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Conserved domains on  [gi|1039950589|ref|WP_065019642|]
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cupin domain-containing protein [Mycolicibacterium fortuitum]

Protein Classification

cupin domain-containing protein( domain architecture ID 14388801)

cupin domain-containing protein similar to Bradyrhizobium japonicum BLR7677, a protein of unknown function

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cupin_BLR7677-like cd02234
Bradyrhizobium japonicum BLR7677 and related proteins, cupin domain; This family includes ...
 41-141 7.21e-44

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: 139.95  E-value: 7.21e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039950589  41 ETLNPLLEQALPNVPGKTFTSAIVDFPPGARAVPHRHGeAFVYAYVLEGSVRSELGDAPAKTYGTGENWVEEPGAHHVLT 120
Cdd:cd02234     1 ETVTVLYSQPLPNIPGKEVTVLLVTYPPGAASPPHRHP-GFVFAYVLEGEVRSQVNGGPPRVYKAGESFYEPPGAHHRVS 79

                          90       100
                  ....*....|....*....|.
gi 1039950589 121 ENPSQTDRAKLLVVFISNTGD 141
Cdd:cd02234    80 RNASATEPAKLLAVFVVDTGA 100
 
Name Accession Description Interval E-value
cupin_BLR7677-like cd02234
Bradyrhizobium japonicum BLR7677 and related proteins, cupin domain; This family includes ...
 41-141 7.21e-44

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: 139.95  E-value: 7.21e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039950589  41 ETLNPLLEQALPNVPGKTFTSAIVDFPPGARAVPHRHGeAFVYAYVLEGSVRSELGDAPAKTYGTGENWVEEPGAHHVLT 120
Cdd:cd02234     1 ETVTVLYSQPLPNIPGKEVTVLLVTYPPGAASPPHRHP-GFVFAYVLEGEVRSQVNGGPPRVYKAGESFYEPPGAHHRVS 79

                          90       100
                  ....*....|....*....|.
gi 1039950589 121 ENPSQTDRAKLLVVFISNTGD 141
Cdd:cd02234    80 RNASATEPAKLLAVFVVDTGA 100
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 62-135 1.45e-08

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: 48.79  E-value: 1.45e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039950589  62 AIVDFPPGARAVPHRHGEAFVYAYVLEGSVRSELGDAPaKTYGTGENWVEEPGAHHVLtENPSQTDrAKLLVVF 135
Cdd:pfam07883   1 GLVTLPPGESSPPHRHPGEDEFFYVLEGEGELTVDGEE-VVLKAGDSVYFPAGVPHRF-RNTGDEP-ARLLDVY 71
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
59-135 2.86e-07

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 46.00  E-value: 2.86e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039950589  59 FTSAIVDFPPGARAVPHRHgEAFVYAYVLEGSVRSELGDAPaKTYGTGENWVEEPGAHHVLTENPSQTdrAKLLVVF 135
Cdd:COG1917    23 LEVVRVTFEPGARTPWHSH-PGEELIYVLEGEGEVEVGGEE-YELKPGDVVFIPPGVPHAFRNLGDEP--AVLLVVF 95
 
Name Accession Description Interval E-value
cupin_BLR7677-like cd02234
Bradyrhizobium japonicum BLR7677 and related proteins, cupin domain; This family includes ...
 41-141 7.21e-44

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: 139.95  E-value: 7.21e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039950589  41 ETLNPLLEQALPNVPGKTFTSAIVDFPPGARAVPHRHGeAFVYAYVLEGSVRSELGDAPAKTYGTGENWVEEPGAHHVLT 120
Cdd:cd02234     1 ETVTVLYSQPLPNIPGKEVTVLLVTYPPGAASPPHRHP-GFVFAYVLEGEVRSQVNGGPPRVYKAGESFYEPPGAHHRVS 79

                          90       100
                  ....*....|....*....|.
gi 1039950589 121 ENPSQTDRAKLLVVFISNTGD 141
Cdd:cd02234    80 RNASATEPAKLLAVFVVDTGA 100
cupin_CV2614-like cd02236
Chromobacterium violaceum CV2614 and related proteins, cupin domain; This family includes ...
 60-140 4.00e-10

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: 53.65  E-value: 4.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039950589  60 TSAIVDFPPGARAVPHRHGeAFVYAYVLEGSVRSELGDAPAKTYGTGENWVEEPGAHHVLtENPSQTDrAKLLVVFISNT 139
Cdd:cd02236    23 TVLRITIPPGAELPWHTHP-VPNAGYVLSGELTVEYEDGKKRTFKAGDAFVEAVNTWHRG-RNGGDEP-VELLVFYAGAK 99


                  .
gi 1039950589 140 G 140
Cdd:cd02236   100 G 100
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
 45-136 7.57e-09

