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Conserved domains on  [gi|1490707202|gb|RLC82363|]
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hypothetical protein DRI81_00065 [Chloroflexi bacterium]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Aconitase_swivel super family cl00215
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ...
1-126 5.01e-56

Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. The aconitase family contains the following proteins: - Iron-responsive element binding protein (IRE-BP). IRE-BP is a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.


The actual alignment was detected with superfamily member PRK03955:

Pssm-ID: 469664 [Multi-domain]  Cd Length: 131  Bit Score: 170.54  E-value: 5.01e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707202   1 MSVPARIVKDGWVEGEALVSPEPLGFLGGVDPDTGVVIEAGHSLEGQCVTGRVLVFPTGKGSTVGSYTLYRLARNKAAPA 80
Cdd:PRK03955    1 MELKGRIISKGKAEGEVIVSKKPISFLGGVDPETGIVIDKEHDLYGESIKGKILVFPHGKGSTVGSYVIYQLAKNGTAPK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1490707202  81 AIINAEADPVVAVGAIIAEIPMLDQVDVTLIHTGDWVRI--RDGEIQV 126
Cdd:PRK03955   81 AIINLEAEPIVATGAIISGIPLVDKVDISKLKDGDRVVVdgDEGEVEI 128
 
Name Accession Description Interval E-value
PRK03955 PRK03955
DUF126 domain-containing protein;
1-126 5.01e-56

DUF126 domain-containing protein;


Pssm-ID: 179684 [Multi-domain]  Cd Length: 131  Bit Score: 170.54  E-value: 5.01e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707202   1 MSVPARIVKDGWVEGEALVSPEPLGFLGGVDPDTGVVIEAGHSLEGQCVTGRVLVFPTGKGSTVGSYTLYRLARNKAAPA 80
Cdd:PRK03955    1 MELKGRIISKGKAEGEVIVSKKPISFLGGVDPETGIVIDKEHDLYGESIKGKILVFPHGKGSTVGSYVIYQLAKNGTAPK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1490707202  81 AIINAEADPVVAVGAIIAEIPMLDQVDVTLIHTGDWVRI--RDGEIQV 126
Cdd:PRK03955   81 AIINLEAEPIVATGAIISGIPLVDKVDISKLKDGDRVVVdgDEGEVEI 128
AcnX2 COG1786
Mevalonate 5-phosphate dehydratase subunit 2, swiveling domain (modified mevalonate pathway) ...
5-127 4.06e-54

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: 165.76  E-value: 4.06e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707202   5 ARIVKDGWVEGEALVSPEPLGFLGGVDPDTGVVIEAGHSLEGQCVTGRVLVFPTGKGSTVGSYTLYRLARNKAAPAAIIN 84
Cdd:COG1786     4 GRKIVGGKAEGEALVSDEPISFLGGVDPKTGVVIDPGHPLYGQSIAGKILVFPTGKGSTVGSYVLYELKKNGTAPAAIIF 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1490707202  85 AEADPVVAVGAIIAEIPMLDQVDV---TLIHTGDWVRIRDGEIQVR 127
Cdd:COG1786    84 READPILALGAIVAGIPLVDLFDEdpfEAIKTGDRVRVDADEGTVE 129
AcnX_swivel cd01356
Putative Aconitase X swivel domain. It is predicted by comparative genomic analysis. The ...
11-120 1.32e-40

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: 131.29  E-value: 1.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707202  11 GWVEGEALVSPEPLGFLGGVDPDTGVVIEAGHSLEGQCVTGRVLVFPTGKGSTVGSYTLYRLARNKAAPAAIINAEADPV 90
Cdd:cd01356     4 GRVEGEALVSREPLSFWGGVDPETGKVIDPHHPLYGESIAGKVLVLPGGKGSTVGSYVLYELARNGTAPAAIVFEEAEPI 83
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1490707202  91 VAVGAIIAEIPM---LDQVDVTLIHTGDWVRIR 120
Cdd:cd01356    84 LAAGAILAGIPLvdsLPEVLFEALKDGDRVRGG 116
AcnX_swivel_put pfam01989
Aconitase X swivel domain; This is a putative aconitase X swivel domain, which has been ...
29-103 3.20e-36

