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Conserved domains on  [gi|1270026881|gb|ATO88293|]
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maltosephosphorylase, partial [Fructilactobacillus sanfranciscensis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13807 super family cl47111
maltose phosphorylase; Provisional
3-219 2.62e-85

maltose phosphorylase; Provisional


The actual alignment was detected with superfamily member PRK13807:

Pssm-ID: 237517 [Multi-domain]  Cd Length: 756  Bit Score: 267.54  E-value: 2.62e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270026881   3 IQIDGVTVDLATVPYTDFEVTLDMQAGVLHRQFTVNG----VRVQVDRFISVATKELADLRWSFTAIDGQThDVQLTALI 78
Cdd:PRK13807   92 IRIDGEELDLAKCEVSDFELELDMKEGVLTRSFTVLKngkeVRVEAERFLSIAQKELAVIKYSVTSLNGEA-KITFDSYL 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270026881  79 DGDVVNEDSNYDEKFWDVLDAEVTNDTAFLMTRTVPNPFGVPQFTVAAQQRFVSDLPAIDVVQE-DKQVGNIFAGQVGA- 156
Cdd:PRK13807  171 DGDVKNEDSNYDEKFWQVLEKGADATRAFIVTKTKPNPFGVPQFTVAAKMSNRTNGKVVPGVETkEKYVENSFTADVKAg 250
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270026881 157 ATQRIEKRVIVTTSRDYADDAAVKHATDtIFASIASATYDDLYDAHTAGWAERWEKADVQITG 219
Cdd:PRK13807  251 ETVTLEKRVIVVTSRDYEESELLKAAED-LLNKAAEKGFEELLAAHTAAWAKRWEKSDVVIEG 312
 
Name Accession Description Interval E-value
PRK13807 PRK13807
maltose phosphorylase; Provisional
3-219 2.62e-85

maltose phosphorylase; Provisional


Pssm-ID: 237517 [Multi-domain]  Cd Length: 756  Bit Score: 267.54  E-value: 2.62e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270026881   3 IQIDGVTVDLATVPYTDFEVTLDMQAGVLHRQFTVNG----VRVQVDRFISVATKELADLRWSFTAIDGQThDVQLTALI 78
Cdd:PRK13807   92 IRIDGEELDLAKCEVSDFELELDMKEGVLTRSFTVLKngkeVRVEAERFLSIAQKELAVIKYSVTSLNGEA-KITFDSYL 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270026881  79 DGDVVNEDSNYDEKFWDVLDAEVTNDTAFLMTRTVPNPFGVPQFTVAAQQRFVSDLPAIDVVQE-DKQVGNIFAGQVGA- 156
Cdd:PRK13807  171 DGDVKNEDSNYDEKFWQVLEKGADATRAFIVTKTKPNPFGVPQFTVAAKMSNRTNGKVVPGVETkEKYVENSFTADVKAg 250
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270026881 157 ATQRIEKRVIVTTSRDYADDAAVKHATDtIFASIASATYDDLYDAHTAGWAERWEKADVQITG 219
Cdd:PRK13807  251 ETVTLEKRVIVVTSRDYEESELLKAAED-LLNKAAEKGFEELLAAHTAAWAKRWEKSDVVIEG 312
ATH1 COG1554
Kojibiose phosphorylase YcjT [Carbohydrate transport and metabolism];
3-219 1.00e-47

Kojibiose phosphorylase YcjT [Carbohydrate transport and metabolism];


Pssm-ID: 441163 [Multi-domain]  Cd Length: 761  Bit Score: 166.85  E-value: 1.00e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270026881   3 IQIDGVTVDLATVPYTDFEVTLDMQAGVLHRQFTV---NGVRVQVD--RFISVATKELADLRWSFTAIDGqTHDVQLTAL 77
Cdd:COG1554    85 LRVDGEPLDLATGELLDYERELDMREGVLTRSFVWrdpAGRRVRVEsrRFVSMADRHLAAIRYEVTPLNF-SGPITIRSA 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270026881  78 IDGDVVNEDSN------YDEKFWDVLDAEVTNDTAFLMTRTVPNPFGVPQFTVAAQQRFVSDLPAIDVVQEDKQVGNIFA 151
Cdd:COG1554   164 LDGRVTNEDDDprryraLDEKHLEPLEKEAEDDRALLVARTRQSGIRVATAARHRVENGENVEAEREVEEEEDLVAETYT 243
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270026881 152 GQVGA-ATQRIEKRVIVTTSRDYADDAAVKHATDTIfASIASATYDDLYDAHTAGWAERWEKADVQITG 219
Cdd:COG1554   244 VDLKPgETLRLEKYVAYHTSRDHAISELADAAERAL-ARARETGFDELLAEQREAWADFWERADVEIEG 311
Glyco_hydro_65N pfam03636
Glycosyl hydrolase family 65, N-terminal domain; This family of glycosyl hydrolases contains ...
2-170 1.00e-23

Glycosyl hydrolase family 65, N-terminal domain; This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. This domain is believed to be essential for catalytic activity although its precise function remains unknown.