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: 50.27  E-value: 7.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039950589  45 PLLEQALPnVPGKTFTSAIVDFPPGARAVPHRH-GEAFvyAYVLEGSVRSELGDAPAKTYGTGENWVEEPGAHHVLTeNP 123
Cdd:cd02235     6 VLQRTDLS-VPGREVVQVRVEIPPGAVAGRHTHpGEES--GYVLEGSLELEVDGQPPVTLKAGDSFFIPAGTVHNAK-NV 81

                          90
                  ....*....|...
gi 1039950589 124 SqTDRAKLLVVFI 136
Cdd:cd02235    82 G-SGPAKLLATYI 93
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 62-135 1.45e-08

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: 48.79  E-value: 1.45e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039950589  62 AIVDFPPGARAVPHRHGEAFVYAYVLEGSVRSELGDAPaKTYGTGENWVEEPGAHHVLtENPSQTDrAKLLVVF 135
Cdd:pfam07883   1 GLVTLPPGESSPPHRHPGEDEFFYVLEGEGELTVDGEE-VVLKAGDSVYFPAGVPHRF-RNTGDEP-ARLLDVY 71
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
59-135 2.86e-07

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 46.00  E-value: 2.86e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039950589  59 FTSAIVDFPPGARAVPHRHgEAFVYAYVLEGSVRSELGDAPaKTYGTGENWVEEPGAHHVLTENPSQTdrAKLLVVF 135
Cdd:COG1917    23 LEVVRVTFEPGARTPWHSH-PGEELIYVLEGEGEVEVGGEE-YELKPGDVVFIPPGVPHAFRNLGDEP--AVLLVVF 95
cupin_ChrR_1 cd20303
Marinobacter hydrocarbonoclasticus anti-ECFsigma factor ChrR, and similar proteins; 2 ...
 62-103 3.32e-05

Marinobacter hydrocarbonoclasticus anti-ECFsigma factor ChrR, and similar proteins; 2 heterologous tandem repeats of cupin domain; This family contains bacterial anti-sigma factor such as ChrR from Marinobacter hydrocarbonoclasticus. 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 ECF sigma factor E (sigmaE), an essential factor to mount a transcriptional response to a singlet oxygen and for viability when carotenoids are limiting. This protein family likely contains two distinct homologous functional domains belonging to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380437 [Multi-domain]  Cd Length: 102  Bit Score: 40.66  E-value: 3.32e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1039950589  62 AIVDFPPGARAVPHRH--GEAFvyaYVLEGSVRSELGDAPAKTY 103
Cdd:cd20303    36 ALVRWAPGTRFPPHSHpgGEEI---LVLEGTFSDEHGDYPAGTW 76
cupin_DAD_ChrR cd02237
2,4'-Dihydroxyacetophenone dioxygenase (DAD) and anti-sigma factor ChrR, and similar proteins; ...
 51-135 3.87e-05

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.


Pssm-ID: 380365 [Multi-domain]  Cd Length: 82  Bit Score: 40.07  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039950589  51 LPNVPGKTFTSAIVDFPPGARAVPHRHGEaFVYAYVLEGSVRSELGDAPAKTYGTgenwvEEPGAHHVLTenpSQTDRAK 130
Cdd:cd02237     6 LLIDPNTGLITAILRMAPGARLPDHEHVG-GEEFYVLDGALTDEDGTAGAGDFVR-----EPPGSRHSAV---APREGCL 76


                  ....*
gi 1039950589 131 LLVVF 135
Cdd:cd02237    77 ILVIL 81
cupin_DAD cd20302
2,4'-Dihydroxyacetophenone dioxygenase (DAD), cupin domain; 2,4'-Dihydroxyacetophenone ...
 63-148 7.19e-05

2,4'-Dihydroxyacetophenone dioxygenase (DAD), cupin domain; 2,4'-Dihydroxyacetophenone dioxygenase (DAD) catalyzes the oxidation of 2,4'-dihydroxyacetophenone to 4-hydroxybenzoate and formate as part of the 4-hydroxyacetophenone catabolic pathway. This enzyme is a homo-tetramer containing one iron per molecule of enzyme. This enzyme is an unusual dioxygenase in that it cleaves a C-C bond in a substituent of the aromatic ring rather than within the ring itself. As a bacterial dioxygenase, DAD plays an important environmental role in the aerobic catabolism of aromatic compounds; expression of this enzyme in appropriately engineered microorganisms has the potential to use these aromatic pollutants as a carbon source and thus remove them from the environment. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380436 [Multi-domain]  Cd Length: 123  Bit Score: 39.83  E-value: 7.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039950589  63 IVDFPPGARAVPHRH-GEafVYAYVLEGSVRSELGDAPAK--TYGtgenwVEEPGAHHVLTeNPSQTDraklLVVFISNT 139
Cdd:cd20302    29 LLRVPPGGSLPRHRHtGP--VHAYTLSGSWRYLEHDWVATagSYV-----YEPAGSIHTLV-VPEEEE----TIVLFIVQ 96


