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Conserved domains on  [gi|1819705762|ref|WP_165374827|]
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cupin domain-containing protein [Sphingomonas montana]

Protein Classification

cupin domain-containing protein( domain architecture ID 1562428)

cupin domain-containing protein, part of a functionally diverse superfamily with the active site generally located at the center of a conserved domain forming a beta-barrel fold

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 40-140 1.15e-30

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.


The actual alignment was detected with superfamily member cd02235:

Pssm-ID: 477354 [Multi-domain]  Cd Length: 100  Bit Score: 106.12  E-value: 1.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819705762  40 GIVWTELQKLPLaSDPSKEESIGIAVIQPSAPAERHSHAENEIGYVLAGASLLEVEGEPTRTIRTGDSFAIPAGRVHRAK 119
Cdd:cd02235     1 GIKRTVLQRTDL-SVPGREVVQVRVEIPPGAVAGRHTHPGEESGYVLEGSLELEVDGQPPVTLKAGDSFFIPAGTVHNAK 79

                          90       100
                  ....*....|....*....|.
gi 1819705762 120 PVGKVPLKVVVTYIVERGQPL 140
Cdd:cd02235    80 NVGSGPAKLLATYIVEKGKPL 100
 
Name Accession Description Interval E-value
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
 40-140 1.15e-30

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.


Pssm-ID: 380363 [Multi-domain]  Cd Length: 100  Bit Score: 106.12  E-value: 1.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819705762  40 GIVWTELQKLPLaSDPSKEESIGIAVIQPSAPAERHSHAENEIGYVLAGASLLEVEGEPTRTIRTGDSFAIPAGRVHRAK 119
Cdd:cd02235     1 GIKRTVLQRTDL-SVPGREVVQVRVEIPPGAVAGRHTHPGEESGYVLEGSLELEVDGQPPVTLKAGDSFFIPAGTVHNAK 79

                          90       100
                  ....*....|....*....|.
gi 1819705762 120 PVGKVPLKVVVTYIVERGQPL 140
Cdd:cd02235    80 NVGSGPAKLLATYIVEKGKPL 100
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 62-132 1.54e-12

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


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 58.81  E-value: 1.54e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1819705762  62 GIAVIQPSAPAERHSHA-ENEIGYVLAGASLLEVEGEPTrTIRTGDSFAIPAGRVHRAKPVGKVPLKVVVTY 132
Cdd:pfam07883   1 GLVTLPPGESSPPHRHPgEDEFFYVLEGEGELTVDGEEV-VLKAGDSVYFPAGVPHRFRNTGDEPARLLDVY 71
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
60-132 7.19e-12

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 58.23  E-value: 7.19e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819705762  60 SIGIAVIQPSAPAERHSHAEN-EIGYVLAGASLLEVEGEpTRTIRTGDSFAIPAGRVHRAKPVGKVPLKVVVTY 132
Cdd:COG0662    28 SVKRITVPPGAELSLHVHPHRdEFFYVLEGTGEVTIGDE-EVELKAGDSVYIPAGVPHRLRNPGDEPLELLEVQ 100
 
Name Accession Description Interval E-value
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
 40-140 1.15e-30

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.


Pssm-ID: 380363 [Multi-domain]  Cd Length: 100  Bit Score: 106.12  E-value: 1.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819705762  40 GIVWTELQKLPLaSDPSKEESIGIAVIQPSAPAERHSHAENEIGYVLAGASLLEVEGEPTRTIRTGDSFAIPAGRVHRAK 119
Cdd:cd02235     1 GIKRTVLQRTDL-SVPGREVVQVRVEIPPGAVAGRHTHPGEESGYVLEGSLELEVDGQPPVTLKAGDSFFIPAGTVHNAK 79

                          90       100
                  ....*....|....*....|.
gi 1819705762 120 PVGKVPLKVVVTYIVERGQPL 140
Cdd:cd02235    80 NVGSGPAKLLATYIVEKGKPL 100
cupin_BLR7677-like cd02234
Bradyrhizobium japonicum BLR7677 and related proteins, cupin domain; This family includes ...
 44-140 1.39e-13

Bradyrhizobium japonicum BLR7677 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLR7677, a Bradyrhizobium japonicum 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.


