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Conserved domains on  [gi|490365918|ref|WP_004245582|]
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MULTISPECIES: cupin domain-containing protein [Enterobacterales]

Protein Classification

cupin domain-containing protein( domain architecture ID 14388817)

cupin domain-containing protein similar to Yersinia enterocolitica KdgF, a pectin degradation protein that catalyzes the linearization of unsaturated uronates from both pectin and alginate, which are polysaccharides found in the cell walls of plants and brown algae, respectively, and represent an important source of carbon

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 26-113 1.02e-32

pectin degradation protein KdgF and related proteins, cupin domain; This family includes bacterial and archaeal pectin degradation protein KdgF that catalyzes the linearization of unsaturated uronates from both pectin and alginate, which are polysaccharides found in the cell walls of plants and brown algae, respectively, and represent an important source of carbon. These polysaccharides, mostly consisting of chains of uronates, can be metabolized by bacteria through a pathway of enzymatic steps to the key metabolite 2-keto-3-deoxygluconate (KDG). Pectin degradation is used by many plant-pathogenic bacteria during infection, and also, pectin and alginate can both represent abundant sources of carbohydrate for the production of biofuels. These proteins belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


:

Pssm-ID: 380366 [Multi-domain]  Cd Length: 104  Bit Score: 110.64  E-value: 1.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365918  26 IQAKFIHGSNFTM-AFWTFKTNAIIPEHKHEHETATSILKGSLKLTVNNRIVYLHAGDSFIIPSWAVHHAIALEPSEVID 104
Cdd:cd02238   16 VRRKILAGGEKLMlVEVRFEKGAVVPLHSHPHEQIGYVLSGRFEFTIGGETRILKPGDSYYIPPNVPHGAEALEDSVLLD 95


                 ....*....
gi 490365918 105 VYTPVREDY 113
Cdd:cd02238   96 VFSPPREDF 104
 
Name Accession Description Interval E-value
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 26-113 1.02e-32

pectin degradation protein KdgF and related proteins, cupin domain; This family includes bacterial and archaeal pectin degradation protein KdgF that catalyzes the linearization of unsaturated uronates from both pectin and alginate, which are polysaccharides found in the cell walls of plants and brown algae, respectively, and represent an important source of carbon. These polysaccharides, mostly consisting of chains of uronates, can be metabolized by bacteria through a pathway of enzymatic steps to the key metabolite 2-keto-3-deoxygluconate (KDG). Pectin degradation is used by many plant-pathogenic bacteria during infection, and also, pectin and alginate can both represent abundant sources of carbohydrate for the production of biofuels. These proteins belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380366 [Multi-domain]  Cd Length: 104  Bit Score: 110.64  E-value: 1.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365918  26 IQAKFIHGSNFTM-AFWTFKTNAIIPEHKHEHETATSILKGSLKLTVNNRIVYLHAGDSFIIPSWAVHHAIALEPSEVID 104
Cdd:cd02238   16 VRRKILAGGEKLMlVEVRFEKGAVVPLHSHPHEQIGYVLSGRFEFTIGGETRILKPGDSYYIPPNVPHGAEALEDSVLLD 95


                 ....*....
gi 490365918 105 VYTPVREDY 113
Cdd:cd02238   96 VFSPPREDF 104
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
14-110 3.79e-13

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 60.63  E-value: 3.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365918  14 MDLNRNEGEESKIQAKFIHGSNFTMAFWTFKTNAIIPEHKHEHETATSILKGSLKLTVNNRIVYLHAGDSFIIPSWAVHH 93
Cdd:COG1917    1 MRLAEIALTGVSVRVLADGEDELEVVRVTFEPGARTPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHA 80

                         90
                 ....*....|....*....
gi 490365918  94 AIAL--EPSEVIDVYTPVR 110
Cdd:COG1917   81 FRNLgdEPAVLLVVFSPGL 99
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 39-106 1.17e-12

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: 58.81  E-value: 1.17e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490365918   39 AFWTFKTNAIIPEHKHEHETATS-ILKGSLKLTVNNRIVYLHAGDSFIIPSWAVHHAIAL--EPSEVIDVY 106
Cdd:pfam07883   1 GLVTLPPGESSPPHRHPGEDEFFyVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTgdEPARLLDVY 71
PRK09943 PRK09943
HTH-type transcriptional regulator PuuR;
29-86 1.99e-03

HTH-type transcriptional regulator PuuR;


Pssm-ID: 182158 [Multi-domain]  Cd Length: 185  Bit Score: 36.31  E-value: 1.99e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490365918  29 KFIHGSN----FTMAFWTFKTNAIIPEH-KHEHETATSILKGSLKLTVNNRIVYLHAGDSFII 86
Cdd:PRK09943  96 KLVHNGNpnrtLAMIFETYQPGTTTGERiKHQGEEIGTVLEGEIVLTINGQDYHLVAGQSYAI 158
 
Name Accession Description Interval E-value
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 26-113 1.02e-32

pectin degradation protein KdgF and related proteins, cupin domain; This family includes bacterial and archaeal pectin degradation protein KdgF that catalyzes the linearization of unsaturated uronates from both pectin and alginate, which are polysaccharides found in the cell walls of plants and brown algae, respectively, and represent an important source of carbon. These polysaccharides, mostly consisting of chains of uronates, can be metabolized by bacteria through a pathway of enzymatic steps to the key metabolite 2-keto-3-deoxygluconate (KDG). Pectin degradation is used by many plant-pathogenic bacteria during infection, and also, pectin and alginate can both represent abundant sources of carbohydrate for the production of biofuels. These proteins belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380366 [Multi-domain]  Cd Length: 104  Bit Score: 110.64  E-value: 1.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365918  26 IQAKFIHGSNFTM-AFWTFKTNAIIPEHKHEHETATSILKGSLKLTVNNRIVYLHAGDSFIIPSWAVHHAIALEPSEVID 104
Cdd:cd02238   16 VRRKILAGGEKLMlVEVRFEKGAVVPLHSHPHEQIGYVLSGRFEFTIGGETRILKPGDSYYIPPNVPHGAEALEDSVLLD 95


                 ....*....
gi 490365918 105 VYTPVREDY 113
Cdd:cd02238   96 VFSPPREDF 104
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
14-110 3.79e-13

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 60.63  E-value: 3.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365918  14 MDLNRNEGEESKIQAKFIHGSNFTMAFWTFKTNAIIPEHKHEHETATSILKGSLKLTVNNRIVYLHAGDSFIIPSWAVHH 93
Cdd:COG1917    1 MRLAEIALTGVSVRVLADGEDELEVVRVTFEPGARTPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHA 80

                         90
                 ....*....|....*....
gi 490365918  94 AIAL--EPSEVIDVYTPVR 110
Cdd:COG1917   81 FRNLgdEPAVLLVVFSPGL 99
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 39-106 1.17e-12

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: 58.81  E-value: 1.17e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490365918   39 AFWTFKTNAIIPEHKHEHETATS-ILKGSLKLTVNNRIVYLHAGDSFIIPSWAVHHAIAL--EPSEVIDVY 106
Cdd:pfam07883   1 GLVTLPPGESSPPHRHPGEDEFFyVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTgdEPARLLDVY 71
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
32-117 6.01e-11

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 55.53  E-value: 6.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365918  32 HGSNFTMAFWTFKTNAIIPEHKHEHETATS-ILKGSLKLTVNNRIVYLHAGDSFIIPSWAVH--HAIALEPSEVIDVYTP 108
Cdd:COG0662   23 GGERLSVKRITVPPGAELSLHVHPHRDEFFyVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHrlRNPGDEPLELLEVQAP 102

                         90
                 ....*....|.
gi 490365918 109 --VREDYVARQ 117
Cdd:COG0662  103 ayLGEDDIVRE 113
cupin_PMI_typeII_C cd02213
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ...
 52-105 2.04e-06

Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal cupin domain of mannose-6-phosphate isomerases (MPIs) which have been classified broadly into two groups, type I and type II, based on domain organization. This family contains type II phosphomannose isomerase (also known as PMI-GDP, phosphomannose isomerase/GDP-D-mannose pyrophosphorylase), a bifunctional enzyme with two domains that catalyze the first and third steps in the GDP-mannose pathway in which fructose 6-phosphate is converted to GDP-D-mannose. The N-terminal domain catalyzes the first and rate-limiting step, the isomerization from D-fructose-6-phosphate to D-mannose-6-phosphate, while the C-terminal cupin domain (represented in this alignment model) converts mannose 1-phosphate to GDP-D-mannose in the final step of the reaction. Although these two domains occur together in one protein in most organisms, they occur as separate proteins in certain cyanobacterial organisms. Also, although type I and type II MPIs have no overall sequence similarity, they share a conserved catalytic motif.


