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Conserved domains on  [gi|28574843|ref|NP_788531|]
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pipe, isoform H [Drosophila melanogaster]

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

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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. ...
 195-380 4.50e-03

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: 38.27  E-value: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574843   195 DFNEYNLPKPIFIN----------LVRDPVERMISWYYYVRnsyRNAIFYRNNPLAPLKPTAWFK-KSYNDCVRSGDPEC 263
Cdd:pfam03567  54 KLKRLFRTSPEEIQhrlknyfkfaFVRDPFERLLSAYRDKC---GGEIIRKYTSDECPGCGTDVTfEEFVRYLLDTLTCR 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574843   264 QYVPLAVRDVegNFKRQTlFFCGhdQDCLPFNSPLAVQIAKRRVETEYAVVGTWEETNitltVLEHYIPRYFARakmiFN 343
Cdd:pfam03567 131 EGLIFNEADR--HWAPQS-WLCH--PCLIKYDFIGRLETLEEDAKLLLRLLGIFGLQS----VPERNLNRIERN----FL 197

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 28574843   344 LYQKSLQNRNR-NNRKPHVDADVRAMVRRNFTHEYDFY 380
Cdd:pfam03567 198 AGRTTHKSSARrQYFKQLRSPELRRRLYKIYYLDFELF 235
 
Name Accession Description Interval E-value
Sulfotransfer_2 pfam03567
Sulfotransferase family; This family includes a variety of sulfotransferase enzymes. ...
 195-380 4.50e-03

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: 38.27  E-value: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574843   195 DFNEYNLPKPIFIN----------LVRDPVERMISWYYYVRnsyRNAIFYRNNPLAPLKPTAWFK-KSYNDCVRSGDPEC 263
Cdd:pfam03567  54 KLKRLFRTSPEEIQhrlknyfkfaFVRDPFERLLSAYRDKC---GGEIIRKYTSDECPGCGTDVTfEEFVRYLLDTLTCR 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574843   264 QYVPLAVRDVegNFKRQTlFFCGhdQDCLPFNSPLAVQIAKRRVETEYAVVGTWEETNitltVLEHYIPRYFARakmiFN 343
Cdd:pfam03567 131 EGLIFNEADR--HWAPQS-WLCH--PCLIKYDFIGRLETLEEDAKLLLRLLGIFGLQS----VPERNLNRIERN----FL 197

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 28574843   344 LYQKSLQNRNR-NNRKPHVDADVRAMVRRNFTHEYDFY 380
Cdd:pfam03567 198 AGRTTHKSSARrQYFKQLRSPELRRRLYKIYYLDFELF 235
 
Name Accession Description Interval E-value
Sulfotransfer_2 pfam03567
Sulfotransferase family; This family includes a variety of sulfotransferase enzymes. ...
 195-380 4.50e-03

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: 38.27  E-value: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574843   195 DFNEYNLPKPIFIN----------LVRDPVERMISWYYYVRnsyRNAIFYRNNPLAPLKPTAWFK-KSYNDCVRSGDPEC 263
Cdd:pfam03567  54 KLKRLFRTSPEEIQhrlknyfkfaFVRDPFERLLSAYRDKC---GGEIIRKYTSDECPGCGTDVTfEEFVRYLLDTLTCR 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574843   264 QYVPLAVRDVegNFKRQTlFFCGhdQDCLPFNSPLAVQIAKRRVETEYAVVGTWEETNitltVLEHYIPRYFARakmiFN 343
Cdd:pfam03567 131 EGLIFNEADR--HWAPQS-WLCH--PCLIKYDFIGRLETLEEDAKLLLRLLGIFGLQS----VPERNLNRIERN----FL 197

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 28574843   344 LYQKSLQNRNR-NNRKPHVDADVRAMVRRNFTHEYDFY 380
Cdd:pfam03567 198 AGRTTHKSSARrQYFKQLRSPELRRRLYKIYYLDFELF 235
 
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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