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Conserved domains on  [gi|674708360|ref|WP_031600812|]
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MULTISPECIES: unsaturated rhamnogalacturonyl hydrolase [Bacillus]

Protein Classification

glycoside hydrolase family 88 protein( domain architecture ID 10538604)

glycoside hydrolase family 88 protein similar to unsaturated chondroitin disaccharide hydrolase, which catalyzes the hydrolysis of unsaturated hyaluronate and chondroitin disaccharides, and also degrades unsaturated heparin disaccharides

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_hydro_88 pfam07470
Glycosyl Hydrolase Family 88; Unsaturated glucuronyl hydrolase catalyzes the hydrolytic ...
16-368 1.20e-156

Glycosyl Hydrolase Family 88; Unsaturated glucuronyl hydrolase catalyzes the hydrolytic release of unsaturated glucuronic acids from oligosaccharides (EC:3.2.1.-) produced by the reactions of polysaccharide lyases.


:

Pssm-ID: 429478  Cd Length: 345  Bit Score: 443.74  E-value: 1.20e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360   16 YAEALAKTIMNTYT---VEELPPANRWHYHQGVFLCGVLRLWEATGEKRYFEYAKAYADLLIDDYGNLlFRRDELDAIQA 92
Cdd:pfam07470   1 YIDRVAGSFMKRYPdgkVIDLPPDNRWDWTNGVFLYGMLEAYEATGDKEYLDYLKAWADSLIDEGGKI-LTPYNLDDINI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360   93 GLILFPLYEQTKDERYVKAAKRLR-GLYRTLNRTSEGGFWHKDGYPYQMWLDGLYMGGPFALKYANLKQEPELFDQVVLQ 171
Cdd:pfam07470  80 GLTLLDLYEHTGDERYIQAAIELAdWVLATPPRTSEGGFWHKDIYPHQMWLDGLFMAGPFLAKYGKLTNEPKYLDEAVYQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360  172 ESLMRKHTKDAKTGLFYHAWDEAKKMPWANeetgcspEFWARSIGWYVMSLADMIEELPKKHPNRHVWKNTLRDMIKSIC 251
Cdd:pfam07470 160 FLLTRRHLYDPETGLYYHGWDESGTEPWAD-------PFWARGNGWYAMALADVLELLPEKHPARQELINILRDLVKALA 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360  252 RYQDkETGLWYQIVDKGDRsDNWLESSGSCLYMYALAKGINQGYLDRAYETTLLKAYQGLIQHKTEtsEDGAFLVKDICV 331
Cdd:pfam07470 233 KYQD-ESGLWHQSLDDPDR-DSYLETSASAGFVYALAKGVNKGYLDKKYLPVAQKAWKALLKNFVD--EDGQLGVVQICG 308
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 674708360  332 GTSAGFYDYYVSRERSTNDLHGAGAFILAMTELEPLF 368
Cdd:pfam07470 309 GTGIGGDDYYRSVPYNSNDPYGVGAFLLASTEYLRLL 345
 
Name Accession Description Interval E-value
Glyco_hydro_88 pfam07470
Glycosyl Hydrolase Family 88; Unsaturated glucuronyl hydrolase catalyzes the hydrolytic ...
16-368 1.20e-156

Glycosyl Hydrolase Family 88; Unsaturated glucuronyl hydrolase catalyzes the hydrolytic release of unsaturated glucuronic acids from oligosaccharides (EC:3.2.1.-) produced by the reactions of polysaccharide lyases.


Pssm-ID: 429478  Cd Length: 345  Bit Score: 443.74  E-value: 1.20e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360   16 YAEALAKTIMNTYT---VEELPPANRWHYHQGVFLCGVLRLWEATGEKRYFEYAKAYADLLIDDYGNLlFRRDELDAIQA 92
Cdd:pfam07470   1 YIDRVAGSFMKRYPdgkVIDLPPDNRWDWTNGVFLYGMLEAYEATGDKEYLDYLKAWADSLIDEGGKI-LTPYNLDDINI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360   93 GLILFPLYEQTKDERYVKAAKRLR-GLYRTLNRTSEGGFWHKDGYPYQMWLDGLYMGGPFALKYANLKQEPELFDQVVLQ 171
Cdd:pfam07470  80 GLTLLDLYEHTGDERYIQAAIELAdWVLATPPRTSEGGFWHKDIYPHQMWLDGLFMAGPFLAKYGKLTNEPKYLDEAVYQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360  172 ESLMRKHTKDAKTGLFYHAWDEAKKMPWANeetgcspEFWARSIGWYVMSLADMIEELPKKHPNRHVWKNTLRDMIKSIC 251
Cdd:pfam07470 160 FLLTRRHLYDPETGLYYHGWDESGTEPWAD-------PFWARGNGWYAMALADVLELLPEKHPARQELINILRDLVKALA 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360  252 RYQDkETGLWYQIVDKGDRsDNWLESSGSCLYMYALAKGINQGYLDRAYETTLLKAYQGLIQHKTEtsEDGAFLVKDICV 331
Cdd:pfam07470 233 KYQD-ESGLWHQSLDDPDR-DSYLETSASAGFVYALAKGVNKGYLDKKYLPVAQKAWKALLKNFVD--EDGQLGVVQICG 308
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 674708360  332 GTSAGFYDYYVSRERSTNDLHGAGAFILAMTELEPLF 368
Cdd:pfam07470 309 GTGIGGDDYYRSVPYNSNDPYGVGAFLLASTEYLRLL 345
YesR COG4225
Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism];
20-367 1.43e-144

Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism];


Pssm-ID: 443369  Cd Length: 336  Bit Score: 412.67  E-value: 1.43e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360  20 LAKTIMNTYTVEELPPANRWHYHQGVFLCGVLRLWEATGEKRYFEYAKAYADLLIDDYGNLLFRRDELDAIQAGLILFPL 99
Cdd:COG4225    1 VADSQLKRYWDIDPGKFPKWDYTQGVTLYGLLKLAEATGDKKYLDYIKRWFDFFIDEGNTYKLPPYNLDDIAPGLALLEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360 100 YEQTKDERYVKAAKRLR-GLYRTLNRTSEGGFWHKDGYPYQMWLDGLYMGGPFALKYANLKQEPELFDQVVLQESLMRKH 178
Cdd:COG4225   81 YEQTGDPKYLKAADTLAdWQLNTQPRTSEGGFWHKKIYPNQLWLDGLYMAVPFLAQYGKLTGDPKYFDDAAKQFLLTTKY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360 179 TKDAKTGLFYHAWDEAKKMPwaneeTGCSPEFWARSIGWYVMSLADMIEELPKKHPNRHVWKNTLRDMIKSICRYQDkET 258
Cdd:COG4225  161 LFDPETGLYYHGWDESREQK-----AGGSPAFWGRGNGWVAMALVDLLDLLPEDHPDRPELLALLKEMAAALAKYQD-ES 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360 259 GLWYQIVDKgdrSDNWLESSGSCLYMYALAKGINQGYLDRAYETTLLKAYQGLIQHkteTSEDGAflVKDICVGTSAGF- 337
Cdd:COG4225  235 GLWHQVLDD---PGNYLETSATAMFTYALAKGVNKGYLDKKYLPAAEKAWNGLLKK---IDEDGS--LTGVCVGTGLGGs 306
                        330       340       350
                 ....*....|....*....|....*....|
gi 674708360 338 YDYYVSRERSTNDLHGAGAFILAMTELEPL 367
Cdd:COG4225  307 LEYYISEPIRTNDPYGVGPFLLAGSEMLKL 336
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
51-144 6.44e-06

Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown.


Pssm-ID: 271199 [Multi-domain]  Cd Length: 327  Bit Score: 47.65  E-value: 6.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360  51 LRLWEATGEKRYFEYAKAYADLLIDDYGNLLFRRDELDAI---------QAGLILF--PLYEQTKDERYVKAAKR-LRGL 118
Cdd:cd04791   96 LHLARATGDPEFLERAARIAERLAARLREDDPGVYWNDAGavragllhgWSGIALFllRLYEATGDPAYLDLAERaLRKD 175
                         90       100       110
                 ....*....|....*....|....*....|
gi 674708360 119 YRTLNRTSEGGFWHKDG----YPYqmWLDG 144
Cdd:cd04791  176 LARCVEDDDGALLQVDEgnrlLPY--LCSG 203
 
Name Accession Description Interval E-value
Glyco_hydro_88 pfam07470
Glycosyl Hydrolase Family 88; Unsaturated glucuronyl hydrolase catalyzes the hydrolytic ...
16-368 1.20e-156

Glycosyl Hydrolase Family 88; Unsaturated glucuronyl hydrolase catalyzes the hydrolytic release of unsaturated glucuronic acids from oligosaccharides (EC:3.2.1.-) produced by the reactions of polysaccharide lyases.


Pssm-ID: 429478  Cd Length: 345  Bit Score: 443.74  E-value: 1.20e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360   16 YAEALAKTIMNTYT---VEELPPANRWHYHQGVFLCGVLRLWEATGEKRYFEYAKAYADLLIDDYGNLlFRRDELDAIQA 92
Cdd:pfam07470   1 YIDRVAGSFMKRYPdgkVIDLPPDNRWDWTNGVFLYGMLEAYEATGDKEYLDYLKAWADSLIDEGGKI-LTPYNLDDINI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360   93 GLILFPLYEQTKDERYVKAAKRLR-GLYRTLNRTSEGGFWHKDGYPYQMWLDGLYMGGPFALKYANLKQEPELFDQVVLQ 171
Cdd:pfam07470  80 GLTLLDLYEHTGDERYIQAAIELAdWVLATPPRTSEGGFWHKDIYPHQMWLDGLFMAGPFLAKYGKLTNEPKYLDEAVYQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360  172 ESLMRKHTKDAKTGLFYHAWDEAKKMPWANeetgcspEFWARSIGWYVMSLADMIEELPKKHPNRHVWKNTLRDMIKSIC 251
Cdd:pfam07470 160 FLLTRRHLYDPETGLYYHGWDESGTEPWAD-------PFWARGNGWYAMALADVLELLPEKHPARQELINILRDLVKALA 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360  252 RYQDkETGLWYQIVDKGDRsDNWLESSGSCLYMYALAKGINQGYLDRAYETTLLKAYQGLIQHKTEtsEDGAFLVKDICV 331
Cdd:pfam07470 233 KYQD-ESGLWHQSLDDPDR-DSYLETSASAGFVYALAKGVNKGYLDKKYLPVAQKAWKALLKNFVD--EDGQLGVVQICG 308
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 674708360  332 GTSAGFYDYYVSRERSTNDLHGAGAFILAMTELEPLF 368
Cdd:pfam07470 309 GTGIGGDDYYRSVPYNSNDPYGVGAFLLASTEYLRLL 345
YesR COG4225
Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism];
20-367 1.43e-144

Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism];


Pssm-ID: 443369  Cd Length: 336  Bit Score: 412.67  E-value: 1.43e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360  20 LAKTIMNTYTVEELPPANRWHYHQGVFLCGVLRLWEATGEKRYFEYAKAYADLLIDDYGNLLFRRDELDAIQAGLILFPL 99
Cdd:COG4225    1 VADSQLKRYWDIDPGKFPKWDYTQGVTLYGLLKLAEATGDKKYLDYIKRWFDFFIDEGNTYKLPPYNLDDIAPGLALLEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360 100 YEQTKDERYVKAAKRLR-GLYRTLNRTSEGGFWHKDGYPYQMWLDGLYMGGPFALKYANLKQEPELFDQVVLQESLMRKH 178
Cdd:COG4225   81 YEQTGDPKYLKAADTLAdWQLNTQPRTSEGGFWHKKIYPNQLWLDGLYMAVPFLAQYGKLTGDPKYFDDAAKQFLLTTKY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360 179 TKDAKTGLFYHAWDEAKKMPwaneeTGCSPEFWARSIGWYVMSLADMIEELPKKHPNRHVWKNTLRDMIKSICRYQDkET 258
Cdd:COG4225  161 LFDPETGLYYHGWDESREQK-----AGGSPAFWGRGNGWVAMALVDLLDLLPEDHPDRPELLALLKEMAAALAKYQD-ES 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360 259 GLWYQIVDKgdrSDNWLESSGSCLYMYALAKGINQGYLDRAYETTLLKAYQGLIQHkteTSEDGAflVKDICVGTSAGF- 337
Cdd:COG4225  235 GLWHQVLDD---PGNYLETSATAMFTYALAKGVNKGYLDKKYLPAAEKAWNGLLKK---IDEDGS--LTGVCVGTGLGGs 306
                        330       340       350
                 ....*....|....*....|....*....|
gi 674708360 338 YDYYVSRERSTNDLHGAGAFILAMTELEPL 367
Cdd:COG4225  307 LEYYISEPIRTNDPYGVGPFLLAGSEMLKL 336
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
51-144 6.44e-06

Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown.


Pssm-ID: 271199 [Multi-domain]  Cd Length: 327  Bit Score: 47.65  E-value: 6.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360  51 LRLWEATGEKRYFEYAKAYADLLIDDYGNLLFRRDELDAI---------QAGLILF--PLYEQTKDERYVKAAKR-LRGL 118
Cdd:cd04791   96 LHLARATGDPEFLERAARIAERLAARLREDDPGVYWNDAGavragllhgWSGIALFllRLYEATGDPAYLDLAERaLRKD 175
                         90       100       110
                 ....*....|....*....|....*....|
gi 674708360 119 YRTLNRTSEGGFWHKDG----YPYqmWLDG 144
Cdd:cd04791  176 LARCVEDDDGALLQVDEgnrlLPY--LCSG 203
LanM-like cd04792
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
51-135 1.00e-03

Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.


Pssm-ID: 271200 [Multi-domain]  Cd Length: 836  Bit Score: 41.14  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708360  51 LRLWEATGEKRYFEYAKAYADLLIDDygnlLFRRDELDAIQ--AGLI--LFPLYEQTKDERYVKAAKRL-RGLYRTLNRT 125
Cdd:cd04792  556 SHLARLLGDPELLEDALELADLLTEA----IIEDEELDIIGgsAGAIlvLLALYERTGDERALELAIACgDHLLKNAVEN 631
                         90
                 ....*....|
gi 674708360 126 SEGGFWHKDG 135
Cdd:cd04792  632 DGGARWKTPA 641
HybA1 COG3533
Beta-L-arabinofuranosidase, GH127 family [Carbohydrate transport and metabolism];
54-115 2.55e-03

Beta-L-arabinofuranosidase, GH127 family [Carbohydrate transport and metabolism];


Pssm-ID: 442754 [Multi-domain]  Cd Length: 597  Bit Score: 39.83  E-value: 2.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 674708360  54 WEATGEKRYFEYAKAYADLLIDDYGNLlfrRDELDA------IQAGLILfpLYEQTKDERYVKAAKRL 115
Cdd:COG3533  142 YRATGKRKLLDVAIRLADWIDDTFGPL---PDQLQGmlghggIEEALVE--LYRVTGDKRYLDLAKRF 204
 
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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