Pssm-ID: 380343 [Multi-domain]  Cd Length: 126  Bit Score: 43.70  E-value: 2.04e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490365918  52 HKHEH--ETATsILKGSLKLTVNNRIVYLHAGDSFIIPSWAVH--HAIALEPSEVIDV 105
Cdd:cd02213   56 QRHHHrsEHWV-VVSGTAEVTLDGKEKLLKEGESIYIPKGTKHrlENPGKIPLEIIEV 112
cupin_QDO_N_C cd02215
quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known ...
 36-108 1.36e-05

quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known as quercetin 2,3-dioxygenase, 2,3QD, QDO and YxaG; EC 1.13.11.24), a mononuclear copper-dependent dioxygenase that catalyzes the cleavage of the flavonol quercetin (5,7,3',4'-tetrahydroxyflavonol) heterocyclic ring to produce 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. Bacillus subtilis quercetin 2,3-dioxygenase (QDO) is a homodimer that shows oxygenase activity with several divalent metals such as Mn2+, Co2+, Fe2+, and Cu2+, although the preferred one appears to be Mn2+. The dioxygen binds to the metal ion of the Cu-QDO-quercetin complex, yielding a Cu2+-superoxo quercetin radical intermediate, which then forms a Cu2+-alkylperoxo complex which then evolves into endoperoxide intermediate that decomposes to the product. Quercetinase is a bicupin with two tandem cupin beta-barrel domains, both of which are included in this alignment model. The pirins, which also belong to the cupin domain family, have been shown to catalyze a reaction involving quercetin and may have a function similar to that of quercetinase.


Pssm-ID: 380345 [Multi-domain]  Cd Length: 122  Bit Score: 41.37  E-value: 1.36e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490365918  36 FTMAFWTFKTNAIIPEHKHEHETAT-SILKGSLKLTVNNRIVYLHAGDSFIIPSWAVH-HAIALEPSEVIDVYTP 108
Cdd:cd02215   32 FTLVTTEGPKGDAIPPHYHKRHHETfYVLEGRLQLWLDGESRLLTPGDFASVPPGTIHaYRMLSPDTRFLGVITP 106
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 38-106 1.54e-05

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: 40.54  E-value: 1.54e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490365918  38 MAFWTFKTNAIIPEHKHEHETATS-ILKGSLKLTVN-NRIVYLHAGDSFIIPSWAVH--HAIALEPSEVIDVY 106
Cdd:cd02208    1 ISVVTLPPGTSSPPHWHPEQDEIFyVLSGEGELTLDdGETVELKAGDIVLIPPGVPHsfVNTSDEPAVFLVVS 73
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 35-92 3.07e-05

Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to Thermotoga maritima TM1459, a manganese-containing cupin that has been shown to cleave C=C bonds in the presence of alkylperoxide as oxidant in vitro. Its biological function is still unknown. This family also includes Halorhodospira halophila Hhal_0468. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.


Pssm-ID: 380351 [Multi-domain]  Cd Length: 91  Bit Score: 39.74  E-value: 3.07e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490365918  35 NFTMAFWTFKTNAIIPEHKHEHETATSILKGSLKLTVNNRIVYLHAGDSFIIPSWAVH 92
Cdd:cd02222   16 NFAMRYFEIEPGGHTPLHTHPWEHEVYVLRGKGVVVIGGEEYPVKPGDVVYIPPNEPH 73
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
 46-106 4.15e-05

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: 39.87  E-value: 4.15e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490365918  46 NAIIPEHKHEHETATSILKGSLKLTVNNR-IVYLHAGDSFIIPSWAVHHA--IALEPSEVIDVY 106
Cdd:cd02235   29 GAVAGRHTHPGEESGYVLEGSLELEVDGQpPVTLKAGDSFFIPAGTVHNAknVGSGPAKLLATY 92
cupin_HP0902-like cd02230
Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes ...
 31-100 1.54e-04

Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes prokaryotic and archaeal proteins homologous to HP0902, a functionally uncharacterized protein from Helicobacter pylori and Spy1581, a protein of unknown function from Streptococcus pyogenes. These proteins demonstrate all-beta cupin folds that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins, and thus may have a putative role in H. pylori pathogenicity.


