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Conserved domains on  [gi|297265885|ref|XP_001111024|]
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3-hydroxyanthranilate 3,4-dioxygenase isoform X2 [Macaca mulatta]

Protein Classification

3-hydroxyanthranilate 3,4-dioxygenase( domain architecture ID 14398376)

3-hydroxyanthranilate 3,4-dioxygenase 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

CATH:  2.60.120.10
Gene Ontology:  GO:0005506|GO:0000334|GO:0006569|GO:0043420|GO:0019805
PubMed:  14697267|19478949|32732435|15909978
SCOP:  3001825

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 ...
 23-173 2.39e-101

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: 293.24  E-value: 2.39e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265885  23 AWVEENRGSFQPPVCNKLMHQE-QLKVMFVGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPA 101
Cdd:cd06123    1 KWIEENRHLLKPPVGNKLLWQDsDFIVMVVGGPNSRKDFHINPGEEFFYQLKGDMVLKVIEPGKFKDVVIKEGEIFLLPA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297265885 102 RVPHSPQRFANTVGLVVERRRLETELDGLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRTGKP 173
Cdd:cd06123   81 RVPHSPQRPADTVGLVIERKRPPGELDGLRWYCENCGELLHEVEFHCDDLGTQLKPAIEEFFASEELRTCKP 152
 
Name Accession Description Interval E-value
cupin_HAO cd06123
3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase ...
 23-173 2.39e-101

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: 293.24  E-value: 2.39e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265885  23 AWVEENRGSFQPPVCNKLMHQE-QLKVMFVGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPA 101
Cdd:cd06123    1 KWIEENRHLLKPPVGNKLLWQDsDFIVMVVGGPNSRKDFHINPGEEFFYQLKGDMVLKVIEPGKFKDVVIKEGEIFLLPA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297265885 102 RVPHSPQRFANTVGLVVERRRLETELDGLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRTGKP 173
Cdd:cd06123   81 RVPHSPQRPADTVGLVIERKRPPGELDGLRWYCENCGELLHEVEFHCDDLGTQLKPAIEEFFASEELRTCKP 152
3-HAO pfam06052
3-hydroxyanthranilic acid dioxygenase; In eukaryotes 3-hydroxyanthranilic acid dioxygenase (EC: ...
 16-163 2.48e-97

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: 283.20  E-value: 2.48e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265885   16 ERRVGVRAWVEENRGSFQPPVCNKLMHQEQLKVMFVGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGE 95
Cdd:pfam06052   4 VTPINIDAWVKENRGLLKPPVCNKCLHQDGFKVMIVGGPNERTDYHIEEGPEWFYQLKGDMVLKVVDEGDARDIVIRQGE 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297265885   96 IFLLPARVPHSPQRFANTVGLVVERRRLETELDGLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFF 163
Cdd:pfam06052  84 IFLLPARVPHSPQRFANTVGLVVERERLGTENDGLRWYCGHCNQVLFESWFYLLDLGTQLPPAILEFY 151
PRK13264 PRK13264
3-hydroxyanthranilate 3,4-dioxygenase; Provisional
 23-170 1.45e-64

3-hydroxyanthranilate 3,4-dioxygenase; Provisional


Pssm-ID: 183930  Cd Length: 177  Bit Score: 200.53  E-value: 1.45e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265885  23 AWVEENRGSFQPPVCNKLMHQE-QLKVMFVGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPA 101
Cdd:PRK13264  11 KWIEEHRHLLKPPVGNKQIWQDsDFIVMVVGGPNARTDFHYDPGEEFFYQLEGDMYLKVQEDGKRRDVPIREGEMFLLPP 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297265885 102 RVPHSPQRFANTVGLVVERRRLETELDGLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRT 170
Cdd:PRK13264  91 HVPHSPQREAGSIGLVIERKRPEGELDGFQWYCDECNHKVHEVEVQLTDIETDLPPVFAAFYASEELRT 159
anthran_nbaC TIGR03037
3-hydroxyanthranilate 3,4-dioxygenase; Members of this protein family, from both bacteria and ...
 22-172 1.58e-56

