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Conserved domains on  [gi|630959898|ref|XP_007876357|]
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uncharacterized protein PFL1_00673 [Pseudozyma flocculosa PF-1]

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 ...
14-164 3.21e-44

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


:

Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 144.93  E-value: 3.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630959898  14 RHFVDAAQPGSVMVVAAPSEMRSAIWGGLMTARAQHLGVRGVVLDGRCRDLEEHRDAKFPVFARGHSTLGQSPFTRPSEL 93
Cdd:COG0684   62 HEAIDLAPPGDVLVIDAGGDTDAALWGELLATAAKARGVAGVVIDGAVRDVAEIRELGFPVFARGVTPRGTKKRVGPGEI 141
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 630959898  94 QVPVTIRDptspsfpaLTVHPGDAVLADIDGVVVVPAHLVDQVLALAAKSRDVDEKCMRDLRNGHGVQETF 164
Cdd:COG0684  142 NVPVSIGG--------VTVRPGDLVVADDDGVVVIPAELAEEVLEAAEAIEAREEFIRERIRAGESLADLY 204
 
Name Accession Description Interval E-value
RraA COG0684
RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal ...
14-164 3.21e-44

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


Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 144.93  E-value: 3.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630959898  14 RHFVDAAQPGSVMVVAAPSEMRSAIWGGLMTARAQHLGVRGVVLDGRCRDLEEHRDAKFPVFARGHSTLGQSPFTRPSEL 93
Cdd:COG0684   62 HEAIDLAPPGDVLVIDAGGDTDAALWGELLATAAKARGVAGVVIDGAVRDVAEIRELGFPVFARGVTPRGTKKRVGPGEI 141
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 630959898  94 QVPVTIRDptspsfpaLTVHPGDAVLADIDGVVVVPAHLVDQVLALAAKSRDVDEKCMRDLRNGHGVQETF 164
Cdd:COG0684  142 NVPVSIGG--------VTVRPGDLVVADDDGVVVIPAELAEEVLEAAEAIEAREEFIRERIRAGESLADLY 204
RraA_family cd16841
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator ...
14-128 2.28e-37

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: 125.65  E-value: 2.28e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630959898  14 RHFVDAAQPGSVMVVAAPSEMRSAIWGGLMTARAQHLGVRGVVLDGRCRDLEEHRDAKFPVFARGHSTLGQSPfTRPSEL 93
Cdd:cd16841   45 REALDEAGPGDVLVVDGGGSLRCALWGDLLATLAKARGWAGIVIDGAVRDVDEIRELDFPVFARGTTPRGSKK-VGPGEV 123
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 630959898  94 QVPVTIRDptspsfpaLTVHPGDAVLADIDGVVVV 128
Cdd:cd16841  124 NVPVTIGG--------VTVNPGDIIVADEDGVVVI 150
RraA-like pfam03737
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
14-126 1.31e-29

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: 105.67  E-value: 1.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630959898   14 RHFVDAAQPGSVMVVAAPSEMRSAiWGGLMTARAQHLGVRGVVLDGRCRDLEEHRDAKFPVFARGHSTLGqSPFTRPSEL 93
Cdd:pfam03737  46 HEALDEAGPGDVLVVDGGGGSRAA-LGDLLATLAKANGWAGIVIDGAVRDVDELRELDFPVFARGTTPRG-SVKRGPGEV 123
                          90       100       110
                  ....*....|....*....|....*....|...
gi 630959898   94 QVPVTIRDptspsfpaLTVHPGDAVLADIDGVV 126
Cdd:pfam03737 124 NVPVTIGG--------VTVRPGDIIVADEDGVV 148
PRK06201 PRK06201
hypothetical protein; Validated
18-157 6.85e-27

hypothetical protein; Validated


Pssm-ID: 180465 [Multi-domain]  Cd Length: 221  Bit Score: 100.80  E-value: 6.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630959898  18 DAAQPGSVMVVAAPSEMRSAIWGGLMTARAQHLGVRGVVLDGRCRDLEEHRDAKFPVFARGHSTLGqsPF-TRPSELQVP 96
Cdd:PRK06201  75 DLARPGDVIVVDGGGDLTNALVGEIMLAIAARRGVAGVVIDGAVRDVAALREMGFPVFARGVTHRG--PYkDGPGEINVP 152
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 630959898  97 VTIrdptspsfPALTVHPGDAVLADIDGVVVVPAHLVDQVLALAAKSRDVDEKCMRDLRNG 157
Cdd:PRK06201 153 VAI--------GGMVIEPGDLIVGDDDGLVAVPPADAEALLEAARAKHAAEAKQLEAIRAG 205
 
