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Conserved domains on  [gi|1550003857|gb|RVM96708|]
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DUF521 domain-containing protein [Sinorhizobium meliloti]

Protein Classification

AcnX_swivel and AcnX domain-containing protein( domain architecture ID 10788030)

AcnX_swivel and AcnX domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AcnX1 COG1679
Mevalonate 5-phosphate dehydratase subunit 1, aconitase superfamily (modified mevalonate ...
151-558 0e+00

Mevalonate 5-phosphate dehydratase subunit 1, aconitase superfamily (modified mevalonate pathway) [Lipid transport and metabolism];


:

Pssm-ID: 441285  Cd Length: 411  Bit Score: 574.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 151 LDLTDGDRAMLDGAESVAVAQAMRIISAMAAQQGALGLVDVTQAHIDGCIYAS--PANLTFAEKMVEMGAKVRIPATMNA 228
Cdd:COG1679     1 MKLTDEEEAMLDGEHGEAKQKAMEILVALGEALGAERLVPITSAHISGVSYKTigDAGLEFLEELADMGAKVRVPTTLNP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 229 ISVDHANWQRQGVPPSFGDPAARLADAYVRMGCRPTFTCSPYLLDSAPGAGEAVAWAESNAVIFANSVLGARTAKHPDFL 308
Cdd:COG1679    81 IGMDLENWEEMGVPEEFAEKQRRIIDAYERMGVRPTFTCTPYLLGNIPRFGEHVAWAESSAVIYANSVLGARTNREGGPS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 309 DLCIALTGRAPLSGVYLDEHRKARRIIDVELP-AGADDafWPLIGYLAGRAAPDRIPLIRGLaPAEPSRDDLKALCAAFG 387
Cdd:COG1679   161 ALAAAITGRTPLYGLHLDENRRPTVLIDVDAPlEGVSD--WGALGYLVGRLAGDRVPVITGL-PRRPTEDQLKALGAAMA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 388 TTSAAPMLHVEGVTPEA-----GGAAVEDADHATITRAELTAAWSALNEGPDEVELVAIGSPHASLAECRALAEALGGRK 462
Cdd:COG1679   238 ASGAVALFHVVGVTPEAptleaAFGGRAPVETITITKADLREVYEELNTGEDDVDLVALGCPHLSLEELRELARLLEGRK 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 463 RHPDVAVIVTAGHEVIAKARGEGILARLQESGVQVLPDLCWCsiSEPVFPTRTRAVMTNSGKYAHYGPGLSGRTVRFGSL 542
Cdd:COG1679   318 VKKGVPLWVCTSRAVKAAADRMGYTAIIEAAGGKVLTDTCMV--VSPAEPMGYKVLATNSGKAAHYLPGLCGVKVRFGSL 395
                         410
                  ....*....|....*.
gi 1550003857 543 ADCVSAALSGRVPPRL 558
Cdd:COG1679   396 AECVEAAVTGRWEGEL 411
AcnX2 COG1786
Mevalonate 5-phosphate dehydratase subunit 2, swiveling domain (modified mevalonate pathway) ...
7-134 1.43e-41

Mevalonate 5-phosphate dehydratase subunit 2, swiveling domain (modified mevalonate pathway) [Lipid transport and metabolism];


:

Pssm-ID: 441392 [Multi-domain]  Cd Length: 131  Bit Score: 146.11  E-value: 1.43e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857   7 ARSILQGSAEGPVIATGEALSFWGGVDPATGCVIDVHHPLHGVPLTGSILMMPSSRGSCTGSGVLLDLVLTGRGPAALVF 86
Cdd:COG1786     4 GRKIVGGKAEGEALVSDEPISFLGGVDPKTGVVIDPGHPLYGQSIAGKILVFPTGKGSTVGSYVLYELKKNGTAPAAIIF 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1550003857  87 SEPEDVLTLGALIASemfgkpLPVLRLAPEA-FAALARAKTARI-GDRAI 134
Cdd:COG1786    84 READPILALGAIVAG------IPLVDLFDEDpFEAIKTGDRVRVdADEGT 127
 
Name Accession Description Interval E-value
AcnX1 COG1679
Mevalonate 5-phosphate dehydratase subunit 1, aconitase superfamily (modified mevalonate ...
151-558 0e+00

Mevalonate 5-phosphate dehydratase subunit 1, aconitase superfamily (modified mevalonate pathway) [Lipid transport and metabolism];


Pssm-ID: 441285  Cd Length: 411  Bit Score: 574.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 151 LDLTDGDRAMLDGAESVAVAQAMRIISAMAAQQGALGLVDVTQAHIDGCIYAS--PANLTFAEKMVEMGAKVRIPATMNA 228
Cdd:COG1679     1 MKLTDEEEAMLDGEHGEAKQKAMEILVALGEALGAERLVPITSAHISGVSYKTigDAGLEFLEELADMGAKVRVPTTLNP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 229 ISVDHANWQRQGVPPSFGDPAARLADAYVRMGCRPTFTCSPYLLDSAPGAGEAVAWAESNAVIFANSVLGARTAKHPDFL 308
Cdd:COG1679    81 IGMDLENWEEMGVPEEFAEKQRRIIDAYERMGVRPTFTCTPYLLGNIPRFGEHVAWAESSAVIYANSVLGARTNREGGPS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 309 DLCIALTGRAPLSGVYLDEHRKARRIIDVELP-AGADDafWPLIGYLAGRAAPDRIPLIRGLaPAEPSRDDLKALCAAFG 387
Cdd:COG1679   161 ALAAAITGRTPLYGLHLDENRRPTVLIDVDAPlEGVSD--WGALGYLVGRLAGDRVPVITGL-PRRPTEDQLKALGAAMA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 388 TTSAAPMLHVEGVTPEA-----GGAAVEDADHATITRAELTAAWSALNEGPDEVELVAIGSPHASLAECRALAEALGGRK 462
Cdd:COG1679   238 ASGAVALFHVVGVTPEAptleaAFGGRAPVETITITKADLREVYEELNTGEDDVDLVALGCPHLSLEELRELARLLEGRK 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 463 RHPDVAVIVTAGHEVIAKARGEGILARLQESGVQVLPDLCWCsiSEPVFPTRTRAVMTNSGKYAHYGPGLSGRTVRFGSL 542
Cdd:COG1679   318 VKKGVPLWVCTSRAVKAAADRMGYTAIIEAAGGKVLTDTCMV--VSPAEPMGYKVLATNSGKAAHYLPGLCGVKVRFGSL 395
                         410
                  ....*....|....*.
gi 1550003857 543 ADCVSAALSGRVPPRL 558
Cdd:COG1679   396 AECVEAAVTGRWEGEL 411
AcnX pfam04412
Aconitase X; Aconitase X (AcnX) is a subfamily of Acn superfamily. It is encoded in the ...
151-533 0e+00

Aconitase X; Aconitase X (AcnX) is a subfamily of Acn superfamily. It is encoded in the genomes of many archaea, proteobacteria and fungi. Among archaea, the pattern of aconitase X occurrence complements that of aconitase A such that together the two enzymes account for aconitase activity in all archaea. This protein catalyzes the dehydration of cis-3-hydroxy-L-proline to delta1-pyrroline-2-carboxylate.


Pssm-ID: 461297  Cd Length: 385  Bit Score: 540.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 151 LDLTDGDRAMLDGAESVAVAQAMRIISAMAAQQGALGLVDVTQAHIDGCIYAS--PANLTFAEKMVEMGAKVRIPATMNA 228
Cdd:pfam04412   1 MYLTDEEEAMLNGEYGEAVQKAMEILVALGEAFGAERLVPVTSAHVSGVSYKTigDAGLEFLEDLADMGAKVRVPTTLNP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 229 ISVDHANWQRQGVPPSFGDPAARLADAYVRMGCRPTFTCSPYLLDSAPGAGEAVAWAESNAVIFANSVLGARTAKHPDFL 308
Cdd:pfam04412  81 AGMDLERWRELGVDEEFAEKQLRIIDAYRRMGVEPTFTCTPYLLGNIPRFGEHLAWSESSAVVYANSVLGARTNREGGPS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 309 DLCIALTGRAPLSGVYLDEHRKARRIIDVElPAGADDAFWPLIGYLAGRAAPDRIPLIRGLAPaePSRDDLKALCAAFGT 388
Cdd:pfam04412 161 ALAAAITGRTPYYGLHLDENRKPTVLVDVE-AEGLDDADYGALGYLVGKKAGDRIPVFTGLEK--PSRDDLKALGAAMAT 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 389 TSAAPMLHVEGVTPEAGGAA-----VEDADHATITRAELTAAWSALNEGPDEVELVAIGSPHASLAECRALAEALGGRKR 463
Cdd:pfam04412 238 SGSVAMYHIVGVTPEAPTLEaafggRPPAERITITREDLEEVREELATGDEKVDLVALGCPHLSLEELRELARLLKGRKK 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 464 HPDVAVIVTAGHEVIAKARGEGILARLQESGVQVLPDLCWCsiSEPVFPTRTRAVMTNSGKYAHYGPGLS 533
Cdd:pfam04412 318 KPKVPLWVTTSREVYELAERMGYVERLERAGVKVLTDTCMV--VSPIIPRGYKNVMTNSGKAAHYLPGLG 385
AcnX cd01355
Putative Aconitase X catalytic domain; Putative Aconitase X catalytic domain. It is predicted ...
158-549 2.03e-170

Putative Aconitase X catalytic domain; Putative Aconitase X catalytic domain. It is predicted by comparative genomic analysis. The proteins are mainly found in archaea and proteobacteria. They are distantly related to Aconitase family of proteins by sequence similarity and seconary structure prediction. The functions have not yet been experimentally characterized. Thus, the prediction should be treated with caution.


Pssm-ID: 153130  Cd Length: 389  Bit Score: 488.03  E-value: 2.03e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 158 RAMLDGAESVAVAQAMRIISAMAAQQGALGLVDVTQAHIDGCIYA--SPANLTFAEKMVEMGAKVRIPATMNAISVDHAn 235
Cdd:cd01355     1 EAILNGEYGEAVAKAMEILVAVGELYGAERLIDIKSAHISGVSYKtiGDAGLEFLERLADQGAKVAVPTTLNPISMDLH- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 236 WQRQGVPPSFGDPAARLADAYVRMGCRPTFTCSPYLLDSAPGAGEAVAWAESNAVIFANSVLGARTAKHPDFLDLCIALT 315
Cdd:cd01355    80 WRELGVDEEFAEKQARLVKAYKAMGVDPTFTCTPYQLENLPKKGEHIAWAESSAVVYANSVLGARTNREGGPSALAAAIT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 316 GRAPLSGVYLDEHRKARRIIDVELPAGADDAFWPLIGYLAGRAAPDRIPLIRGLaPAEPSRDDLKALCAAFGTTSAAPML 395
Cdd:cd01355   160 GRTPEYGVHLDENRKARLIVEVEAAEPLDDSDYGALGYLVGKIAGDRIPVITGL-DARPSEDELKALGAAMATSGSVAMF 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 396 HVEGVTPEAGGAAVEDADHATITRAELTAAWSALNEGPDEVELVAIGSPHASLAECRALAEALGGRKRHPDVAVIVTAGH 475
Cdd:cd01355   239 HIVGVTPEAPTLGLDAAETVELTRADLDEARENLNADGSEPDLVVLGCPHASLEELRKLADLLAGRRVAPSVPLYVTTSR 318
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550003857 476 EVIAKARGEgiLARLQESGVQVLPDLCWCsISEPVFPTRTRAVMTNSGKYAHYGPGLSGRTVRFGSLADCVSAA 549
Cdd:cd01355   319 AVYAKRMGY--VDVIEKLGARVLTDTCMV-VSPVNEPNGYKNVMTNSGKAAHYLPGNTGVEVAFGELEDCIEAA 389
AcnX2 COG1786
Mevalonate 5-phosphate dehydratase subunit 2, swiveling domain (modified mevalonate pathway) ...
7-134 1.43e-41

Mevalonate 5-phosphate dehydratase subunit 2, swiveling domain (modified mevalonate pathway) [Lipid transport and metabolism];


