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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796052545 338 TITEAEHELSVLHTHPNDELFWVESGELDFVASPELSVRLKAGEGVVIPKGMLHGTRVVSPSCTYTVTAI 407
Cdd:cd07002    25 RLVEPRGELSVTHVHDGDELCHVVSGTMRFVSGLGSSTILNAGEGVVIKRNRLHGALILSEECVYEIYSI 94

Streptomyces achromogenes SznF and related proteins, C-terminal cupin domain; This family includes bacterial proteins similar to Streptomyces achromogenes SznF, containing an N-terminal helical region that mediates dimerization, a central heme oxygenase domain, and a C-terminal cupin domain. SznF is a metalloenzyme that catalyzes an oxidative rearrangement of the guanidine group of N(omega)-methyl-L-arginine to generate an N-nitrosourea product, during the biosynthesis of streptozotocin, an N-nitrosourea natural product and an approved cancer chemotherapeutic. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold generally capable of homodimerization. However, in SznF, the cupin domain is not involved in dimerization.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796052545 338 TITEAEHELSVLHTHPNDELFWVESGELDFVASPELSVRLKAGEGVVIPKGMLHGTRVVSPSCTYTVTAI 407
Cdd:cd07002    25 RLVEPRGELSVTHVHDGDELCHVVSGTMRFVSGLGSSTILNAGEGVVIKRNRLHGALILSEECVYEIYSI 94

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2796052545  346 LSVLHTHPN-DELFWVESGELDF-VASPELSV----RLKAGEGVVIPKGMLH 391
Cdd:smart00835  42 MLPPHYHPRaTELLYVVRGEGRVgVVDPNGNKvydaRLREGDVFVVPQGHPH 93

Streptomyces achromogenes SznF and related proteins, C-terminal cupin domain; This family includes bacterial proteins similar to Streptomyces achromogenes SznF, containing an N-terminal helical region that mediates dimerization, a central heme oxygenase domain, and a C-terminal cupin domain. SznF is a metalloenzyme that catalyzes an oxidative rearrangement of the guanidine group of N(omega)-methyl-L-arginine to generate an N-nitrosourea product, during the biosynthesis of streptozotocin, an N-nitrosourea natural product and an approved cancer chemotherapeutic. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold generally capable of homodimerization. However, in SznF, the cupin domain is not involved in dimerization.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796052545 338 TITEAEHELSVLHTHPNDELFWVESGELDFVASPELSVRLKAGEGVVIPKGMLHGTRVVSPSCTYTVTAI 407
Cdd:cd07002    25 RLVEPRGELSVTHVHDGDELCHVVSGTMRFVSGLGSSTILNAGEGVVIKRNRLHGALILSEECVYEIYSI 94

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

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2796052545 349 LHTHPNDELFWVESGELDFVASPElSVRLKAGEGVVIPKGMLHGTRVVSPS 399
Cdd:COG1917    38 WHSHPGEELIYVLEGEGEVEVGGE-EYELKPGDVVFIPPGVPHAFRNLGDE 87

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2796052545 349 LHTHPN-DELFWVESGELDFVASPElSVRLKAGEGVVIPKGMLHGTR 394
Cdd:COG0662    42 LHVHPHrDEFFYVLEGTGEVTIGDE-EVELKAGDSVYIPAGVPHRLR 87

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2796052545  346 LSVLHTHPN-DELFWVESGELDF-VASPELSV----RLKAGEGVVIPKGMLH 391
Cdd:smart00835  42 MLPPHYHPRaTELLYVVRGEGRVgVVDPNGNKvydaRLREGDVFVVPQGHPH 93

Klebsiella pneumoniae yp_001338853.1 and related proteins, cupin domain; This family includes bacterial proteins homologous to Klebsiella pneumoniae yp_001338853.1, an uncharacterized conserved protein with double-stranded beta-helix domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796052545 333 KPVDLTITEAEHELSVL-----------HTHPNDELFW-VESGELDFVASPELSVRLKAGEGVVIPKGMLHGTR 394
Cdd:cd07008    15 EPIRSVITETDDSAIVVwhvkpgqeiaaHIHPHGQDTWiVLSGEGEYLLGDGQTVPIKAGDIVIAPAGQVHGAR 88

Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3.4) catalyzes the manganese-dependent oxidative decarboxylation of oxalate to carbon dioxide and hydrogen peroxide (H2O2). It is widespread in fungi and various plant tissues and may play a role in plant signaling and defense. This enzyme has been employed in a widely used assay for detecting urinary oxalate levels. Also, the gene encoding OxOx from barley roots has been expressed in oilseed rape in order to provide a defense against externally supplied oxalic acid. In germin, the predominant protein produced during the early phase of wheat germination, it is believed that H2O2 production is employed as a defense mechanism in response to infection by pathogens. Germin is also a marker of growth onset in cell walls in germinating cereals. The H2O2 produced by OxOx, together with the Ca2+ released by degradation of calcium oxalate, are thought to mediate cell wall cross-linking at high concentrations. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2796052545 349 LHTHPN-DELFWVESGELD--FVASPELSV---RLKAGEGVVIPKGMLH 391
Cdd:cd02241    85 PHTHPRaTELLYVVEGTLYvgFVDENGNRLftkTLNPGDVFVFPQGLIH 133

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2796052545 342 AEHELSVlHTHPNDELFWVESGELDFVASPElSVRLKAGEGVVIPKGMLHGTRVVSPS 399
Cdd:cd02230    20 AGQELSE-HTAPGDATVQVLEGEAEFTIGGE-TVTLKAGELIVMPANVPHALKAEEDF 75

Pseudomonas aeruginosa PA3510 and related proteins, cupin domain; This family includes bacterial proteins homologous to PA3510, a Pseudomonas aeruginosa protein of unknown function with a beta-barrel fold that belongs to the cupin superfamily.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796052545 333 KPVDLTITEAEH-ELSV----------LHTHPNDELFWVESGELDFV---ASPELSVRLKAGEGVVIPKGMLHGTRVVS 397
Cdd:cd02225    41 KHDDPNIIPAEHfTLSTmrlppgqggaLHTHEVEEVFFVLQGRLTVFwedEGEEHERELGPRDMISVPAGVYRGFKNIG 119