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Conserved domains on  [gi|764453410|gb|AJR23524|]
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dimethylmenaquinone methyltransferase [Sphingobium sp. YBL2]

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 COG0684
RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal ...
52-281 9.14e-50

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


:

Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 164.57  E-value: 9.14e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410  52 PKVPDDILERMREVTLEEAWATLRSAgFNHQYEDGWLSIFPDKVLVGRALTSQWLPGRPDIQTVlekqgaddgrkgamna 131
Cdd:COG0684    1 PRLDAELLERLAAVSTATVSDALDRL-LRGALDPGIRPLHPGARLVGPAVTVRYRPGDNLMLHE---------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410 132 wPVDMLQKGDVYVSDHFGlKQDGPSIGDNVGNAIYARSGNGVVYDGAVRDINGLRELpNFVSFVRSYDPSHHFGamatga 211
Cdd:COG0684   64 -AIDLAPPGDVLVIDAGG-DTDAALWGELLATAAKARGVAGVVIDGAVRDVAEIREL-GFPVFARGVTPRGTKK------ 134
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410 212 rlNSTMVGINGPIRIGKATAMPGDVVLGRDGGVLFIPPQLAEKVVKLSENTRLRDMFGHMRLREGRYTAG 281
Cdd:COG0684  135 --RVGPGEINVPVSIGGVTVRPGDLVVADDDGVVVIPAELAEEVLEAAEAIEAREEFIRERIRAGESLAD 202
 
Name Accession Description Interval E-value
RraA COG0684
RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal ...
52-281 9.14e-50

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


Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 164.57  E-value: 9.14e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410  52 PKVPDDILERMREVTLEEAWATLRSAgFNHQYEDGWLSIFPDKVLVGRALTSQWLPGRPDIQTVlekqgaddgrkgamna 131
Cdd:COG0684    1 PRLDAELLERLAAVSTATVSDALDRL-LRGALDPGIRPLHPGARLVGPAVTVRYRPGDNLMLHE---------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410 132 wPVDMLQKGDVYVSDHFGlKQDGPSIGDNVGNAIYARSGNGVVYDGAVRDINGLRELpNFVSFVRSYDPSHHFGamatga 211
Cdd:COG0684   64 -AIDLAPPGDVLVIDAGG-DTDAALWGELLATAAKARGVAGVVIDGAVRDVAEIREL-GFPVFARGVTPRGTKK------ 134
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410 212 rlNSTMVGINGPIRIGKATAMPGDVVLGRDGGVLFIPPQLAEKVVKLSENTRLRDMFGHMRLREGRYTAG 281
Cdd:COG0684  135 --RVGPGEINVPVSIGGVTVRPGDLVVADDDGVVVIPAELAEEVLEAAEAIEAREEFIRERIRAGESLAD 202
PRK08245 PRK08245
hypothetical protein; Validated
54-302 8.62e-19

hypothetical protein; Validated


Pssm-ID: 236200  Cd Length: 240  Bit Score: 83.80  E-value: 8.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410  54 VPDDILERMREVTLEEAWATLRSAGFNHQYEDGWLSIFPD-KVLVGRALTSQWLPGRPDIQTVLEKQGADDGRKGAMNAW 132
Cdd:PRK08245   6 LSPATREALKRVSTATLTTALFKRGLRNQFIRGVRPLRPGgPRMVGPAFTLRFVPAREDLNTPESFADPESPQRAAIETC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410 133 PvdmlqKGDVYVSDHFGLKQDGpSIGDNVGNAIYARSGNGVVYDGAVRDINGLRELPNfvsfvrsydPSHHFGAMATGAR 212
Cdd:PRK08245  86 P-----PGCVLVVDARGDARAG-SFGDILCTRLKKRGVAGLVTDGGVRDSPGIAALGL---------PVWCAGPSAPTNL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410 213 LNSTMVGINGPIRIGKATAMPGDVVLGRDGGVLFIPPQLAEKVVKLS-ENTRLRDmFGHMRLREGR-----YTAgqidtr 286
Cdd:PRK08245 151 TGLTAVDINVPIGCGGVAVFPGDIIVADDDGVVVIPAALADEVAAEAvEQERWED-FIREEVAAGAslpglYPP------ 223
                        250
                 ....*....|....*.
gi 764453410 287 wTDAIEADFFAWLQAN 302
Cdd:PRK08245 224 -NAETKAEYEAWRKKR 238
RraA_family cd16841
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator ...
81-247 5.47e-12

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: 62.86  E-value: 5.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410  81 HQYEDGWL-SIFPDKVLVGRALTSQWLPGrpdiqtvlekqgaDDGRKGAMnawpVDMLQKGDVYVSDhFGLKQDGPSIGD 159
Cdd:cd16841   11 GGVLPGIIrPLGGGARFVGPAVTVKCFPD-------------DNLLVREA----LDEAGPGDVLVVD-GGGSLRCALWGD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410 160 NVGNAIYARSGNGVVYDGAVRDINGLRELPnfvsfvrsydpshhFGAMATGARLNST----MVGINGPIRIGKATAMPGD 235
Cdd:cd16841   73 LLATLAKARGWAGIVIDGAVRDVDEIRELD--------------FPVFARGTTPRGSkkvgPGEVNVPVTIGGVTVNPGD 138
                        170
                 ....*....|..
gi 764453410 236 VVLGRDGGVLFI 247
Cdd:cd16841  139 IIVADEDGVVVI 150
RraA-like pfam03737
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
134-245 2.99e-08

