NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767962555|ref|XP_011537972|]
View 

fucose mutarotase isoform X1 [Homo sapiens]

Protein Classification

RbsD/FucU family protein( domain architecture ID 10008334)

RbsD/FucU family protein similar to Streptococcus pneumoniae fucose mutarotase, a component of the fucose-utilization pathway, which catalyzes the interconversion between alpha-L-fucose and beta-L-fucose

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
FucU COG4154
L-fucose mutarotase/ribose pyranase, RbsD/FucU family [Carbohydrate transport and metabolism];
4-172 6.02e-68

L-fucose mutarotase/ribose pyranase, RbsD/FucU family [Carbohydrate transport and metabolism];


:

Pssm-ID: 443323  Cd Length: 143  Bit Score: 203.09  E-value: 6.02e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962555   4 LKGVPALLSPELLYALARMGHGDEIVLADLNFPASSicqCGPMEIRADGLGIPQLLEAVLKLLPLDTYVESPAAVMELVP 83
Cdd:COG4154    2 LKGIDPLLSPELLKVLAEMGHGDEIVLADANFPAES---LARRVVRLDGHSAPELLEAILSLFPLDTFVDDPVVRMEVVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962555  84 SDKERglqTPVWTEYESILRRAGcvgslqpchfVFQRALAKIERFEFYERAKKAFAVVATGpaqcwawllcrETALYGNL 163
Cdd:COG4154   79 GPDEV---PPVWAEYQAIIAKAE----------GRPVPIERLERFAFYERAKKAYAVVATG-----------ETRLYGNI 134

                 ....*....
gi 767962555 164 ILRKGVLAL 172
Cdd:COG4154  135 ILKKGVIPP 143
 
Name Accession Description Interval E-value
FucU COG4154
L-fucose mutarotase/ribose pyranase, RbsD/FucU family [Carbohydrate transport and metabolism];
4-172 6.02e-68

L-fucose mutarotase/ribose pyranase, RbsD/FucU family [Carbohydrate transport and metabolism];


Pssm-ID: 443323  Cd Length: 143  Bit Score: 203.09  E-value: 6.02e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962555   4 LKGVPALLSPELLYALARMGHGDEIVLADLNFPASSicqCGPMEIRADGLGIPQLLEAVLKLLPLDTYVESPAAVMELVP 83
Cdd:COG4154    2 LKGIDPLLSPELLKVLAEMGHGDEIVLADANFPAES---LARRVVRLDGHSAPELLEAILSLFPLDTFVDDPVVRMEVVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962555  84 SDKERglqTPVWTEYESILRRAGcvgslqpchfVFQRALAKIERFEFYERAKKAFAVVATGpaqcwawllcrETALYGNL 163
Cdd:COG4154   79 GPDEV---PPVWAEYQAIIAKAE----------GRPVPIERLERFAFYERAKKAYAVVATG-----------ETRLYGNI 134

                 ....*....
gi 767962555 164 ILRKGVLAL 172
Cdd:COG4154  135 ILKKGVIPP 143
RbsD_FucU pfam05025
RbsD / FucU transport protein family; The Escherichia coli high-affinity ribose-transport ...
5-169 1.12e-52

RbsD / FucU transport protein family; The Escherichia coli high-affinity ribose-transport system consists of six proteins encoded by the rbs operon (rbsD, rbsA, rbsC, rbsB, rbsK and rbsR). RbsD was originally thought to be a high affinity ribose transport protein, but further analysis shows that it is a D-ribose pyranase. It catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose. It also catalyzes the conversion between beta-allofuranose and beta-allopyranose. This family also includes FucU a component of the fucose operon and is a L-fucose mutarotase, involved in the anomeric conversion of L-fucose. It also exhibits a pyranase activity for D-ribose. Both have been classified in the RbsD/FucU family of proteins. Members of this family are ubiquitous having been found in organizms from eubacteria to mammals.


Pssm-ID: 428264  Cd Length: 132  Bit Score: 164.12  E-value: 1.12e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962555    5 KGVPALLSPELLYALARMGHGDEIVLADLNFPASSICQCGPMEIRADGLGIPQLLEAVLKLLPLD-TYVESPAavmelVP 83
Cdd:pfam05025   1 MKKSGILNPELLKVLAEMGHGDEIVIADAGFPIPSGVERIDLALRAGGPSFLDVLDAVLSELPVEkVYVAEEI-----VE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962555   84 SDkerglqTPVWTEYESILRRAGCvgslqpchfvfqrALAKIERFEFYERAKKAFAVVATGpaqcwawllcrETALYGNL 163
Cdd:pfam05025  76 GN------PEVWAEYLALLPKAEG-------------EIEYVEHEAFKERAKKAKAVVRTG-----------ETTPYANI 125

                  ....*.
gi 767962555  164 ILRKGV 169
Cdd:pfam05025 126 ILKKGV 131
fucU PRK15420
L-fucose mutarotase; Provisional
4-169 1.24e-35

