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Conserved domains on  [gi|771650330|ref|WP_045232786|]
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4-carboxy-4-hydroxy-2-oxoadipate aldolase/oxaloacetate decarboxylase [Agrobacterium rubi]

Protein Classification

RraA family protein( domain architecture ID 10002149)

RraA family protein such as Saccharomyces cerevisiae 4-hydroxy-4-methyl-2-oxoglutarate (HMG) aldolase, which catalyzes the aldol cleavage of HMG into 2 molecules of pyruvate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RraA-like super family cl00480
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
 9-221 1.09e-69

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.


The actual alignment was detected with superfamily member PRK09262:

Pssm-ID: 444930  Cd Length: 225  Bit Score: 212.48  E-value: 1.09e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330   9 ERPSKADIDALSKFSPATIHEAQGRKGALSSRLKPVDYRMKLCGPAFTVKCAPRDNIMLQLAINYAKPGDIIVVSAGEYE 88
Cdd:PRK09262  10 ERADAAVVDRLAEFGVATVHEAQGRVGLLKPYMRPIYQGARIAGTAVTVLVQPGDNWMMHVAVEQCQPGDVLVVAPTSPC 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330  89 EAGSFGDVLANACLAKGIGGLVTDTGVRDTLQLRDLGFPVFSLSVCIKGTVKETIAAVNDSIIIGGEIINPGDIIVGDAD 168
Cdd:PRK09262  90 TDGFFGDLLATSLQARGVRGLVIDAGVRDVRTLTEMGFPVWSRAISAQGTVKATLGSVNVPVVCAGALVNPGDVVVADDD 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 771650330 169 GLVVVRREDAQESARLSQIREDAEAGYIEAYKQGKSVIEVSNLEPVLKAKGLV 221
Cdd:PRK09262 170 GVVVVPRAQAAAVADAAEAREANEESKRERLAAGELGLDIYKMRERLAKKGLR 222
 
Name Accession Description Interval E-value
PRK09262 PRK09262
hypothetical protein; Provisional
 9-221 1.09e-69

hypothetical protein; Provisional


Pssm-ID: 181735  Cd Length: 225  Bit Score: 212.48  E-value: 1.09e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330   9 ERPSKADIDALSKFSPATIHEAQGRKGALSSRLKPVDYRMKLCGPAFTVKCAPRDNIMLQLAINYAKPGDIIVVSAGEYE 88
Cdd:PRK09262  10 ERADAAVVDRLAEFGVATVHEAQGRVGLLKPYMRPIYQGARIAGTAVTVLVQPGDNWMMHVAVEQCQPGDVLVVAPTSPC 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330  89 EAGSFGDVLANACLAKGIGGLVTDTGVRDTLQLRDLGFPVFSLSVCIKGTVKETIAAVNDSIIIGGEIINPGDIIVGDAD 168
Cdd:PRK09262  90 TDGFFGDLLATSLQARGVRGLVIDAGVRDVRTLTEMGFPVWSRAISAQGTVKATLGSVNVPVVCAGALVNPGDVVVADDD 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 771650330 169 GLVVVRREDAQESARLSQIREDAEAGYIEAYKQGKSVIEVSNLEPVLKAKGLV 221
Cdd:PRK09262 170 GVVVVPRAQAAAVADAAEAREANEESKRERLAAGELGLDIYKMRERLAKKGLR 222
RraA COG0684
RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal ...
 9-208 4.14e-68

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


Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 207.71  E-value: 4.14e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330   9 ERPSKADIDALSKFSPATIHEAQGRK--GALSSRLKPVDYRMKLCGPAFTVKCAPRDNIMLQLAINYAKPGDIIVVSAGE 86
Cdd:COG0684    1 PRLDAELLERLAAVSTATVSDALDRLlrGALDPGIRPLHPGARLVGPAVTVRYRPGDNLMLHEAIDLAPPGDVLVIDAGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330  87 YEEAGSFGDVLANACLAKGIGGLVTDTGVRDTLQLRDLGFPVFSLSVCIKGTVKE-TIAAVNDSIIIGGEIINPGDIIVG 165
Cdd:COG0684   81 DTDAALWGELLATAAKARGVAGVVIDGAVRDVAEIRELGFPVFARGVTPRGTKKRvGPGEINVPVSIGGVTVRPGDLVVA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 771650330 166 DADGLVVVRREDAQESARLSQIREDAEAGYIEAYKQGKSVIEV 208
Cdd:COG0684  161 DDDGVVVIPAELAEEVLEAAEAIEAREEFIRERIRAGESLADL 203
ligK_PcmE TIGR02798
4-carboxy-4-hydroxy-2-oxoadipate aldolase/oxaloacetate decarboxylase; Members of this protein ...
 9-220 1.37e-54

4-carboxy-4-hydroxy-2-oxoadipate aldolase/oxaloacetate decarboxylase; Members of this protein family 4-carboxy-4-hydroxy-2-oxoadipate aldolase, also called 4-oxalocitramalate aldolase. This enzyme of the protocatechuate 4,5-cleavage pathway converts its substrate to pyruvate plus oxaloacetate. Protocatechuate is an intermediate in many pathways for degrading aromatic compounds, including lignin, fluorene, etc. Hara, et al. showed the LigK gene was not only a 4-carboxy-4-hydroxy-2-oxoadipate aldolase but also the enzyme of the following step, oxaloacetate decarboxylase.


Pssm-ID: 131845  Cd Length: 222  Bit Score: 174.26  E-value: 1.37e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330    9 ERPSKADIDALSKFSPATIHEAQGRKGALSSRLKPVDYRMKLCGPAFTVKCAPRDNIMLQLAINYAKPGDIIVVSAGEYE 88
Cdd:TIGR02798   8 ERADLAAVDGLAAFGVATVHEAMGRVGLLAPYMRPIYTGARVCGTAVTVLLQPGDNWMMHVAAEQIQEGDVVVAACTAEC 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330   89 EAGSFGDVLANACLAKGIGGLVTDTGVRDTLQLRDLGFPVFSLSVCIKGTVKETIAAVNDSIIIGGEIINPGDIIVGDAD 168
Cdd:TIGR02798  88 EDGYFGDLLATSFQARGCRGLIIDAGVRDVRDLTEMNFPVWSKAIHAKGTVKATLGSVNIPVVCANALVNPGDVVVADDD 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 771650330  169 GLVVVRREDAQESARLSQIREDAEAGYIEAYKQGKSVIEVSNLEPVLKAKGL 220
Cdd:TIGR02798 168 GVVVVPRANAGAVLDAAQAREANEEAKRVKLASGVLGLDMYKMREPLEKAGL 219
RraA_family cd16841
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator ...
 25-173 2.90e-53

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: 168.02  E-value: 2.90e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330  25 ATIHEAQGRK-GALSSRLKPVDYRMKLCGPAFTVKCAPRDNIMLQLAINYAKPGDIIVVSAGEYEEAGSFGDVLANACLA 103
Cdd:cd16841    1 ADLSDALDRLgGVLPGIIRPLGGGARFVGPAVTVKCFPDDNLLVREALDEAGPGDVLVVDGGGSLRCALWGDLLATLAKA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330 104 KGIGGLVTDTGVRDTLQLRDLGFPVFSLSVCIKGTVKETIAAVNDSIIIGGEIINPGDIIVGDADGLVVV 173
Cdd:cd16841   81 RGWAGIVIDGAVRDVDEIRELDFPVFARGTTPRGSKKVGPGEVNVPVTIGGVTVNPGDIIVADEDGVVVI 150
RraA-like pfam03737
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
 25-171 4.82e-45

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: 147.27  E-value: 4.82e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330   25 ATIHEA---QGRKGALSSRLKPVdYRMKLCGPAFTVKCAPRDNIMLQLAINYAKPGDIIVVsAGEYEEAGSFGDVLANAC 101
Cdd:pfam03737   1 ADLSDAlgsYGGRLGAMPGIRPL-NPGPFVGPAVTVKCFPEDNLLVHEALDEAGPGDVLVV-DGGGGSRAALGDLLATLA 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330  102 LAKGIGGLVTDTGVRDTLQLRDLGFPVFSLSVCIKGTVKETIAAVNDSIIIGGEIINPGDIIVGDADGLV 171
Cdd:pfam03737  79 KANGWAGIVIDGAVRDVDELRELDFPVFARGTTPRGSVKRGPGEVNVPVTIGGVTVRPGDIIVADEDGVV 148
 
