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Conserved domains on  [gi|1721662966|gb|QEC55241|]
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rhamnogalacturonan acetylesterase [Flavisolibacter ginsenosidimutans]

Protein Classification

rhamnogalacturonan acetylesterase( domain architecture ID 10110667)

rhamnogalacturonan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases; belongs to the SGNH/GDSL hydrolase family

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Rhamnogalacturan_acetylesterase_like cd01821
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan ...
27-246 4.45e-84

Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria.


:

Pssm-ID: 238859  Cd Length: 198  Bit Score: 249.44  E-value: 4.45e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966  27 PVFYVIGDSTVKNGDGTGKgsLWGWGDFIAPYFDTtKIRIENDALGGRSSRTFITEGRWEKVLSKLKKGDYVIMQFGHND 106
Cdd:cd01821     1 PTIFLAGDSTVADYDPGAP--QAGWGQALPQYLDT-GITVVNHAKGGRSSRSFRDEGRWDAILKLIKPGDYVLIQFGHND 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966 107 SGPLDDtarargtmkgigeeskevynpimKKQEVVYTYGHYMRQYIRDAKAKGAVAIVCSPIPRNDWKEGK-VTRSVESY 185
Cdd:cd01821    78 QKPKDP-----------------------EYTEPYTTYKEYLRRYIAEARAKGATPILVTPVTRRTFDEGGkVEDTLGDY 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721662966 186 AGWAQQVAKEEGAYFIDLNNLVATKYEALGADAVK---PFFPGDHTHTNIDGAKLNAEIVAAQL 246
Cdd:cd01821   135 PAAMRELAAEEGVPLIDLNAASRALYEAIGPEKSKkyfPEGPGDNTHFSEKGADVVARLVAEEL 198
 
Name Accession Description Interval E-value
Rhamnogalacturan_acetylesterase_like cd01821
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan ...
27-246 4.45e-84

Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria.


Pssm-ID: 238859  Cd Length: 198  Bit Score: 249.44  E-value: 4.45e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966  27 PVFYVIGDSTVKNGDGTGKgsLWGWGDFIAPYFDTtKIRIENDALGGRSSRTFITEGRWEKVLSKLKKGDYVIMQFGHND 106
Cdd:cd01821     1 PTIFLAGDSTVADYDPGAP--QAGWGQALPQYLDT-GITVVNHAKGGRSSRSFRDEGRWDAILKLIKPGDYVLIQFGHND 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966 107 SGPLDDtarargtmkgigeeskevynpimKKQEVVYTYGHYMRQYIRDAKAKGAVAIVCSPIPRNDWKEGK-VTRSVESY 185
Cdd:cd01821    78 QKPKDP-----------------------EYTEPYTTYKEYLRRYIAEARAKGATPILVTPVTRRTFDEGGkVEDTLGDY 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721662966 186 AGWAQQVAKEEGAYFIDLNNLVATKYEALGADAVK---PFFPGDHTHTNIDGAKLNAEIVAAQL 246
Cdd:cd01821   135 PAAMRELAAEEGVPLIDLNAASRALYEAIGPEKSKkyfPEGPGDNTHFSEKGADVVARLVAEEL 198
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
23-247 1.04e-31

Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];


Pssm-ID: 442045 [Multi-domain]  Cd Length: 191  Bit Score: 115.51  E-value: 1.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966  23 QKDKPVFYVIGDSTVkngDGTGKGSLWGWGDFIAPYFDTTKIRIENDALGGRSSRTFITegRWEKVLSKLkKGDYVIMQF 102
Cdd:COG2755     5 AGKPLRIVALGDSIT---AGYGASRERGWPALLARRLAAADVRVVNAGISGATTADLLA--RLDRDLLAL-KPDLVVIEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966 103 GHNDsgplddtarargTMKGIGEESKEVYNpimkkqevvytyghYMRQYIRDAKAKGAVA--IVCSPIPRndWKEGKVTR 180
Cdd:COG2755    79 GTND------------LLRGLGVSPEEFRA--------------NLEALIDRLRAAGPGArvVLVTPPPR--LRPNYLNE 130
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721662966 181 SVESYAGWAQQVAKEEGAYFIDLNNLVAtkyealGADAVKPFFPGDHTHTNIDGAKLNAEIVAAQLK 247
Cdd:COG2755   131 RIEAYNAAIRELAAEYGVPLVDLYAALR------DAGDLPDLLTADGLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
31-237 4.42e-11

GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are similar to pfam00657.


