam03737   1 ADLSDA-----------LGSYGGRLGampgirplnpgpFVGPAVTVKCFpEDNLLVHEALDEAGPGDVLVVDGGG-GSRA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969    73 LLGDMLAEKAAKNGWEGIVVYGCIRDVDVIAQTDLGVQALASHPLKTDKRGIGDLNVAVTFGGVTFRPGEFVYADNNGII 152
Cdd:pfam03737  69 ALGDLLATLAKANGWAGIVIDGAVRDVDELRELDFPVFARGTTPRGSVKRGPGEVNVPVTIGGVTVRPGDIIVADEDGVV 148
RraA COG0684
RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal ...
 5-158 4.33e-37

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


Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 126.44  E-value: 4.33e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969   5 TPDLCDAYPEL-VQVVEPMFSNFGGRDSFGGEIVTIKCFE-DNSLVKEQVDKDGKGKVLVVDGGGSLRRALLGDMLAEKA 82
Cdd:COG0684  16 TATVSDALDRLlRGALDPGIRPLHPGARLVGPAVTVRYRPgDNLMLHEAIDLAPPGDVLVIDAGGDTDAALWGELLATAA 95

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596969  83 AKNGWEGIVVYGCIRDVDVIAQTDLGVQALASHPLKTDKR-GIGDLNVAVTFGGVTFRPGEFVYADNNGIIVSPQAL 158
Cdd:COG0684  96 KARGVAGVVIDGAVRDVAEIRELGFPVFARGVTPRGTKKRvGPGEINVPVSIGGVTVRPGDLVVADDDGVVVIPAEL 172
PRK06201 PRK06201
hypothetical protein; Validated
 34-158 2.07e-23

hypothetical protein; Validated


Pssm-ID: 180465 [Multi-domain]  Cd Length: 221  Bit Score: 91.55  E-value: 2.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969   34 GEIVTIKCFE-DNSLVKEQVDKDGKGKVLVVDGGGSLRRALLGDMLAEKAAKNGWEGIVVYGCIRDVDVIAQTDLGVQAL 112
Cdd:PRK06201  55 GTALTVRTRPgDNLMIHRALDLARPGDVIVVDGGGDLTNALVGEIMLAIAARRGVAGVVIDGAVRDVAALREMGFPVFAR 134

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15596969  113 ASHPLKTDKRGIGDLNVAVTFGGVTFRPGEFVYADNNGIIVSPQAL 158
Cdd:PRK06201 135 GVTHRGPYKDGPGEINVPVAIGGMVIEPGDLIVGDDDGLVAVPPAD 180
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 34-156 2.56e-17

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 77.75  E-value: 2.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969   34 GEIVTIKCFE-DNSLVKEQVDKDGKGKVLVVDGGGSlRRALLGDmLAEKAAKN-GWEGIVVYGCIRDVDVIAQTDLGVQA 111
Cdd:PRK07028 265 GKAVTVQTFAgDWAKPVEAIDVAKPGDVIVIYNSSK-DIAPWGE-LATLSCLNkGIAGVVIDGAVRDVDEIRKLGFPVFA 342

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 15596969  112 LASHPLKTDKRGIGDLNVAVTFGGVTFRPGEFVYADNNGIIVSPQ 156
Cdd:PRK07028 343 RAIVPNAGEPKGFGEINAEIVCGGQTVRPGDWIIGDENGVVVVPK 387
PRK12764 PRK12764
fumarylacetoacetate hydrolase family protein;
49-158 1.96e-15

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 237193 [Multi-domain]  Cd Length: 500  Bit Score: 72.48  E-value: 1.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969   49 KEQVDKDGKGKVLVVDGGGSLRRALLGDMLAEKAAKNGWEGIVVYGCIRDVDVIAQTDLGVQALASHPLKTDKRGIG-DL 127
Cdd:PRK12764 337 KRAFDSVNPGEVLVIEARGEKGTGTLGDILALRAQVRGAAGVVTDGGVRDYAAVAELGLPVFFAGPHPAVLGRRHVPwDV 416

                         90       100       110
                 ....*....|....*....|....*....|.
gi 15596969  128 NVAVTFGGVTFRPGEFVYADNNGIIVSPQAL 158
Cdd:PRK12764 417 DITVACGGATVQPGDVIVGDDDGVVVIPPAL 447
PRK08245 PRK08245
hypothetical protein; Validated
 58-158 2.50e-14

hypothetical protein; Validated


Pssm-ID: 236200  Cd Length: 240  Bit Score: 67.62  E-value: 2.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969   58 GKVLVVDGGGSLRRALLGDMLAEKAAKNGWEGIVVYGCIRDVDVIAQTDLGV-QALASHPLKTDKRGIGDLNVAVTFGGV 136
Cdd:PRK08245  88 GCVLVVDARGDARAGSFGDILCTRLKKRGVAGLVTDGGVRDSPGIAALGLPVwCAGPSAPTNLTGLTAVDINVPIGCGGV 167

                         90       100
                 ....*....|....*....|..
gi 15596969  137 TFRPGEFVYADNNGIIVSPQAL 158
Cdd:PRK08245 168 AVFPGDIIVADDDGVVVIPAAL 189
PRK09262 PRK09262
hypothetical protein; Provisional
 44-157 6.06e-07

hypothetical protein; Provisional


Pssm-ID: 181735  Cd Length: 225  Bit Score: 47.23  E-value: 6.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596969   44 DNSLVKEQVDKDGKGKVLVV-------DGggslrraLLGDMLAEKAAKNGWEGIVVYGCIRDVDVIAQTDLGVQALASHP 116
Cdd:PRK09262  64 DNWMMHVAVEQCQPGDVLVVaptspctDG-------FFGDLLATSLQARGVRGLVIDAGVRDVRTLTEMGFPVWSRAISA 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 15596969  117 LKTDKRGIGDLNVAVTFGGVTFRPGEFVYADNNGIIVSPQA 157
Cdd:PRK09262 137 QGTVKATLGSVNVPVVCAGALVNPGDVVVADDDGVVVVPRA 177
 
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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