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Conserved domains on  [gi|1129014406|ref|WP_075334877|]
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cupin domain-containing protein [Pseudonocardia sp. Ae717_Ps2]

Protein Classification

cupin domain-containing protein( domain architecture ID 14401328)

cupin domain-containing protein similar to Streptomyces glaucescens TcmJ, a quinone-forming monooxygenase involved in the modification of aromatic polyketides synthesized by polyketide synthases of types II and III

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cupin_TcmJ-like cd06991
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ...
 35-139 1.20e-51

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: 159.38  E-value: 1.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129014406  35 RGADLRIVLSPRSGGAQEGLLVIATIRPGESVTEHYHPYSEERVTVLGGAMELTVGEHRHEIGPDSSFVIPRGMRHRMTC 114
Cdd:cd06991     1 RGGDLRILLSPKTVGATSGFMGTLTLAPGERVSEHYHPYSEEFLYVVRGRLVVRVDGEPVVLEAGEALLVPRGVRHRLEN 80

                          90       100
                  ....*....|....*....|....*
gi 1129014406 115 LGDAPVRAVLTMSPLAPRPEWGHVD 139
Cdd:cd06991    81 AGDEPARLVFHLSPLAPRPELGHVD 105
 
Name Accession Description Interval E-value
cupin_TcmJ-like cd06991
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ...
 35-139 1.20e-51

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: 159.38  E-value: 1.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129014406  35 RGADLRIVLSPRSGGAQEGLLVIATIRPGESVTEHYHPYSEERVTVLGGAMELTVGEHRHEIGPDSSFVIPRGMRHRMTC 114
Cdd:cd06991     1 RGGDLRILLSPKTVGATSGFMGTLTLAPGERVSEHYHPYSEEFLYVVRGRLVVRVDGEPVVLEAGEALLVPRGVRHRLEN 80

                          90       100
                  ....*....|....*....|....*
gi 1129014406 115 LGDAPVRAVLTMSPLAPRPEWGHVD 139
Cdd:cd06991    81 AGDEPARLVFHLSPLAPRPELGHVD 105
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
55-128 7.89e-16

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 68.63  E-value: 7.89e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1129014406  55 LVIATIRPGESVTEHYHPYSEERVTVLGGAMELTVGEHRHEIGPDSSFVIPRGMRHRMTCLGDAPVRAVLTMSP 128
Cdd:COG0662    29 VKRITVPPGAELSLHVHPHRDEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRLRNPGDEPLELLEVQAP 102
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 56-123 1.37e-15

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: 66.51  E-value: 1.37e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1129014406  56 VIATIRPGESVTEHYHPYSEERVTVLGGAMELTVGEHRHEIGPDSSFVIPRGMRHRMTCLGDAPVRAV 123
Cdd:pfam07883   1 GLVTLPPGESSPPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLL 68
PRK09943 PRK09943
HTH-type transcriptional regulator PuuR;
15-128 5.70e-06

HTH-type transcriptional regulator PuuR;


Pssm-ID: 182158 [Multi-domain]  Cd Length: 185  Bit Score: 43.63  E-value: 5.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129014406  15 ERPAEPVTVVRTDDVSPLPGRGADLRIVlspRSGGAQEGL-LVIATIRPGESVTEHYHPYSEERVTVLGGAMELTVGEHR 93
Cdd:PRK09943   71 EKPDEPQVVINQDDLIEMGSQGVSMKLV---HNGNPNRTLaMIFETYQPGTTTGERIKHQGEEIGTVLEGEIVLTINGQD 147

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1129014406  94 HEIGPDSSFVIPRGMRHRMTCLGDAPVRAVLTMSP 128
Cdd:PRK09943  148 YHLVAGQSYAINTGIPHSFSNTSAGICRIISAHTP 182
 
Name Accession Description Interval E-value
cupin_TcmJ-like cd06991
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ...
 35-139 1.20e-51

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: 159.38  E-value: 1.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129014406  35 RGADLRIVLSPRSGGAQEGLLVIATIRPGESVTEHYHPYSEERVTVLGGAMELTVGEHRHEIGPDSSFVIPRGMRHRMTC 114
Cdd:cd06991     1 RGGDLRILLSPKTVGATSGFMGTLTLAPGERVSEHYHPYSEEFLYVVRGRLVVRVDGEPVVLEAGEALLVPRGVRHRLEN 80

