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Conserved domains on  [gi|1660930253|gb|TLN88769|]
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putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase [Acinetobacter baumannii]

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;
5-167 3.53e-94

ribonuclease E inhibitor RraA;


:

Pssm-ID: 236487  Cd Length: 159  Bit Score: 269.70  E-value: 3.53e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253   5 PFVTCDLLDDNPEkDLQVVTPSmdgkfFKSYGARQTFGGQVVTVKCFEDNSRVKELLATDGTGKVLVVDGGASMRCALMG 84
Cdd:PRK09372    2 EYDTSDLCDIYPD-DVRVVEPL-----FSSFGGRSSFGGPITTVKCFEDNGLVKELLEEPGEGRVLVVDGGGSLRRALVG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253  85 DMIAESAVKNNWNGVVIYGCVRDVDALATLDLGVHALAAIPQKSNRKGIGEVDIPLYFGGVTIQSGDFIYADNNGIVIAK 164
Cdd:PRK09372   76 DNLAELAVDNGWEGIVVYGCVRDVDELAELDIGIQALAAIPVKSDKEGIGERDVPVNFGGVTFFPGDYLYADNDGIIVSP 155


                  ...
gi 1660930253 165 EKL 167
Cdd:PRK09372  156 EPL 158
 
Name Accession Description Interval E-value
PRK09372 PRK09372
ribonuclease E inhibitor RraA;
5-167 3.53e-94

ribonuclease E inhibitor RraA;


Pssm-ID: 236487  Cd Length: 159  Bit Score: 269.70  E-value: 3.53e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253   5 PFVTCDLLDDNPEkDLQVVTPSmdgkfFKSYGARQTFGGQVVTVKCFEDNSRVKELLATDGTGKVLVVDGGASMRCALMG 84
Cdd:PRK09372    2 EYDTSDLCDIYPD-DVRVVEPL-----FSSFGGRSSFGGPITTVKCFEDNGLVKELLEEPGEGRVLVVDGGGSLRRALVG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253  85 DMIAESAVKNNWNGVVIYGCVRDVDALATLDLGVHALAAIPQKSNRKGIGEVDIPLYFGGVTIQSGDFIYADNNGIVIAK 164
Cdd:PRK09372   76 DNLAELAVDNGWEGIVVYGCVRDVDELAELDIGIQALAAIPVKSDKEGIGERDVPVNFGGVTFFPGDYLYADNDGIIVSP 155


                  ...
gi 1660930253 165 EKL 167
Cdd:PRK09372  156 EPL 158
NOT-MenG TIGR01935
RraA famliy; The E. coli member of this family has been characterized as a regulator of RNase ...
 8-163 1.12e-73

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: 217.58  E-value: 1.12e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253   8 TCDLLDDNPEKdLQVVTPsmdgkFFKSYGARQTFGGQVVTVKCFEDNSRVKELLATDGTGKVLVVDGGASMRCALMGDMI 87
Cdd:TIGR01935   1 TPDLCDAYPDK-VRVLEP-----MFRNFGGRAAFAGPIVTVKCFEDNSLVREVLEQPGAGRVLVVDGGGSLRCALLGDNL 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1660930253  88 AESAVKNNWNGVVIYGCVRDVDALATLDLGVHALAAIPQKSNRKGIGEVDIPLYFGGVTIQSGDFIYADNNGIVIA 163
Cdd:TIGR01935  75 AVLAEENGWEGVIVNGCVRDVAELAGMDLGVKALAAHPRKTEKRGAGEVDVPVTFAGVTFVPGDYLYADEDGILVS 150
RraA_family cd16841
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator ...
 9-162 1.59e-56

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: 174.18  E-value: 1.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253   9 CDLLDDNPEKDlqvvtpSMDGKFFKSYGARQTFGGQVVTVKCFEDNSR-VKELLATDGTGKVLVVDGGASMRCALMGDMI 87
Cdd:cd16841     1 ADLSDALDRLG------GVLPGIIRPLGGGARFVGPAVTVKCFPDDNLlVREALDEAGPGDVLVVDGGGSLRCALWGDLL 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1660930253  88 AESAVKNNWNGVVIYGCVRDVDALATLDLGVHALAAIPQKSNRKGIGEVDIPLYFGGVTIQSGDFIYADNNGIVI 162
Cdd:cd16841    75 ATLAKARGWAGIVIDGAVRDVDEIRELDFPVFARGTTPRGSKKVGPGEVNVPVTIGGVTVNPGDIIVADEDGVVV 149
RraA-like pfam03737
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
 38-161 5.65e-50