Name Accession Description Interval E-value
PRK09262 PRK09262
hypothetical protein; Provisional
 9-221 1.09e-69

hypothetical protein; Provisional


Pssm-ID: 181735  Cd Length: 225  Bit Score: 212.48  E-value: 1.09e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330   9 ERPSKADIDALSKFSPATIHEAQGRKGALSSRLKPVDYRMKLCGPAFTVKCAPRDNIMLQLAINYAKPGDIIVVSAGEYE 88
Cdd:PRK09262  10 ERADAAVVDRLAEFGVATVHEAQGRVGLLKPYMRPIYQGARIAGTAVTVLVQPGDNWMMHVAVEQCQPGDVLVVAPTSPC 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330  89 EAGSFGDVLANACLAKGIGGLVTDTGVRDTLQLRDLGFPVFSLSVCIKGTVKETIAAVNDSIIIGGEIINPGDIIVGDAD 168
Cdd:PRK09262  90 TDGFFGDLLATSLQARGVRGLVIDAGVRDVRTLTEMGFPVWSRAISAQGTVKATLGSVNVPVVCAGALVNPGDVVVADDD 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 771650330 169 GLVVVRREDAQESARLSQIREDAEAGYIEAYKQGKSVIEVSNLEPVLKAKGLV 221
Cdd:PRK09262 170 GVVVVPRAQAAAVADAAEAREANEESKRERLAAGELGLDIYKMRERLAKKGLR 222
RraA COG0684
RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal ...
 9-208 4.14e-68

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


Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 207.71  E-value: 4.14e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330   9 ERPSKADIDALSKFSPATIHEAQGRK--GALSSRLKPVDYRMKLCGPAFTVKCAPRDNIMLQLAINYAKPGDIIVVSAGE 86
Cdd:COG0684    1 PRLDAELLERLAAVSTATVSDALDRLlrGALDPGIRPLHPGARLVGPAVTVRYRPGDNLMLHEAIDLAPPGDVLVIDAGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330  87 YEEAGSFGDVLANACLAKGIGGLVTDTGVRDTLQLRDLGFPVFSLSVCIKGTVKE-TIAAVNDSIIIGGEIINPGDIIVG 165
Cdd:COG0684   81 DTDAALWGELLATAAKARGVAGVVIDGAVRDVAEIRELGFPVFARGVTPRGTKKRvGPGEINVPVSIGGVTVRPGDLVVA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 771650330 166 DADGLVVVRREDAQESARLSQIREDAEAGYIEAYKQGKSVIEV 208
Cdd:COG0684  161 DDDGVVVIPAELAEEVLEAAEAIEAREEFIRERIRAGESLADL 203
ligK_PcmE TIGR02798
4-carboxy-4-hydroxy-2-oxoadipate aldolase/oxaloacetate decarboxylase; Members of this protein ...
 9-220 1.37e-54

4-carboxy-4-hydroxy-2-oxoadipate aldolase/oxaloacetate decarboxylase; Members of this protein family 4-carboxy-4-hydroxy-2-oxoadipate aldolase, also called 4-oxalocitramalate aldolase. This enzyme of the protocatechuate 4,5-cleavage pathway converts its substrate to pyruvate plus oxaloacetate. Protocatechuate is an intermediate in many pathways for degrading aromatic compounds, including lignin, fluorene, etc. Hara, et al. showed the LigK gene was not only a 4-carboxy-4-hydroxy-2-oxoadipate aldolase but also the enzyme of the following step, oxaloacetate decarboxylase.


Pssm-ID: 131845  Cd Length: 222  Bit Score: 174.26  E-value: 1.37e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330    9 ERPSKADIDALSKFSPATIHEAQGRKGALSSRLKPVDYRMKLCGPAFTVKCAPRDNIMLQLAINYAKPGDIIVVSAGEYE 88
Cdd:TIGR02798   8 ERADLAAVDGLAAFGVATVHEAMGRVGLLAPYMRPIYTGARVCGTAVTVLLQPGDNWMMHVAAEQIQEGDVVVAACTAEC 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330   89 EAGSFGDVLANACLAKGIGGLVTDTGVRDTLQLRDLGFPVFSLSVCIKGTVKETIAAVNDSIIIGGEIINPGDIIVGDAD 168
Cdd:TIGR02798  88 EDGYFGDLLATSFQARGCRGLIIDAGVRDVRDLTEMNFPVWSKAIHAKGTVKATLGSVNIPVVCANALVNPGDVVVADDD 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 771650330  169 GLVVVRREDAQESARLSQIREDAEAGYIEAYKQGKSVIEVSNLEPVLKAKGL 220
Cdd:TIGR02798 168 GVVVVPRANAGAVLDAAQAREANEEAKRVKLASGVLGLDMYKMREPLEKAGL 219
RraA_family cd16841
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator ...
 25-173 2.90e-53

