NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907162098|ref|XP_036020889|]
View 

protein-tyrosine sulfotransferase 1 isoform X1 [Mus musculus]

Protein Classification

sulfotransferase family protein( domain architecture ID 10604284)

sulfotransferase family protein may catalyze the transfer of sulfate from a donor such as 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to an acceptor substrate; such as protein-tyrosine sulfotransferases that catalyze the O-sulfation of tyrosine residues within acidic motifs of polypeptides

CATH:  3.40.50.300
EC:  2.8.2.-
Gene Ontology:  GO:0050656|GO:0008146|GO:0016020
PubMed:  31270211|9584614
SCOP:  4006221

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_3 pfam13469
Sulfotransferase family;
72-261 2.14e-62

Sulfotransferase family;


:

Pssm-ID: 463887  Cd Length: 173  Bit Score: 197.51  E-value: 2.14e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162098  72 IFIGGVPRSGTTLMRAMLDAHPDIRCGEET-RVIPRILALKQMWSRSskekirldeagvtdevldsamqaflLEVIVKHG 150
Cdd:pfam13469   1 IFIVGLPRSGTTLLHRLLAAHPDVRPPEETwFVIPRILALLQAWGKS-------------------------LEALARVP 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162098 151 EPAPYLCNKDPFALKSLTYLARLFPNAKFLLMVRDGrasVHSMISRKVTIAGFDLNSYR--------DCLTKWNRAIETM 222
Cdd:pfam13469  56 SYARWLCDKSPSHLFHLDLLLKAFPDAKFIHLHRDP---VDTVISSYCSLFGFTLSSYStaflrdigLALARWSRAYERL 132
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907162098 223 YNQCMEVGYKKCMLVHYEQLVLHPERWMRTLLKFLHIPW 261
Cdd:pfam13469 133 MAARARVPPGRFLDVRYEDLVADPEGTLRRILEFLGLPW 171
 
Name Accession Description Interval E-value
Sulfotransfer_3 pfam13469
Sulfotransferase family;
72-261 2.14e-62

Sulfotransferase family;


Pssm-ID: 463887  Cd Length: 173  Bit Score: 197.51  E-value: 2.14e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162098  72 IFIGGVPRSGTTLMRAMLDAHPDIRCGEET-RVIPRILALKQMWSRSskekirldeagvtdevldsamqaflLEVIVKHG 150
Cdd:pfam13469   1 IFIVGLPRSGTTLLHRLLAAHPDVRPPEETwFVIPRILALLQAWGKS-------------------------LEALARVP 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162098 151 EPAPYLCNKDPFALKSLTYLARLFPNAKFLLMVRDGrasVHSMISRKVTIAGFDLNSYR--------DCLTKWNRAIETM 222
Cdd:pfam13469  56 SYARWLCDKSPSHLFHLDLLLKAFPDAKFIHLHRDP---VDTVISSYCSLFGFTLSSYStaflrdigLALARWSRAYERL 132
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907162098 223 YNQCMEVGYKKCMLVHYEQLVLHPERWMRTLLKFLHIPW 261
Cdd:pfam13469 133 MAARARVPPGRFLDVRYEDLVADPEGTLRRILEFLGLPW 171
 
Name Accession Description Interval E-value
Sulfotransfer_3 pfam13469
Sulfotransferase family;
72-261 2.14e-62

Sulfotransferase family;


Pssm-ID: 463887  Cd Length: 173  Bit Score: 197.51  E-value: 2.14e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162098  72 IFIGGVPRSGTTLMRAMLDAHPDIRCGEET-RVIPRILALKQMWSRSskekirldeagvtdevldsamqaflLEVIVKHG 150
Cdd:pfam13469   1 IFIVGLPRSGTTLLHRLLAAHPDVRPPEETwFVIPRILALLQAWGKS-------------------------LEALARVP 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162098 151 EPAPYLCNKDPFALKSLTYLARLFPNAKFLLMVRDGrasVHSMISRKVTIAGFDLNSYR--------DCLTKWNRAIETM 222
Cdd:pfam13469  56 SYARWLCDKSPSHLFHLDLLLKAFPDAKFIHLHRDP---VDTVISSYCSLFGFTLSSYStaflrdigLALARWSRAYERL 132
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907162098 223 YNQCMEVGYKKCMLVHYEQLVLHPERWMRTLLKFLHIPW 261
Cdd:pfam13469 133 MAARARVPPGRFLDVRYEDLVADPEGTLRRILEFLGLPW 171
Sulfotransfer_4 pfam17784
Sulfotransferase domain; This family of proteins are distantly related to sulfotransferase ...
170-240 6.54e-04

Sulfotransferase domain; This family of proteins are distantly related to sulfotransferase enzymes. This protein in S. mansonii has been shown to be involved in resistance to oxamniquine and to have sulfotransferase activity.


Pssm-ID: 465504  Cd Length: 215  Bit Score: 40.70  E-value: 6.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162098 170 LARLFPNAKFLLMVRDG-------RASVHSMISRKVTIAGFDLNSYRDCLTKWNRAIETMYNQCMEVGY--------KKC 234
Cdd:pfam17784  84 LLEAYPDAKVILTVRDPdkwlksmRNTILAMLTWPLRFLLAWLDPLLGFLRRFGRLLRALLRGFFGADGrfedeanlRAA 163

                  ....*.
gi 1907162098 235 MLVHYE 240
Cdd:pfam17784 164 YERHNE 169
 
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