Pssm-ID: 441392 [Multi-domain]  Cd Length: 131  Bit Score: 146.11  E-value: 1.43e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857   7 ARSILQGSAEGPVIATGEALSFWGGVDPATGCVIDVHHPLHGVPLTGSILMMPSSRGSCTGSGVLLDLVLTGRGPAALVF 86
Cdd:COG1786     4 GRKIVGGKAEGEALVSDEPISFLGGVDPKTGVVIDPGHPLYGQSIAGKILVFPTGKGSTVGSYVLYELKKNGTAPAAIIF 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1550003857  87 SEPEDVLTLGALIASemfgkpLPVLRLAPEA-FAALARAKTARI-GDRAI 134
Cdd:COG1786    84 READPILALGAIVAG------IPLVDLFDEDpFEAIKTGDRVRVdADEGT 127
AcnX_swivel cd01356
Putative Aconitase X swivel domain. It is predicted by comparative genomic analysis. The ...
10-114 1.22e-36

Putative Aconitase X swivel domain. It is predicted by comparative genomic analysis. The proteins are mainly found in archaea and proteobacteria. They are distantly related to Aconitase family of proteins by sequence similarity and seconary structure prediction. The functions have not yet been experimentally characterized. Thus, the prediction should be treated with caution.


Pssm-ID: 238658  Cd Length: 123  Bit Score: 132.45  E-value: 1.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857  10 ILQGSAEGPVIATGEALSFWGGVDPATGCVIDVHHPLHGVPLTGSILMMPSSRGSCTGSGVLLDLVLTGRGPAALVFSEP 89
Cdd:cd01356     1 IVRGRVEGEALVSREPLSFWGGVDPETGKVIDPHHPLYGESIAGKVLVLPGGKGSTVGSYVLYELARNGTAPAAIVFEEA 80
                          90       100
                  ....*....|....*....|....*
gi 1550003857  90 EDVLTLGALIASEMFGKPLPVLRLA 114
Cdd:cd01356    81 EPILAAGAILAGIPLVDSLPEVLFE 105
AcnX_swivel_put pfam01989
Aconitase X swivel domain; This is a putative aconitase X swivel domain, which has been ...
31-101 2.13e-27

Aconitase X swivel domain; This is a putative aconitase X swivel domain, which has been predicted by comparative genomic analysis. The domain is mainly found in archaeal and proteobacterial proteins. As such, the prediction should be treated with caution. One member of this entry from Aeropyrum pernix which has been annotated as a putative aconitase, has been characterized in vitro and catalyzes the dehydration of mevalonate 5-phosphate to form trans-anhydromevalonate 5-phosphate, a previously unknown intermediate, being involved in a "modified" mevalonate pathway.


Pssm-ID: 426551  Cd Length: 75  Bit Score: 104.86  E-value: 2.13e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550003857  31 GVDPATGCVIDVHHPLHGVPLTGSILMMPSSRGSCTGSGVLLDLVLTGRGPAALVFSEPEDVLTLGALIAS 101
Cdd:pfam01989   1 GVDPETGVVIDPGHPLYGQSIAGKILVFPGGKGSTVGSYVLYELKKNGTAPAAIIFREADPILALGAIVAG 71
PRK03955 PRK03955
DUF126 domain-containing protein;
8-100 2.57e-22

DUF126 domain-containing protein;


Pssm-ID: 179684 [Multi-domain]  Cd Length: 131  Bit Score: 92.73  E-value: 2.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857   8 RSILQGSAEGPVIATGEALSFWGGVDPATGCVIDVHHPLHGVPLTGSILMMPSSRGSCTGSGVLLDLVLTGRGPAALVFS 87
Cdd:PRK03955    6 RIISKGKAEGEVIVSKKPISFLGGVDPETGIVIDKEHDLYGESIKGKILVFPHGKGSTVGSYVIYQLAKNGTAPKAIINL 85
                          90
                  ....*....|...
gi 1550003857  88 EPEDVLTLGALIA 100
Cdd:PRK03955   86 EAEPIVATGAIIS 98
 
