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Conserved domains on  [gi|19424120|ref|NP_061846|]
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dolichol-phosphate mannosyltransferase subunit 3 isoform 1 [Homo sapiens]

Protein Classification

dolichol-phosphate mannosyltransferase subunit 3( domain architecture ID 10550626)

dolichol-phosphate mannosyltransferase subunit 3 is a stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; it tethers catalytic subunit DPM1 to the ER; DPM synthase generates mannosyl donors for glycosylphosphatidylinositols, N-glycan and protein O- and C-mannosylation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DPM3 pfam08285
Dolichol-phosphate mannosyltransferase subunit 3 (DPM3); This family corresponds to subunit 3 ...
 31-120 4.73e-33

Dolichol-phosphate mannosyltransferase subunit 3 (DPM3); This family corresponds to subunit 3 of dolichol-phosphate mannosyltransferase, an enzyme which generates mannosyl donors for glycosylphosphatidylinositols, N-glycan and protein O- and C-mannosylation. DPM3 is an integral membrane protein and plays a role in stabilising the dolichol-phosphate mannosyl transferase complex.


:

Pssm-ID: 462416  Cd Length: 89  Bit Score: 110.71  E-value: 4.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424120    31 MTKLAQWLWGLAILGSTWVALTTGALGLElPLSCQEVLWPLPAYLLVSAGCYALGTVGYRVATFHDCEDAARELQSQIQE 110
Cdd:pfam08285   1 MTRAQQWLSAALLLSSLWLALLLGLVPLP-PKIQDEIIPVLPFWALVSFGAYSLAVLGYGVLTFNDCPEAAKELQKEIKE 79

                          90
                  ....*....|
gi 19424120   111 ARADLARRGL 120
Cdd:pfam08285  80 AKADLRAKGV 89
 
Name Accession Description Interval E-value
DPM3 pfam08285
Dolichol-phosphate mannosyltransferase subunit 3 (DPM3); This family corresponds to subunit 3 ...
 31-120 4.73e-33

Dolichol-phosphate mannosyltransferase subunit 3 (DPM3); This family corresponds to subunit 3 of dolichol-phosphate mannosyltransferase, an enzyme which generates mannosyl donors for glycosylphosphatidylinositols, N-glycan and protein O- and C-mannosylation. DPM3 is an integral membrane protein and plays a role in stabilising the dolichol-phosphate mannosyl transferase complex.


Pssm-ID: 462416  Cd Length: 89  Bit Score: 110.71  E-value: 4.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424120    31 MTKLAQWLWGLAILGSTWVALTTGALGLElPLSCQEVLWPLPAYLLVSAGCYALGTVGYRVATFHDCEDAARELQSQIQE 110
Cdd:pfam08285   1 MTRAQQWLSAALLLSSLWLALLLGLVPLP-PKIQDEIIPVLPFWALVSFGAYSLAVLGYGVLTFNDCPEAAKELQKEIKE 79

                          90
                  ....*....|
gi 19424120   111 ARADLARRGL 120
Cdd:pfam08285  80 AKADLRAKGV 89
 
Name Accession Description Interval E-value
DPM3 pfam08285
Dolichol-phosphate mannosyltransferase subunit 3 (DPM3); This family corresponds to subunit 3 ...
 31-120 4.73e-33

Dolichol-phosphate mannosyltransferase subunit 3 (DPM3); This family corresponds to subunit 3 of dolichol-phosphate mannosyltransferase, an enzyme which generates mannosyl donors for glycosylphosphatidylinositols, N-glycan and protein O- and C-mannosylation. DPM3 is an integral membrane protein and plays a role in stabilising the dolichol-phosphate mannosyl transferase complex.


Pssm-ID: 462416  Cd Length: 89  Bit Score: 110.71  E-value: 4.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424120    31 MTKLAQWLWGLAILGSTWVALTTGALGLElPLSCQEVLWPLPAYLLVSAGCYALGTVGYRVATFHDCEDAARELQSQIQE 110
Cdd:pfam08285   1 MTRAQQWLSAALLLSSLWLALLLGLVPLP-PKIQDEIIPVLPFWALVSFGAYSLAVLGYGVLTFNDCPEAAKELQKEIKE 79

                          90
                  ....*....|
gi 19424120   111 ARADLARRGL 120
Cdd:pfam08285  80 AKADLRAKGV 89
 
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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