Pssm-ID: 380362 [Multi-domain]  Cd Length: 103  Bit Score: 62.52  E-value: 1.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819705762  44 TELQKLPLASDPSKEESIGIAVIQPSAPAERHSHAENEIGYVLAGASLLEVEGEPTRTIRTGDSFAIPAGRVHR--AKPV 121
Cdd:cd02234     4 TVLYSQPLPNIPGKEVTVLLVTYPPGAASPPHRHPGFVFAYVLEGEVRSQVNGGPPRVYKAGESFYEPPGAHHRvsRNAS 83

                          90
                  ....*....|....*....
gi 1819705762 122 GKVPLKVVVTYIVERGQPL 140
Cdd:cd02234    84 ATEPAKLLAVFVVDTGAPE 102
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 62-132 1.54e-12

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


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 58.81  E-value: 1.54e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1819705762  62 GIAVIQPSAPAERHSHA-ENEIGYVLAGASLLEVEGEPTrTIRTGDSFAIPAGRVHRAKPVGKVPLKVVVTY 132
Cdd:pfam07883   1 GLVTLPPGESSPPHRHPgEDEFFYVLEGEGELTVDGEEV-VLKAGDSVYFPAGVPHRFRNTGDEPARLLDVY 71
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
60-132 7.19e-12

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 58.23  E-value: 7.19e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819705762  60 SIGIAVIQPSAPAERHSHAEN-EIGYVLAGASLLEVEGEpTRTIRTGDSFAIPAGRVHRAKPVGKVPLKVVVTY 132
Cdd:COG0662    28 SVKRITVPPGAELSLHVHPHRdEFFYVLEGTGEVTIGDE-EVELKAGDSVYIPAGVPHRLRNPGDEPLELLEVQ 100
cupin_CV2614-like cd02236
Chromobacterium violaceum CV2614 and related proteins, cupin domain; This family includes ...
 60-139 8.37e-12

Chromobacterium violaceum CV2614 and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to CV2614, a Chromobacterium violaceum 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.


Pssm-ID: 380364 [Multi-domain]  Cd Length: 102  Bit Score: 57.89  E-value: 8.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819705762  60 SIGIAVIQPSAPAERHSHAENEIGYVLAGASLLEVEGEPTRTIRTGDSFAIPAGRVHRAKPVGKVPLKVVVTYIVERGQP 139
Cdd:cd02236    23 TVLRITIPPGAELPWHTHPVPNAGYVLSGELTVEYEDGKKRTFKAGDAFVEAVNTWHRGRNGGDEPVELLVFYAGAKGVP 102
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
60-132 4.31e-10

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 53.31  E-value: 4.31e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819705762  60 SIGIAVIQPSAPAERHSHAENEIGYVLAGASLLEVEGEpTRTIRTGDSFAIPAGRVHRAKPVGKVPLKVVVTY 132
Cdd:COG1917    24 EVVRVTFEPGARTPWHSHPGEELIYVLEGEGEVEVGGE-EYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVVF 95
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 61-132 1.74e-09

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.


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 50.94  E-value: 1.74e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819705762  61 IGIAVIQPSAPAERHSHAE-NEIGYVLAGASLLEVEGEPTRTIRTGDSFAIPAGRVHRAKPVGKVPLKVVVTY 132
Cdd:cd02208     1 ISVVTLPPGTSSPPHWHPEqDEIFYVLSGEGELTLDDGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVVS 73
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 60-127 4.03e-09

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.


Pssm-ID: 380344 [Multi-domain]  Cd Length: 100  Bit Score: 50.59  E-value: 4.03e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819705762  60 SIGIAVIQPSAPAERHSHAEN-EIGYVLAGASLLEVEGEPtRTIRTGDSFAIPAGRVHRAKPVGKVPLK 127
Cdd:cd02214    20 SLAHARVPPGESTLPHRLKGSeEVYYILEGEGTMEIDGEP-REVGPGDAVLIPPGAVQRIENTGEEDLV 87
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
61-130 5.32e-09

