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Conserved domains on  [gi|530537386]
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Chain B, B-agarase

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Agarase_CBM pfam17992
Agarase CBM like domain; This is the N-terminal CBM-like domain in exo-beta-agarase proteins ...
7-200 4.78e-98

Agarase CBM like domain; This is the N-terminal CBM-like domain in exo-beta-agarase proteins (EC:3.2.1.81) found in the marine microbe Saccharophagus degradans. This enzyme catalyzes a critical step in the metabolism of agarose by S. degradans through cleaving agarose oligomers into neoagarobiose products that can be further processed into monomers. The CBM-like domain is structurally very similar to some CBM families. A loop in the CBM-like domain is involved in forming the roof of the active site channel. The contribution of the CBM-like domain to formation of the active site of the enzyme supports a role in substrate recognition explaining the exo-mode of beta-agarase action.


:

Pssm-ID: 436194  Cd Length: 182  Bit Score: 300.82  E-value: 4.78e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537386    7 DFENDQVPSNIHFLNARASIETYTGingepSKGLKLAMQSKQHSYTGLAIVPEQPWDWSEFTSASLYFDIVSVGDHSTQF 86
Cdd:pfam17992   1 DFENGQVPKEVKFENAKASLVDQGG-----DKALKVKLNSKNNHYASFSIVPEQPWDWSEYPSFSIAFDITNPGDRSTQL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537386   87 YLDVTDQNGAVFTRSIDIPVGKMQSYYAKLSGHDLEVPdsgdvndLNLASGLRSNPPTWTSDDRQFVWMWGVKNLDLSGI 166
Cdd:pfam17992  76 YITVTDKNGAVYTRSVVVPAGSAKTYYAELKGHDLQDP-------LNVSSGLRSNPPSWQSDYVQAIWMWGSKNLDTSAI 148
                         170       180       190
                  ....*....|....*....|....*....|....
gi 530537386  167 AKISLSVQSAMHDKTVIIDNIRIQPNPPQDENFL 200
Cdd:pfam17992 149 TKISFSVQGVLEDKQVTIDNIRVIPPPKMDENFL 182
GanA super family cl34369
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
520-665 3.62e-06

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


The actual alignment was detected with superfamily member COG1874:

Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 50.31  E-value: 3.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537386 520 TRQAFSKLLKAKYKTIAALNNAWGL-----KLSSWAEFDLGVDVKALPVtDTLRADYSMLLSAYADQYFKVVHGAVEHYM 594
Cdd:COG1874  161 CAAAFRDWLRERYGTLDALNEAWGTafwsqRYTDWDEIEPPRLTPTTAN-PSLRLDFRRFSSDQVLEYLRAQRDILREAG 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537386 595 PNHLY---LGARFPDWGMPmevvkAAAKYADVVSYNSYKEGLPK--QKWAFLAEL------DKPSIIGEFHIGAMDHGSY 663
Cdd:COG1874  240 PDVPVttnFMGPFPGLDYW-----KLARDLDVVSWDNYPDGSAAdpDEIAFAHDLmrglkgGGPFMVMEQWPGWVNWGPY 314

                 ..
gi 530537386 664 HP 665
Cdd:COG1874  315 NP 316
 
Name Accession Description Interval E-value
Agarase_CBM pfam17992
Agarase CBM like domain; This is the N-terminal CBM-like domain in exo-beta-agarase proteins ...
7-200 4.78e-98

Agarase CBM like domain; This is the N-terminal CBM-like domain in exo-beta-agarase proteins (EC:3.2.1.81) found in the marine microbe Saccharophagus degradans. This enzyme catalyzes a critical step in the metabolism of agarose by S. degradans through cleaving agarose oligomers into neoagarobiose products that can be further processed into monomers. The CBM-like domain is structurally very similar to some CBM families. A loop in the CBM-like domain is involved in forming the roof of the active site channel. The contribution of the CBM-like domain to formation of the active site of the enzyme supports a role in substrate recognition explaining the exo-mode of beta-agarase action.


