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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252781   6 NLAQKFSLFSEQWQPKVVAEMNDYQFKVVRIAGDFIWHSHLETDETLMVVEGVLRVDFRDGHVLVKAGEMIVVPRGVEHK 85
Cdd:cd02226    1 NLAEKLAAIDEYWSPKIVAEVNDQVVKLAKLKGEFVWHKHDDEDELFLVLEGELTIDFRDRDVTLGPGEFFVVPKGVEHR 80

                         90
                 ....*....|....
gi 490252781  86 TSAETEAKLMLIEP 99
Cdd:cd02226   81 PVAEEETVVLLIEP 94

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252781   6 NLAQKFSLFSEQWQPKVVAEMNDYQFKVVRIAGDFIWHSHLETDETLMVVEGVLRVDFRDGHVLVKAGEMIVVPRGVEHK 85
Cdd:cd02226    1 NLAEKLAAIDEYWSPKIVAEVNDQVVKLAKLKGEFVWHKHDDEDELFLVLEGELTIDFRDRDVTLGPGEFFVVPKGVEHR 80

                         90
                 ....*....|....
gi 490252781  86 TSAETEAKLMLIEP 99
Cdd:cd02226   81 PVAEEETVVLLIEP 94

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252781   38 GDFIWHSHLETDETLMVVEGVLRVDFRDGHVLVKAGEMIVVPRGVEHKTSAETEAKLMLI 97
Cdd:pfam07883   9 ESSPPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLL 68

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252781   6 NLAQKFSLFSEQWQPKVVAEMNDYQFKVVRIAGDFIWHSHLETDETLMVVEGVLRVDFRDGHVLVKAGEMIVVPRGVEHK 85
Cdd:cd02226    1 NLAEKLAAIDEYWSPKIVAEVNDQVVKLAKLKGEFVWHKHDDEDELFLVLEGELTIDFRDRDVTLGPGEFFVVPKGVEHR 80

                         90
                 ....*....|....
gi 490252781  86 TSAETEAKLMLIEP 99
Cdd:cd02226   81 PVAEEETVVLLIEP 94

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

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490252781  27 NDYQFKVVRIA----GDFIWHSHlETDETLMVVEGVLRVDFRDGHVLVKAGEMIVVPRGVEHKTSAETEAKLMLI 97
Cdd:COG1917   19 GEDELEVVRVTfepgARTPWHSH-PGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLL 92

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490252781  24 AEMNDYQFKVVRIAG----DFIWHSHLETDETLMVVEGVLRVDFRDGHVLVKAGEMIVVPRGVEH 84
Cdd:cd02215   25 GESTGGAFTLVTTEGpkgdAIPPHYHKRHHETFYVLEGRLQLWLDGESRLLTPGDFASVPPGTIH 89

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490252781  43 HSHLETDETLMVVEGVLRVDFRDGHVLVKAGEMIVVPRGVEHKTSAETEAKLMLIE 98
Cdd:cd02213   56 QRHHHRSEHWVVVSGTAEVTLDGKEKLLKEGESIYIPKGTKHRLENPGKIPLEIIE 111

TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of the tetracenomycin (TCM) polyketide synthase (PKS) type II complex in Streptomyces glaucescens. TcmJ is a quinone-forming monooxygenase involved in the modification of aromatic polyketides synthesized by polyketide synthases of types II and III. Orthologs of TcmJ include the Streptomyces BenD (benastatin biosynthetic pathway), the Streptomyces olivaceus ElmJ (polyketide antibiotic elloramycin biosynthetic pathway), the Actinomadura hibisca PdmL (pradimicin biosynthetic pathway), the Streptomyces cyaneus CurC (curamycin biosynthetic pathway), the Streptomyces rishiriensis Lct30 (lactonamycin biosynthetic pathway), and the Streptomyces WhiE II (spore pigment polyketide biosynthetic pathway). 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
                 ....*....|....*....|....*....|....*....|....*....|
gi 490252781  37 AGDFIW-HSHLETDETLMVVEGVLRVDFRDGHVLVKAGEMIVVPRGVEHK 85
Cdd:cd06991   28 PGERVSeHYHPYSEEFLYVVRGRLVVRVDGEPVVLEAGEALLVPRGVRHR 77

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
                  ....*....|....*....|....*....|....*....|....*....
gi 490252781   43 HSHLETDETLMVVEGVLRV-------DFRDGHVLVKAGEMIVVPRGVEH 84
Cdd:pfam00190  49 HWHPNATEILYVLQGRGRVgfvvpgnGNRVFHKVLREGDVFVVPQGLPH 97

AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization domain of the bacterial gene regulatory protein AraC. The domain is found in conjunction with the helix-turn-helix (HTH) DNA-binding motif pfam00165. This domain is distantly related to the Cupin domain pfam00190.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 490252781   40 FIWHSHLETdETLMVVEGVLRVDFRDGHVLVKAGEMIVVPRGVEHKTSAETEA 92
Cdd:pfam02311  16 FPPHVHDFY-VIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEPESED 67

Granulicella tundricola hydroxynitrile lyase (GtHNL) and related proteins, cupin domain; This family includes archaeal, eukaryotic, and bacterial proteins homologous to hydroxynitrile lyase from Granulicella tundricola (GtHNL), a novel class of HNLs that does not show any sequence or structural similarity to any other HNL and does not contain conserved motifs typical of HNLs. HNLs comprise a diverse group of enzymes that vary in terms of their substrate specificity, enantioselectivity and the need for a co-factor. In plants, they catalyze the reversible cleavage of cyanohydrins, yielding HCN and aldehydes or ketones. Also included in this family is TM1010 from Thermotoga maritima, a protein of unknown function. Some but not all members of this family have N- or C-terminal carboxymuconolactone decarboxylase domains in addition to the cupin domain. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 490252781  42 WHSHlETDETLMVVEGVLRVDFRDGHV-LVKAGEMIVVPRGVEH 84
Cdd:cd02233   34 WHTH-PGGQILIVTSGVGWVQEEGGPPqELRPGDVVWIPPGVKH 76

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490252781  43 HSHlETDETLMVVEGVLRVDFRDGHVLVK----AGEMIVVPRGVEH--KTSAETEAKLMLI 97
Cdd:cd02225   69 HTH-EVEEVFFVLQGRLTVFWEDEGEEHErelgPRDMISVPAGVYRgfKNIGEEDALMQVM 128

Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, archaeal, and eukaryotic proteins similar to Bh2720, a Bacillus halodurans protein of unknown function with a cupin beta-barrel fold.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 490252781  45 HLETDETLMVVEGVLRVDFRDGHVLVKAGEMIVVPRGVEH 84
Cdd:cd02223   29 HDDVDQFLRIEEGEGKAIMGGFESEVKDGDAIIVPAGTWH 68