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 50.79  E-value: 5.32e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1819705762  61 IGIAVIQP-SAPAERHSHAEN-EIGYVLAGASLLEVEGEPTRtIRTGDSFAIPAGRVHRAKPVGKVPLKVVV 130
Cdd:COG3837    30 VNLITLPPgASSSPYHAHSAEeEFVYVLEGELTLRIGGEEYV-LEPGDSVGFPAGVPHRLRNRGDEPARYLV 100
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 66-119 6.53e-08

pectin degradation protein KdgF and related proteins, cupin domain; This family includes bacterial and archaeal pectin degradation protein KdgF that catalyzes the linearization of unsaturated uronates from both pectin and alginate, which are polysaccharides found in the cell walls of plants and brown algae, respectively, and represent an important source of carbon. These polysaccharides, mostly consisting of chains of uronates, can be metabolized by bacteria through a pathway of enzymatic steps to the key metabolite 2-keto-3-deoxygluconate (KDG). Pectin degradation is used by many plant-pathogenic bacteria during infection, and also, pectin and alginate can both represent abundant sources of carbohydrate for the production of biofuels. These proteins belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380366 [Multi-domain]  Cd Length: 104  Bit Score: 47.46  E-value: 6.53e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1819705762  66 IQPSAPAERHSHaENE-IGYVLAGASLLEVEGEpTRTIRTGDSFAIPAGRVHRAK 119
Cdd:cd02238    34 FEKGAVVPLHSH-PHEqIGYVLSGRFEFTIGGE-TRILKPGDSYYIPPNVPHGAE 86
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 62-126 6.80e-07

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.


Pssm-ID: 380393 [Multi-domain]  Cd Length: 76  Bit Score: 44.15  E-value: 6.80e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819705762  62 GIAVIQPSAPAERHSHAENEIGYVLAGASLLEVEGEpTRTIRTGDSFAIPAGRVHRAKPVGKVPL 126
Cdd:cd06988     5 AWCVVRPGTTSTPHSHHEYEIFIVISGKGIVVVDGE-REPVKAGDVVYIPPGTEHYVKNDGDEDF 68
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
 63-130 1.06e-06

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.


Pssm-ID: 380339 [Multi-domain]  Cd Length: 90  Bit Score: 44.03  E-value: 1.06e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819705762  63 IAVIQP-SAPAERHSHAENEIGYVLAGASLLEVEGEpTRTIRTGDSFAIPAGRVHRAKPVGKVPLKVVV 130
Cdd:cd02209    20 LVTLPPgGSGGEPYSHEGEEFGYVLEGELELTVGGE-TYVLEAGDSIYFDSDVPHRYRNPGDEPARVLW 87
COG3450 COG3450
Predicted enzyme of the cupin superfamily [General function prediction only];
51-113 3.64e-06

Predicted enzyme of the cupin superfamily [General function prediction only];


Pssm-ID: 442673  Cd Length: 108  Bit Score: 43.05  E-value: 3.64e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819705762  51 LASDPSKEESIGIAVIQPSApaERHSHAENEIGYVLAGASLLEVEGEPTRTIRTGDSFAIPAG 113
Cdd:COG3450    30 LFTSPDGGVSAGVWECTPGK--FRWDYDEDEFCYILEGRVTVTDDDGEPVEFGAGDSFVFPAG 90
cupin_PMI_typeII_C cd02213
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ...
 74-129 4.44e-06

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.


Pssm-ID: 380343 [Multi-domain]  Cd Length: 126  Bit Score: 43.31  E-value: 4.44e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1819705762  74 RHSHAeNEIGYVLAGASLLEVEGEpTRTIRTGDSFAIPAGRVHRAKPVGKVPLKVV 129
Cdd:cd02213    57 RHHHR-SEHWVVVSGTAEVTLDGK-EKLLKEGESIYIPKGTKHRLENPGKIPLEII 110
cupin_BacB cd06975
Bacillus subtilis bacilysin and related proteins, cupin domain; Bacilysin (BacB, also known as ...
 43-118 2.93e-05

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.