                  ....*....
gi 1039950589 140 GDNLKVDDD 148
Cdd:cd20302    97 GALIFLDED 105
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 63-135 1.70e-04

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: 37.85  E-value: 1.70e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039950589  63 IVDFPPGARAVPHRHGEAFVYAYVLEGSVRSELGDAPAKTYGTGENWVEEPGAHHVLtENPSQTDrAKLLVVF 135
Cdd:cd02208     3 VVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDDGETVELKAGDIVLIPPGVPHSF-VNTSDEP-AVFLVVS 73
cupin_MAE_RS03005 cd06987
Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes ...
 52-125 3.46e-04

Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes bacterial and some eukaryotic proteins homologous to MAE_RS03005, a Microcystis aeruginosa protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380392 [Multi-domain]  Cd Length: 122  Bit Score: 38.01  E-value: 3.46e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039950589  52 PNVPGKTFTSAIVDFPPGARAVPHRHGEAFVYAYVLEGSVRSELGDAPAkTYGTGENWVEEPGAHHVLTENPSQ 125
Cdd:cd06987    21 PEGDGVPFTVVVEIFDPGGRTPPNTHPAAHEMFFVLAGEGRAYCDGQRV-PLRPGDALVVPPGSEHVIENTGSG 93
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 62-142 3.50e-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: 38.02  E-value: 3.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039950589  62 AIVDFPPGARAVPHRHGEAFVYAYVLEGSVRSELGDAPAKTY----GTGENWVEEPGAHHVlTENPSqTDRAKLLVVFIS 137
Cdd:COG2140     6 GLTVLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRARtvdvGPGDVVYVPPGYGHY-IINTG-DEPLVFLAVFDD 83


                  ....*
gi 1039950589 138 NTGDN 142
Cdd:COG2140    84 DAGSD 88
Cupin_7 pfam12973
ChrR Cupin-like domain; Members of this family are part of the cupin superfamily. This family ...
 56-103 3.71e-04

ChrR Cupin-like domain; Members of this family are part of the cupin superfamily. This family includes the transcriptional activator ChrR.


Pssm-ID: 463764 [Multi-domain]  Cd Length: 91  Bit Score: 37.61  E-value: 3.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039950589  56 GKTFTSAIVDFPPGARAVPHRH--GEAFvyaYVLEGSVRSELGDAPAKTY 103
Cdd:pfam12973  21 EKARATSLVRYAPGSRFPAHRHpgGEEI---LVLEGVFSDEHGDYPAGTY 67
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 31-135 3.87e-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: 38.23  E-value: 3.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039950589  31 EATTTSLPPSETLnplleqalpnvpgktfTSAIVDFPPGARAVPHRHGEAFVYAYVLEGSVRSELGDAPAK----TYGTG 106
Cdd:cd02240    15 IATVTNFPISKDL----------------SSALVRVAPGAMRELHWHPNTAEWQYVISGSARVTVFDEDGRfetfNLGAG 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1039950589 107 ENWVEEPG-AHHVltENPSQTDrAKLLVVF 135
Cdd:cd02240    79 DVGYVPSGsGHHI--ENIGDED-AEFLLIF 105
cupin_BLR2406-like cd02210
Bradyrhizobium japonicum BLR2406 and related proteins, cupin domain; This family includes ...
 63-97 3.91e-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: 37.50  E-value: 3.91e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1039950589  63 IVDFPPGARAVPHRHGEAFVYAYVLEGSVRSELGD 97
Cdd:cd02210    15 VVTIPPGARTGAHHHGEHETAIYVLSGRAETRYGD 49
RmlC COG4101
Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only];
63-134 9.79e-04

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


Pssm-ID: 443277  Cd Length: 146  Bit Score: 37.25  E-value: 9.79e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039950589  63 IVDFPPGARAVPHRHGEAFVYAYVLEGSVRSELGDAPAKTY--GTGENWVEEPGAHHVlTENPSQTDRAKLLVV 134
Cdd:COG4101    50 LVTIPPGARAKAHHHGEHETAIYVLSGRAETRYGERLEHRVvtEPGDFIFIPPGVPHQ-EINLSDTEPAVAVIA 122
COG3435 COG3435
Gentisate 1,2-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
58-97 1.68e-03

Gentisate 1,2-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442661 [Multi-domain]  Cd Length: 316  Bit Score: 37.14  E-value: 1.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1039950589  58 TFTSAIVDFPPGARAVPHRHGEAFVYaYVLEGSVRSELGD 97
Cdd:COG3435   227 TIGAFMQLLPPGFHTRPHRHTGSAVY-HVVEGSGRSIVGG 265
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
56-147 1.70e-03