Pssm-ID: 380358 [Multi-domain]  Cd Length: 83  Bit Score: 37.87  E-value: 1.54e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365918  31 IHGSNFTMAFWTFKTNAIIPEHKHEHETATSILKGSLKLTVNNRIVYLHAGDSFIIPSWAVHHAIALEPS 100
Cdd:cd02230    6 VQDDGLRVTLFAFDAGQELSEHTAPGDATVQVLEGEAEFTIGGETVTLKAGELIVMPANVPHALKAEEDF 75
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
 62-107 2.00e-04

XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; This family contains transcriptional regulators containing an N-terminal XRE (Xenobiotic Response Element) family helix-turn-helix (HTH) DNA-binding domain and a C-terminal cupin domain. Included in this family is Escherichia coli transcription factor SutR (YdcN) that plays a regulatory role in sulfur utilization; it regulates a set of genes involved in the generation of sulfate and its reduction, the synthesis of cysteine, the synthesis of enzymes containing Fe-S as cofactors, and the modification of tRNA with use of sulfur-containing substrates. This family belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380339 [Multi-domain]  Cd Length: 90  Bit Score: 37.87  E-value: 2.00e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 490365918  62 ILKGSLKLTVNNRIVYLHAGDSFIIPSWAVH--HAIALEPSEVIDVYT 107
Cdd:cd02209   43 VLEGELELTVGGETYVLEAGDSIYFDSDVPHryRNPGDEPARVLWVIT 90
cupin_YdbB-like cd02226
Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial ...
 52-103 4.60e-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: 36.65  E-value: 4.60e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490365918  52 HKHEHETAT-SILKGSLKLTVNNRIVYLHAGDSFIIPSWAVHHAIALEPSEVI 103
Cdd:cd02226   38 HKHDDEDELfLVLEGELTIDFRDRDVTLGPGEFFVVPKGVEHRPVAEEETVVL 90
PRK09943 PRK09943
HTH-type transcriptional regulator PuuR;
29-86 1.99e-03

HTH-type transcriptional regulator PuuR;


Pssm-ID: 182158 [Multi-domain]  Cd Length: 185  Bit Score: 36.31  E-value: 1.99e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490365918  29 KFIHGSN----FTMAFWTFKTNAIIPEH-KHEHETATSILKGSLKLTVNNRIVYLHAGDSFII 86
Cdd:PRK09943  96 KLVHNGNpnrtLAMIFETYQPGTTTGERiKHQGEEIGTVLEGEIVLTINGQDYHLVAGQSYAI 158
cupin_BacB cd06975
Bacillus subtilis bacilysin and related proteins, cupin domain; Bacilysin (BacB, also known as ...
 18-103 2.58e-03

Bacillus subtilis bacilysin and related proteins, cupin domain; Bacilysin (BacB, also known as AerE in Microcystis aeruginosa) is a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. It is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF aeruginosin biosynthesis gene cluster in Microcystis aeruginosa.


Pssm-ID: 380380 [Multi-domain]  Cd Length: 93  Bit Score: 34.86  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365918  18 RNEGEESKIQAKFIHGSNFTMAFWTFKTNAIIPEHKHEHETATSILKGSLKLTVNNRIVYLHA-GDSFIIPSWAVHHAIA 96
Cdd:cd06975    1 KTIKLETGVELQFFVGSWTEIMLSYIPPGAKMPLHQHREEQIGMILNGELEMTVGGEEQELEPlGDVYYAPPNVPHGAVN 80


                 ....*..
gi 490365918  97 LEPSEVI 103
Cdd:cd06975   81 PSDETAV 87
cupin_MAE_RS03005 cd06987
Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes ...
 33-93 2.70e-03

Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes bacterial and some eukaryotic proteins homologous to MAE_RS03005, a Microcystis aeruginosa 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: 380392 [Multi-domain]  Cd Length: 122  Bit Score: 35.32  E-value: 2.70e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490365918  33 GSNFTMAFWTFKtnaiiPEHK---HEHETATS---ILKGSLKLTVNNRIVYLHAGDSFIIPSWAVHH 93
Cdd:cd06987   25 GVPFTVVVEIFD-----PGGRtppNTHPAAHEmffVLAGEGRAYCDGQRVPLRPGDALVVPPGSEHV 86
 
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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