Pssm-ID: 380380 [Multi-domain]  Cd Length: 93  Bit Score: 40.26  E-value: 2.93e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819705762  43 WTELQklplasdpskeesigIAVIQPSAPAERHSHAENEIGYVLAGASLLEVEGEPTRTIRTGDSFAIPAGRVHRA 118
Cdd:cd06975    18 WTEIM---------------LSYIPPGAKMPLHQHREEQIGMILNGELEMTVGGEEQELEPLGDVYYAPPNVPHGA 78
cupin_Pac13-like cd20295
monomeric dehydratase Pac13 and related proteins, cupin domain; This family includes a small ...
 57-131 3.04e-04

monomeric dehydratase Pac13 and related proteins, cupin domain; This family includes a small monomeric dehydratase Pac13 that mediates the formation of the 3'-deoxynucleotide of pacidamycins, which are uradyl peptide antibiotics (UPAs). Pac13 is involved in the formation of the unique 3'-deoxyuridine moiety found in these UPAs; it catalyzes the dehydration of uridine-5'-aldehyde. The similarity of the 3'-deoxy pacidamycin moiety with synthetic anti-retrovirals, offers a potential opportunity for the utilization of Pac13 in the biocatalytic generation of antiviral compounds. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380429 [Multi-domain]  Cd Length: 101  Bit Score: 37.58  E-value: 3.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819705762  57 KEESIGIAVIQPSAPAERHSHAEN-EIGYVLAGASLLEVEGEPTRtIRTGDSFAIPAGRVHRAkpVGKVPLKVVVT 131
Cdd:cd20295    18 DDPPASVHLVEVEEGHEEHYHKKStEIYYVLEGEGIFELDGEAVP-VKPGDLVLIPPGTRHRA--VGKMKILLIVI 90
cupin_TM1112-like cd02227
Thermotoga maritima TM1112 and related proteins, cupin domain; This family includes bacterial ...
 69-113 3.15e-04

Thermotoga maritima TM1112 and related proteins, cupin domain; This family includes bacterial and plant proteins homologous to TM1112, a Thermotoga maritima protein of unknown function with a cupin beta barrel domain. TM1112 (also known as DUF861) is a subfamily of RmlC-like cupins with a conserved "jelly roll-like" beta-barrel fold; structures indicate that a monomer is the biologically-relevant form.


Pssm-ID: 380356 [Multi-domain]  Cd Length: 69  Bit Score: 37.17  E-value: 3.15e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1819705762  69 SAPAERHSH-AENEIGYVLAGASLLEVEGEPTRTIRTGDSFAIPAG 113
Cdd:cd02227     7 CTPGKFPWNyDEDEFCYILEGEVRVTPEDGEPVTFKAGDLVVFPAG 52
cupin_TcmJ-like cd06991
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ...
 62-131 3.83e-04

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.


Pssm-ID: 380396 [Multi-domain]  Cd Length: 105  Bit Score: 37.66  E-value: 3.83e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1819705762  62 GIAVIQPSAPAERHSHA-ENEIGYVLAGASLLEVEGEPTRtIRTGDSFAIPAGRVHRAKPVGKVPLKVVVT 131
Cdd:cd06991    22 GTLTLAPGERVSEHYHPySEEFLYVVRGRLVVRVDGEPVV-LEAGEALLVPRGVRHRLENAGDEPARLVFH 91
cupin_YdbB-like cd02226
Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial ...
 75-129 4.57e-04

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.


Pssm-ID: 380355 [Multi-domain]  Cd Length: 94  Bit Score: 37.04  E-value: 4.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1819705762  75 HSHA-ENEIGYVLAGASLLEVEGEpTRTIRTGDSFAIPAGRVHRakPVGKVPLKVV 129
Cdd:cd02226    38 HKHDdEDELFLVLEGELTIDFRDR-DVTLGPGEFFVVPKGVEHR--PVAEEETVVL 90
cupin_Bh2720-like cd02223
Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, ...
 42-132 4.61e-04

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.


Pssm-ID: 380352 [Multi-domain]  Cd Length: 98  Bit Score: 37.14  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819705762  42 VWT--ELQkLPLASDPSKEEsIGiaviqpsapAERHSHAENEIgYVLAGASLLEVEGEpTRTIRTGDSFAIPAGRVHRAK 119
Cdd:cd02223     5 LWTgkNLQ-LVLMSIPPGED-IG---------LEVHDDVDQFL-RIEEGEGKAIMGGF-ESEVKDGDAIIVPAGTWHNVI 71

                          90
                  ....*....|...
gi 1819705762 120 PVGKVPLKVVVTY 132
Cdd:cd02223    72 NTGNEPLKLYTIY 84
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 73-127 5.21e-04

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.


Pssm-ID: 396749 [Multi-domain]  Cd Length: 134  Bit Score: 37.80  E-value: 5.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1819705762  73 ERHSHAENEIGYVLAGASLLEVEGEpTRTIRTGDSFAIPAGRVHRAKPVGKVPLK 127
Cdd:pfam02311  17 PPHVHDFYVIGYIERGVGRFRLNGR-TYHLGPGDLFLLPPGEPHDYEPESEDGWR 70
cupin_RhaR_RhaS-like_N cd06977
HTH-type transcriptional activator RhaR and RhaS and related proteins, N-terminal cupin domain; ...
 58-116 5.40e-04

HTH-type transcriptional activator RhaR and RhaS and related proteins, N-terminal cupin domain; Members of this family contain an N-terminal cupin domain and a C-terminal AraC/XylS family helix-turn-helix (HTH) DNA-binding domain, including the HTH-type transcription activators RhaS and RhaR. RhaS and RhaR respond to the availability of L-rhamnose and activate transcription of the operons in the Escherichia coli L-rhamnose catabolic regulon. The E. coli RhaR protein activates expression of the rhaSR operon in the presence of its effector, L-rhamnose. The resulting RhaS protein (plus L-rhamnose) activates expression of the L-rhamnose catabolic operon rhaBAD as well as the transport operon rhaT. These proteins bind DNA as dimers, via their HTH motifs. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380382 [Multi-domain]  Cd Length: 147  Bit Score: 38.01  E-value: 5.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1819705762  58 EESIGIAVIQPSAPAERHSHAENEIGYVLAGASLLEVEGEPTRtIRTGDSFAIPAGRVH 116
Cdd:cd06977     1 NQPVAVEPRAPQEPFPEHTHDFHEIVIVTKGSGIHVLNGHPYR-ITAGDVFYIRPDDRH 58
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 56-132 7.50e-04

Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds and both domains are included in this alignment. Each OxDC cupin domain contains one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380367 [Multi-domain]  Cd Length: 145  Bit Score: 37.46  E-value: 7.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819705762  56 SKEESIGIAVIQPSAPAERHSHA-ENEIGYVLAGASLLEVEGEPTR----TIRTGDSFAIPAGRVHRAKPVGKVPLKVVV 130
Cdd:cd02240    24 SKDLSSALVRVAPGAMRELHWHPnTAEWQYVISGSARVTVFDEDGRfetfNLGAGDVGYVPSGSGHHIENIGDEDAEFLL 103


                  ..
gi 1819705762 131 TY 132
Cdd:cd02240   104 IF 105
cupin_BacB_C cd10547
Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model ...
 61-118 8.08e-04

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.


Pssm-ID: 380415 [Multi-domain]  Cd Length: 92  Bit Score: 36.47  E-value: 8.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1819705762  61 IGIAVIQPSAPAERHSHAENEIGYVLAGASLLEVEGEpTRTIRTGDSFAIPAGRVHRA 118
Cdd:cd10547    21 IMISQIPPGGKMPLHQHRGEQIGIILNGKYDMTVGGE-EQELGYGKIYYAPPNVSHSG 77
MannoseP_isomer pfam01050
Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the ...
 54-129 8.14e-04

Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the mannose-6-phosphate isomerases. The type II phosphomannose isomerases are bifunctional enzymes. This Pfam entry covers the isomerase domain. The guanosine diphospho-D-mannose pyrophosphorylase domain is in another Pfam entry, see pfam00483.