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: 168.02  E-value: 2.90e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330  25 ATIHEAQGRK-GALSSRLKPVDYRMKLCGPAFTVKCAPRDNIMLQLAINYAKPGDIIVVSAGEYEEAGSFGDVLANACLA 103
Cdd:cd16841    1 ADLSDALDRLgGVLPGIIRPLGGGARFVGPAVTVKCFPDDNLLVREALDEAGPGDVLVVDGGGSLRCALWGDLLATLAKA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330 104 KGIGGLVTDTGVRDTLQLRDLGFPVFSLSVCIKGTVKETIAAVNDSIIIGGEIINPGDIIVGDADGLVVV 173
Cdd:cd16841   81 RGWAGIVIDGAVRDVDEIRELDFPVFARGTTPRGSKKVGPGEVNVPVTIGGVTVNPGDIIVADEDGVVVI 150
RraA-like pfam03737
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
 25-171 4.82e-45

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: 147.27  E-value: 4.82e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330   25 ATIHEA---QGRKGALSSRLKPVdYRMKLCGPAFTVKCAPRDNIMLQLAINYAKPGDIIVVsAGEYEEAGSFGDVLANAC 101
Cdd:pfam03737   1 ADLSDAlgsYGGRLGAMPGIRPL-NPGPFVGPAVTVKCFPEDNLLVHEALDEAGPGDVLVV-DGGGGSRAALGDLLATLA 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330  102 LAKGIGGLVTDTGVRDTLQLRDLGFPVFSLSVCIKGTVKETIAAVNDSIIIGGEIINPGDIIVGDADGLV 171
Cdd:pfam03737  79 KANGWAGIVIDGAVRDVDELRELDFPVFARGTTPRGSVKRGPGEVNVPVTIGGVTVRPGDIIVADEDGVV 148
PRK06201 PRK06201
hypothetical protein; Validated
 2-203 3.92e-43

hypothetical protein; Validated


Pssm-ID: 180465 [Multi-domain]  Cd Length: 221  Bit Score: 144.71  E-value: 3.92e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330   2 IHIKDIAERPSKADIDALSKFSPATIHEAQGRKGALSSRLKPVDYRMKLCGPAFTVKCAPRDNIMLQLAINYAKPGDIIV 81
Cdd:PRK06201   5 FRVLPSWPRVDAALVEAFRELPVANISDSMNRMTAGGAGLRPMHRGGRLAGTALTVRTRPGDNLMIHRALDLARPGDVIV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330  82 VSAGEYEEAGSFGDVLANACLAKGIGGLVTDTGVRDTLQLRDLGFPVFSLSVCIKGTVKETIAAVNDSIIIGGEIINPGD 161
Cdd:PRK06201  85 VDGGGDLTNALVGEIMLAIAARRGVAGVVIDGAVRDVAALREMGFPVFARGVTHRGPYKDGPGEINVPVAIGGMVIEPGD 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 771650330 162 IIVGDADGLVVVRREDAQESARLSQIREDAEAGYIEAYKQGK 203
Cdd:PRK06201 165 LIVGDDDGLVAVPPADAEALLEAARAKHAAEAKQLEAIRAGR 206
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 17-212 5.08e-27

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 107.03  E-value: 5.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330  17 DALSKFSPATIHEAQGRKGALSSrLKPVDYRMKLCGPAFTVKCAPRDNIMLQLAINYAKPGDIIVVSAGEYEEAgSFGDV 96
Cdd:PRK07028 231 EIFMQVSTPNISDAMHRKGAMKG-IKPLVRGTKMVGKAVTVQTFAGDWAKPVEAIDVAKPGDVIVIYNSSKDIA-PWGEL 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330  97 LANACLAKGIGGLVTDTGVRDTLQLRDLGFPVFSLSVCIKGTVKETIAAVNDSIIIGGEIINPGDIIVGDADGLVVVRRE 176
Cdd:PRK07028 309 ATLSCLNKGIAGVVIDGAVRDVDEIRKLGFPVFARAIVPNAGEPKGFGEINAEIVCGGQTVRPGDWIIGDENGVVVVPKE 388