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: 157.67  E-value: 5.65e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253  38 RQTFGGQVVTVKCF-EDNSRVKELLATDGTGKVLVVDGGaSMRCALMGDMIAESAVKNNWNGVVIYGCVRDVDALATLDL 116
Cdd:pfam03737  25 PGPFVGPAVTVKCFpEDNLLVHEALDEAGPGDVLVVDGG-GGSRAALGDLLATLAKANGWAGIVIDGAVRDVDELRELDF 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1660930253 117 GVHALAAIPQKSNRKGIGEVDIPLYFGGVTIQSGDFIYADNNGIV 161
Cdd:pfam03737 104 PVFARGTTPRGSVKRGPGEVNVPVTIGGVTVRPGDIIVADEDGVV 148
RraA COG0684
RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal ...
 32-162 3.22e-32

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


Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 114.11  E-value: 3.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253  32 FKSYGARQTFGGQVVTVKCFE-DNSRVKELLATDGTGKVLVVDGGASMRCALMGDMIAESAVKNNWNGVVIYGCVRDVDA 110
Cdd:COG0684    35 IRPLHPGARLVGPAVTVRYRPgDNLMLHEAIDLAPPGDVLVIDAGGDTDAALWGELLATAAKARGVAGVVIDGAVRDVAE 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1660930253 111 LATLDLGVHALAAIPQKS-NRKGIGEVDIPLYFGGVTIQSGDFIYADNNGIVI 162
Cdd:COG0684   115 IRELGFPVFARGVTPRGTkKRVGPGEINVPVSIGGVTVRPGDLVVADDDGVVV 167
 
Name Accession Description Interval E-value
PRK09372 PRK09372
ribonuclease E inhibitor RraA;
5-167 3.53e-94

ribonuclease E inhibitor RraA;


Pssm-ID: 236487  Cd Length: 159  Bit Score: 269.70  E-value: 3.53e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253   5 PFVTCDLLDDNPEkDLQVVTPSmdgkfFKSYGARQTFGGQVVTVKCFEDNSRVKELLATDGTGKVLVVDGGASMRCALMG 84
Cdd:PRK09372    2 EYDTSDLCDIYPD-DVRVVEPL-----FSSFGGRSSFGGPITTVKCFEDNGLVKELLEEPGEGRVLVVDGGGSLRRALVG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253  85 DMIAESAVKNNWNGVVIYGCVRDVDALATLDLGVHALAAIPQKSNRKGIGEVDIPLYFGGVTIQSGDFIYADNNGIVIAK 164
Cdd:PRK09372   76 DNLAELAVDNGWEGIVVYGCVRDVDELAELDIGIQALAAIPVKSDKEGIGERDVPVNFGGVTFFPGDYLYADNDGIIVSP 155


                  ...
gi 1660930253 165 EKL 167
Cdd:PRK09372  156 EPL 158
NOT-MenG TIGR01935
RraA famliy; The E. coli member of this family has been characterized as a regulator of RNase ...
 8-163 1.12e-73

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: 217.58  E-value: 1.12e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253   8 TCDLLDDNPEKdLQVVTPsmdgkFFKSYGARQTFGGQVVTVKCFEDNSRVKELLATDGTGKVLVVDGGASMRCALMGDMI 87
Cdd:TIGR01935   1 TPDLCDAYPDK-VRVLEP-----MFRNFGGRAAFAGPIVTVKCFEDNSLVREVLEQPGAGRVLVVDGGGSLRCALLGDNL 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1660930253  88 AESAVKNNWNGVVIYGCVRDVDALATLDLGVHALAAIPQKSNRKGIGEVDIPLYFGGVTIQSGDFIYADNNGIVIA 163
Cdd:TIGR01935  75 AVLAEENGWEGVIVNGCVRDVAELAGMDLGVKALAAHPRKTEKRGAGEVDVPVTFAGVTFVPGDYLYADEDGILVS 150
PRK12487 PRK12487
putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase;
6-167 3.68e-73