Pssm-ID: 463889  Cd Length: 176  Bit Score: 60.25  E-value: 4.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966  31 VIGDSTVkngDGTGKGSLW-GWGDFIAPYF--DTTKIRIENDALGGRSSRtFITEGRWEKVLSKlkKGDYVIMQFGHNDS 107
Cdd:pfam13472   1 ALGDSIT---AGYGATGGDrSYPGWLARLLarRLGADVVNNLGISGATTR-LDLLERLDDVLRL--KPDLVVILLGTNDL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966 108 GPLDDTARARGtmkgigeeskevynpimkkqevvytyghYMRQYIRDAKAKGAVAIV----CSPIPRNDWKEGKVTRS-V 182
Cdd:pfam13472  75 GRGVSAARAAA----------------------------NLEALIDALRAAGPDARVlligPLPVGPPPPLDERRLNArI 126
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1721662966 183 ESYAGWAQQVAKEEGAYFIDLNNLVATkyealGADAVKPFFPGDHTHTNIDGAKL 237
Cdd:pfam13472 127 AEYNAAIREVAAERGVPYVDLWDALRD-----DGGWLPDLLADDGLHPNAAGYRL 176
 
Name Accession Description Interval E-value
Rhamnogalacturan_acetylesterase_like cd01821
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan ...
27-246 4.45e-84

Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria.


Pssm-ID: 238859  Cd Length: 198  Bit Score: 249.44  E-value: 4.45e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966  27 PVFYVIGDSTVKNGDGTGKgsLWGWGDFIAPYFDTtKIRIENDALGGRSSRTFITEGRWEKVLSKLKKGDYVIMQFGHND 106
Cdd:cd01821     1 PTIFLAGDSTVADYDPGAP--QAGWGQALPQYLDT-GITVVNHAKGGRSSRSFRDEGRWDAILKLIKPGDYVLIQFGHND 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966 107 SGPLDDtarargtmkgigeeskevynpimKKQEVVYTYGHYMRQYIRDAKAKGAVAIVCSPIPRNDWKEGK-VTRSVESY 185
Cdd:cd01821    78 QKPKDP-----------------------EYTEPYTTYKEYLRRYIAEARAKGATPILVTPVTRRTFDEGGkVEDTLGDY 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721662966 186 AGWAQQVAKEEGAYFIDLNNLVATKYEALGADAVK---PFFPGDHTHTNIDGAKLNAEIVAAQL 246
Cdd:cd01821   135 PAAMRELAAEEGVPLIDLNAASRALYEAIGPEKSKkyfPEGPGDNTHFSEKGADVVARLVAEEL 198
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
23-247 1.04e-31

Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];


Pssm-ID: 442045 [Multi-domain]  Cd Length: 191  Bit Score: 115.51  E-value: 1.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966  23 QKDKPVFYVIGDSTVkngDGTGKGSLWGWGDFIAPYFDTTKIRIENDALGGRSSRTFITegRWEKVLSKLkKGDYVIMQF 102
Cdd:COG2755     5 AGKPLRIVALGDSIT---AGYGASRERGWPALLARRLAAADVRVVNAGISGATTADLLA--RLDRDLLAL-KPDLVVIEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966 103 GHNDsgplddtarargTMKGIGEESKEVYNpimkkqevvytyghYMRQYIRDAKAKGAVA--IVCSPIPRndWKEGKVTR 180
Cdd:COG2755    79 GTND------------LLRGLGVSPEEFRA--------------NLEALIDRLRAAGPGArvVLVTPPPR--LRPNYLNE 130
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721662966 181 SVESYAGWAQQVAKEEGAYFIDLNNLVAtkyealGADAVKPFFPGDHTHTNIDGAKLNAEIVAAQLK 247
Cdd:COG2755   131 RIEAYNAAIRELAAEYGVPLVDLYAALR------DAGDLPDLLTADGLHPNAAGYRLIAEAVLPALK 191
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
31-245 1.28e-11

SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.


