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Conserved domains on  [gi|767914244|ref|XP_011531032|]
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3-hydroxyanthranilate 3,4-dioxygenase isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cupin_HAO cd06123
3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase ...
 1-125 9.03e-85

3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase (HAO or 3HAO) is a non-heme iron-dependent extradiol dioxygenase that catalyzes the oxidative ring opening of 3-hydroxyanthranilate (3-HAA) in the final enzymatic step of the kynurenine biosynthetic pathway in which tryptophan is converted to quinolinate, an endogenous neurotoxin, making HAO a target for pharmacological downregulation. Quinolate is also the universal de novo precursor to the pyridine ring of nicotinamide adenine dinucleotide. The enzyme forms homodimers, with two metal binding sites per molecule. One of the bound metal ions occupies the proposed ferrous-coordinated active site, which is located in a conserved double-strand beta-helix domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


:

Pssm-ID: 380378  Cd Length: 153  Bit Score: 249.33  E-value: 9.03e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914244   1 MFIGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPARVPHSPQRFANTVGLVVERRRLETELD 80
Cdd:cd06123   28 MVVGGPNSRKDFHINPGEEFFYQLKGDMVLKVIEPGKFKDVVIKEGEIFLLPARVPHSPQRPADTVGLVIERKRPPGELD 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767914244  81 GLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRTGKP 125
Cdd:cd06123  108 GLRWYCENCGELLHEVEFHCDDLGTQLKPAIEEFFASEELRTCKP 152
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 175-226 1.10e-03

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


The actual alignment was detected with superfamily member cd07006:

Pssm-ID: 477354 [Multi-domain]  Cd Length: 89  Bit Score: 37.34  E-value: 1.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767914244 175 TQVIAYGQ--GSSEGLRQNVDVWLWQLEGSSVVTMGGRRLSLAPDDSLLVLAGT 226
Cdd:cd07006   14 TMVLAPGDteGGPDNRHRGSDQWLYVVSGSGEAIVEGERVALKPGSLLLIEAGE 67
 
Name Accession Description Interval E-value
cupin_HAO cd06123
3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase ...
 1-125 9.03e-85

3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase (HAO or 3HAO) is a non-heme iron-dependent extradiol dioxygenase that catalyzes the oxidative ring opening of 3-hydroxyanthranilate (3-HAA) in the final enzymatic step of the kynurenine biosynthetic pathway in which tryptophan is converted to quinolinate, an endogenous neurotoxin, making HAO a target for pharmacological downregulation. Quinolate is also the universal de novo precursor to the pyridine ring of nicotinamide adenine dinucleotide. The enzyme forms homodimers, with two metal binding sites per molecule. One of the bound metal ions occupies the proposed ferrous-coordinated active site, which is located in a conserved double-strand beta-helix domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380378  Cd Length: 153  Bit Score: 249.33  E-value: 9.03e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914244   1 MFIGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPARVPHSPQRFANTVGLVVERRRLETELD 80
Cdd:cd06123   28 MVVGGPNSRKDFHINPGEEFFYQLKGDMVLKVIEPGKFKDVVIKEGEIFLLPARVPHSPQRPADTVGLVIERKRPPGELD 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767914244  81 GLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRTGKP 125
Cdd:cd06123  108 GLRWYCENCGELLHEVEFHCDDLGTQLKPAIEEFFASEELRTCKP 152
3-HAO pfam06052
3-hydroxyanthranilic acid dioxygenase; In eukaryotes 3-hydroxyanthranilic acid dioxygenase (EC: ...
 1-115 1.27e-75

3-hydroxyanthranilic acid dioxygenase; In eukaryotes 3-hydroxyanthranilic acid dioxygenase (EC:1.13.11.6) is part of the kynurenine pathway for the degradation of tryptophan and the biosynthesis of nicotinic acid.The prokaryotic homolog is involved in the 2-nitrobenzoate degradation pathway.


