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        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084522561  24 VSRVMLKSEAGNVTLFAFDLGQELSEHSTPYDALVQVLDGEAEIRISGKAFVLKSGEAIIMPANDPHAVKAVKQFKMLLT 103
Cdd:cd02230     1 VSRTLVQDDGLRVTLFAFDAGQELSEHTAPGDATVQVLEGEAEFTIGGETVTLKAGELIVMPANVPHALKAEEDFKMLLT 80

                  ...
gi 1084522561 104 MLK 106
Cdd:cd02230    81 LIK 83

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        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084522561  24 VSRVMLKSEAGNVTLFAFDLGQELSEHSTPYDALVQVLDGEAEIRISGKAFVLKSGEAIIMPANDPHAVKAVKQFKMLLT 103
Cdd:cd02230     1 VSRTLVQDDGLRVTLFAFDAGQELSEHTAPGDATVQVLEGEAEFTIGGETVTLKAGELIVMPANVPHALKAEEDFKMLLT 80

                  ...
gi 1084522561 104 MLK 106
Cdd:cd02230    81 LIK 83

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
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1084522561  38 LFAFDLGQELSEHSTPY-DALVQVLDGEAEIRISGKAFVLKSGEAIIMPANDPHAVKAV 95
Cdd:pfam07883   2 LVTLPPGESSPPHRHPGeDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNT 60

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        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084522561  24 VSRVMLKSEAGNVTLFAFDLGQELSEHSTPYDALVQVLDGEAEIRISGKAFVLKSGEAIIMPANDPHAVKAVKQFKMLLT 103
Cdd:cd02230     1 VSRTLVQDDGLRVTLFAFDAGQELSEHTAPGDATVQVLEGEAEFTIGGETVTLKAGELIVMPANVPHALKAEEDFKMLLT 80

                  ...
gi 1084522561 104 MLK 106
Cdd:cd02230    81 LIK 83

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084522561  21 GSIVSRVMLKSEAG-NVTLFAFDLGQELSEHSTPYDALVQVLDGEAEIRISGKAFVLKSGEAIIMPANDPHAVKAVKQFK 99
Cdd:COG1917     9 TGVSVRVLADGEDElEVVRVTFEPGARTPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGDEP 88

                  ...
gi 1084522561 100 MLL 102
Cdd:COG1917    89 AVL 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
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1084522561  38 LFAFDLGQELSEHSTPY-DALVQVLDGEAEIRISGKAFVLKSGEAIIMPANDPHAVKAV 95
Cdd:pfam07883   2 LVTLPPGESSPPHRHPGeDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNT 60

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084522561  41 FDLGQELSEHSTPYDALVQVLDGEAEIRISGKAFV-LKSGEAIIMPANDPHAVKAV--KQFKMLLTM 104
Cdd:cd02235    26 IPPGAVAGRHTHPGEESGYVLEGSLELEVDGQPPVtLKAGDSFFIPAGTVHNAKNVgsGPAKLLATY 92

Uncharacterized conserved protein, cupin superfamily [Function unknown];

                          10        20        30
                  ....*....|....*....|....*....|...
gi 1084522561  60 VLDGEAEIRISGKAFVLKSGEAIIMPANDPHAV 92
Cdd:COG3837    56 VLEGELTLRIGGEEYVLEPGDSVGFPAGVPHRL 88

Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains bacterial proteins including TTHA0104 (also called TT1209), a putative antibiotic synthesis protein from Thermus thermophilus. TTHA0104 is a cupin-like protein. The 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).

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1084522561  38 LFAFDLGQELSEHSTP-YDALVQVLDGEAEIRISGKAFVLKSGEAIIMPANDPHAVK 93
Cdd:cd06122    31 LYCLEPGQSQKVHAHAgSDKVYFVLEGEGRFTVGDEERELGAGEAVLAPAGVPHGVR 87

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1084522561  48 SEHSTPYDALVQVLDGEAEIRISGKAFVLKSGEAIIMPANDPHavkavkQFK 99
Cdd:cd02222    31 PLHTHPWEHEVYVLRGKGVVVIGGEEYPVKPGDVVYIPPNEPH------QFR 76

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
                  ....*....|....*....|....*....|.
gi 1084522561  60 VLDGEAEIRISGKAFVLKSGEAIIMPANDPH 90
Cdd:cd02214    46 ILEGEGTMEIDGEPREVGPGDAVLIPPGAVQ 76

Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to dimethylsulfoniopropionate lyase DddK from marine bacterium Pelagibacter. DddK cleaves dimethylsulfoniopropionate (DMSP), the organic osmolyte and antioxidant produced in marine environments, and yields acrylate and the climate-active gas dimethyl sulfide (DMS). DddK contains a double-stranded beta-helical motif which utilizes various divalent metal ions as cofactors for catalytic activity; however, nickel, an abundant metal ion in marine environments, confers the highest DMSP lyase activity. Also included in this family is Plu4264, a Photorhabdus luminescens manganese-containing cupin shown to have similar metal binding site to TM1287 decarboxylase, but two very different substrate binding pockets. The Plu4264 binding pocket shows a cavity and substrate entry point more than twice as large as and more hydrophobic than TM1287, suggesting that Plu4264 accepts a substrate that is significantly larger than that of TM1287, a putative oxalate decarboxylase. Thus, the function of Plu4264 could be similar to that of TM1287 but with a larger, less charged substrate. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.

                          10        20        30
                  ....*....|....*....|....*....|....
gi 1084522561  60 VLDGEAEIRISGKAFVLKSGEAIIMPANDPHAVK 93
Cdd:cd06988    28 VISGKGIVVVDGEREPVKAGDVVYIPPGTEHYVK 61