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 771650330 177 DAQESARLSQIREDAEAGYIEAYKQGKSVIEVSNLE 212
Cdd:PRK07028 389 RAYEIARRALEVKKTEDRIREEIRRGRTLSEVIELK 424
PRK08245 PRK08245
hypothetical protein; Validated
 10-206 2.59e-25

hypothetical protein; Validated


Pssm-ID: 236200  Cd Length: 240  Bit Score: 98.82  E-value: 2.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330  10 RPSKADIDALSKFSPATIHEAQGRKGALSS---RLKPVDYRMK-LCGPAFTVKCAP-----------RDNIMLQ-LAINY 73
Cdd:PRK08245   5 RLSPATREALKRVSTATLTTALFKRGLRNQfirGVRPLRPGGPrMVGPAFTLRFVParedlntpesfADPESPQrAAIET 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330  74 AKPGDIIVVSAGEYEEAGSFGDVLANACLAKGIGGLVTDTGVRDTLQLRDLGFPVFSLSVCIKGTV-KETIAAVNDSIII 152
Cdd:PRK08245  85 CPPGCVLVVDARGDARAGSFGDILCTRLKKRGVAGLVTDGGVRDSPGIAALGLPVWCAGPSAPTNLtGLTAVDINVPIGC 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 771650330 153 GGEIINPGDIIVGDADGLVVVRREDAQESARLSQIREDAEAGYIEAYKQGKSVI 206
Cdd:PRK08245 165 GGVAVFPGDIIVADDDGVVVIPAALADEVAAEAVEQERWEDFIREEVAAGASLP 218
PRK12764 PRK12764
fumarylacetoacetate hydrolase family protein;
70-205 2.44e-20

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 237193 [Multi-domain]  Cd Length: 500  Bit Score: 88.66  E-value: 2.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330  70 AINYAKPGDIIVVSAGEYEEAGSFGDVLANACLAKGIGGLVTDTGVRDTLQLRDLGFPVFSLSV--CIKGTvKETIAAVN 147
Cdd:PRK12764 339 AFDSVNPGEVLVIEARGEKGTGTLGDILALRAQVRGAAGVVTDGGVRDYAAVAELGLPVFFAGPhpAVLGR-RHVPWDVD 417

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 771650330 148 DSIIIGGEIINPGDIIVGDADGLVVVRREDAQESARLSQIREDAEAGYIEAYKQGKSV 205
Cdd:PRK12764 418 ITVACGGATVQPGDVIVGDDDGVVVIPPALAEEVADDAIAQEHEEAFIAERVAEGASV 475
PRK09372 PRK09372
ribonuclease E inhibitor RraA;
47-174 4.10e-09

ribonuclease E inhibitor RraA;


Pssm-ID: 236487  Cd Length: 159  Bit Score: 53.60  E-value: 4.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330  47 RMKLCGPAFTVKCaPRDNIMLQLAINYAKPGDIIVVSAGeyeeaGS-----FGDVLANACLAKGIGGLVTDTGVRDTLQL 121
Cdd:PRK09372  29 RSSFGGPITTVKC-FEDNGLVKELLEEPGEGRVLVVDGG-----GSlrralVGDNLAELAVDNGWEGIVVYGCVRDVDEL 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 771650330 122 RDLGFPVFSLSVCIKGTVKETIAAVNDSIIIGGEIINPGDIIVGDADGLVVVR 174
Cdd:PRK09372 103 AELDIGIQALAAIPVKSDKEGIGERDVPVNFGGVTFFPGDYLYADNDGIIVSP 155
PRK12487 PRK12487
putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase;
56-172 1.47e-06

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


Pssm-ID: 183553  Cd Length: 163  Bit Score: 46.49  E-value: 1.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771650330  56 TVKCaPRDNIMLQLAINYAKPGDIIVVSAGEYEEAGSFGDVLANACLAKGIGGLVTDTGVRDTLQLRDLGFPVFSLSVCI 135
Cdd:PRK12487  38 TVRC-FEDNSKVKEVLAQDGKGKVLVVDGGGSCRRALLGDQIAQSALDNGWEGIVINGCVRDVGALSTMDLGVKALGASP 116

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 771650330 136 KGTVKETIAAVNDSIIIGGEIINPGDIIVGDADGLVV 172
Cdd:PRK12487 117 IKTEKRGQGEVNVTLTMGNVIIEPGDMLYADENGIAV 153
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 67-89 5.15e-03

Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion transport and metabolism];


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 37.20  E-value: 5.15e-03
                         10        20
                 ....*....|....*....|...
gi 771650330  67 LQLAINYAKPGDIIVVSAGEYEE 89
Cdd:COG3420   24 LQAAIDAAPPGDTIEVPPGTYEG 46
 
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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