Pssm-ID: 238141 [Multi-domain]  Cd Length: 187  Bit Score: 61.66  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966  31 VIGDSTVKNGDGTGKGSLWGWGDFIAPYFDTTKIRIENDALGGRSSRTFITEGRWEKVLSKlKKGDYVIMQFGHNDSGPL 110
Cdd:cd00229     3 VIGDSITAGYGASSGSTFYSLLLYLLLLAGGPGVEVINLGVSGATTADALRRLGLRLALLK-DKPDLVIIELGTNDLGRG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966 111 DDTARArgtmkgigeeskevynpimkkqevvyTYGHYMRQYIRDAK--AKGAVAIVCSPIPRNdWKEGKVTRSVESYAGW 188
Cdd:cd00229    82 GDTSID--------------------------EFKANLEELLDALRerAPGAKVILITPPPPP-PREGLLGRALPRYNEA 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721662966 189 AQQVAKEEGA----YFIDLNNLVatkyealgADAVKPFFPGDHTHTNIDGAKLNAEIVAAQ 245
Cdd:cd00229   135 IKAVAAENPApsgvDLVDLAALL--------GDEDKSLYSPDGIHPNPAGHKLIAEALASA 187
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
31-237 4.42e-11

GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are similar to pfam00657.


Pssm-ID: 463889  Cd Length: 176  Bit Score: 60.25  E-value: 4.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966  31 VIGDSTVkngDGTGKGSLW-GWGDFIAPYF--DTTKIRIENDALGGRSSRtFITEGRWEKVLSKlkKGDYVIMQFGHNDS 107
Cdd:pfam13472   1 ALGDSIT---AGYGATGGDrSYPGWLARLLarRLGADVVNNLGISGATTR-LDLLERLDDVLRL--KPDLVVILLGTNDL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966 108 GPLDDTARARGtmkgigeeskevynpimkkqevvytyghYMRQYIRDAKAKGAVAIV----CSPIPRNDWKEGKVTRS-V 182
Cdd:pfam13472  75 GRGVSAARAAA----------------------------NLEALIDALRAAGPDARVlligPLPVGPPPPLDERRLNArI 126
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1721662966 183 ESYAGWAQQVAKEEGAYFIDLNNLVATkyealGADAVKPFFPGDHTHTNIDGAKL 237
Cdd:pfam13472 127 AEYNAAIREVAAERGVPYVDLWDALRD-----DGGWLPDLLADDGLHPNAAGYRL 176
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
30-242 1.86e-07

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 50.26  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966  30 YVIGDSTVKnGDGTGKGSLWGWGDFIAPYF-------DTTKIRIENDALGGRSSRT-FITEGRWEKVLS---KLKKGDYV 98
Cdd:pfam00657   2 VAFGDSLTD-GGGDGPGGRFSWGDLLADFLarklgvpGSGYNHGANFAIGGATIEDlPIQLEQLLRLISdvkDQAKPDLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966  99 IMQFGHNDSGPlddtarargtMKGIGEESKEVYNPIMkkqEVVYTYGHYMRQYIRDAKAKGAVAIVCSPIPRNDWKEGKV 178
Cdd:pfam00657  81 TIFIGANDLCN----------FLSSPARSKKRVPDLL---DELRANLPQLGLGARKFWVHGLGPLGCTPPKGCYELYNAL 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721662966 179 TRS----VESYAGWAQQVAKEEGAYFIDLNNLVATKYEALGADavkpfFPGDHTHTNIDGAKLNAEIV 242
Cdd:pfam00657 148 AEEynerLNELVNSLAAAAEDANVVYVDIYGFEDPTDPCCGIG-----LEPDGLHPSEKGYKAVAEAI 210
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
24-245 1.35e-05

SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.


Pssm-ID: 238872  Cd Length: 191  Bit Score: 44.59  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966  24 KDKPVFyvIGDSTvknGDGTGkgslwgWGDFIAPY----FDTTKIRIENDALGGrsSRTFITEGRWEKVLSKlKKGDYVI 99
Cdd:cd01834     1 GDRIVF--IGNSI---TDRGG------YVGYVETYlaarYPELKLTFRNLGWSG--DTVSDLAARRDRDVLP-AKPDVVS 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721662966 100 MQFGHNDSG-PLDDTARArgtmkgigEESKEVYNpimkkqevvytygHYMRQYIRDAKAKGAVAIvcSPIP-----RNDW 173
Cdd:cd01834    67 IMFGINDSFrGFDDPVGL--------EKFKTNLR-------------RLIDRLKNKESAPRIVLV--SPIAyeaneDPLP 123
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721662966 174 KEGKVTRSVESYAGWAQQVAKEEGAYFIDLNN-----LVATKYEALGADAVkpffpgdhtHTNIDGAKLNAEIVAAQ 245
Cdd:cd01834   124 DGAEYNANLAAYADAVRELAAENGVAFVDLFTpmkeaFQKAGEAVLTVDGV---------HPNEAGHRALARLWLEA 191
 
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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