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: 179.58  E-value: 1.58e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265885   22 RAWVEENRGSFQPPVCNKLMHQE-QLKVMFVGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLP 100
Cdd:TIGR03037   4 KKWIDEHKHLLKPPVGNQQIWQDsEFMVTVVGGPNARTDFHDDPGEEFFYQLKGEMYLKVTEEGKREDVPIREGDIFLLP 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297265885  101 ARVPHSPQRFANTVGLVVERRRLETELDGLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRTGK 172
Cdd:TIGR03037  84 PHVPHSPQRPAGSIGLVIERKRPQGELDGFQWFCPQCGHKLHRAEVQLENIVTDLPPVFEHFYSNEDARTCK 155
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
48-106 3.36e-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: 3.36e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 297265885  48 VMFVGGPNTRKDYHIEEGEEVFYQLEGdmVLRVLEQGKhrDVVIRQGEIFLLPARVPHS 106
Cdd:COG1917   26 VRVTFEPGARTPWHSHPGEELIYVLEG--EGEVEVGGE--EYELKPGDVVFIPPGVPHA 80
 
Name Accession Description Interval E-value
cupin_HAO cd06123
3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase ...
 23-173 2.39e-101

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: 293.24  E-value: 2.39e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265885  23 AWVEENRGSFQPPVCNKLMHQE-QLKVMFVGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPA 101
Cdd:cd06123    1 KWIEENRHLLKPPVGNKLLWQDsDFIVMVVGGPNSRKDFHINPGEEFFYQLKGDMVLKVIEPGKFKDVVIKEGEIFLLPA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297265885 102 RVPHSPQRFANTVGLVVERRRLETELDGLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRTGKP 173
Cdd:cd06123   81 RVPHSPQRPADTVGLVIERKRPPGELDGLRWYCENCGELLHEVEFHCDDLGTQLKPAIEEFFASEELRTCKP 152
3-HAO pfam06052
3-hydroxyanthranilic acid dioxygenase; In eukaryotes 3-hydroxyanthranilic acid dioxygenase (EC: ...
 16-163 2.48e-97

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: 283.20  E-value: 2.48e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265885   16 ERRVGVRAWVEENRGSFQPPVCNKLMHQEQLKVMFVGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGE 95
Cdd:pfam06052   4 VTPINIDAWVKENRGLLKPPVCNKCLHQDGFKVMIVGGPNERTDYHIEEGPEWFYQLKGDMVLKVVDEGDARDIVIRQGE 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297265885   96 IFLLPARVPHSPQRFANTVGLVVERRRLETELDGLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFF 163
Cdd:pfam06052  84 IFLLPARVPHSPQRFANTVGLVVERERLGTENDGLRWYCGHCNQVLFESWFYLLDLGTQLPPAILEFY 151
PRK13264 PRK13264
3-hydroxyanthranilate 3,4-dioxygenase; Provisional
 23-170 1.45e-64

3-hydroxyanthranilate 3,4-dioxygenase; Provisional


Pssm-ID: 183930  Cd Length: 177  Bit Score: 200.53  E-value: 1.45e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265885  23 AWVEENRGSFQPPVCNKLMHQE-QLKVMFVGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPA 101
Cdd:PRK13264  11 KWIEEHRHLLKPPVGNKQIWQDsDFIVMVVGGPNARTDFHYDPGEEFFYQLEGDMYLKVQEDGKRRDVPIREGEMFLLPP 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297265885 102 RVPHSPQRFANTVGLVVERRRLETELDGLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRT 170
Cdd:PRK13264  91 HVPHSPQREAGSIGLVIERKRPEGELDGFQWYCDECNHKVHEVEVQLTDIETDLPPVFAAFYASEELRT 159
anthran_nbaC TIGR03037
3-hydroxyanthranilate 3,4-dioxygenase; Members of this protein family, from both bacteria and ...
 22-172 1.58e-56