Name Accession Description Interval E-value
AcnX1 COG1679
Mevalonate 5-phosphate dehydratase subunit 1, aconitase superfamily (modified mevalonate ...
151-558 0e+00

Mevalonate 5-phosphate dehydratase subunit 1, aconitase superfamily (modified mevalonate pathway) [Lipid transport and metabolism];


Pssm-ID: 441285  Cd Length: 411  Bit Score: 574.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 151 LDLTDGDRAMLDGAESVAVAQAMRIISAMAAQQGALGLVDVTQAHIDGCIYAS--PANLTFAEKMVEMGAKVRIPATMNA 228
Cdd:COG1679     1 MKLTDEEEAMLDGEHGEAKQKAMEILVALGEALGAERLVPITSAHISGVSYKTigDAGLEFLEELADMGAKVRVPTTLNP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 229 ISVDHANWQRQGVPPSFGDPAARLADAYVRMGCRPTFTCSPYLLDSAPGAGEAVAWAESNAVIFANSVLGARTAKHPDFL 308
Cdd:COG1679    81 IGMDLENWEEMGVPEEFAEKQRRIIDAYERMGVRPTFTCTPYLLGNIPRFGEHVAWAESSAVIYANSVLGARTNREGGPS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 309 DLCIALTGRAPLSGVYLDEHRKARRIIDVELP-AGADDafWPLIGYLAGRAAPDRIPLIRGLaPAEPSRDDLKALCAAFG 387
Cdd:COG1679   161 ALAAAITGRTPLYGLHLDENRRPTVLIDVDAPlEGVSD--WGALGYLVGRLAGDRVPVITGL-PRRPTEDQLKALGAAMA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 388 TTSAAPMLHVEGVTPEA-----GGAAVEDADHATITRAELTAAWSALNEGPDEVELVAIGSPHASLAECRALAEALGGRK 462
Cdd:COG1679   238 ASGAVALFHVVGVTPEAptleaAFGGRAPVETITITKADLREVYEELNTGEDDVDLVALGCPHLSLEELRELARLLEGRK 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 463 RHPDVAVIVTAGHEVIAKARGEGILARLQESGVQVLPDLCWCsiSEPVFPTRTRAVMTNSGKYAHYGPGLSGRTVRFGSL 542
Cdd:COG1679   318 VKKGVPLWVCTSRAVKAAADRMGYTAIIEAAGGKVLTDTCMV--VSPAEPMGYKVLATNSGKAAHYLPGLCGVKVRFGSL 395
                         410
                  ....*....|....*.
gi 1550003857 543 ADCVSAALSGRVPPRL 558
Cdd:COG1679   396 AECVEAAVTGRWEGEL 411
AcnX pfam04412
Aconitase X; Aconitase X (AcnX) is a subfamily of Acn superfamily. It is encoded in the ...
151-533 0e+00

Aconitase X; Aconitase X (AcnX) is a subfamily of Acn superfamily. It is encoded in the genomes of many archaea, proteobacteria and fungi. Among archaea, the pattern of aconitase X occurrence complements that of aconitase A such that together the two enzymes account for aconitase activity in all archaea. This protein catalyzes the dehydration of cis-3-hydroxy-L-proline to delta1-pyrroline-2-carboxylate.


Pssm-ID: 461297  Cd Length: 385  Bit Score: 540.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 151 LDLTDGDRAMLDGAESVAVAQAMRIISAMAAQQGALGLVDVTQAHIDGCIYAS--PANLTFAEKMVEMGAKVRIPATMNA 228
Cdd:pfam04412   1 MYLTDEEEAMLNGEYGEAVQKAMEILVALGEAFGAERLVPVTSAHVSGVSYKTigDAGLEFLEDLADMGAKVRVPTTLNP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 229 ISVDHANWQRQGVPPSFGDPAARLADAYVRMGCRPTFTCSPYLLDSAPGAGEAVAWAESNAVIFANSVLGARTAKHPDFL 308
Cdd:pfam04412  81 AGMDLERWRELGVDEEFAEKQLRIIDAYRRMGVEPTFTCTPYLLGNIPRFGEHLAWSESSAVVYANSVLGARTNREGGPS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 309 DLCIALTGRAPLSGVYLDEHRKARRIIDVElPAGADDAFWPLIGYLAGRAAPDRIPLIRGLAPaePSRDDLKALCAAFGT 388
Cdd:pfam04412 161 ALAAAITGRTPYYGLHLDENRKPTVLVDVE-AEGLDDADYGALGYLVGKKAGDRIPVFTGLEK--PSRDDLKALGAAMAT 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 389 TSAAPMLHVEGVTPEAGGAA-----VEDADHATITRAELTAAWSALNEGPDEVELVAIGSPHASLAECRALAEALGGRKR 463
Cdd:pfam04412 238 SGSVAMYHIVGVTPEAPTLEaafggRPPAERITITREDLEEVREELATGDEKVDLVALGCPHLSLEELRELARLLKGRKK 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 464 HPDVAVIVTAGHEVIAKARGEGILARLQESGVQVLPDLCWCsiSEPVFPTRTRAVMTNSGKYAHYGPGLS 533
Cdd:pfam04412 318 KPKVPLWVTTSREVYELAERMGYVERLERAGVKVLTDTCMV--VSPIIPRGYKNVMTNSGKAAHYLPGLG 385
AcnX cd01355
Putative Aconitase X catalytic domain; Putative Aconitase X catalytic domain. It is predicted ...
158-549 2.03e-170

Putative Aconitase X catalytic domain; Putative Aconitase X catalytic domain. It is predicted by comparative genomic analysis. The proteins are mainly found in archaea and proteobacteria. They are distantly related to Aconitase family of proteins by sequence similarity and seconary structure prediction. The functions have not yet been experimentally characterized. Thus, the prediction should be treated with caution.


Pssm-ID: 153130  Cd Length: 389  Bit Score: 488.03  E-value: 2.03e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 158 RAMLDGAESVAVAQAMRIISAMAAQQGALGLVDVTQAHIDGCIYA--SPANLTFAEKMVEMGAKVRIPATMNAISVDHAn 235
Cdd:cd01355     1 EAILNGEYGEAVAKAMEILVAVGELYGAERLIDIKSAHISGVSYKtiGDAGLEFLERLADQGAKVAVPTTLNPISMDLH- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 236 WQRQGVPPSFGDPAARLADAYVRMGCRPTFTCSPYLLDSAPGAGEAVAWAESNAVIFANSVLGARTAKHPDFLDLCIALT 315
Cdd:cd01355    80 WRELGVDEEFAEKQARLVKAYKAMGVDPTFTCTPYQLENLPKKGEHIAWAESSAVVYANSVLGARTNREGGPSALAAAIT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 316 GRAPLSGVYLDEHRKARRIIDVELPAGADDAFWPLIGYLAGRAAPDRIPLIRGLaPAEPSRDDLKALCAAFGTTSAAPML 395
Cdd:cd01355   160 GRTPEYGVHLDENRKARLIVEVEAAEPLDDSDYGALGYLVGKIAGDRIPVITGL-DARPSEDELKALGAAMATSGSVAMF 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857 396 HVEGVTPEAGGAAVEDADHATITRAELTAAWSALNEGPDEVELVAIGSPHASLAECRALAEALGGRKRHPDVAVIVTAGH 475
Cdd:cd01355   239 HIVGVTPEAPTLGLDAAETVELTRADLDEARENLNADGSEPDLVVLGCPHASLEELRKLADLLAGRRVAPSVPLYVTTSR 318
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550003857 476 EVIAKARGEgiLARLQESGVQVLPDLCWCsISEPVFPTRTRAVMTNSGKYAHYGPGLSGRTVRFGSLADCVSAA 549
Cdd:cd01355   319 AVYAKRMGY--VDVIEKLGARVLTDTCMV-VSPVNEPNGYKNVMTNSGKAAHYLPGNTGVEVAFGELEDCIEAA 389
AcnX2 COG1786
Mevalonate 5-phosphate dehydratase subunit 2, swiveling domain (modified mevalonate pathway) ...
7-134 1.43e-41

Mevalonate 5-phosphate dehydratase subunit 2, swiveling domain (modified mevalonate pathway) [Lipid transport and metabolism];


Pssm-ID: 441392 [Multi-domain]  Cd Length: 131  Bit Score: 146.11  E-value: 1.43e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857   7 ARSILQGSAEGPVIATGEALSFWGGVDPATGCVIDVHHPLHGVPLTGSILMMPSSRGSCTGSGVLLDLVLTGRGPAALVF 86
Cdd:COG1786     4 GRKIVGGKAEGEALVSDEPISFLGGVDPKTGVVIDPGHPLYGQSIAGKILVFPTGKGSTVGSYVLYELKKNGTAPAAIIF 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1550003857  87 SEPEDVLTLGALIASemfgkpLPVLRLAPEA-FAALARAKTARI-GDRAI 134
Cdd:COG1786    84 READPILALGAIVAG------IPLVDLFDEDpFEAIKTGDRVRVdADEGT 127
AcnX_swivel cd01356
Putative Aconitase X swivel domain. It is predicted by comparative genomic analysis. The ...
10-114 1.22e-36

Putative Aconitase X swivel domain. It is predicted by comparative genomic analysis. The proteins are mainly found in archaea and proteobacteria. They are distantly related to Aconitase family of proteins by sequence similarity and seconary structure prediction. The functions have not yet been experimentally characterized. Thus, the prediction should be treated with caution.


Pssm-ID: 238658  Cd Length: 123  Bit Score: 132.45  E-value: 1.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857  10 ILQGSAEGPVIATGEALSFWGGVDPATGCVIDVHHPLHGVPLTGSILMMPSSRGSCTGSGVLLDLVLTGRGPAALVFSEP 89
Cdd:cd01356     1 IVRGRVEGEALVSREPLSFWGGVDPETGKVIDPHHPLYGESIAGKVLVLPGGKGSTVGSYVLYELARNGTAPAAIVFEEA 80
                          90       100
                  ....*....|....*....|....*
gi 1550003857  90 EDVLTLGALIASEMFGKPLPVLRLA 114
Cdd:cd01356    81 EPILAAGAILAGIPLVDSLPEVLFE 105
AcnX_swivel_put pfam01989
Aconitase X swivel domain; This is a putative aconitase X swivel domain, which has been ...
31-101 2.13e-27

Aconitase X swivel domain; This is a putative aconitase X swivel domain, which has been predicted by comparative genomic analysis. The domain is mainly found in archaeal and proteobacterial proteins. As such, the prediction should be treated with caution. One member of this entry from Aeropyrum pernix which has been annotated as a putative aconitase, has been characterized in vitro and catalyzes the dehydration of mevalonate 5-phosphate to form trans-anhydromevalonate 5-phosphate, a previously unknown intermediate, being involved in a "modified" mevalonate pathway.


Pssm-ID: 426551  Cd Length: 75  Bit Score: 104.86  E-value: 2.13e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550003857  31 GVDPATGCVIDVHHPLHGVPLTGSILMMPSSRGSCTGSGVLLDLVLTGRGPAALVFSEPEDVLTLGALIAS 101
Cdd:pfam01989   1 GVDPETGVVIDPGHPLYGQSIAGKILVFPGGKGSTVGSYVLYELKKNGTAPAAIIFREADPILALGAIVAG 71
PRK03955 PRK03955
DUF126 domain-containing protein;
8-100 2.57e-22

DUF126 domain-containing protein;


Pssm-ID: 179684 [Multi-domain]  Cd Length: 131  Bit Score: 92.73  E-value: 2.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550003857   8 RSILQGSAEGPVIATGEALSFWGGVDPATGCVIDVHHPLHGVPLTGSILMMPSSRGSCTGSGVLLDLVLTGRGPAALVFS 87
Cdd:PRK03955    6 RIISKGKAEGEVIVSKKPISFLGGVDPETGIVIDKEHDLYGESIKGKILVFPHGKGSTVGSYVIYQLAKNGTAPKAIINL 85
                          90
                  ....*....|...
gi 1550003857  88 EPEDVLTLGALIA 100
Cdd:PRK03955   86 EAEPIVATGAIIS 98
 
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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