NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1635381375|ref|NP_001357392|]
View 

beta-galactosidase-1-like protein 2 isoform d precursor [Homo sapiens]

Protein Classification

alpha-amylase family protein( domain architecture ID 1562432)

alpha-amylase family protein may catalyze the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
AmyAc_family super family cl38930
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
53-149 3.93e-58

Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; and C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost this catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


The actual alignment was detected with superfamily member pfam01301:

Pssm-ID: 453893  Cd Length: 316  Bit Score: 183.61  E-value: 3.93e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635381375  53 NFMLEDSTFWIFGGSIHYFRVPREYWRDRLLKMKACGLNTLTTYVPWNLHEPERGKFDFSGNLDLEAFVLMAAEIGLWVI 132
Cdd:pfam01301   1 SFLIDGKRFRLISGSIHYFRIPPEMWPDRLQKAKALGLNAIETYVFWNLHEPEPGQYDFSGILDLVKFIKLAQEAGLYVI 80
                          90
                  ....*....|....*..
gi 1635381375 133 LRPGPYICSEMDLGGLP 149
Cdd:pfam01301  81 LRPGPYICAEWDFGGLP 97
 
Name Accession Description Interval E-value
Glyco_hydro_35 pfam01301
Glycosyl hydrolases family 35;
53-149 3.93e-58

Glycosyl hydrolases family 35;


Pssm-ID: 396048  Cd Length: 316  Bit Score: 183.61  E-value: 3.93e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635381375  53 NFMLEDSTFWIFGGSIHYFRVPREYWRDRLLKMKACGLNTLTTYVPWNLHEPERGKFDFSGNLDLEAFVLMAAEIGLWVI 132
Cdd:pfam01301   1 SFLIDGKRFRLISGSIHYFRIPPEMWPDRLQKAKALGLNAIETYVFWNLHEPEPGQYDFSGILDLVKFIKLAQEAGLYVI 80
                          90
                  ....*....|....*..
gi 1635381375 133 LRPGPYICSEMDLGGLP 149
Cdd:pfam01301  81 LRPGPYICAEWDFGGLP 97
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
50-149 1.20e-25

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


Pssm-ID: 224786 [Multi-domain]  Cd Length: 673  Bit Score: 101.73  E-value: 1.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635381375  50 KGWNFMLEDSTFWIFGGSIHYFRVPREYWRDRLLKMKACGLNTLTT-YVPWNLHEPERGKFDFSgNLDLEaFVLMAAEIG 128
Cdd:COG1874     4 DGYSFIRDGRRILLYGGDYYPERWPRETWMDDLRKMKALGLNTVRIgYFAWNLHEPEEGKFDFT-WLDEI-FLERAYKAG 81
                          90       100
                  ....*....|....*....|..
gi 1635381375 129 LWVILRPGP-YICSEMDLGGLP 149
Cdd:COG1874    82 LYVILRTGPtGAPPAWLAKKYP 103
PLN03059 PLN03059
beta-galactosidase; Provisional
63-149 3.47e-23

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 94.69  E-value: 3.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635381375  63 IFGGSIHYFRVPREYWRDRLLKMKACGLNTLTTYVPWNLHEPERGKFDFSGNLDLEAFVLMAAEIGLWVILRPGPYICSE 142
Cdd:PLN03059   46 LISGSIHYPRSTPEMWPDLIQKAKDGGLDVIQTYVFWNGHEPSPGNYYFEDRYDLVKFIKVVQAAGLYVHLRIGPYICAE 125

                  ....*..
gi 1635381375 143 MDLGGLP 149
Cdd:PLN03059  126 WNFGGFP 132
 
Name Accession Description Interval E-value
Glyco_hydro_35 pfam01301
Glycosyl hydrolases family 35;
53-149 3.93e-58

Glycosyl hydrolases family 35;


Pssm-ID: 396048  Cd Length: 316  Bit Score: 183.61  E-value: 3.93e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635381375  53 NFMLEDSTFWIFGGSIHYFRVPREYWRDRLLKMKACGLNTLTTYVPWNLHEPERGKFDFSGNLDLEAFVLMAAEIGLWVI 132
Cdd:pfam01301   1 SFLIDGKRFRLISGSIHYFRIPPEMWPDRLQKAKALGLNAIETYVFWNLHEPEPGQYDFSGILDLVKFIKLAQEAGLYVI 80
                          90
                  ....*....|....*..
gi 1635381375 133 LRPGPYICSEMDLGGLP 149
Cdd:pfam01301  81 LRPGPYICAEWDFGGLP 97
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
50-149 1.20e-25

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


Pssm-ID: 224786 [Multi-domain]  Cd Length: 673  Bit Score: 101.73  E-value: 1.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635381375  50 KGWNFMLEDSTFWIFGGSIHYFRVPREYWRDRLLKMKACGLNTLTT-YVPWNLHEPERGKFDFSgNLDLEaFVLMAAEIG 128
Cdd:COG1874     4 DGYSFIRDGRRILLYGGDYYPERWPRETWMDDLRKMKALGLNTVRIgYFAWNLHEPEEGKFDFT-WLDEI-FLERAYKAG 81
                          90       100
                  ....*....|....*....|..
gi 1635381375 129 LWVILRPGP-YICSEMDLGGLP 149
Cdd:COG1874    82 LYVILRTGPtGAPPAWLAKKYP 103
PLN03059 PLN03059
beta-galactosidase; Provisional
63-149 3.47e-23

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 94.69  E-value: 3.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635381375  63 IFGGSIHYFRVPREYWRDRLLKMKACGLNTLTTYVPWNLHEPERGKFDFSGNLDLEAFVLMAAEIGLWVILRPGPYICSE 142
Cdd:PLN03059   46 LISGSIHYPRSTPEMWPDLIQKAKDGGLDVIQTYVFWNGHEPSPGNYYFEDRYDLVKFIKVVQAAGLYVHLRIGPYICAE 125

                  ....*..
gi 1635381375 143 MDLGGLP 149
Cdd:PLN03059  126 WNFGGFP 132
Glyco_hydro_42 pfam02449
Beta-galactosidase; This group of beta-galactosidase enzymes belong to the glycosyl hydrolase ...
71-136 8.77e-10

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: 56.13  E-value: 8.77e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1635381375  71 FRVPREYWRDRLLKMKACGLNTLT-TYVPWNLHEPERGKFDFSGnldLEAFVLMAAEIGLWVILRPG 136
Cdd:pfam02449   5 EQWPEETWEEDIRLMKEAGVNVVRiGIFAWAKLEPEEGKYDFEW---LDEVIDLLAKAGIKVILATP 68
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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