                          90       100
                  ....*....|....*....|....*
gi 1129014406 115 LGDAPVRAVLTMSPLAPRPEWGHVD 139
Cdd:cd06991    81 AGDEPARLVFHLSPLAPRPELGHVD 105
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
55-128 7.89e-16

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 68.63  E-value: 7.89e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1129014406  55 LVIATIRPGESVTEHYHPYSEERVTVLGGAMELTVGEHRHEIGPDSSFVIPRGMRHRMTCLGDAPVRAVLTMSP 128
Cdd:COG0662    29 VKRITVPPGAELSLHVHPHRDEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRLRNPGDEPLELLEVQAP 102
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 56-123 1.37e-15

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: 66.51  E-value: 1.37e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1129014406  56 VIATIRPGESVTEHYHPYSEERVTVLGGAMELTVGEHRHEIGPDSSFVIPRGMRHRMTCLGDAPVRAV 123
Cdd:pfam07883   1 GLVTLPPGESSPPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLL 68
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
41-130 2.83e-13

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 61.40  E-value: 2.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129014406  41 IVLSPRSGGAQEGLLVIATIRPGESVTEHYHPYsEERVTVLGGAMELTVGEHRHEIGPDSSFVIPRGMRHRMTCLGDAPV 120
Cdd:COG1917    11 VSVRVLADGEDELEVVRVTFEPGARTPWHSHPG-EELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGDEPA 89

                          90
                  ....*....|
gi 1129014406 121 RAVLTMSPLA 130
Cdd:COG1917    90 VLLVVFSPGL 99
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
23-139 1.92e-12

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 59.65  E-value: 1.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129014406  23 VVRTDDVSPlPGRGADLRiVLSPRSGGAQEGLLVIaTIRPGESVTE-HYHPYSEERVTVLGGAMELTVGEHRHEIGPDSS 101
Cdd:COG3837     1 IVNLDDLPG-PEAGRRYR-RLGDALGLTRLGVNLI-TLPPGASSSPyHAHSAEEEFVYVLEGELTLRIGGEEYVLEPGDS 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1129014406 102 FVIPRGMRHRMTCLGDAPVRAVLTMSPLAPRPEWGHVD 139
Cdd:COG3837    78 VGFPAGVPHRLRNRGDEPARYLVVGTRAPYPDSFDYWD 115
cupin_PMI_typeII_C cd02213
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ...
 59-121 4.50e-11

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: 56.41  E-value: 4.50e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1129014406  59 TIRPGESVTEHYHPYSEERVTVLGGAMELTVGEHRHEIGPDSSFVIPRGMRHRMTCLGDAPVR 121
Cdd:cd02213    46 TVNPGKRLSLQRHHHRSEHWVVVSGTAEVTLDGKEKLLKEGESIYIPKGTKHRLENPGKIPLE 108
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 55-125 1.46e-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: 51.33  E-value: 1.46e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1129014406  55 LVIATIRPGESVTEHYHPYSEERVTVLGGAMELTVG-EHRHEIGPDSSFVIPRGMRHRMTCLGDAPVRAVLT 125
Cdd:cd02208     1 ISVVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDdGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVV 72
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
 43-127 1.55e-09

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: 51.35  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129014406  43 LSPRSGGAQ-EGLLViaTIRPGESVTEHY-HPySEERVTVLGGAMELTVGEHRHEIGPDSSFVIPRGMRHRMTCLGDAPV 120
Cdd:cd02209     7 LSPGLPGRKmEPFLV--TLPPGGSGGEPYsHE-GEEFGYVLEGELELTVGGETYVLEAGDSIYFDSDVPHRYRNPGDEPA 83


                  ....*..
gi 1129014406 121 RAVLTMS 127
Cdd:cd02209    84 RVLWVIT 90
cupin_UGlyAH_N cd02211
(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family ...
 30-124 2.51e-09

(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.


Pssm-ID: 380341 [Multi-domain]  Cd Length: 117  Bit Score: 51.75  E-value: 2.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129014406  30 SPLPG-RGADLRIVLSPRSGG--AQegllVIATIRPGESVTEHYHPYSEER-VTVLGGAMELTVGEHRHEIGPDSSFVIP 105
Cdd:cd02211     3 SVLPGwENTRASVLASPKLGAtfVQ----YLVEVEPGGGSTAPEGGEGIERfLYVLEGEVELTVGGETHTLTAGGYAYLP 78

                          90
                  ....*....|....*....
gi 1129014406 106 RGMRHRMTCLGDAPVRAVL 124
Cdd:cd02211    79 PGTKHSLRNAGDEPARLLW 97
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 48-135 2.72e-09

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: 51.32  E-value: 2.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129014406  48 GGAQEGLLVIATIRPGESVTEHYHPysEERVT-VLGGAMELTVGEHRHEIGPDSSFVIPRGMRHRMTCLGDApvRAVLTM 126
Cdd:cd02238    22 AGGEKLMLVEVRFEKGAVVPLHSHP--HEQIGyVLSGRFEFTIGGETRILKPGDSYYIPPNVPHGAEALEDS--VLLDVF 97


                  ....*....
gi 1129014406 127 SPlaPRPEW 135
Cdd:cd02238    98 SP--PREDF 104
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 58-119 1.18e-08

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: 49.44  E-value: 1.18e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1129014406  58 ATIRPGESVTEHYHPYSEERVTVLGGAMELTVGEHRHEIGPDSSFVIPRGMRHRMTCLGDAP 119
Cdd:cd02214    24 ARVPPGESTLPHRLKGSEEVYYILEGEGTMEIDGEPREVGPGDAVLIPPGAVQRIENTGEED 85
PRK09943 PRK09943
HTH-type transcriptional regulator PuuR;
15-128 5.70e-06

HTH-type transcriptional regulator PuuR;


Pssm-ID: 182158 [Multi-domain]  Cd Length: 185  Bit Score: 43.63  E-value: 5.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129014406  15 ERPAEPVTVVRTDDVSPLPGRGADLRIVlspRSGGAQEGL-LVIATIRPGESVTEHYHPYSEERVTVLGGAMELTVGEHR 93
Cdd:PRK09943   71 EKPDEPQVVINQDDLIEMGSQGVSMKLV---HNGNPNRTLaMIFETYQPGTTTGERIKHQGEEIGTVLEGEIVLTINGQD 147

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1129014406  94 HEIGPDSSFVIPRGMRHRMTCLGDAPVRAVLTMSP 128
Cdd:PRK09943  148 YHLVAGQSYAINTGIPHSFSNTSAGICRIISAHTP 182
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 59-121 1.02e-05

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.


Pssm-ID: 380351 [Multi-domain]  Cd Length: 91  Bit Score: 41.28  E-value: 1.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1129014406  59 TIRPGESVTEHYHPYsEERVTVLGGAMELTVGEHRHEIGPDSSFVIPRGMRHRMTCLGDAPVR 121
Cdd:cd02222    23 EIEPGGHTPLHTHPW-EHEVYVLRGKGVVVIGGEEYPVKPGDVVYIPPNEPHQFRNTGDEPLG 84
PRK11171 PRK11171
(S)-ureidoglycine aminohydrolase;
30-124 1.23e-05

(S)-ureidoglycine aminohydrolase;


Pssm-ID: 183011 [Multi-domain]  Cd Length: 266  Bit Score: 43.35  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129014406  30 SPLPG-RGADLRIVLSPRSGG--AQegllVIATIRPGESVTEHYHPYSEERVT-VLGGAMELTVGEHRHEIGPDSSFVIP 105
Cdd:PRK11171   39 SVLPGwENTRAWVLARPGLGAtfSQ----YLVEVEPGGGSDQPEPDEGAETFLfVVEGEITLTLEGKTHALSEGGYAYLP 114

                          90
                  ....*....|....*....
gi 1129014406 106 RGMRHRMTCLGDAPVRAVL 124
Cdd:PRK11171  115 PGSDWTLRNAGAEDARFHW 133
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
 47-126 1.26e-05

