NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1549766828|gb|RVK74302|]
View 

transcriptional regulator [Sinorhizobium meliloti]

Protein Classification

dimethylsulfoniopropionate lyase( domain architecture ID 11245792)

dimethylsulfoniopropionate (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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DMSP_lyase pfam16867
Dimethlysulfonioproprionate lyase; Breaks down into dimethylsulfoniopropionate (DMSP) into ...
 28-190 8.04e-82

Dimethlysulfonioproprionate lyase; Breaks down into dimethylsulfoniopropionate (DMSP) into acrylate and dimethyl sulfide.


:

Pssm-ID: 435615  Cd Length: 162  Bit Score: 240.01  E-value: 8.04e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549766828  28 SRRSILQISSALEVPGVERRGHGSRLPVCSHLEPALSIETEHEpLRRLIDRFRAVEPFLAWRRRTgCDGSASANFLEGHA 107
Cdd:pfam16867   2 RRRSLAQRFARLATPLPERDRPGGRLPVCAHLEAALAPAEGDE-IRDLARALAAVEPALTWRRTY-SGGPASADFADGYA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549766828 108 NAMIVGPGGLEERRDVWLGVTLMAPHVRYPDHEHAPEEVYLVLSKGEFRQGEGEWFSPGLGGSFYNEPGIRHAMRSVDTP 187
Cdd:pfam16867  80 YAEILGPRGLEERDDVWLGFVLLGPHVRYPDHHHPPEESYLVLSGGEWRQGEADWFPPGIGEIIHNPPGIVHAMRSVETP 159


                  ...
gi 1549766828 188 LLA 190
Cdd:pfam16867 160 LLA 162
 
Name Accession Description Interval E-value
DMSP_lyase pfam16867
Dimethlysulfonioproprionate lyase; Breaks down into dimethylsulfoniopropionate (DMSP) into ...
 28-190 8.04e-82

Dimethlysulfonioproprionate lyase; Breaks down into dimethylsulfoniopropionate (DMSP) into acrylate and dimethyl sulfide.


Pssm-ID: 435615  Cd Length: 162  Bit Score: 240.01  E-value: 8.04e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549766828  28 SRRSILQISSALEVPGVERRGHGSRLPVCSHLEPALSIETEHEpLRRLIDRFRAVEPFLAWRRRTgCDGSASANFLEGHA 107
Cdd:pfam16867   2 RRRSLAQRFARLATPLPERDRPGGRLPVCAHLEAALAPAEGDE-IRDLARALAAVEPALTWRRTY-SGGPASADFADGYA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549766828 108 NAMIVGPGGLEERRDVWLGVTLMAPHVRYPDHEHAPEEVYLVLSKGEFRQGEGEWFSPGLGGSFYNEPGIRHAMRSVDTP 187
Cdd:pfam16867  80 YAEILGPRGLEERDDVWLGFVLLGPHVRYPDHHHPPEESYLVLSGGEWRQGEADWFPPGIGEIIHNPPGIVHAMRSVETP 159


                  ...
gi 1549766828 188 LLA 190
Cdd:pfam16867 160 LLA 162
cupin_DddQ cd20282
dimethylsulfoniopropionate lyase DddQ, cupin domain; Dimethylsulfoniopropionate (DMSP) is ...
 111-191 1.17e-15

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: 69.22  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549766828 111 IVGPGGLEERRDVWLGVTLMAPHVRYPDHEHAPEEVYLVLS-KGEFRQGEGEWFSPGLGGSFYNEPGIRHAMRSVDTPLL 189
Cdd:cd20282     8 LIGPEGPFVSDELRLGVGYWGPGLDYPWHHHAAEEIYLVLAgSAEFLSEGQPPRRLGPGDTVFHASNQPHAMRTGDEPLL 87


                  ..
gi 1549766828 190 AF 191
Cdd:cd20282    88 AL 89
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
117-192 3.56e-05

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 40.99  E-value: 3.56e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1549766828 117 LEERRDVWLGVTLMAPHVRYPDHEHAPEEVYLVLSkGEFR-QGEGEWFSPGLGGSFYNEPGIRHAMRSV-DTPLLAFW 192
Cdd:COG1917    17 ADGEDELEVVRVTFEPGARTPWHSHPGEELIYVLE-GEGEvEVGGEEYELKPGDVVFIPPGVPHAFRNLgDEPAVLLV 93
 
Name Accession Description Interval E-value
DMSP_lyase pfam16867
Dimethlysulfonioproprionate lyase; Breaks down into dimethylsulfoniopropionate (DMSP) into ...
 28-190 8.04e-82

Dimethlysulfonioproprionate lyase; Breaks down into dimethylsulfoniopropionate (DMSP) into acrylate and dimethyl sulfide.


Pssm-ID: 435615  Cd Length: 162  Bit Score: 240.01  E-value: 8.04e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549766828  28 SRRSILQISSALEVPGVERRGHGSRLPVCSHLEPALSIETEHEpLRRLIDRFRAVEPFLAWRRRTgCDGSASANFLEGHA 107
Cdd:pfam16867   2 RRRSLAQRFARLATPLPERDRPGGRLPVCAHLEAALAPAEGDE-IRDLARALAAVEPALTWRRTY-SGGPASADFADGYA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549766828 108 NAMIVGPGGLEERRDVWLGVTLMAPHVRYPDHEHAPEEVYLVLSKGEFRQGEGEWFSPGLGGSFYNEPGIRHAMRSVDTP 187
Cdd:pfam16867  80 YAEILGPRGLEERDDVWLGFVLLGPHVRYPDHHHPPEESYLVLSGGEWRQGEADWFPPGIGEIIHNPPGIVHAMRSVETP 159


                  ...
gi 1549766828 188 LLA 190
Cdd:pfam16867 160 LLA 162
cupin_DddQ cd20282
dimethylsulfoniopropionate lyase DddQ, cupin domain; Dimethylsulfoniopropionate (DMSP) is ...
 111-191 1.17e-15

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: 69.22  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549766828 111 IVGPGGLEERRDVWLGVTLMAPHVRYPDHEHAPEEVYLVLS-KGEFRQGEGEWFSPGLGGSFYNEPGIRHAMRSVDTPLL 189
Cdd:cd20282     8 LIGPEGPFVSDELRLGVGYWGPGLDYPWHHHAAEEIYLVLAgSAEFLSEGQPPRRLGPGDTVFHASNQPHAMRTGDEPLL 87


                  ..
gi 1549766828 190 AF 191
Cdd:cd20282    88 AL 89
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
117-192 3.56e-05

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 40.99  E-value: 3.56e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1549766828 117 LEERRDVWLGVTLMAPHVRYPDHEHAPEEVYLVLSkGEFR-QGEGEWFSPGLGGSFYNEPGIRHAMRSV-DTPLLAFW 192
Cdd:COG1917    17 ADGEDELEVVRVTFEPGARTPWHSHPGEELIYVLE-GEGEvEVGGEEYELKPGDVVFIPPGVPHAFRNLgDEPAVLLV 93
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH