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Conserved domains on  [gi|749394889|gb|AJF18458|]
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mogA, partial [Xenopus laevis]

Protein Classification

trehalase domain-containing protein( domain architecture ID 108014)

trehalase domain-containing protein may catalyze the hydrolysis of alpha,alpha-trehalose to form alpha- and beta-D-glucose

CAZY:  GH37
EC:  3.2.1.28
Gene Ontology:  GO:0004555|GO:0005991

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Trehalase super family cl17346
Trehalase; Trehalase (EC:3.2.1.28) is known to recycle trehalose to glucose. Trehalose is a ...
1-206 1.86e-90

Trehalase; Trehalase (EC:3.2.1.28) is known to recycle trehalose to glucose. Trehalose is a physiological hallmark of heat-shock response in yeast and protects of proteins and membranes against a variety of stresses. This family is found in conjunction with pfam07492 in fungi.


The actual alignment was detected with superfamily member pfam03200:

Pssm-ID: 418443  Cd Length: 494  Bit Score: 273.85  E-value: 1.86e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749394889    1 SQVMADISQLLGEDGG--HYLHDNRILTDNALLHQQHWSERLGAYADYGNHTHNTALEWVRPRAAPgqdprslPPPQLIR 78
Cdd:pfam03200 262 ARSMASIAEFLGEDDDaeKYAKTENLLSDNDLLDKLHWSEEEGAYCDFGNHTEAVRLKWVEVRAGP-------PQPELIR 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749394889   79 VVRKPPRLQYVGALGYVSFFPFFLQVLNPSSPHLGRLLDHIRDSDKVWTPYGIRSLSKSSSLYLQRNTEHDAPYWRGPVW 158
Cdd:pfam03200 335 VTRDDPELQLVCHKGYVSLFPFLLKLLPPDSPKLEKLLDLIRDPEELWSDYGLRSLSKSSPLYGKRNTEHDEPYWRGPIW 414
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 749394889  159 INMNYLAVRALYLYSHMEGPHRDRLASLYRELRQNLLANLYRQYKDTG 206
Cdd:pfam03200 415 ININYLILSALHHYYDVDGPYRDKAKEIYKELRTNLVNNIYRQYKETG 462
 
Name Accession Description Interval E-value
Glyco_hydro_63 pfam03200
Glycosyl hydrolase family 63 C-terminal domain; This is a family of eukaryotic enzymes ...
1-206 1.86e-90

Glycosyl hydrolase family 63 C-terminal domain; This is a family of eukaryotic enzymes belonging to glycosyl hydrolase family 63. They catalyze the specific cleavage of the non-reducing terminal glucose residue from Glc(3)Man(9)GlcNAc(2). Mannosyl oligosaccharide glucosidase EC:3.2.1.106 is the first enzyme in the N-linked oligosaccharide processing pathway. This family represents the C-terminal catalytic domain.


Pssm-ID: 397353  Cd Length: 494  Bit Score: 273.85  E-value: 1.86e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749394889    1 SQVMADISQLLGEDGG--HYLHDNRILTDNALLHQQHWSERLGAYADYGNHTHNTALEWVRPRAAPgqdprslPPPQLIR 78
Cdd:pfam03200 262 ARSMASIAEFLGEDDDaeKYAKTENLLSDNDLLDKLHWSEEEGAYCDFGNHTEAVRLKWVEVRAGP-------PQPELIR 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749394889   79 VVRKPPRLQYVGALGYVSFFPFFLQVLNPSSPHLGRLLDHIRDSDKVWTPYGIRSLSKSSSLYLQRNTEHDAPYWRGPVW 158
Cdd:pfam03200 335 VTRDDPELQLVCHKGYVSLFPFLLKLLPPDSPKLEKLLDLIRDPEELWSDYGLRSLSKSSPLYGKRNTEHDEPYWRGPIW 414
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 749394889  159 INMNYLAVRALYLYSHMEGPHRDRLASLYRELRQNLLANLYRQYKDTG 206
Cdd:pfam03200 415 ININYLILSALHHYYDVDGPYRDKAKEIYKELRTNLVNNIYRQYKETG 462
GDB1 COG3408
Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];
2-176 6.94e-03

Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];


Pssm-ID: 442634 [Multi-domain]  Cd Length: 353  Bit Score: 36.78  E-value: 6.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749394889   2 QVMADISQLLGEDGGHYLHDNRILTDNALLHQQHWSERLGAYADYgnhthntalewvrpRAAPGQDPRSLPPPQLIRVvr 81
Cdd:COG3408  171 RALAELARALGDPELAARWRELAERLKESFNERFWNEELGYLADA--------------LDGDGRPDDSIRPNQLFAH-- 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749394889  82 kpprlqyvgalgyvsffPFFLQVLNPSspHLGRLLDHIRDSDkVWTPYGIRslskssslylqrnTE-------HDAPYWR 154
Cdd:COG3408  235 -----------------ALPTGILDPE--RARAVLRRLVSPE-LLTPWGLR-------------TLspgdpayNPMAYHN 281
                        170       180
                 ....*....|....*....|..
gi 749394889 155 GPVWINMNYLAVRALYLYSHME 176
Cdd:COG3408  282 GSVWPWLNGLYAEGLLRYGFRE 303
 
Name Accession Description Interval E-value
Glyco_hydro_63 pfam03200
Glycosyl hydrolase family 63 C-terminal domain; This is a family of eukaryotic enzymes ...
1-206 1.86e-90

Glycosyl hydrolase family 63 C-terminal domain; This is a family of eukaryotic enzymes belonging to glycosyl hydrolase family 63. They catalyze the specific cleavage of the non-reducing terminal glucose residue from Glc(3)Man(9)GlcNAc(2). Mannosyl oligosaccharide glucosidase EC:3.2.1.106 is the first enzyme in the N-linked oligosaccharide processing pathway. This family represents the C-terminal catalytic domain.


Pssm-ID: 397353  Cd Length: 494  Bit Score: 273.85  E-value: 1.86e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749394889    1 SQVMADISQLLGEDGG--HYLHDNRILTDNALLHQQHWSERLGAYADYGNHTHNTALEWVRPRAAPgqdprslPPPQLIR 78
Cdd:pfam03200 262 ARSMASIAEFLGEDDDaeKYAKTENLLSDNDLLDKLHWSEEEGAYCDFGNHTEAVRLKWVEVRAGP-------PQPELIR 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749394889   79 VVRKPPRLQYVGALGYVSFFPFFLQVLNPSSPHLGRLLDHIRDSDKVWTPYGIRSLSKSSSLYLQRNTEHDAPYWRGPVW 158
Cdd:pfam03200 335 VTRDDPELQLVCHKGYVSLFPFLLKLLPPDSPKLEKLLDLIRDPEELWSDYGLRSLSKSSPLYGKRNTEHDEPYWRGPIW 414
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 749394889  159 INMNYLAVRALYLYSHMEGPHRDRLASLYRELRQNLLANLYRQYKDTG 206
Cdd:pfam03200 415 ININYLILSALHHYYDVDGPYRDKAKEIYKELRTNLVNNIYRQYKETG 462
GDB1 COG3408
Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];
2-176 6.94e-03

Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];


Pssm-ID: 442634 [Multi-domain]  Cd Length: 353  Bit Score: 36.78  E-value: 6.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749394889   2 QVMADISQLLGEDGGHYLHDNRILTDNALLHQQHWSERLGAYADYgnhthntalewvrpRAAPGQDPRSLPPPQLIRVvr 81
Cdd:COG3408  171 RALAELARALGDPELAARWRELAERLKESFNERFWNEELGYLADA--------------LDGDGRPDDSIRPNQLFAH-- 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749394889  82 kpprlqyvgalgyvsffPFFLQVLNPSspHLGRLLDHIRDSDkVWTPYGIRslskssslylqrnTE-------HDAPYWR 154
Cdd:COG3408  235 -----------------ALPTGILDPE--RARAVLRRLVSPE-LLTPWGLR-------------TLspgdpayNPMAYHN 281
                        170       180
                 ....*....|....*....|..
gi 749394889 155 GPVWINMNYLAVRALYLYSHME 176
Cdd:COG3408  282 GSVWPWLNGLYAEGLLRYGFRE 303
 
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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