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: 41.41  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129014406  47 SGGAQEGLLVIATIRPGESVTEHYHPySEERVTVLGGAMELTV-GEHRHEIGPDSSFVIPRGMRHRMTCLGDAPVRAVLT 125
Cdd:cd02235    13 SVPGREVVQVRVEIPPGAVAGRHTHP-GEESGYVLEGSLELEVdGQPPVTLKAGDSFFIPAGTVHNAKNVGSGPAKLLAT 91


                  .
gi 1129014406 126 M 126
Cdd:cd02235    92 Y 92
cupin_RemF-like cd06979
Streptomyces resistomycificus RemF cyclase and related proteins, cupin domain; RemF cyclase is ...
 59-128 8.39e-05

Streptomyces resistomycificus RemF cyclase and related proteins, cupin domain; RemF cyclase is a manganese-containing polyketide cyclase present in bacteria that is involved in the biosynthesis of resistomycin, the aromatic pentacyclic metabolite in Streptomyces resistomycificus. Structure of this enzyme shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold that forms a homodimer. It contains an unusual octahedral zinc-binding site in a large hydrophobic pocket that may represent the active site. The zinc ion, coordinated to four histidine side chains and two water molecules, could act as a Lewis acid in the aldol condensation reaction catalyzed by RemF, reminiscent of class II aldolases.


Pssm-ID: 380384 [Multi-domain]  Cd Length: 93  Bit Score: 38.98  E-value: 8.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1129014406  59 TIRPGESVT-EHYHPYSEERVTVLGGAMELTVGEHRHEIGPDSSFVIPRGMRHRMTCLGDAPVRAVLTMSP 128
Cdd:cd06979    23 EVSPNAGMPpPHYHEDWEETIYGLEGSVTLTLPGKTVEVGPGDSIFIPRGEVHGFVNRSGGPTCRLCVLAP 93
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 55-124 1.58e-04

Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 441743 [Multi-domain]  Cd Length: 115  Bit Score: 38.79  E-value: 1.58e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1129014406  55 LVIATIRPGESVTEHYHPYSEERVTVLGGAMELTV----GEHRH-EIGPDSSFVIPRGMRHRMTCLGDAPVRAVL 124
Cdd:COG2140     5 GGLTVLEPGGVREEHWHPNAAEWYYVLSGEARMTVqdppGRARTvDVGPGDVVYVPPGYGHYIINTGDEPLVFLA 79
cupin_HP0902-like cd02230
Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes ...
 55-128 1.62e-04

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.


Pssm-ID: 380358 [Multi-domain]  Cd Length: 83  Bit Score: 37.87  E-value: 1.62e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1129014406  55 LVIATIRPGESVTEHYHPYsEERVTVLGGAMELTVGEHRHEIGPDSSFVIPRGMRHRMTCLGDAPVraVLTMSP 128
Cdd:cd02230    13 VTLFAFDAGQELSEHTAPG-DATVQVLEGEAEFTIGGETVTLKAGELIVMPANVPHALKAEEDFKM--LLTLIK 83
cupin_YdbB-like cd02226
Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial ...
 69-111 3.60e-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: 37.42  E-value: 3.60e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1129014406  69 HYHPYSEERVTVLGGAMELTVGEHRHEIGPDSSFVIPRGMRHR 111
Cdd:cd02226    38 HKHDDEDELFLVLEGELTIDFRDRDVTLGPGEFFVVPKGVEHR 80
cupin_XcTcmJ-like cd07006
Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes ...
 59-123 8.06e-04

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.


Pssm-ID: 380409 [Multi-domain]  Cd Length: 89  Bit Score: 36.19  E-value: 8.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1129014406  59 TIRPGESV--TEHYHPYSEERVTVLGGAMELTVGEHRHEIGPDSSFVIPRGMRHRMTCLGDAPVRAV 123
Cdd:cd07006    16 VLAPGDTEggPDNRHRGSDQWLYVVSGSGEAIVEGERVALKPGSLLLIEAGETHEIRNTGDEPLKTL 82
RmlC COG4101
Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only];
10-128 9.80e-04