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


Pssm-ID: 183553  Cd Length: 163  Bit Score: 216.75  E-value: 3.68e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253   6 FVTCDLLDDNPEKdLQVVTPSmdgkfFKSYGARQTFGGQVVTVKCFEDNSRVKELLATDGTGKVLVVDGGASMRCALMGD 85
Cdd:PRK12487    3 DLLPDLFDHYEDK-LTLLNLP-----FKNFGGKRIFWGEIVTVRCFEDNSKVKEVLAQDGKGKVLVVDGGGSCRRALLGD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253  86 MIAESAVKNNWNGVVIYGCVRDVDALATLDLGVHALAAIPQKSNRKGIGEVDIPLYFGGVTIQSGDFIYADNNGIVIAKE 165
Cdd:PRK12487   77 QIAQSALDNGWEGIVINGCVRDVGALSTMDLGVKALGASPIKTEKRGQGEVNVTLTMGNVIIEPGDMLYADENGIAVSKE 156


                  ..
gi 1660930253 166 KL 167
Cdd:PRK12487  157 AL 158
RraA_entero TIGR02998
regulator of ribonuclease activity A; This family includes a number of closely related ...
 9-167 2.16e-57

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: 176.92  E-value: 2.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253   9 CDLLDDnpekDLQVVTPsmdgkFFKSYGARQTFGGQVVTVKCFEDNSRVKELLATDGTGKVLVVDGGASMRCALMGDMIA 88
Cdd:TIGR02998   9 CDFYAD----LVDVVEP-----IFSNFGGRSSFGGKVVTVKCFEHNGLINELLEQNGTGRVLVIDGGGSTRRALIDAELA 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1660930253  89 ESAVKNNWNGVVIYGCVRDVDALATLDLGVHALAAIPQKSNRKGIGEVDIPLYFGGVTIQSGDFIYADNNGIVIAKEKL 167
Cdd:TIGR02998  80 QLAANNGWEGIVVYGAVRQVDALEELDIGIQALAAIPVGADEQGIGESDIAVNFAGVTFFPDDYIYADNTGIILSPEPL 158
RraA_family cd16841
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator ...
 9-162 1.59e-56

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: 174.18  E-value: 1.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253   9 CDLLDDNPEKDlqvvtpSMDGKFFKSYGARQTFGGQVVTVKCFEDNSR-VKELLATDGTGKVLVVDGGASMRCALMGDMI 87
Cdd:cd16841     1 ADLSDALDRLG------GVLPGIIRPLGGGARFVGPAVTVKCFPDDNLlVREALDEAGPGDVLVVDGGGSLRCALWGDLL 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1660930253  88 AESAVKNNWNGVVIYGCVRDVDALATLDLGVHALAAIPQKSNRKGIGEVDIPLYFGGVTIQSGDFIYADNNGIVI 162
Cdd:cd16841    75 ATLAKARGWAGIVIDGAVRDVDEIRELDFPVFARGTTPRGSKKVGPGEVNVPVTIGGVTVNPGDIIVADEDGVVV 149
RraA-like pfam03737
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
 38-161 5.65e-50

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: 157.67  E-value: 5.65e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253  38 RQTFGGQVVTVKCF-EDNSRVKELLATDGTGKVLVVDGGaSMRCALMGDMIAESAVKNNWNGVVIYGCVRDVDALATLDL 116
Cdd:pfam03737  25 PGPFVGPAVTVKCFpEDNLLVHEALDEAGPGDVLVVDGG-GGSRAALGDLLATLAKANGWAGIVIDGAVRDVDELRELDF 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1660930253 117 GVHALAAIPQKSNRKGIGEVDIPLYFGGVTIQSGDFIYADNNGIV 161
Cdd:pfam03737 104 PVFARGTTPRGSVKRGPGEVNVPVTIGGVTVRPGDIIVADEDGVV 148
RraA COG0684
RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal ...
 32-162 3.22e-32

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


Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 114.11  E-value: 3.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253  32 FKSYGARQTFGGQVVTVKCFE-DNSRVKELLATDGTGKVLVVDGGASMRCALMGDMIAESAVKNNWNGVVIYGCVRDVDA 110
Cdd:COG0684    35 IRPLHPGARLVGPAVTVRYRPgDNLMLHEAIDLAPPGDVLVIDAGGDTDAALWGELLATAAKARGVAGVVIDGAVRDVAE 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1660930253 111 LATLDLGVHALAAIPQKS-NRKGIGEVDIPLYFGGVTIQSGDFIYADNNGIVI 162
Cdd:COG0684   115 IRELGFPVFARGVTPRGTkKRVGPGEINVPVSIGGVTVRPGDLVVADDDGVVV 167
PRK06201 PRK06201
hypothetical protein; Validated
 40-161 7.76e-21

hypothetical protein; Validated


Pssm-ID: 180465 [Multi-domain]  Cd Length: 221  Bit Score: 85.00  E-value: 7.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253  40 TFGGQVVTVKCFE-DNSRVKELLATDGTGKVLVVDGGASMRCALMGDMIAESAVKNNWNGVVIYGCVRDVDALATLDLGV 118
Cdd:PRK06201   52 RLAGTALTVRTRPgDNLMIHRALDLARPGDVIVVDGGGDLTNALVGEIMLAIAARRGVAGVVIDGAVRDVAALREMGFPV 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1660930253 119 HALAAIPQKSNRKGIGEVDIPLYFGGVTIQSGDFIYADNNGIV 161
Cdd:PRK06201  132 FARGVTHRGPYKDGPGEINVPVAIGGMVIEPGDLIVGDDDGLV 174
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 24-166 1.12e-16

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 76.21  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253  24 TPSMDGkfFKSYGARQTFGGQVVTVKCFE-DNSRVKELLATDGTGKVLVVDGGaSMRCALMGDMIAESAVKNNWNGVVIY 102
Cdd:PRK07028  248 KGAMKG--IKPLVRGTKMVGKAVTVQTFAgDWAKPVEAIDVAKPGDVIVIYNS-SKDIAPWGELATLSCLNKGIAGVVID 324

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1660930253 103 GCVRDVDALATLDLGVHALAAIPQKSNRKGIGEVDIPLYFGGVTIQSGDFIYADNNGI-VIAKEK 166
Cdd:PRK07028  325 GAVRDVDEIRKLGFPVFARAIVPNAGEPKGFGEINAEIVCGGQTVRPGDWIIGDENGVvVVPKER 389
PRK12764 PRK12764
fumarylacetoacetate hydrolase family protein;
65-162 1.53e-12

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 237193 [Multi-domain]  Cd Length: 500  Bit Score: 64.39  E-value: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253  65 GTGKVLVVDGGASMRCALMGDMIAESAVKNNWNGVVIYGCVRDVDALATLDLGVHALAAIPQKSNRKGIG-EVDIPLYFG 143
Cdd:PRK12764  344 NPGEVLVIEARGEKGTGTLGDILALRAQVRGAAGVVTDGGVRDYAAVAELGLPVFFAGPHPAVLGRRHVPwDVDITVACG 423

                          90
                  ....*....|....*....
gi 1660930253 144 GVTIQSGDFIYADNNGIVI 162
Cdd:PRK12764  424 GATVQPGDVIVGDDDGVVV 442
PRK08245 PRK08245
hypothetical protein; Validated
 67-162 8.33e-10

hypothetical protein; Validated


Pssm-ID: 236200  Cd Length: 240  Bit Score: 55.68  E-value: 8.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1660930253  67 GKVLVVDGGASMRCALMGDMIAESAVKNNWNGVVIYGCVRDVDALATLDLGV-HALAAIPqkSNRKGIGEVDI--PLYFG 143
Cdd:PRK08245   88 GCVLVVDARGDARAGSFGDILCTRLKKRGVAGLVTDGGVRDSPGIAALGLPVwCAGPSAP--TNLTGLTAVDInvPIGCG 165

                          90
                  ....*....|....*....
gi 1660930253 144 GVTIQSGDFIYADNNGIVI 162
Cdd:PRK08245  166 GVAVFPGDIIVADDDGVVV 184
 
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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