Pssm-ID: 460999 [Multi-domain]  Cd Length: 237  Bit Score: 94.56  E-value: 1.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270026881   2 IIQIDGVTVDLATVPYTDFEVTLDMQAGVLHRQFTV-----NGVRVQVDRFISVATKELADLRWSFTAIDGQThDVQLTA 76
Cdd:pfam03636  75 RLRIDGEPFDLDTGEILDYRRTLDMREGVLTRSFTWrspagRTVRVEFERFVSMADPHLAAIRYEITPLNFSG-EITVRS 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270026881  77 LIDGDVVNEDSNYDEKfwdvlDAEvtNDTAFLMTRTVPNPfgvpqFTVAAQQRFVSDLPAIDVV-QEDKQVGNIFAGQVG 155
Cdd:pfam03636 154 GLDGDVTNLGDFHDPR-----VAE--ADGIWLVARTRPSG-----ITVAMAMRHRVDLDGKPLEeADERTIAQTFTVELK 221
                         170
                  ....*....|....*.
gi 1270026881 156 A-ATQRIEKRVIVTTS 170
Cdd:pfam03636 222 AgETVTLEKYVAVATS 237
 
Name Accession Description Interval E-value
PRK13807 PRK13807
maltose phosphorylase; Provisional
3-219 2.62e-85

maltose phosphorylase; Provisional


Pssm-ID: 237517 [Multi-domain]  Cd Length: 756  Bit Score: 267.54  E-value: 2.62e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270026881   3 IQIDGVTVDLATVPYTDFEVTLDMQAGVLHRQFTVNG----VRVQVDRFISVATKELADLRWSFTAIDGQThDVQLTALI 78
Cdd:PRK13807   92 IRIDGEELDLAKCEVSDFELELDMKEGVLTRSFTVLKngkeVRVEAERFLSIAQKELAVIKYSVTSLNGEA-KITFDSYL 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270026881  79 DGDVVNEDSNYDEKFWDVLDAEVTNDTAFLMTRTVPNPFGVPQFTVAAQQRFVSDLPAIDVVQE-DKQVGNIFAGQVGA- 156
Cdd:PRK13807  171 DGDVKNEDSNYDEKFWQVLEKGADATRAFIVTKTKPNPFGVPQFTVAAKMSNRTNGKVVPGVETkEKYVENSFTADVKAg 250
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270026881 157 ATQRIEKRVIVTTSRDYADDAAVKHATDtIFASIASATYDDLYDAHTAGWAERWEKADVQITG 219
Cdd:PRK13807  251 ETVTLEKRVIVVTSRDYEESELLKAAED-LLNKAAEKGFEELLAAHTAAWAKRWEKSDVVIEG 312
ATH1 COG1554
Kojibiose phosphorylase YcjT [Carbohydrate transport and metabolism];
3-219 1.00e-47

Kojibiose phosphorylase YcjT [Carbohydrate transport and metabolism];


Pssm-ID: 441163 [Multi-domain]  Cd Length: 761  Bit Score: 166.85  E-value: 1.00e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270026881   3 IQIDGVTVDLATVPYTDFEVTLDMQAGVLHRQFTV---NGVRVQVD--RFISVATKELADLRWSFTAIDGqTHDVQLTAL 77
Cdd:COG1554    85 LRVDGEPLDLATGELLDYERELDMREGVLTRSFVWrdpAGRRVRVEsrRFVSMADRHLAAIRYEVTPLNF-SGPITIRSA 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270026881  78 IDGDVVNEDSN------YDEKFWDVLDAEVTNDTAFLMTRTVPNPFGVPQFTVAAQQRFVSDLPAIDVVQEDKQVGNIFA 151
Cdd:COG1554   164 LDGRVTNEDDDprryraLDEKHLEPLEKEAEDDRALLVARTRQSGIRVATAARHRVENGENVEAEREVEEEEDLVAETYT 243
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270026881 152 GQVGA-ATQRIEKRVIVTTSRDYADDAAVKHATDTIfASIASATYDDLYDAHTAGWAERWEKADVQITG 219
Cdd:COG1554   244 VDLKPgETLRLEKYVAYHTSRDHAISELADAAERAL-ARARETGFDELLAEQREAWADFWERADVEIEG 311
Glyco_hydro_65N pfam03636
Glycosyl hydrolase family 65, N-terminal domain; This family of glycosyl hydrolases contains ...
2-170 1.00e-23

Glycosyl hydrolase family 65, N-terminal domain; This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. This domain is believed to be essential for catalytic activity although its precise function remains unknown.


Pssm-ID: 460999 [Multi-domain]  Cd Length: 237  Bit Score: 94.56  E-value: 1.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270026881   2 IIQIDGVTVDLATVPYTDFEVTLDMQAGVLHRQFTV-----NGVRVQVDRFISVATKELADLRWSFTAIDGQThDVQLTA 76
Cdd:pfam03636  75 RLRIDGEPFDLDTGEILDYRRTLDMREGVLTRSFTWrspagRTVRVEFERFVSMADPHLAAIRYEITPLNFSG-EITVRS 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270026881  77 LIDGDVVNEDSNYDEKfwdvlDAEvtNDTAFLMTRTVPNPfgvpqFTVAAQQRFVSDLPAIDVV-QEDKQVGNIFAGQVG 155
Cdd:pfam03636 154 GLDGDVTNLGDFHDPR-----VAE--ADGIWLVARTRPSG-----ITVAMAMRHRVDLDGKPLEeADERTIAQTFTVELK 221
                         170
                  ....*....|....*.
gi 1270026881 156 A-ATQRIEKRVIVTTS 170
Cdd:pfam03636 222 AgETVTLEKYVAVATS 237
 
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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