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Conserved domains on  [gi|1034585100|ref|XP_016876289|]
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protein O-mannosyl-transferase TMTC4 isoform X6 [Homo sapiens]

Protein Classification

DUF1736 domain-containing protein( domain architecture ID 10552345)

DUF1736 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TMTC_DUF1736 pfam08409
Protein O-mannosyl-transferase TMTC, DUF1736; This domain of unknown function is found in ...
369-443 6.30e-39

Protein O-mannosyl-transferase TMTC, DUF1736; This domain of unknown function is found in O-mannosyl -transferases TMTC1-4, and constitutes a loop between TM7 and TM8 located in the ER lumen that contains a small hydrophobic, but not membrane-embedded helix. This loop is critical for catalysis and binding of ligands, especially the lipid-linked sugar moiety. TMTCs transfers mannosyl residues to the hydroxyl group of serine or threonine residues. The 4 members of the TMTC family are O-mannosyl-transferases acting primarily on the cadherin superfamily; each member has distinct roles in decorating the cadherin domains with O-linked mannose glycans at specific regions. These proteins also act as O-mannosyl-transferase on other proteins such as PDIA3.


:

Pssm-ID: 462468  Cd Length: 75  Bit Score: 135.35  E-value: 6.30e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034585100 369 GTGPPAFTEVDNPASFADSMLVRAVNYNYYYSLNAWLLLCPWWLCFDWSMGCIPLIKSISDWRVIALAALWFCLI 443
Cdd:pfam08409   1 GGQLPVFSASDNPAAFSPSLLTRTLTYNYLPALNAWLLLFPSWLCFDWSMGSIPLIESLSDPRNLATLAFYGALA 75
 
Name Accession Description Interval E-value
TMTC_DUF1736 pfam08409
Protein O-mannosyl-transferase TMTC, DUF1736; This domain of unknown function is found in ...
369-443 6.30e-39

Protein O-mannosyl-transferase TMTC, DUF1736; This domain of unknown function is found in O-mannosyl -transferases TMTC1-4, and constitutes a loop between TM7 and TM8 located in the ER lumen that contains a small hydrophobic, but not membrane-embedded helix. This loop is critical for catalysis and binding of ligands, especially the lipid-linked sugar moiety. TMTCs transfers mannosyl residues to the hydroxyl group of serine or threonine residues. The 4 members of the TMTC family are O-mannosyl-transferases acting primarily on the cadherin superfamily; each member has distinct roles in decorating the cadherin domains with O-linked mannose glycans at specific regions. These proteins also act as O-mannosyl-transferase on other proteins such as PDIA3.


Pssm-ID: 462468  Cd Length: 75  Bit Score: 135.35  E-value: 6.30e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034585100 369 GTGPPAFTEVDNPASFADSMLVRAVNYNYYYSLNAWLLLCPWWLCFDWSMGCIPLIKSISDWRVIALAALWFCLI 443
Cdd:pfam08409   1 GGQLPVFSASDNPAAFSPSLLTRTLTYNYLPALNAWLLLFPSWLCFDWSMGSIPLIESLSDPRNLATLAFYGALA 75
 
Name Accession Description Interval E-value
TMTC_DUF1736 pfam08409
Protein O-mannosyl-transferase TMTC, DUF1736; This domain of unknown function is found in ...
369-443 6.30e-39

Protein O-mannosyl-transferase TMTC, DUF1736; This domain of unknown function is found in O-mannosyl -transferases TMTC1-4, and constitutes a loop between TM7 and TM8 located in the ER lumen that contains a small hydrophobic, but not membrane-embedded helix. This loop is critical for catalysis and binding of ligands, especially the lipid-linked sugar moiety. TMTCs transfers mannosyl residues to the hydroxyl group of serine or threonine residues. The 4 members of the TMTC family are O-mannosyl-transferases acting primarily on the cadherin superfamily; each member has distinct roles in decorating the cadherin domains with O-linked mannose glycans at specific regions. These proteins also act as O-mannosyl-transferase on other proteins such as PDIA3.


Pssm-ID: 462468  Cd Length: 75  Bit Score: 135.35  E-value: 6.30e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034585100 369 GTGPPAFTEVDNPASFADSMLVRAVNYNYYYSLNAWLLLCPWWLCFDWSMGCIPLIKSISDWRVIALAALWFCLI 443
Cdd:pfam08409   1 GGQLPVFSASDNPAAFSPSLLTRTLTYNYLPALNAWLLLFPSWLCFDWSMGSIPLIESLSDPRNLATLAFYGALA 75
 
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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