Pssm-ID: 399210  Cd Length: 151  Bit Score: 226.19  E-value: 1.27e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914244    1 MFIGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPARVPHSPQRFANTVGLVVERRRLETELD 80
Cdd:pfam06052  37 MIVGGPNERTDYHIEEGPEWFYQLKGDMVLKVVDEGDARDIVIRQGEIFLLPARVPHSPQRFANTVGLVVERERLGTEND 116

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767914244   81 GLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFF 115
Cdd:pfam06052 117 GLRWYCGHCNQVLFESWFYLLDLGTQLPPAILEFY 151
PRK13264 PRK13264
3-hydroxyanthranilate 3,4-dioxygenase; Provisional
 1-122 5.19e-54

3-hydroxyanthranilate 3,4-dioxygenase; Provisional


Pssm-ID: 183930  Cd Length: 177  Bit Score: 172.02  E-value: 5.19e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914244   1 MFIGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPARVPHSPQRFANTVGLVVERRRLETELD 80
Cdd:PRK13264  38 MVVGGPNARTDFHYDPGEEFFYQLEGDMYLKVQEDGKRRDVPIREGEMFLLPPHVPHSPQREAGSIGLVIERKRPEGELD 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767914244  81 GLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRT 122
Cdd:PRK13264 118 GFQWYCDECNHKVHEVEVQLTDIETDLPPVFAAFYASEELRT 159
anthran_nbaC TIGR03037
3-hydroxyanthranilate 3,4-dioxygenase; Members of this protein family, from both bacteria and ...
 1-124 2.05e-49

3-hydroxyanthranilate 3,4-dioxygenase; Members of this protein family, from both bacteria and eukaryotes, are the enzyme 3-hydroxyanthranilate 3,4-dioxygenase. This enzyme acts on the tryptophan metabolite 3-hydroxyanthranilate and produces 2-amino-3-carboxymuconate semialdehyde, which can rearrange spontaneously to quinolinic acid and feed into nicotinamide biosynthesis, or undergo further enzymatic degradation.


Pssm-ID: 132082  Cd Length: 159  Bit Score: 159.55  E-value: 2.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914244    1 MFIGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPARVPHSPQRFANTVGLVVERRRLETELD 80
Cdd:TIGR03037  32 TVVGGPNARTDFHDDPGEEFFYQLKGEMYLKVTEEGKREDVPIREGDIFLLPPHVPHSPQRPAGSIGLVIERKRPQGELD 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 767914244   81 GLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRTGK 124
Cdd:TIGR03037 112 GFQWFCPQCGHKLHRAEVQLENIVTDLPPVFEHFYSNEDARTCK 155
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
6-58 3.04e-04

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 39.06  E-value: 3.04e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767914244   6 PNTRKDYHIEEGEEVFYQLEGdmVLRVLEQGKhrDVVIRQGEIFLLPARVPHS 58
Cdd:COG1917   32 PGARTPWHSHPGEELIYVLEG--EGEVEVGGE--EYELKPGDVVFIPPGVPHA 80
cupin_XcTcmJ-like cd07006
Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes ...
 175-226 1.10e-03

Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to plant pathogen Xanthomonas campestris tetracenomycin polyketide synthesis protein XcTcmJ, a protein encoded by the tcmJ gene. XcTcmJ is annotated as being involved in tetracenomycin polyketide biosynthesis. Also included is Xc5357 from a different strain of X. campestris. Structure studies show that binding of zinc induces conformational changes and serves a functional role in this cupin protein. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380409 [Multi-domain]  Cd Length: 89  Bit Score: 37.34  E-value: 1.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767914244 175 TQVIAYGQ--GSSEGLRQNVDVWLWQLEGSSVVTMGGRRLSLAPDDSLLVLAGT 226
Cdd:cd07006   14 TMVLAPGDteGGPDNRHRGSDQWLYVVSGSGEAIVEGERVALKPGSLLLIEAGE 67
 
Name Accession Description Interval E-value
cupin_HAO cd06123
3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase ...
 1-125 9.03e-85

3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase (HAO or 3HAO) is a non-heme iron-dependent extradiol dioxygenase that catalyzes the oxidative ring opening of 3-hydroxyanthranilate (3-HAA) in the final enzymatic step of the kynurenine biosynthetic pathway in which tryptophan is converted to quinolinate, an endogenous neurotoxin, making HAO a target for pharmacological downregulation. Quinolate is also the universal de novo precursor to the pyridine ring of nicotinamide adenine dinucleotide. The enzyme forms homodimers, with two metal binding sites per molecule. One of the bound metal ions occupies the proposed ferrous-coordinated active site, which is located in a conserved double-strand beta-helix domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380378  Cd Length: 153  Bit Score: 249.33  E-value: 9.03e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914244   1 MFIGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPARVPHSPQRFANTVGLVVERRRLETELD 80
Cdd:cd06123   28 MVVGGPNSRKDFHINPGEEFFYQLKGDMVLKVIEPGKFKDVVIKEGEIFLLPARVPHSPQRPADTVGLVIERKRPPGELD 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767914244  81 GLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRTGKP 125
Cdd:cd06123  108 GLRWYCENCGELLHEVEFHCDDLGTQLKPAIEEFFASEELRTCKP 152
3-HAO pfam06052
3-hydroxyanthranilic acid dioxygenase; In eukaryotes 3-hydroxyanthranilic acid dioxygenase (EC: ...
 1-115 1.27e-75

3-hydroxyanthranilic acid dioxygenase; In eukaryotes 3-hydroxyanthranilic acid dioxygenase (EC:1.13.11.6) is part of the kynurenine pathway for the degradation of tryptophan and the biosynthesis of nicotinic acid.The prokaryotic homolog is involved in the 2-nitrobenzoate degradation pathway.


