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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766903732  10 KEYNQDKFTKRIIFKSGESV-VFVLNFMPGQELPTHQHPGTAVFIlVLDGGGTVTVNGEESALVKDDVISCE-GEEHfSF 87
Cdd:COG1917    4 AEIALTGVSVRVLADGEDELeVVRVTFEPGARTPWHSHPGEELIY-VLEGEGEVEVGGEEYELKPGDVVFIPpGVPH-AF 81

                         90
                 ....*....|....*
gi 766903732  88 KNTGSTPTSLYVVLS 102
Cdd:COG1917   82 RNLGDEPAVLLVVFS 96

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766903732  10 KEYNQDKFTKRIIFKSGESV-VFVLNFMPGQELPTHQHPGTAVFIlVLDGGGTVTVNGEESALVKDDVISCE-GEEHfSF 87
Cdd:COG1917    4 AEIALTGVSVRVLADGEDELeVVRVTFEPGARTPWHSHPGEELIY-VLEGEGEVEVGGEEYELKPGDVVFIPpGVPH-AF 81

                         90
                 ....*....|....*
gi 766903732  88 KNTGSTPTSLYVVLS 102
Cdd:COG1917   82 RNLGDEPAVLLVVFS 96

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        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766903732  12 YNQDKFTKRIIFKSGESVVFVLNFMPGQELPTHQHPGTAVFILVLDGGGTVTVNGEESALVKDDVISC-EGEEHfSFKNT 90
Cdd:cd06122   11 FSPEKMQKITLFESERLFCDLYCLEPGQSQKVHAHAGSDKVYFVLEGEGRFTVGDEERELGAGEAVLApAGVPH-GVRNT 89

                         90
                 ....*....|..
gi 766903732  91 GSTPTSLYVVLS 102
Cdd:cd06122   90 GAERLVLLVFMA 101

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766903732  10 KEYNQDKFTKRIIFKSGESV-VFVLNFMPGQELPTHQHPGTAVFIlVLDGGGTVTVNGEESALVKDDVISCE-GEEHfSF 87
Cdd:COG1917    4 AEIALTGVSVRVLADGEDELeVVRVTFEPGARTPWHSHPGEELIY-VLEGEGEVEVGGEEYELKPGDVVFIPpGVPH-AF 81

                         90
                 ....*....|....*
gi 766903732  88 KNTGSTPTSLYVVLS 102
Cdd:COG1917   82 RNLGDEPAVLLVVFS 96

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        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766903732  12 YNQDKFTKRIIFKSGESVVFVLNFMPGQELPTHQHPGTAVFILVLDGGGTVTVNGEESALVKDDVISC-EGEEHfSFKNT 90
Cdd:cd06122   11 FSPEKMQKITLFESERLFCDLYCLEPGQSQKVHAHAGSDKVYFVLEGEGRFTVGDEERELGAGEAVLApAGVPH-GVRNT 89

                         90
                 ....*....|..
gi 766903732  91 GSTPTSLYVVLS 102
Cdd:cd06122   90 GAERLVLLVFMA 101

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766903732   6 LLPVKEYNQ---DKFTKRIIFKSGESVVFVLNFMPGQELPTHQHP-GTAVFIlVLDGGGT-VTVNGEESALVKDD-VISC 79
Cdd:cd07008    2 IFDVAEFVQfsdEEPIRSVITETDDSAIVVWHVKPGQEIAAHIHPhGQDTWI-VLSGEGEyLLGDGQTVPIKAGDiVIAP 80

                         90
                 ....*....|....*
gi 766903732  80 EGEEHfSFKNTGSTP 94
Cdd:cd07008   81 AGQVH-GARNTGDEP 94

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 766903732  30 VFVLNFMPGQELPTHQHPGTAVFILVLDGGGTVTVNGEESALVK-DDVISCEGEEHFSFKNTGSTPTSLYVV 100
Cdd:cd02208    1 ISVVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDDGETVELKaGDIVLIPPGVPHSFVNTSDEPAVFLVV 72

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 766903732  37 PGQELPTHQHPGT-AVFILvlDGGGTVTVNGEESALVKDDVISCEGEEHFSFKNTGSTP 94
Cdd:cd02222   26 PGGHTPLHTHPWEhEVYVL--RGKGVVVIGGEEYPVKPGDVVYIPPNEPHQFRNTGDEP 82

Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to plant pathogen Xanthomonas campestris tetracenomycin polyketide synthesis protein XcTcmJ, a protein encoded by the tcmJ gene. XcTcmJ is annotated as being involved in tetracenomycin polyketide biosynthesis. Also included is Xc5357 from a different strain of X. campestris. Structure studies show that binding of zinc induces conformational changes and serves a functional role in this cupin protein. 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 766903732  20 RIIFKSGESVVFVLNFMPGQEL--PTHQHPGTAVFILVLDGGGTVTVNGEESALVKDDVISCE-GEEHfSFKNTGSTP 94
Cdd:cd07006    2 RVLAGTERSQAATMVLAPGDTEggPDNRHRGSDQWLYVVSGSGEAIVEGERVALKPGSLLLIEaGETH-EIRNTGDEP 78

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766903732  31 FVLNFM---PGQELPTHQHPGTAVFIlVLDGGGTVTV--NGE--ESALVKDDVISC-EGEEHfSFKNTGSTPTSLYVVLS 102
Cdd:cd02225   53 FTLSTMrlpPGQGGALHTHEVEEVFF-VLQGRLTVFWedEGEehERELGPRDMISVpAGVYR-GFKNIGEEDALMQVMLG 130