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: 52.12  E-value: 2.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410  134 VDMLQKGDVYVSDhfGLKQDGPSIGDNVGNAIYARSGNGVVYDGAVRDINGLRELPnfvsfvrsydpshhFGAMATGAR- 212
Cdd:pfam03737  49 LDEAGPGDVLVVD--GGGGSRAALGDLLATLAKANGWAGIVIDGAVRDVDELRELD--------------FPVFARGTTp 112
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 764453410  213 ---LNSTMVGINGPIRIGKATAMPGDVVLGRDGGVL 245
Cdd:pfam03737 113 rgsVKRGPGEVNVPVTIGGVTVRPGDIIVADEDGVV 148
 
Name Accession Description Interval E-value
RraA COG0684
RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal ...
52-281 9.14e-50

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


Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 164.57  E-value: 9.14e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410  52 PKVPDDILERMREVTLEEAWATLRSAgFNHQYEDGWLSIFPDKVLVGRALTSQWLPGRPDIQTVlekqgaddgrkgamna 131
Cdd:COG0684    1 PRLDAELLERLAAVSTATVSDALDRL-LRGALDPGIRPLHPGARLVGPAVTVRYRPGDNLMLHE---------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410 132 wPVDMLQKGDVYVSDHFGlKQDGPSIGDNVGNAIYARSGNGVVYDGAVRDINGLRELpNFVSFVRSYDPSHHFGamatga 211
Cdd:COG0684   64 -AIDLAPPGDVLVIDAGG-DTDAALWGELLATAAKARGVAGVVIDGAVRDVAEIREL-GFPVFARGVTPRGTKK------ 134
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410 212 rlNSTMVGINGPIRIGKATAMPGDVVLGRDGGVLFIPPQLAEKVVKLSENTRLRDMFGHMRLREGRYTAG 281
Cdd:COG0684  135 --RVGPGEINVPVSIGGVTVRPGDLVVADDDGVVVIPAELAEEVLEAAEAIEAREEFIRERIRAGESLAD 202
PRK08245 PRK08245
hypothetical protein; Validated
54-302 8.62e-19

hypothetical protein; Validated


Pssm-ID: 236200  Cd Length: 240  Bit Score: 83.80  E-value: 8.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410  54 VPDDILERMREVTLEEAWATLRSAGFNHQYEDGWLSIFPD-KVLVGRALTSQWLPGRPDIQTVLEKQGADDGRKGAMNAW 132
Cdd:PRK08245   6 LSPATREALKRVSTATLTTALFKRGLRNQFIRGVRPLRPGgPRMVGPAFTLRFVPAREDLNTPESFADPESPQRAAIETC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410 133 PvdmlqKGDVYVSDHFGLKQDGpSIGDNVGNAIYARSGNGVVYDGAVRDINGLRELPNfvsfvrsydPSHHFGAMATGAR 212
Cdd:PRK08245  86 P-----PGCVLVVDARGDARAG-SFGDILCTRLKKRGVAGLVTDGGVRDSPGIAALGL---------PVWCAGPSAPTNL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410 213 LNSTMVGINGPIRIGKATAMPGDVVLGRDGGVLFIPPQLAEKVVKLS-ENTRLRDmFGHMRLREGR-----YTAgqidtr 286
Cdd:PRK08245 151 TGLTAVDINVPIGCGGVAVFPGDIIVADDDGVVVIPAALADEVAAEAvEQERWED-FIREEVAAGAslpglYPP------ 223
                        250
                 ....*....|....*.
gi 764453410 287 wTDAIEADFFAWLQAN 302
Cdd:PRK08245 224 -NAETKAEYEAWRKKR 238
PRK12764 PRK12764
fumarylacetoacetate hydrolase family protein;
41-276 7.38e-18

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 237193 [Multi-domain]  Cd Length: 500  Bit Score: 84.04  E-value: 7.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410  41 AWtGERFPDGRPKVP-----DDILERMREVTLEEAWATLRSAGFNHQYEDGWLSIFPDKVLVGRALTSQWLPGRPDiqtV 115
Cdd:PRK12764 250 AY-GSREAAGLAPQAagplsPELKAKLASVATATLSAQLRKRGLNNVSIDGLTPTRPGRRMVGRARTLRYVPNRED---L 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410 116 LEKQGaddgrkGAMNAW--PVDMLQKGDVYVSDHFGLKQDGpSIGDNVGNAIYARSGNGVVYDGAVRDINGLRELPNFVs 193
Cdd:PRK12764 326 FKEHG------GGFNAQkrAFDSVNPGEVLVIEARGEKGTG-TLGDILALRAQVRGAAGVVTDGGVRDYAAVAELGLPV- 397
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410 194 fvrsydpshhFGAMATGARLNSTMV--GINGPIRIGKATAMPGDVVLGRDGGVLFIPPQLAEKVVKLSENTRLRDMFGHM 271
Cdd:PRK12764 398 ----------FFAGPHPAVLGRRHVpwDVDITVACGGATVQPGDVIVGDDDGVVVIPPALAEEVADDAIAQEHEEAFIAE 467

                 ....*
gi 764453410 272 RLREG 276
Cdd:PRK12764 468 RVAEG 472
RraA_family cd16841
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator ...
81-247 5.47e-12

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: 62.86  E-value: 5.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410  81 HQYEDGWL-SIFPDKVLVGRALTSQWLPGrpdiqtvlekqgaDDGRKGAMnawpVDMLQKGDVYVSDhFGLKQDGPSIGD 159
Cdd:cd16841   11 GGVLPGIIrPLGGGARFVGPAVTVKCFPD-------------DNLLVREA----LDEAGPGDVLVVD-GGGSLRCALWGD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410 160 NVGNAIYARSGNGVVYDGAVRDINGLRELPnfvsfvrsydpshhFGAMATGARLNST----MVGINGPIRIGKATAMPGD 235
Cdd:cd16841   73 LLATLAKARGWAGIVIDGAVRDVDEIRELD--------------FPVFARGTTPRGSkkvgPGEVNVPVTIGGVTVNPGD 138
                        170
                 ....*....|..
gi 764453410 236 VVLGRDGGVLFI 247
Cdd:cd16841  139 IIVADEDGVVVI 150
PRK06201 PRK06201
hypothetical protein; Validated
135-294 2.06e-08

hypothetical protein; Validated


Pssm-ID: 180465 [Multi-domain]  Cd Length: 221  Bit Score: 53.80  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410 135 DMLQKGDVYVSDHFGLKQDGpSIGDNVGnAIYARSG-NGVVYDGAVRDINGLRE--LPNFVSFVRsydpshHFGAMATGA 211
Cdd:PRK06201  75 DLARPGDVIVVDGGGDLTNA-LVGEIML-AIAARRGvAGVVIDGAVRDVAALREmgFPVFARGVT------HRGPYKDGP 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410 212 rlnstmvG-INGPIRIGKATAMPGDVVLGRDGGVLFIPPQLAEKV---VKLSENTRLRDMfghMRLREGRYtagqiDTRW 287
Cdd:PRK06201 147 -------GeINVPVAIGGMVIEPGDLIVGDDDGLVAVPPADAEALleaARAKHAAEAKQL---EAIRAGRY-----DRSW 211

                 ....*..
gi 764453410 288 TDAIEAD 294
Cdd:PRK06201 212 VDRALAR 218
RraA-like pfam03737
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
134-245 2.99e-08

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: 52.12  E-value: 2.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410  134 VDMLQKGDVYVSDhfGLKQDGPSIGDNVGNAIYARSGNGVVYDGAVRDINGLRELPnfvsfvrsydpshhFGAMATGAR- 212
Cdd:pfam03737  49 LDEAGPGDVLVVD--GGGGSRAALGDLLATLAKANGWAGIVIDGAVRDVDELRELD--------------FPVFARGTTp 112
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 764453410  213 ---LNSTMVGINGPIRIGKATAMPGDVVLGRDGGVL 245
Cdd:pfam03737 113 rgsVKRGPGEVNVPVTIGGVTVRPGDIIVADEDGVV 148
PRK09262 PRK09262
hypothetical protein; Provisional
134-276 3.51e-06

hypothetical protein; Provisional


Pssm-ID: 181735  Cd Length: 225  Bit Score: 47.23  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410 134 VDMLQKGDVYV-------SDHFglkqdgpsIGDNVGNAIYARSGNGVVYDGAVRDINGLRELpNFVSFVRsydpshhfgA 206
Cdd:PRK09262  72 VEQCQPGDVLVvaptspcTDGF--------FGDLLATSLQARGVRGLVIDAGVRDVRTLTEM-GFPVWSR---------A 133
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410 207 MATGARLNSTMVGINGPIRIGKATAMPGDVVLGRDGGVLFIPPQLAEKVVKLSENTRLRDMFGHMRLREG 276
Cdd:PRK09262 134 ISAQGTVKATLGSVNVPVVCAGALVNPGDVVVADDDGVVVVPRAQAAAVADAAEAREANEESKRERLAAG 203
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
172-266 4.00e-05

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 45.01  E-value: 4.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764453410 172 GVVYDGAVRDINGLRELpNFVSFVRSYDPS----HHFGAmatgarlnstmvgINGPIRIGKATAMPGDVVLGRDGGVLFI 247
Cdd:PRK07028 320 GVVIDGAVRDVDEIRKL-GFPVFARAIVPNagepKGFGE-------------INAEIVCGGQTVRPGDWIIGDENGVVVV 385
                         90       100
                 ....*....|....*....|....*
gi 764453410 248 PPQLAEKV------VKLSENtRLRD 266
Cdd:PRK07028 386 PKERAYEIarraleVKKTED-RIRE 409
 
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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