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: 179.58  E-value: 1.58e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265885   22 RAWVEENRGSFQPPVCNKLMHQE-QLKVMFVGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLP 100
Cdd:TIGR03037   4 KKWIDEHKHLLKPPVGNQQIWQDsEFMVTVVGGPNARTDFHDDPGEEFFYQLKGEMYLKVTEEGKREDVPIREGDIFLLP 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297265885  101 ARVPHSPQRFANTVGLVVERRRLETELDGLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRTGK 172
Cdd:TIGR03037  84 PHVPHSPQRPAGSIGLVIERKRPQGELDGFQWFCPQCGHKLHRAEVQLENIVTDLPPVFEHFYSNEDARTCK 155
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
 54-106 5.63e-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: 5.63e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 297265885  54 PNTRKDYHIEEGEEVFYQLEGDMVLRVleQGKhRDVVIRQGEIFLLPARVPHS 106
Cdd:cd02235   28 PGAVAGRHTHPGEESGYVLEGSLELEV--DGQ-PPVTLKAGDSFFIPAGTVHN 77
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 54-113 1.28e-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: 39.77  E-value: 1.28e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297265885  54 PNTRKDYHI-EEGEEVFYQLEGDMVLRVLEQGKhrdVVIRQGEIFLLPARVPHSpqrFANT 113
Cdd:cd02208    8 PGTSSPPHWhPEQDEIFYVLSGEGELTLDDGET---VELKAGDIVLIPPGVPHS---FVNT 62
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
48-106 3.36e-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: 3.36e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 297265885  48 VMFVGGPNTRKDYHIEEGEEVFYQLEGdmVLRVLEQGKhrDVVIRQGEIFLLPARVPHS 106
Cdd:COG1917   26 VRVTFEPGARTPWHSHPGEELIYVLEG--EGEVEVGGE--EYELKPGDVVFIPPGVPHA 80
cupin_YdbB-like cd02226
Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial ...
 63-107 5.75e-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: 38.19  E-value: 5.75e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 297265885  63 EEGEEVFYQLEGDMVLRVleqgKHRDVVIRQGEIFLLPARVPHSP 107
Cdd:cd02226   41 DDEDELFLVLEGELTIDF----RDRDVTLGPGEFFVVPKGVEHRP 81
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
60-113 5.79e-04

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 38.85  E-value: 5.79e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 297265885  60 YHiEEGEEVFYQLEGDMVLRVlEQGKHRdvvIRQGEIFLLPARVPHspqRFANT 113
Cdd:COG3837   46 AH-SAEEEFVYVLEGELTLRI-GGEEYV---LEPGDSVGFPAGVPH---RLRNR 91
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
45-113 2.82e-03

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 37.04  E-value: 2.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265885  45 QLKVMFVGgPNTRKDYHI-EEGEEVFYQLEGDMVLRVLEQgkhrDVVIRQGEIFLLPARVPHspqRFANT 113
Cdd:COG0662   28 SVKRITVP-PGAELSLHVhPHRDEFFYVLEGTGEVTIGDE----EVELKAGDSVYIPAGVPH---RLRNP 89
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 54-113 3.80e-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: 35.31  E-value: 3.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297265885   54 PNTRKDYHIEEGE-EVFYQLEGDMVLRVLEQgkhrDVVIRQGEIFLLPARVPHspqRFANT 113
Cdd:pfam07883   7 PGESSPPHRHPGEdEFFYVLEGEGELTVDGE----EVVLKAGDSVYFPAGVPH---RFRNT 60
RmlC COG4101
Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only];
54-107 4.01e-03

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


Pssm-ID: 443277  Cd Length: 146  Bit Score: 36.87  E-value: 4.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 297265885  54 PNTR-KDYHIEEGEEVFYQLEGDMVLRVLEQGKHRdVVIRQGEIFLLPARVPHSP 107
Cdd:COG4101   55 PGARaKAHHHGEHETAIYVLSGRAETRYGERLEHR-VVTEPGDFIFIPPGVPHQE 108
 
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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