L-fucose mutarotase; Provisional


Pssm-ID: 185318  Cd Length: 140  Bit Score: 121.13  E-value: 1.24e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962555   4 LKGVPALLSPELLYALARMGHGDEIVLADLNFPASSIcqcGPMEIRADGLGIPQLLEAVLKLLPLDTYVeSPAAVMELVP 83
Cdd:PRK15420   2 LKTISPLISPELLKVLAEMGHGDEIIFSDAHFPAHSM---GPQVIRADGLLVSDLLQAIIPLFELDSYA-PPLVMMAAVE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962555  84 SDKergLQTPVWTEYESILRRAGcvgslqPChfvfqRALAKIERFEFYERAKKAFAVVATGpaqcwawllcrETALYGNL 163
Cdd:PRK15420  78 GDT---LDPEVERRYRNALSLQA------PC-----PDIIRINRFAFYERAQKAFAIVITG-----------ERAKYGNI 132

                 ....*.
gi 767962555 164 ILRKGV 169
Cdd:PRK15420 133 LLKKGV 138
 
Name Accession Description Interval E-value
FucU COG4154
L-fucose mutarotase/ribose pyranase, RbsD/FucU family [Carbohydrate transport and metabolism];
4-172 6.02e-68

L-fucose mutarotase/ribose pyranase, RbsD/FucU family [Carbohydrate transport and metabolism];


Pssm-ID: 443323  Cd Length: 143  Bit Score: 203.09  E-value: 6.02e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962555   4 LKGVPALLSPELLYALARMGHGDEIVLADLNFPASSicqCGPMEIRADGLGIPQLLEAVLKLLPLDTYVESPAAVMELVP 83
Cdd:COG4154    2 LKGIDPLLSPELLKVLAEMGHGDEIVLADANFPAES---LARRVVRLDGHSAPELLEAILSLFPLDTFVDDPVVRMEVVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962555  84 SDKERglqTPVWTEYESILRRAGcvgslqpchfVFQRALAKIERFEFYERAKKAFAVVATGpaqcwawllcrETALYGNL 163
Cdd:COG4154   79 GPDEV---PPVWAEYQAIIAKAE----------GRPVPIERLERFAFYERAKKAYAVVATG-----------ETRLYGNI 134

                 ....*....
gi 767962555 164 ILRKGVLAL 172
Cdd:COG4154  135 ILKKGVIPP 143
RbsD_FucU pfam05025
RbsD / FucU transport protein family; The Escherichia coli high-affinity ribose-transport ...
5-169 1.12e-52

RbsD / FucU transport protein family; The Escherichia coli high-affinity ribose-transport system consists of six proteins encoded by the rbs operon (rbsD, rbsA, rbsC, rbsB, rbsK and rbsR). RbsD was originally thought to be a high affinity ribose transport protein, but further analysis shows that it is a D-ribose pyranase. It catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose. It also catalyzes the conversion between beta-allofuranose and beta-allopyranose. This family also includes FucU a component of the fucose operon and is a L-fucose mutarotase, involved in the anomeric conversion of L-fucose. It also exhibits a pyranase activity for D-ribose. Both have been classified in the RbsD/FucU family of proteins. Members of this family are ubiquitous having been found in organizms from eubacteria to mammals.


Pssm-ID: 428264  Cd Length: 132  Bit Score: 164.12  E-value: 1.12e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962555    5 KGVPALLSPELLYALARMGHGDEIVLADLNFPASSICQCGPMEIRADGLGIPQLLEAVLKLLPLD-TYVESPAavmelVP 83
Cdd:pfam05025   1 MKKSGILNPELLKVLAEMGHGDEIVIADAGFPIPSGVERIDLALRAGGPSFLDVLDAVLSELPVEkVYVAEEI-----VE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962555   84 SDkerglqTPVWTEYESILRRAGCvgslqpchfvfqrALAKIERFEFYERAKKAFAVVATGpaqcwawllcrETALYGNL 163
Cdd:pfam05025  76 GN------PEVWAEYLALLPKAEG-------------EIEYVEHEAFKERAKKAKAVVRTG-----------ETTPYANI 125

                  ....*.
gi 767962555  164 ILRKGV 169
Cdd:pfam05025 126 ILKKGV 131
fucU PRK15420
L-fucose mutarotase; Provisional
4-169 1.24e-35

L-fucose mutarotase; Provisional


Pssm-ID: 185318  Cd Length: 140  Bit Score: 121.13  E-value: 1.24e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962555   4 LKGVPALLSPELLYALARMGHGDEIVLADLNFPASSIcqcGPMEIRADGLGIPQLLEAVLKLLPLDTYVeSPAAVMELVP 83
Cdd:PRK15420   2 LKTISPLISPELLKVLAEMGHGDEIIFSDAHFPAHSM---GPQVIRADGLLVSDLLQAIIPLFELDSYA-PPLVMMAAVE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962555  84 SDKergLQTPVWTEYESILRRAGcvgslqPChfvfqRALAKIERFEFYERAKKAFAVVATGpaqcwawllcrETALYGNL 163
Cdd:PRK15420  78 GDT---LDPEVERRYRNALSLQA------PC-----PDIIRINRFAFYERAQKAFAIVITG-----------ERAKYGNI 132

                 ....*.
gi 767962555 164 ILRKGV 169
Cdd:PRK15420 133 LLKKGV 138
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH