NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767941753|ref|XP_011533680|]
View 

uronyl 2-sulfotransferase isoform X2 [Homo sapiens]

Protein Classification

sulfotransferase family protein( domain architecture ID 366236)

sulfotransferase family protein may catalyze the transfer of sulfate from a donor such as 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to an acceptor substrate

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Sulfotransfer_2 super family cl22970
Sulfotransferase family; This family includes a variety of sulfotransferase enzymes. ...
 105-205 5.49e-09

Sulfotransferase family; This family includes a variety of sulfotransferase enzymes. Chondroitin 6-sulfotransferase catalyzes the transfer of sulfate to position 6 of the N-acetylgalactosamine residue of chondroitin. This family also includes Heparan sulfate 2-O-sulfotransferase (HS2ST) and Heparan sulfate 6-sulfotransferase (HS6ST). Heparan sulfate (HS) is a co-receptor for a number of growth factors, morphogens, and adhesion proteins. HS biosynthetic modifications may determine the strength and outcome of HS-ligand interactions. Mice that lack HS2ST undergo developmental failure only after midgestation,the most dramatic effect being the complete failure of kidney development. Heparan sulphate 6- O -sulfotransferase (HS6ST) catalyzes the transfer of sulphate from adenosine 3'-phosphate, 5'-phosphosulphate to the 6th position of the N -sulphoglucosamine residue in heparan sulphate.


The actual alignment was detected with superfamily member pfam03567:

Pssm-ID: 451469  Cd Length: 238  Bit Score: 54.84  E-value: 5.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941753  105 VVYNRVGKCGSRTVVLLLRILSEKHGFNL-VTSDIHNKTRLTKNEQMELIKNISTAEQPYLFTRHVHFLNFSrfggdqpv 183
Cdd:pfam03567   6 ILYCRVPKVASTSWKRVLCVLQGLAQFDKrDPLRICSNLVHSSSSVNKKLKRLFRTSPEEIQHRLKNYFKFA-------- 77

                          90       100
                  ....*....|....*....|..
gi 767941753  184 yinIIRDPVNRFLSNYFFRRFG 205
Cdd:pfam03567  78 ---FVRDPFERLLSAYRDKCGG 96
 
Name Accession Description Interval E-value
Sulfotransfer_2 pfam03567
Sulfotransferase family; This family includes a variety of sulfotransferase enzymes. ...
 105-205 5.49e-09

Sulfotransferase family; This family includes a variety of sulfotransferase enzymes. Chondroitin 6-sulfotransferase catalyzes the transfer of sulfate to position 6 of the N-acetylgalactosamine residue of chondroitin. This family also includes Heparan sulfate 2-O-sulfotransferase (HS2ST) and Heparan sulfate 6-sulfotransferase (HS6ST). Heparan sulfate (HS) is a co-receptor for a number of growth factors, morphogens, and adhesion proteins. HS biosynthetic modifications may determine the strength and outcome of HS-ligand interactions. Mice that lack HS2ST undergo developmental failure only after midgestation,the most dramatic effect being the complete failure of kidney development. Heparan sulphate 6- O -sulfotransferase (HS6ST) catalyzes the transfer of sulphate from adenosine 3'-phosphate, 5'-phosphosulphate to the 6th position of the N -sulphoglucosamine residue in heparan sulphate.


Pssm-ID: 427369  Cd Length: 238  Bit Score: 54.84  E-value: 5.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941753  105 VVYNRVGKCGSRTVVLLLRILSEKHGFNL-VTSDIHNKTRLTKNEQMELIKNISTAEQPYLFTRHVHFLNFSrfggdqpv 183
Cdd:pfam03567   6 ILYCRVPKVASTSWKRVLCVLQGLAQFDKrDPLRICSNLVHSSSSVNKKLKRLFRTSPEEIQHRLKNYFKFA-------- 77

                          90       100
                  ....*....|....*....|..
gi 767941753  184 yinIIRDPVNRFLSNYFFRRFG 205
Cdd:pfam03567  78 ---FVRDPFERLLSAYRDKCGG 96
 
Name Accession Description Interval E-value
Sulfotransfer_2 pfam03567
Sulfotransferase family; This family includes a variety of sulfotransferase enzymes. ...
 105-205 5.49e-09

Sulfotransferase family; This family includes a variety of sulfotransferase enzymes. Chondroitin 6-sulfotransferase catalyzes the transfer of sulfate to position 6 of the N-acetylgalactosamine residue of chondroitin. This family also includes Heparan sulfate 2-O-sulfotransferase (HS2ST) and Heparan sulfate 6-sulfotransferase (HS6ST). Heparan sulfate (HS) is a co-receptor for a number of growth factors, morphogens, and adhesion proteins. HS biosynthetic modifications may determine the strength and outcome of HS-ligand interactions. Mice that lack HS2ST undergo developmental failure only after midgestation,the most dramatic effect being the complete failure of kidney development. Heparan sulphate 6- O -sulfotransferase (HS6ST) catalyzes the transfer of sulphate from adenosine 3'-phosphate, 5'-phosphosulphate to the 6th position of the N -sulphoglucosamine residue in heparan sulphate.


Pssm-ID: 427369  Cd Length: 238  Bit Score: 54.84  E-value: 5.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941753  105 VVYNRVGKCGSRTVVLLLRILSEKHGFNL-VTSDIHNKTRLTKNEQMELIKNISTAEQPYLFTRHVHFLNFSrfggdqpv 183
Cdd:pfam03567   6 ILYCRVPKVASTSWKRVLCVLQGLAQFDKrDPLRICSNLVHSSSSVNKKLKRLFRTSPEEIQHRLKNYFKFA-------- 77

                          90       100
                  ....*....|....*....|..
gi 767941753  184 yinIIRDPVNRFLSNYFFRRFG 205
Cdd:pfam03567  78 ---FVRDPFERLLSAYRDKCGG 96
 
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