Name Accession Description Interval E-value
RraA COG0684
RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal ...
14-164 3.21e-44

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


Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 144.93  E-value: 3.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630959898  14 RHFVDAAQPGSVMVVAAPSEMRSAIWGGLMTARAQHLGVRGVVLDGRCRDLEEHRDAKFPVFARGHSTLGQSPFTRPSEL 93
Cdd:COG0684   62 HEAIDLAPPGDVLVIDAGGDTDAALWGELLATAAKARGVAGVVIDGAVRDVAEIRELGFPVFARGVTPRGTKKRVGPGEI 141
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 630959898  94 QVPVTIRDptspsfpaLTVHPGDAVLADIDGVVVVPAHLVDQVLALAAKSRDVDEKCMRDLRNGHGVQETF 164
Cdd:COG0684  142 NVPVSIGG--------VTVRPGDLVVADDDGVVVIPAELAEEVLEAAEAIEAREEFIRERIRAGESLADLY 204
RraA_family cd16841
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator ...
14-128 2.28e-37

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: 125.65  E-value: 2.28e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630959898  14 RHFVDAAQPGSVMVVAAPSEMRSAIWGGLMTARAQHLGVRGVVLDGRCRDLEEHRDAKFPVFARGHSTLGQSPfTRPSEL 93
Cdd:cd16841   45 REALDEAGPGDVLVVDGGGSLRCALWGDLLATLAKARGWAGIVIDGAVRDVDEIRELDFPVFARGTTPRGSKK-VGPGEV 123
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 630959898  94 QVPVTIRDptspsfpaLTVHPGDAVLADIDGVVVV 128
Cdd:cd16841  124 NVPVTIGG--------VTVNPGDIIVADEDGVVVI 150
RraA-like pfam03737
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
14-126 1.31e-29

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: 105.67  E-value: 1.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630959898   14 RHFVDAAQPGSVMVVAAPSEMRSAiWGGLMTARAQHLGVRGVVLDGRCRDLEEHRDAKFPVFARGHSTLGqSPFTRPSEL 93
Cdd:pfam03737  46 HEALDEAGPGDVLVVDGGGGSRAA-LGDLLATLAKANGWAGIVIDGAVRDVDELRELDFPVFARGTTPRG-SVKRGPGEV 123
                          90       100       110
                  ....*....|....*....|....*....|...
gi 630959898   94 QVPVTIRDptspsfpaLTVHPGDAVLADIDGVV 126
Cdd:pfam03737 124 NVPVTIGG--------VTVRPGDIIVADEDGVV 148
PRK06201 PRK06201
hypothetical protein; Validated
18-157 6.85e-27

hypothetical protein; Validated


Pssm-ID: 180465 [Multi-domain]  Cd Length: 221  Bit Score: 100.80  E-value: 6.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630959898  18 DAAQPGSVMVVAAPSEMRSAIWGGLMTARAQHLGVRGVVLDGRCRDLEEHRDAKFPVFARGHSTLGqsPF-TRPSELQVP 96
Cdd:PRK06201  75 DLARPGDVIVVDGGGDLTNALVGEIMLAIAARRGVAGVVIDGAVRDVAALREMGFPVFARGVTHRG--PYkDGPGEINVP 152
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 630959898  97 VTIrdptspsfPALTVHPGDAVLADIDGVVVVPAHLVDQVLALAAKSRDVDEKCMRDLRNG 157
Cdd:PRK06201 153 VAI--------GGMVIEPGDLIVGDDDGLVAVPPADAEALLEAARAKHAAEAKQLEAIRAG 205
PRK08245 PRK08245
hypothetical protein; Validated
12-170 4.71e-24

hypothetical protein; Validated


Pssm-ID: 236200  Cd Length: 240  Bit Score: 93.81  E-value: 4.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630959898  12 PDRHFVDAAQPGSVMVVAAPSEMRSAIWGGLMTARAQHLGVRGVVLDGRCRDLEEHRDAKFPVFARGHStlgqSPFT--- 88
Cdd:PRK08245  77 PQRAAIETCPPGCVLVVDARGDARAGSFGDILCTRLKKRGVAGLVTDGGVRDSPGIAALGLPVWCAGPS----APTNltg 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630959898  89 -RPSELQVPVTIRDptspsfpaLTVHPGDAVLADIDGVVVVPAHLVDQVLALAAKSRDVDEKCMRDLRNGHGVQ------ 161
Cdd:PRK08245 153 lTAVDINVPIGCGG--------VAVFPGDIIVADDDGVVVIPAALADEVAAEAVEQERWEDFIREEVAAGASLPglyppn 224
                        170
                 ....*....|...
gi 630959898 162 -ET---FAKWRGK 170
Cdd:PRK08245 225 aETkaeYEAWRKK 237
PRK09262 PRK09262
hypothetical protein; Provisional
17-157 1.25e-20