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: 118.73  E-value: 3.20e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490707202  29 GVDPDTGVVIEAGHSLEGQCVTGRVLVFPTGKGSTVGSYTLYRLARNKAAPAAIINAEADPVVAVGAIIAEIPML 103
Cdd:pfam01989   1 GVDPETGVVIDPGHPLYGQSIAGKILVFPGGKGSTVGSYVLYELKKNGTAPAAIIFREADPILALGAIVAGIPLV 75
 
Name Accession Description Interval E-value
PRK03955 PRK03955
DUF126 domain-containing protein;
1-126 5.01e-56

DUF126 domain-containing protein;


Pssm-ID: 179684 [Multi-domain]  Cd Length: 131  Bit Score: 170.54  E-value: 5.01e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707202   1 MSVPARIVKDGWVEGEALVSPEPLGFLGGVDPDTGVVIEAGHSLEGQCVTGRVLVFPTGKGSTVGSYTLYRLARNKAAPA 80
Cdd:PRK03955    1 MELKGRIISKGKAEGEVIVSKKPISFLGGVDPETGIVIDKEHDLYGESIKGKILVFPHGKGSTVGSYVIYQLAKNGTAPK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1490707202  81 AIINAEADPVVAVGAIIAEIPMLDQVDVTLIHTGDWVRI--RDGEIQV 126
Cdd:PRK03955   81 AIINLEAEPIVATGAIISGIPLVDKVDISKLKDGDRVVVdgDEGEVEI 128
AcnX2 COG1786
Mevalonate 5-phosphate dehydratase subunit 2, swiveling domain (modified mevalonate pathway) ...
5-127 4.06e-54

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: 165.76  E-value: 4.06e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707202   5 ARIVKDGWVEGEALVSPEPLGFLGGVDPDTGVVIEAGHSLEGQCVTGRVLVFPTGKGSTVGSYTLYRLARNKAAPAAIIN 84
Cdd:COG1786     4 GRKIVGGKAEGEALVSDEPISFLGGVDPKTGVVIDPGHPLYGQSIAGKILVFPTGKGSTVGSYVLYELKKNGTAPAAIIF 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1490707202  85 AEADPVVAVGAIIAEIPMLDQVDV---TLIHTGDWVRIRDGEIQVR 127
Cdd:COG1786    84 READPILALGAIVAGIPLVDLFDEdpfEAIKTGDRVRVDADEGTVE 129
AcnX_swivel cd01356
Putative Aconitase X swivel domain. It is predicted by comparative genomic analysis. The ...
11-120 1.32e-40

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: 131.29  E-value: 1.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707202  11 GWVEGEALVSPEPLGFLGGVDPDTGVVIEAGHSLEGQCVTGRVLVFPTGKGSTVGSYTLYRLARNKAAPAAIINAEADPV 90
Cdd:cd01356     4 GRVEGEALVSREPLSFWGGVDPETGKVIDPHHPLYGESIAGKVLVLPGGKGSTVGSYVLYELARNGTAPAAIVFEEAEPI 83
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1490707202  91 VAVGAIIAEIPM---LDQVDVTLIHTGDWVRIR 120
Cdd:cd01356    84 LAAGAILAGIPLvdsLPEVLFEALKDGDRVRGG 116
AcnX_swivel_put pfam01989
Aconitase X swivel domain; This is a putative aconitase X swivel domain, which has been ...
29-103 3.20e-36

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: 118.73  E-value: 3.20e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490707202  29 GVDPDTGVVIEAGHSLEGQCVTGRVLVFPTGKGSTVGSYTLYRLARNKAAPAAIINAEADPVVAVGAIIAEIPML 103
Cdd:pfam01989   1 GVDPETGVVIDPGHPLYGQSIAGKILVFPGGKGSTVGSYVLYELKKNGTAPAAIIFREADPILALGAIVAGIPLV 75
 
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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