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 36.27  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039950589  56 GKTFTSAIVDFPPGARAVPHRHGEAFVYAYVLEGSVRSELGDAPaKTYGTGENWVEEPGAHHVLtENPSQTDrAKLLVVF 135
Cdd:COG0662    24 GERLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGEVTIGDEE-VELKAGDSVYIPAGVPHRL-RNPGDEP-LELLEVQ 100

                          90
                  ....*....|..
gi 1039950589 136 isnTGDNLKVDD 147
Cdd:COG0662   101 ---APAYLGEDD 109
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
52-134 2.12e-03

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 35.76  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039950589  52 PNVPGKTFTSAIVDFPPGARAVP---HRHGEAFVYayVLEGSVRSELGDapaKTY--GTGENWVEEPGAHHVLtENPSQT 126
Cdd:COG3837    21 DALGLTRLGVNLITLPPGASSSPyhaHSAEEEFVY--VLEGELTLRIGG---EEYvlEPGDSVGFPAGVPHRL-RNRGDE 94


                  ....*...
gi 1039950589 127 DrAKLLVV 134
Cdd:COG3837    95 P-ARYLVV 101
cupin_BLL6423-like cd02231
Bradyrhizobium japonicum BLL6423 and related proteins, cupin domain; This family includes ...
 63-97 3.72e-03

Bradyrhizobium japonicum BLL6423 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLL6423, a Bradyrhizobium japonicum protein of unknown function; it includes a structure of an uncharacterized protein from Novosphingobium aromaticivorans. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380359  Cd Length: 108  Bit Score: 34.84  E-value: 3.72e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1039950589  63 IVDFPPGARAVPHRHgEAFVYAYVLEGSVRSELGD 97
Cdd:cd02231    40 VVDFPPGAESPMHRT-ESLDYGIVLEGEIELELDD 73
cupin_bxe_c0505 cd06980
uncharacterized protein bxe_c0505, cupin domain; This family includes mostly bacterial ...
 67-121 4.35e-03

uncharacterized protein bxe_c0505, cupin domain; This family includes mostly bacterial proteins homologous to bxe_c0505, a Burkholderia xenovorans 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: 380385 [Multi-domain]  Cd Length: 105  Bit Score: 34.85  E-value: 4.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039950589  67 PPGARAVPHRHGEAFVYAYVLEGSVRSELGDAPAKTYGTGENWVEEPGAHHVLTE 121
Cdd:cd06980    31 GGEGPTGWHYHDCDFQMVYVLKGWVKFEFEGGGEVRLEAGDCVYQPPGIRHNVLD 85
cupin_GDO-like_C cd06992
gentisate 1,2-dioxygenase, 1-hydroxy-2-naphthoate dioxygenase, and salicylate 1,2-dioxygenase ...
 67-97 4.53e-03

gentisate 1,2-dioxygenase, 1-hydroxy-2-naphthoate dioxygenase, and salicylate 1,2-dioxygenase bicupin aromatic ring-cleaving dioxygenases, C-terminal cupin domain; This model represents the C-terminal cupin domains of three closely related bicupin aromatic ring-cleaving dioxygenases: gentisate 1,2-dioxygenase (GDO), salicylate 1,2-dioxygenase (SDO), and 1-hydroxy-2-naphthoate dioxygenase (NDO). GDO catalyzes the cleavage of the gentisate (2,5-dihydroxybenzoate) aromatic ring, a key step in the gentisate degradation pathway allowing soil bacteria to utilize 2,5-xylenol, 3,5-xylenol, and m-cresol as sole carbon and energy sources. NDO catalyzes the cleavage of 1-hydroxy-2-naphthoate as part of the bacterial phenanthrene degradation pathway. SDO is a ring cleavage dioxygenase from Pseudaminobacter salicylatoxidans that oxidizes salicylate to 2-oxohepta-3,5-dienedioic acid via a novel ring fission mechanism. SDO differs from other known GDO's and NDO's in its unique ability to oxidatively cleave many different salicylate, gentisate, and 1-hydroxy-2- naphthoate substrates with high catalytic efficiency. The active site of this enzyme is located in the N-terminal domain but could be influenced by changes in the C-terminal domain, which lacks the strictly conserved metal-binding residues found in other cupin domains and is thought to be an inactive vestigial remnant.


Pssm-ID: 380397 [Multi-domain]  Cd Length: 99  Bit Score: 34.77  E-value: 4.53e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1039950589  67 PPGARAVPHRHGEAFVYaYVLEGSVRSELGD 97
Cdd:cd06992    27 RAGFSTRPHRSTASAVY-HVVEGSGRTVIGG 56
 
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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