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


Pssm-ID: 443277  Cd Length: 146  Bit Score: 37.25  E-value: 9.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129014406  10 PALPAERPAEPVTVVRTDDVSPLPGR-GADLRIVLSPRSGGAQEGLLVIATIRPGESVTEHYHPYSEERVTVLGGAMELT 88
Cdd:COG4101     2 STLTIDWAHAGVRVVRPGLDATTAGKqGLDYFEGISAETVGSTGLWMGLVTIPPGARAKAHHHGEHETAIYVLSGRAETR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1129014406  89 VG---EHRHEIGPDSSFVIPRGMRHRMTCLGDA-PVRAVLTMSP 128
Cdd:COG4101    82 YGerlEHRVVTEPGDFIFIPPGVPHQEINLSDTePAVAVIARTD 125
cupin_Moth_1897 cd06984
uncharacterized Methanocaldococcus jannaschii Moth_1897 and related proteins, cupin domain; ...
 52-126 3.54e-03

uncharacterized Methanocaldococcus jannaschii Moth_1897 and related proteins, cupin domain; This family includes archaeal and bacterial proteins homologous to Moth_1897, a Methanocaldococcus jannaschii 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: 380389 [Multi-domain]  Cd Length: 83  Bit Score: 34.53  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129014406  52 EGLLVIATIRPGESVTEHYHP-----YseervtVLGGAMELTVGEHRHEIGPDSSFVIPRGMRHRMTCLGDAPVRaVLTM 126
Cdd:cd06984    10 HAQIVHITLKPGESLKKHITPvdvffY------VLEGEGIVEIGEEKQEVEADTLIESPANIPHCLYNESDADLR-VLVI 82
cupin_OxOx cd02241
Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3. ...
 55-123 3.67e-03

Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3.4) catalyzes the manganese-dependent oxidative decarboxylation of oxalate to carbon dioxide and hydrogen peroxide (H2O2). It is widespread in fungi and various plant tissues and may play a role in plant signaling and defense. This enzyme has been employed in a widely used assay for detecting urinary oxalate levels. Also, the gene encoding OxOx from barley roots has been expressed in oilseed rape in order to provide a defense against externally supplied oxalic acid. In germin, the predominant protein produced during the early phase of wheat germination, it is believed that H2O2 production is employed as a defense mechanism in response to infection by pathogens. Germin is also a marker of growth onset in cell walls in germinating cereals. The H2O2 produced by OxOx, together with the Ca2+ released by degradation of calcium oxalate, are thought to mediate cell wall cross-linking at high concentrations. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380368  Cd Length: 191  Bit Score: 35.65  E-value: 3.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1129014406  55 LVIATIRPGESVTEHYHPYSEERVTVLGGamELTVG--------EHRHEIGPDSSFVIPRGMRHRMTCLGDAPVRAV 123
Cdd:cd02241    72 MARGDLAPCGVNPPHTHPRATELLYVVEG--TLYVGfvdengnrLFTKTLNPGDVFVFPQGLIHFQFNPGCEPAVFV 146
cupin_BacB cd06975
Bacillus subtilis bacilysin and related proteins, cupin domain; Bacilysin (BacB, also known as ...
 55-98 3.80e-03

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: 34.48  E-value: 3.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1129014406  55 LVIATIRPGESVTEHYHPysEERV-TVLGGAMELTVGEHRHEIGP 98
Cdd:cd06975    21 IMLSYIPPGAKMPLHQHR--EEQIgMILNGELEMTVGGEEQELEP 63
cupin_Bh2720-like cd02223
Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, ...
 55-119 4.59e-03

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: 34.44  E-value: 4.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1129014406  55 LVIATIRPGESVTEHYHPYSEERVTVLGGAMELTVGEHRHEIGPDSSFVIPRGMRHRMTCLGDAP 119
Cdd:cd02223    13 LVLMSIPPGEDIGLEVHDDVDQFLRIEEGEGKAIMGGFESEVKDGDAIIVPAGTWHNVINTGNEP 77
cpsB PRK15460
mannose-1-phosphate guanyltransferase; Provisional
 59-120 7.23e-03

mannose-1-phosphate guanyltransferase; Provisional


Pssm-ID: 185357 [Multi-domain]  Cd Length: 478  Bit Score: 35.33  E-value: 7.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1129014406  59 TIRPGESVTEHYHPYSEERVTVLGGAMELTVGEHRHEIGPDSSFVIPRGMRHRMTCLGDAPV 120
Cdd:PRK15460  391 TVKPGEGLSVQMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPL 452
 
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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