hypothetical protein; Provisional


Pssm-ID: 181735  Cd Length: 225  Bit Score: 84.60  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630959898  17 VDAAQPGSVMVVAAPSEMRSAIWGGLMTARAQHLGVRGVVLDGRCRDLEEHRDAKFPVFARGHSTLGQSPFTRPSeLQVP 96
Cdd:PRK09262  72 VEQCQPGDVLVVAPTSPCTDGFFGDLLATSLQARGVRGLVIDAGVRDVRTLTEMGFPVWSRAISAQGTVKATLGS-VNVP 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 630959898  97 VTIRDPtspsfpalTVHPGDAVLADIDGVVVVPAHLVDQVLALAAKSRDVDEKCMRDLRNG 157
Cdd:PRK09262 151 VVCAGA--------LVNPGDVVVADDDGVVVVPRAQAAAVADAAEAREANEESKRERLAAG 203
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
17-130 1.05e-14

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 70.43  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630959898  17 VDAAQPGSVMVVAAPSEmRSAIWGGLMTARAQHLGVRGVVLDGRCRDLEEHRDAKFPVFARGHSTLGQSP--FtrpSELQ 94
Cdd:PRK07028 284 IDVAKPGDVIVIYNSSK-DIAPWGELATLSCLNKGIAGVVIDGAVRDVDEIRKLGFPVFARAIVPNAGEPkgF---GEIN 359
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 630959898  95 VPVTIrdptspsfPALTVHPGDAVLADIDGVVVVPA 130
Cdd:PRK07028 360 AEIVC--------GGQTVRPGDWIIGDENGVVVVPK 387
PRK12764 PRK12764
fumarylacetoacetate hydrolase family protein;
17-170 1.97e-13

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 237193 [Multi-domain]  Cd Length: 500  Bit Score: 67.09  E-value: 1.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630959898  17 VDAAQPGSVMVVAAPSEMRSAIWGGLMTARAQHLGVRGVVLDGRCRDLEEHRDAKFPVFARG-H-STLGQSPFtrPSELQ 94
Cdd:PRK12764 340 FDSVNPGEVLVIEARGEKGTGTLGDILALRAQVRGAAGVVTDGGVRDYAAVAELGLPVFFAGpHpAVLGRRHV--PWDVD 417
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 630959898  95 VPVtirdptspSFPALTVHPGDAVLADIDGVVVVPAHLVDQVLALAAKSRDVDEKCMRDLRNGHGVQETF---AKWRGK 170
Cdd:PRK12764 418 ITV--------ACGGATVQPGDVIVGDDDGVVVIPPALAEEVADDAIAQEHEEAFIAERVAEGASVDGLYpmnAEWRAK 488
PRK09372 PRK09372
ribonuclease E inhibitor RraA;
22-132 1.66e-07

ribonuclease E inhibitor RraA;


Pssm-ID: 236487  Cd Length: 159  Bit Score: 48.21  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630959898  22 PGSVMVVAAPSEMRSAIWGGLMTARAQHLGVRGVVLDGRCRDLEEHRDAKFPVFArghstLGQSPftRPS------ELQV 95
Cdd:PRK09372  57 EGRVLVVDGGGSLRRALVGDNLAELAVDNGWEGIVVYGCVRDVDELAELDIGIQA-----LAAIP--VKSdkegigERDV 129
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 630959898  96 PVTirdptspsFPALTVHPGDAVLADIDGVVVVPAHL 132
Cdd:PRK09372 130 PVN--------FGGVTFFPGDYLYADNDGIIVSPEPL 158
PRK12487 PRK12487
putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase;
20-127 4.42e-06

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


Pssm-ID: 183553  Cd Length: 163  Bit Score: 44.56  E-value: 4.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 630959898  20 AQPGS--VMVVAAPSEMRSAIWGGLMTARAQHLGVRGVVLDGRCRDLEEHRDAKFPVFArghstLGQSPFTRPS----EL 93
Cdd:PRK12487  53 AQDGKgkVLVVDGGGSCRRALLGDQIAQSALDNGWEGIVINGCVRDVGALSTMDLGVKA-----LGASPIKTEKrgqgEV 127
                         90       100       110
                 ....*....|....*....|....*....|....
gi 630959898  94 QVPVTIRdptspsfpALTVHPGDAVLADIDGVVV 127
Cdd:PRK12487 128 NVTLTMG--------NVIIEPGDMLYADENGIAV 153
 
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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