                 ....*.
gi 766903732 103 KIPDER 108
Cdd:cd02225  131 TGKPGR 136

Anti-sigma factor ChrR, cupin superfamily [Signal transduction mechanisms];

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 766903732  19 KRIIFKSGESV---VFVLNFMPGQELPTHQHPGTAvFILVLDGG 59
Cdd:COG3806   55 RRARLDRGGEGgraTSLLRIAPGSAFPEHTHRGGE-ETLVLEGA 97

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        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 766903732  27 ESVVFVLNFMPGQELPTHQHPGTaVFILVLDGGGTVTVNGEESALVK--DDVISCEGEEHfSFKNTGSTPTSL---YVV 100
Cdd:cd02235   18 EVVQVRVEIPPGAVAGRHTHPGE-ESGYVLEGSLELEVDGQPPVTLKagDSFFIPAGTVH-NAKNVGSGPAKLlatYIV 94

2,4'-Dihydroxyacetophenone dioxygenase (DAD) and anti-sigma factor ChrR, and similar proteins; cupin domain; This family includes the proteins 2,4'-Dihydroxyacetophenone dioxygenase (DAD) and anti-sigma factor ChrR. DAD catalyzes the oxidation of 2,4'-dihydroxyacetophenone to 4-hydroxybenzoate and formate as part of the 4-hydroxyacetophenone catabolic pathway. The enzyme is a homotetramer containing one iron per molecule of enzyme. Anti-sigma factor ChrR is a member of the ZAS (Zn2+ anti-sigma) subfamily of group IV anti-sigmas. It inhibits transcriptional activity by binding to the Rsp extra cytoplasmic function (ECF) sigma factor E (sigmaE). Some ChrR members contain tandem repeats of two distinct homologous functional domains. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 766903732  24 KSGESVVFVLNFMPGQELPTHQHPGTaVFILVLDGGGTVTvngEESALVKDDVISCEGEEHFSF 87
Cdd:cd02237   10 PNTGLITAILRMAPGARLPDHEHVGG-EEFYVLDGALTDE---DGTAGAGDFVREPPGSRHSAV 69

Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 766903732  47 PGTAVFILVLDGGGTVTVNGEESALVKDDVISCEGEEHFSFKNTGSTPTSLYVV 100
Cdd:COG3257   79 PGAETFLFVLEGEVTLTLGGETHELTPGGYAYLPPGTPWTLRNAGDEPARFHWI 132

cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11.20), which catalyzes the conversion of cysteine to cysteine sulfinic acid, the first step in the biosynthesis of essential oxidized cysteine metabolites such as sulfate, hypotaurine, and taurine. CDO also plays an important role in the regulation of intracellular cysteine levels in mammals; CDO expression is altered in cancer cells, and abnormal or deficient CDO activity has been linked to Parkinson's disease, Alzheimer's disease, and rheumatoid arthritis. CDO is an iron-dependent thiol dioxygenase that uses molecular oxygen to oxidize the sulfhydryl group of cysteine to generate cysteine sulfinic acid. The CDO active site contains an amino acid-derived cofactor. These enzymes are found in prokaryotes as well as eukaryotes and belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 766903732  17 FTKRIIFKSGESVVFVLNFMPGQELPTHQHPGTAVFILVLDG 58
Cdd:cd10548    1 YTRNLLYRDPDFELLLLCWPPGQGSPIHDHGGSWCVVKVLEG 42

(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family includes the N-terminal cupin domain of (S)-ureidoglycine aminohydrolase (UGlyAH), an enzyme that converts (S)-ureidoglycine into (S)-ureidoglycolate and ammonia, providing the final substrate to the ureide pathway. The ureide pathway has recently been identified as the metabolic route of purine catabolism in plants and some bacteria where, uric acid, which is a major product of the early stage of purine catabolism, is degraded into glyoxylate and ammonia via stepwise reactions by seven different enzymes. Thus, this pathway has a possible physiological role in mobilization of purine ring nitrogen for further assimilation. This enzyme from Arabidopsis thaliana(AtUGlyAH) has been shown to bind a Mn2+ ion, via the C-terminal cupin domain, which acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction. The structure of AtUGlyAH shows a bi-cupin fold with a conserved "jelly roll-like" beta-barrel fold and an octameric functional unit. Several structural homologs of UGlyAH, including the Escherichia coli ortholog YlbA (also known as GlxB6), also exhibit similar features.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 766903732  52 FILVLDGGGTVTVNGEESALVKDDVISCEGEEHFSFKNTGSTPTSLYVV 100
Cdd:cd02211   50 FLYVLEGEVELTVGGETHTLTAGGYAYLPPGTKHSLRNAGDEPARLLWY 98

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 766903732  37 PGQELPTHQHPGTAVFILVLDGGGTVTVNGEESALVKDDVIS-CEGEEHFsFKNTGSTP 94
Cdd:cd02214   28 PGESTLPHRLKGSEEVYYILEGEGTMEIDGEPREVGPGDAVLiPPGAVQR-IENTGEED 85

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 766903732  22 IFKSGESVVFVLNFMPGQELPTHQHPGTAVFIlVLDGGGTVTVNGEE 68
Cdd:cd06975   13 FFVGSWTEIMLSYIPPGAKMPLHQHREEQIGM-ILNGELEMTVGGEE 58