Bacteroides fragilis BF4112 and related proteins, cupin domain; This family includes archaeal and bacterial proteins homologous to BF4112, a Bacteroides fragilis 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490451684  13 PRVELKDALNLSGCELSINELPANVSVPFVHSHKQNEELYLVLKGGGTLFIDGEETTVSEGDAIRIDPDGKRCFKADA-Q 91
Cdd:cd06985    1 GKVFLKEALGLTGAEISFNSLPAGAAVPFVHSHKENEEIYIILKGKGEFQVDGEVFPVKEGSVIRVAPDGKRSWRNTSdE 80

                         90       100
                 ....*....|....*....|.
gi 490451684  92 GMKFICIQTKRGSLEQYTMDD 112
Cdd:cd06985   81 PLIYICIQAKEGSLEQYTITD 101

Bacteroides fragilis BF4112 and related proteins, cupin domain; This family includes archaeal and bacterial proteins homologous to BF4112, a Bacteroides fragilis 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490451684  13 PRVELKDALNLSGCELSINELPANVSVPFVHSHKQNEELYLVLKGGGTLFIDGEETTVSEGDAIRIDPDGKRCFKADA-Q 91
Cdd:cd06985    1 GKVFLKEALGLTGAEISFNSLPAGAAVPFVHSHKENEEIYIILKGKGEFQVDGEVFPVKEGSVIRVAPDGKRSWRNTSdE 80

                         90       100
                 ....*....|....*....|.
gi 490451684  92 GMKFICIQTKRGSLEQYTMDD 112
Cdd:cd06985   81 PLIYICIQAKEGSLEQYTITD 101

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 490451684   32 ELPANVSVPFvHSHKQNEELYLVLKGGGTLFIDGEETTVSEGDAIRIDPDGKRCFKADAQG-MKFICI 98
Cdd:pfam07883   4 TLPPGESSPP-HRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEpARLLDV 70

Bacteroides fragilis BF4112 and related proteins, cupin domain; This family includes archaeal and bacterial proteins homologous to BF4112, a Bacteroides fragilis 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490451684  13 PRVELKDALNLSGCELSINELPANVSVPFVHSHKQNEELYLVLKGGGTLFIDGEETTVSEGDAIRIDPDGKRCFKADA-Q 91
Cdd:cd06985    1 GKVFLKEALGLTGAEISFNSLPAGAAVPFVHSHKENEEIYIILKGKGEFQVDGEVFPVKEGSVIRVAPDGKRSWRNTSdE 80

                         90       100
                 ....*....|....*....|.
gi 490451684  92 GMKFICIQTKRGSLEQYTMDD 112
Cdd:cd06985   81 PLIYICIQAKEGSLEQYTITD 101

Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490451684  43 HSHKQNEELYLVLKGGGTLFIDGEETTVSEGDAIRIDPDGKRCFKADAQG-MKFICI 98
Cdd:cd02214   35 HRLKGSEEVYYILEGEGTMEIDGEPREVGPGDAVLIPPGAVQRIENTGEEdLVFLCI 91

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 490451684   32 ELPANVSVPFvHSHKQNEELYLVLKGGGTLFIDGEETTVSEGDAIRIDPDGKRCFKADAQG-MKFICI 98
Cdd:pfam07883   4 TLPPGESSPP-HRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEpARLLDV 70

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

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490451684  26 CELSINELPANVSVPFvHSHkQNEELYLVLKGGGTLFIDGEETTVSEGDAIRIDPDGKRCFKADAQG-MKFICIQT 100
Cdd:COG1917   23 LEVVRVTFEPGARTPW-HSH-PGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGDEpAVLLVVFS 96

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 490451684  28 LSINELPANVSVPFvHSHKQNEELYLVLKGGGTLFID-GEETTVSEGDAIRIDPDGKRCFKADA-QGMKFICI 98
Cdd:cd02208    1 ISVVTLPPGTSSPP-HWHPEQDEIFYVLSGEGELTLDdGETVELKAGDIVLIPPGVPHSFVNTSdEPAVFLVV 72

Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial proteins homologous to TM1287 decarboxylase, a Thermotoga maritima manganese-containing cupin thought to catalyze the conversion of oxalate to formate and carbon dioxide, due to its similarity to oxalate decarboxylase (OXDC) from Bacillus subtilis. TM1287 shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold and forms a homodimer.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490451684  16 ELKDALNLsgceLSINELPANVSVPFvHSHKQNEELYLVLKGGGTLFIDGEETTVSEGDAIrIDPDG 82
Cdd:cd02221   13 ELKGKGRL----FARVTLPPGSSIGY-HQHEGEFEIYYILSGEGLYTDNGKEYEVKAGDVT-FTRDG 73

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.

                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 490451684  43 HSHKQNEELYLVLKGGGTLFIDGEETTVSEGDAIRIDP 80
Cdd:cd06987   44 NTHPAAHEMFFVLAGEGRAYCDGQRVPLRPGDALVVPP 81

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490451684  27 ELSINELPANVSVPFVHSHKQnEELYLVLKGGGTLFIDGEETTVSEGDAIRIDPD 81
Cdd:cd02209   17 EPFLVTLPPGGSGGEPYSHEG-EEFGYVLEGELELTVGGETYVLEAGDSIYFDSD 70

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
                 ....*....|....*....|....*....|....*....|.
gi 490451684  34 PANVSVPFvHSHKQNEELYLVLKGGGTLFIDGEETTVSEGD 74
Cdd:cd02215   40 PKGDAIPP-HYHKRHHETFYVLEGRLQLWLDGESRLLTPGD 79

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
                 ....*....|....*....|....*....|....*.
gi 490451684  43 HSHKQNEELYLVLKGGGTLFIDGEETTVSEGDAIRI 78
Cdd:cd02213   56 QRHHHRSEHWVVVSGTAEVTLDGKEKLLKEGESIYI 91

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
                 ....*....|....*....|....*....|....*....|..
gi 490451684  43 HSHKQNEELYLVLKGGGTLFIDGEETTVSEGDAIRIdPDGKR 84
Cdd:cd06991   35 HYHPYSEEFLYVVRGRLVVRVDGEPVVLEAGEALLV-PRGVR 75

Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model represents the C-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin 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. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 490451684  26 CELSINELPANVSVPFvHSHKqNEELYLVLKGGGTLFIDGEETTVSEGDA 75
Cdd:cd10547   19 FEIMISQIPPGGKMPL-HQHR-GEQIGIILNGKYDMTVGGEEQELGYGKI 66