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Conserved domains on  [gi|189217888|ref|NP_001121368|]
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carbohydrate sulfotransferase 8 [Homo sapiens]

Protein Classification

sulfotransferase family protein (domain architecture ID 10507897)

sulfotransferase family protein such as heparan-sulfate 6-O-sulfotransferases, which catalyze the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Sulfotransfer_2 pfam03567
Sulfotransferase family; This family includes a variety of sulfotransferase enzymes. ...
187-416 1.29e-62

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: 335378  Cd Length: 232  Bit Score: 201.48  E-value: 1.29e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217888  187 EDRHRVLYCEVPKAGCSNWKRVLMVLAGLASSTAD---IQHNTVHYGSA-------LKRLDTFDRQGILHRLSTYTKMLF 256
Cdd:pfam03567   1 APDHKIVYCRVPKVASTSWKRVLCVLSGENKFLADprtINDTWAHSKRScgwshgsFRDLSRLTSCEIRKRLRKYFKFAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217888  257 VREPFERLVSAFRDKFEHPNSyyhpvfGKAILARYRanasrealrtGSGVRFPEFVQYLLD-VHRPVGMDIHWDHVSRLC 335
Cdd:pfam03567  81 VRDPFERLVSAYRNKCVGANY------GSDMTCRGR----------GSGVSFEEFLECLLDlAPERTPFDRHWAPQCDLC 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217888  336 SPCLIDYDFVGKFESMEDDANFFLSLIRAPRNLT--------FPRFKDRHSQeARTTARIAHQYFAQLSALQRQRTYDFY 407
Cdd:pfam03567 145 HPCLIKYDLVGKYETLEEDASALLRLLGRLRRQGvplyglgkIPRGETANST-HRSKSRLEAEYFVRIDPKLRRRLYEIY 223

                  ....*....
gi 189217888  408 YMDYLMFNY 416
Cdd:pfam03567 224 EFDFELFGY 232
 
Name Accession Description Interval E-value
Sulfotransfer_2 pfam03567
Sulfotransferase family; This family includes a variety of sulfotransferase enzymes. ...
187-416 1.29e-62

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: 335378  Cd Length: 232  Bit Score: 201.48  E-value: 1.29e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217888  187 EDRHRVLYCEVPKAGCSNWKRVLMVLAGLASSTAD---IQHNTVHYGSA-------LKRLDTFDRQGILHRLSTYTKMLF 256
Cdd:pfam03567   1 APDHKIVYCRVPKVASTSWKRVLCVLSGENKFLADprtINDTWAHSKRScgwshgsFRDLSRLTSCEIRKRLRKYFKFAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217888  257 VREPFERLVSAFRDKFEHPNSyyhpvfGKAILARYRanasrealrtGSGVRFPEFVQYLLD-VHRPVGMDIHWDHVSRLC 335
Cdd:pfam03567  81 VRDPFERLVSAYRNKCVGANY------GSDMTCRGR----------GSGVSFEEFLECLLDlAPERTPFDRHWAPQCDLC 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217888  336 SPCLIDYDFVGKFESMEDDANFFLSLIRAPRNLT--------FPRFKDRHSQeARTTARIAHQYFAQLSALQRQRTYDFY 407
Cdd:pfam03567 145 HPCLIKYDLVGKYETLEEDASALLRLLGRLRRQGvplyglgkIPRGETANST-HRSKSRLEAEYFVRIDPKLRRRLYEIY 223

                  ....*....
gi 189217888  408 YMDYLMFNY 416
Cdd:pfam03567 224 EFDFELFGY 232
 
Name Accession Description Interval E-value
Sulfotransfer_2 pfam03567
Sulfotransferase family; This family includes a variety of sulfotransferase enzymes. ...
187-416 1.29e-62

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: 335378  Cd Length: 232  Bit Score: 201.48  E-value: 1.29e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217888  187 EDRHRVLYCEVPKAGCSNWKRVLMVLAGLASSTAD---IQHNTVHYGSA-------LKRLDTFDRQGILHRLSTYTKMLF 256
Cdd:pfam03567   1 APDHKIVYCRVPKVASTSWKRVLCVLSGENKFLADprtINDTWAHSKRScgwshgsFRDLSRLTSCEIRKRLRKYFKFAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217888  257 VREPFERLVSAFRDKFEHPNSyyhpvfGKAILARYRanasrealrtGSGVRFPEFVQYLLD-VHRPVGMDIHWDHVSRLC 335
Cdd:pfam03567  81 VRDPFERLVSAYRNKCVGANY------GSDMTCRGR----------GSGVSFEEFLECLLDlAPERTPFDRHWAPQCDLC 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217888  336 SPCLIDYDFVGKFESMEDDANFFLSLIRAPRNLT--------FPRFKDRHSQeARTTARIAHQYFAQLSALQRQRTYDFY 407
Cdd:pfam03567 145 HPCLIKYDLVGKYETLEEDASALLRLLGRLRRQGvplyglgkIPRGETANST-HRSKSRLEAEYFVRIDPKLRRRLYEIY 223

                  ....*....
gi 189217888  408 YMDYLMFNY 416
Cdd:pfam03567 224 EFDFELFGY 232
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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