Pssm-ID: 399210  Cd Length: 151  Bit Score: 226.19  E-value: 1.27e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914244    1 MFIGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPARVPHSPQRFANTVGLVVERRRLETELD 80
Cdd:pfam06052  37 MIVGGPNERTDYHIEEGPEWFYQLKGDMVLKVVDEGDARDIVIRQGEIFLLPARVPHSPQRFANTVGLVVERERLGTEND 116

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767914244   81 GLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFF 115
Cdd:pfam06052 117 GLRWYCGHCNQVLFESWFYLLDLGTQLPPAILEFY 151
PRK13264 PRK13264
3-hydroxyanthranilate 3,4-dioxygenase; Provisional
 1-122 5.19e-54

3-hydroxyanthranilate 3,4-dioxygenase; Provisional


Pssm-ID: 183930  Cd Length: 177  Bit Score: 172.02  E-value: 5.19e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914244   1 MFIGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPARVPHSPQRFANTVGLVVERRRLETELD 80
Cdd:PRK13264  38 MVVGGPNARTDFHYDPGEEFFYQLEGDMYLKVQEDGKRRDVPIREGEMFLLPPHVPHSPQREAGSIGLVIERKRPEGELD 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767914244  81 GLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRT 122
Cdd:PRK13264 118 GFQWYCDECNHKVHEVEVQLTDIETDLPPVFAAFYASEELRT 159
anthran_nbaC TIGR03037
3-hydroxyanthranilate 3,4-dioxygenase; Members of this protein family, from both bacteria and ...
 1-124 2.05e-49

3-hydroxyanthranilate 3,4-dioxygenase; Members of this protein family, from both bacteria and eukaryotes, are the enzyme 3-hydroxyanthranilate 3,4-dioxygenase. This enzyme acts on the tryptophan metabolite 3-hydroxyanthranilate and produces 2-amino-3-carboxymuconate semialdehyde, which can rearrange spontaneously to quinolinic acid and feed into nicotinamide biosynthesis, or undergo further enzymatic degradation.


Pssm-ID: 132082  Cd Length: 159  Bit Score: 159.55  E-value: 2.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914244    1 MFIGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPARVPHSPQRFANTVGLVVERRRLETELD 80
Cdd:TIGR03037  32 TVVGGPNARTDFHDDPGEEFFYQLKGEMYLKVTEEGKREDVPIREGDIFLLPPHVPHSPQRPAGSIGLVIERKRPQGELD 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 767914244   81 GLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRTGK 124
Cdd:TIGR03037 112 GFQWFCPQCGHKLHRAEVQLENIVTDLPPVFEHFYSNEDARTCK 155
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
 6-58 4.47e-06

Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLL4011, a Bradyrhizobium diazoefficiens protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380363 [Multi-domain]  Cd Length: 100  Bit Score: 44.11  E-value: 4.47e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767914244   6 PNTRKDYHIEEGEEVFYQLEGDMVLRVleQGKhRDVVIRQGEIFLLPARVPHS 58
Cdd:cd02235   28 PGAVAGRHTHPGEESGYVLEGSLELEV--DGQ-PPVTLKAGDSFFIPAGTVHN 77
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 6-65 1.36e-04

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 39.39  E-value: 1.36e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767914244   6 PNTRKDYHI-EEGEEVFYQLEGDMVLRVLEQGKhrdVVIRQGEIFLLPARVPHSpqrFANT 65
Cdd:cd02208    8 PGTSSPPHWhPEQDEIFYVLSGEGELTLDDGET---VELKAGDIVLIPPGVPHS---FVNT 62
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
6-58 3.04e-04

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 39.06  E-value: 3.04e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767914244   6 PNTRKDYHIEEGEEVFYQLEGdmVLRVLEQGKhrDVVIRQGEIFLLPARVPHS 58
Cdd:COG1917   32 PGARTPWHSHPGEELIYVLEG--EGEVEVGGE--EYELKPGDVVFIPPGVPHA 80
cupin_YdbB-like cd02226
Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial ...
 15-59 3.89e-04

Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial proteins homologous to YdbB, a Bacillus subtilis protein of unknown function. It also includes protein Nmb1881 From Neisseria meningitidis, also of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380355 [Multi-domain]  Cd Length: 94  Bit Score: 38.58  E-value: 3.89e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767914244  15 EEGEEVFYQLEGDMVLRVleqgKHRDVVIRQGEIFLLPARVPHSP 59
Cdd:cd02226   41 DDEDELFLVLEGELTIDF----RDRDVTLGPGEFFVVPKGVEHRP 81
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
12-65 5.66e-04

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 38.46  E-value: 5.66e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767914244  12 YHiEEGEEVFYQLEGDMVLRVlEQGKHRdvvIRQGEIFLLPARVPHspqRFANT 65
Cdd:COG3837   46 AH-SAEEEFVYVLEGELTLRI-GGEEYV---LEPGDSVGFPAGVPH---RLRNR 91
cupin_XcTcmJ-like cd07006
Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes ...
 175-226 1.10e-03

Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to plant pathogen Xanthomonas campestris tetracenomycin polyketide synthesis protein XcTcmJ, a protein encoded by the tcmJ gene. XcTcmJ is annotated as being involved in tetracenomycin polyketide biosynthesis. Also included is Xc5357 from a different strain of X. campestris. Structure studies show that binding of zinc induces conformational changes and serves a functional role in this cupin protein. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380409 [Multi-domain]  Cd Length: 89  Bit Score: 37.34  E-value: 1.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767914244 175 TQVIAYGQ--GSSEGLRQNVDVWLWQLEGSSVVTMGGRRLSLAPDDSLLVLAGT 226
Cdd:cd07006   14 TMVLAPGDteGGPDNRHRGSDQWLYVVSGSGEAIVEGERVALKPGSLLLIEAGE 67
RmlC COG4101
Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only];
6-59 2.55e-03

Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only];


Pssm-ID: 443277  Cd Length: 146  Bit Score: 37.25  E-value: 2.55e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767914244   6 PNTR-KDYHIEEGEEVFYQLEGDMVLRVLEQGKHRdVVIRQGEIFLLPARVPHSP 59
Cdd:COG4101   55 PGARaKAHHHGEHETAIYVLSGRAETRYGERLEHR-VVTEPGDFIFIPPGVPHQE 108
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 6-65 2.72e-03

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 35.70  E-value: 2.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767914244    6 PNTRKDYHIEEGE-EVFYQLEGDMVLRVLEQgkhrDVVIRQGEIFLLPARVPHspqRFANT 65
Cdd:pfam07883   7 PGESSPPHRHPGEdEFFYVLEGEGELTVDGE----EVVLKAGDSVYFPAGVPH---RFRNT 60
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
6-65 3.56e-03

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 36.27  E-value: 3.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767914244   6 PNTRKDYHI-EEGEEVFYQLEGDMVLRVLEQgkhrDVVIRQGEIFLLPARVPHspqRFANT 65
Cdd:COG0662   36 PGAELSLHVhPHRDEFFYVLEGTGEVTIGDE----EVELKAGDSVYIPAGVPH---RLRNP 89
cupin_BLR2406-like cd02210
Bradyrhizobium japonicum BLR2406 and related proteins, cupin domain; This family includes ...
 6-59 7.08e-03

Bradyrhizobium japonicum BLR2406 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLR2406, a Bradyrhizobium japonicum protein of unknown function with a cupin beta barrel domain. Proteins in this subfamily appear to align closest to RmlC carbohydrate epimerase which is involved in dTDP-L-rhamnose production, and belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380340 [Multi-domain]  Cd Length: 98  Bit Score: 35.18  E-value: 7.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767914244   6 PNTRKDYHIEEGEE-VFYQLEGDMVLRVLEQGKHRDVViRQGEIFLLPARVPHSP 59
Cdd:cd02210   20 PGARTGAHHHGEHEtAIYVLSGRAETRYGDRLEHRAEA-GPGDFIYIPPGVPHQE 73
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 12-60 8.04e-03

Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 441743 [Multi-domain]  Cd Length: 115  Bit Score: 35.33  E-value: 8.04e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 767914244  12 YHIEEGEeVFYQLEGDMVLRVLEQ-GKHRDVVIRQGEIFLLPARVPHSPQ 60
Cdd:COG2140   20 WHPNAAE-WYYVLSGEARMTVQDPpGRARTVDVGPGDVVYVPPGYGHYII 68
 
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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