Pssm-ID: 426015 [Multi-domain]  Cd Length: 151  Bit Score: 37.40  E-value: 8.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819705762  54 DPSKEESIGIAVIQPSA--PAERHSH-AENEIgyVLAGASLLEVEGEpTRTIRTGDSFAIPAGRVHRAKPVGKVPLKVV 129
Cdd:pfam01050  58 DEGERYQVKRITVKPGArlSLQMHHHrAEHWI--VVSGTARVTKGGE-TFLLTENESTYIPLGTIHRLENPGKIPLELI 133
cupin_BLR2406-like cd02210
Bradyrhizobium japonicum BLR2406 and related proteins, cupin domain; This family includes ...
 56-118 8.98e-04

Bradyrhizobium japonicum BLR2406 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLR2406, a Bradyrhizobium japonicum protein of unknown function with a cupin beta barrel domain. Proteins in this subfamily appear to align closest to RmlC carbohydrate epimerase which is involved in dTDP-L-rhamnose production, and belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380340 [Multi-domain]  Cd Length: 98  Bit Score: 36.34  E-value: 8.98e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819705762  56 SKEESIGIAVIQPSAPAERHSHAENEIG-YVLAGASLLEV--EGEPTRTIRTGDSFAIPAGRVHRA 118
Cdd:cd02210     8 AKGLWMGVVTIPPGARTGAHHHGEHETAiYVLSGRAETRYgdRLEHRAEAGPGDFIYIPPGVPHQE 73
cupin_reut_a1446 cd06981
Cupriavidus pinatubonensis reut_a1446 and related proteins, cupin domain; This family includes ...
 79-117 9.09e-04

Cupriavidus pinatubonensis reut_a1446 and related proteins, cupin domain; This family includes bacterial and some eukaryotic proteins homologous to reut_a1446, a Cupriavidus pinatubonensis protein of unknown function that may be related to mannose-6-phosphate isomerase. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380386  Cd Length: 103  Bit Score: 36.31  E-value: 9.09e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1819705762  79 ENEIGYVLAGASLLEVEGEPTRTIRTGDSFAIPAGRVHR 117
Cdd:cd06981    48 EDEWVLLLQGEAELEFEDGEEVELKPGDYLLIPAHCRHR 86
cupin_HNL-like cd02233
Granulicella tundricola hydroxynitrile lyase (GtHNL) and related proteins, cupin domain; This ...
 40-116 1.00e-03

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.


Pssm-ID: 380361 [Multi-domain]  Cd Length: 106  Bit Score: 36.38  E-value: 1.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819705762  40 GIVWTElqklPLASDPSKEE-SIGIAVIQPSAPAERHSHAENEIGYVLAGASLLEVEGEPTRTIRTGDSFAIPAGRVH 116
Cdd:cd02233     3 GTVWLD----PLFPADEPSRvSVANVTFEPGARTAWHTHPGGQILIVTSGVGWVQEEGGPPQELRPGDVVWIPPGVKH 76
Cupin_3 pfam05899
EutQ-like cupin domain; This entry represents the cupin domain, with a conserved jelly ...
 79-113 1.48e-03

EutQ-like cupin domain; This entry represents the cupin domain, with a conserved jelly roll-like beta-barrel fold capable of homodimerization found in bacteria, plant and fungi. It is present in EutQ family from the eut operon, involved in ethanolamine degradation. EutQ is essential during anoxic growth and has acetate kinase activity. The cupin domain from EutQ does not possess the His residues responsible for metal coordination in other classes of cupins. This domain is also found in (S)-ureidoglycine aminohydrolase (UGlyAH) from E.coli, which is involved in the anaerobic nitrogen utilization via the assimilation of allantoin. It catalyzes the deamination of allantoin to produce S-ureidoglycolate and ammonia from S-ureidoglycine.


Pssm-ID: 399116 [Multi-domain]  Cd Length: 74  Bit Score: 35.34  E-value: 1.48e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1819705762  79 ENEIGYVLAGASLLEVEGEPTRTIRTGDSFAIPAG 113
Cdd:pfam05899  25 EDETCYILSGEVTVTPEGGKTVTLRAGDLVVLPKG 59
cupin_DddQ cd20282
dimethylsulfoniopropionate lyase DddQ, cupin domain; Dimethylsulfoniopropionate (DMSP) is ...
 75-145 1.54e-03