Pssm-ID: 436194  Cd Length: 182  Bit Score: 300.82  E-value: 4.78e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537386    7 DFENDQVPSNIHFLNARASIETYTGingepSKGLKLAMQSKQHSYTGLAIVPEQPWDWSEFTSASLYFDIVSVGDHSTQF 86
Cdd:pfam17992   1 DFENGQVPKEVKFENAKASLVDQGG-----DKALKVKLNSKNNHYASFSIVPEQPWDWSEYPSFSIAFDITNPGDRSTQL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537386   87 YLDVTDQNGAVFTRSIDIPVGKMQSYYAKLSGHDLEVPdsgdvndLNLASGLRSNPPTWTSDDRQFVWMWGVKNLDLSGI 166
Cdd:pfam17992  76 YITVTDKNGAVYTRSVVVPAGSAKTYYAELKGHDLQDP-------LNVSSGLRSNPPSWQSDYVQAIWMWGSKNLDTSAI 148
                         170       180       190
                  ....*....|....*....|....*....|....
gi 530537386  167 AKISLSVQSAMHDKTVIIDNIRIQPNPPQDENFL 200
Cdd:pfam17992 149 TKISFSVQGVLEDKQVTIDNIRVIPPPKMDENFL 182
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
520-665 3.62e-06

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 50.31  E-value: 3.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537386 520 TRQAFSKLLKAKYKTIAALNNAWGL-----KLSSWAEFDLGVDVKALPVtDTLRADYSMLLSAYADQYFKVVHGAVEHYM 594
Cdd:COG1874  161 CAAAFRDWLRERYGTLDALNEAWGTafwsqRYTDWDEIEPPRLTPTTAN-PSLRLDFRRFSSDQVLEYLRAQRDILREAG 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537386 595 PNHLY---LGARFPDWGMPmevvkAAAKYADVVSYNSYKEGLPK--QKWAFLAEL------DKPSIIGEFHIGAMDHGSY 663
Cdd:COG1874  240 PDVPVttnFMGPFPGLDYW-----KLARDLDVVSWDNYPDGSAAdpDEIAFAHDLmrglkgGGPFMVMEQWPGWVNWGPY 314

                 ..
gi 530537386 664 HP 665
Cdd:COG1874  315 NP 316
Glyco_hydro_42 pfam02449
Beta-galactosidase; This group of beta-galactosidase enzymes belong to the glycosyl hydrolase ...
460-629 1.58e-05

Beta-galactosidase; This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues.


Pssm-ID: 396834  Cd Length: 376  Bit Score: 48.04  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537386  460 PEFKVRAMETARVVSEEIKNSPWCVGVFIDNQksFGRPD----SDKAQygipihtlgrpsegvptrQAFSKLLKAKYKTI 535
Cdd:pfam02449 106 PVYREYAARIVEALAERYGDHPALIGWHIDNE--YGCHVsecyCETCE------------------RAFRKWLKNRYGTI 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537386  536 AALNNAWGLKL-----SSWAEFDLGVDVKALPVTdTLRADYSMLLSAYADQYFKVVHGAVEHYMPN----HLYLGARFPD 606
Cdd:pfam02449 166 DALNEAWGTAFwsqtySDFDEIEPPRPAPTFPNP-SQILDYRRFSSDQLLEFYRAEREIIREYSPDipvtTNFMGSYFKD 244
                         170       180
                  ....*....|....*....|...
gi 530537386  607 WGMpmevvKAAAKYADVVSYNSY 629
Cdd:pfam02449 245 LDY-----FKWAKELDFVSWDSY 262
 
Name Accession Description Interval E-value
Agarase_CBM pfam17992
Agarase CBM like domain; This is the N-terminal CBM-like domain in exo-beta-agarase proteins ...
7-200 4.78e-98

Agarase CBM like domain; This is the N-terminal CBM-like domain in exo-beta-agarase proteins (EC:3.2.1.81) found in the marine microbe Saccharophagus degradans. This enzyme catalyzes a critical step in the metabolism of agarose by S. degradans through cleaving agarose oligomers into neoagarobiose products that can be further processed into monomers. The CBM-like domain is structurally very similar to some CBM families. A loop in the CBM-like domain is involved in forming the roof of the active site channel. The contribution of the CBM-like domain to formation of the active site of the enzyme supports a role in substrate recognition explaining the exo-mode of beta-agarase action.


Pssm-ID: 436194  Cd Length: 182  Bit Score: 300.82  E-value: 4.78e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537386    7 DFENDQVPSNIHFLNARASIETYTGingepSKGLKLAMQSKQHSYTGLAIVPEQPWDWSEFTSASLYFDIVSVGDHSTQF 86
Cdd:pfam17992   1 DFENGQVPKEVKFENAKASLVDQGG-----DKALKVKLNSKNNHYASFSIVPEQPWDWSEYPSFSIAFDITNPGDRSTQL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537386   87 YLDVTDQNGAVFTRSIDIPVGKMQSYYAKLSGHDLEVPdsgdvndLNLASGLRSNPPTWTSDDRQFVWMWGVKNLDLSGI 166
Cdd:pfam17992  76 YITVTDKNGAVYTRSVVVPAGSAKTYYAELKGHDLQDP-------LNVSSGLRSNPPSWQSDYVQAIWMWGSKNLDTSAI 148
                         170       180       190
                  ....*....|....*....|....*....|....
gi 530537386  167 AKISLSVQSAMHDKTVIIDNIRIQPNPPQDENFL 200
Cdd:pfam17992 149 TKISFSVQGVLEDKQVTIDNIRVIPPPKMDENFL 182
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
520-665 3.62e-06

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 50.31  E-value: 3.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537386 520 TRQAFSKLLKAKYKTIAALNNAWGL-----KLSSWAEFDLGVDVKALPVtDTLRADYSMLLSAYADQYFKVVHGAVEHYM 594
Cdd:COG1874  161 CAAAFRDWLRERYGTLDALNEAWGTafwsqRYTDWDEIEPPRLTPTTAN-PSLRLDFRRFSSDQVLEYLRAQRDILREAG 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537386 595 PNHLY---LGARFPDWGMPmevvkAAAKYADVVSYNSYKEGLPK--QKWAFLAEL------DKPSIIGEFHIGAMDHGSY 663
Cdd:COG1874  240 PDVPVttnFMGPFPGLDYW-----KLARDLDVVSWDNYPDGSAAdpDEIAFAHDLmrglkgGGPFMVMEQWPGWVNWGPY 314

                 ..
gi 530537386 664 HP 665
Cdd:COG1874  315 NP 316
Glyco_hydro_42 pfam02449
Beta-galactosidase; This group of beta-galactosidase enzymes belong to the glycosyl hydrolase ...
460-629 1.58e-05

Beta-galactosidase; This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues.


Pssm-ID: 396834  Cd Length: 376  Bit Score: 48.04  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537386  460 PEFKVRAMETARVVSEEIKNSPWCVGVFIDNQksFGRPD----SDKAQygipihtlgrpsegvptrQAFSKLLKAKYKTI 535
Cdd:pfam02449 106 PVYREYAARIVEALAERYGDHPALIGWHIDNE--YGCHVsecyCETCE------------------RAFRKWLKNRYGTI 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530537386  536 AALNNAWGLKL-----SSWAEFDLGVDVKALPVTdTLRADYSMLLSAYADQYFKVVHGAVEHYMPN----HLYLGARFPD 606
Cdd:pfam02449 166 DALNEAWGTAFwsqtySDFDEIEPPRPAPTFPNP-SQILDYRRFSSDQLLEFYRAEREIIREYSPDipvtTNFMGSYFKD 244
                         170       180
                  ....*....|....*....|...
gi 530537386  607 WGMpmevvKAAAKYADVVSYNSY 629
Cdd:pfam02449 245 LDY-----FKWAKELDFVSWDSY 262
 
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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