dimethylsulfoniopropionate lyase DddQ, cupin domain; Dimethylsulfoniopropionate (DMSP) is produced worldwide in large amounts, mainly by marine phytoplankton and macroalgae. DMSP lyase catalyzes the cleavage of DMSP to generate the volatile dimethyl sulfide (DMS) and plays a major role in the biogeochemical cycling of sulfur. When released into the atmosphere from the oceans, DMS is oxidized, forming cloud condensation nuclei that may influence weather and climate. DMSP lyase belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380418 [Multi-domain]  Cd Length: 103  Bit Score: 36.09  E-value: 1.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1819705762  75 HSHAENEIGYVLAGASLLEVEGEPTRTIRTGDSFAIPAGRVHRAKPVGKvPLkvvVTYIVERGQPLARPAR 145
Cdd:cd20282    36 HHHAAEEIYLVLAGSAEFLSEGQPPRRLGPGDTVFHASNQPHAMRTGDE-PL---LALVLWRGADLATLPV 102
RmlC COG4101
Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only];
60-118 1.77e-03

Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only];


Pssm-ID: 443277  Cd Length: 146  Bit Score: 36.48  E-value: 1.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1819705762  60 SIGIAVIQPSAPAERHSHAENEIG-YVLAG-ASLLEVEGEPTRTI-RTGDSFAIPAGRVHRA 118
Cdd:COG4101    47 WMGLVTIPPGARAKAHHHGEHETAiYVLSGrAETRYGERLEHRVVtEPGDFIFIPPGVPHQE 108
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 75-130 1.96e-03

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.


Pssm-ID: 395138  Cd Length: 151  Bit Score: 36.16  E-value: 1.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1819705762  75 HSHAeNEIGYVLAGASLLE--VEGEPTR----TIRTGDSFAIPAGRVHRAKPVGKVPLKVVV 130
Cdd:pfam00190  51 HPNA-TEILYVLQGRGRVGfvVPGNGNRvfhkVLREGDVFVVPQGLPHFQYNIGDEPAVAFV 111
cupin_BacB_N cd20307
Bacillus subtilis bacilysin and related proteins, N-terminal cupin domain; This model ...
 63-97 2.21e-03

Bacillus subtilis bacilysin and related proteins, N-terminal cupin domain; This model represents the N-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.


Pssm-ID: 380441 [Multi-domain]  Cd Length: 100  Bit Score: 35.32  E-value: 2.21e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1819705762  63 IAVIQPSAPAERHSHAENEIGYVLAGASLLEVEGE 97
Cdd:cd20307    28 LSYIAPGAVVELHQHPESQIGMVLSGELEMNVGGV 62
cupin_ARD cd02232
acireductone dioxygenase (ARD), cupin domain; Acireductone dioxygenase (ARD; also known as 1, ...
 75-117 2.35e-03

acireductone dioxygenase (ARD), cupin domain; Acireductone dioxygenase (ARD; also known as 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase) catalyzes the oxidation of 1,2-dihydroxy-3-keto-5-methylthiopentene to yield two different products depending on which active site metal is present (Fe2+ or Ni2+) as part of the methionine salvage pathway. The ARD apo-enzyme, obtained after the metal is removed, is catalytically inactive. The Fe(II)-ARD reaction yields an alpha-keto acid and formic acid, while Ni(II)-ARD instead catalyzes a shunt out of the methionine salvage pathway, yielding methylthiocarboxylic acid, formic acid, and CO. ARD belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization


Pssm-ID: 380360  Cd Length: 134  Bit Score: 35.98  E-value: 2.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1819705762  75 HSHAENEIGYVLAGASLLEVEGEPTRTIR----TGDSFAIPAGRVHR 117
Cdd:cd02232    65 HLHEDDEVRFILDGSGYFDVRDKDDEWIRilveKGDLIVVPAGIYHR 111
cupin_SPO2919-like cd02224
Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase ...
 61-113 4.45e-03

Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase with a cupin domain; This family includes proteins similar to sugar phosphate isomerase SPO2919 from Silicibacter pomeroyi and Afe_0303 from Acidithiobacillus ferrooxidans, but are as yet uncharacterized. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.


Pssm-ID: 380353 [Multi-domain]  Cd Length: 105  Bit Score: 34.77  E-value: 4.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1819705762  61 IGIAVIQP-SAPAERHSH-AENEIGYVLAGASLLEVEGEpTRTIRTGDSFAIPAG 113
Cdd:cd02224    19 VNLERLPPgARSSPRHWHsAEEEFVYVLSGEGTLRLDGE-EVLPRPGDFVGFPAG 72
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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