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Conserved domains on  [gi|795612028|ref|XP_011918394|]
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PREDICTED: transmembrane protein 169 [Cercocebus atys]

Protein Classification

TMEM169 domain-containing protein( domain architecture ID 10633347)

TMEM169 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TMEM169 pfam15052
TMEM169 protein family; This domain is thought to be structured transmembrane helices and ...
 147-277 2.96e-89

TMEM169 protein family; This domain is thought to be structured transmembrane helices and includes the intermediary cytoplasmic domain. It is found in eukaryotes, and is approximately 130 amino acids in length.


:

Pssm-ID: 464471  Cd Length: 131  Bit Score: 261.85  E-value: 2.96e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795612028  147 RMACQVGADRGPHVVLWTLVCLPVVFILSFVVSFYYGTITWYNIFLVYNEERTFWHKISYCPCLILFYPVLIMAMASSLG 226
Cdd:pfam15052   1 KDICRCGLDRGPHIFLWSLICLPFVFVLSFVYSFYYGTLTWYNIFLVYNEERSFLHKITVCPLLILFYPFLIVLFTLGLG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 795612028  227 LYAAVVQLSWSWGAWWQAARDMEKGFCGWLCSKLGLEDCSPYSIVELLESD 277
Cdd:pfam15052  81 LYAAVVQLSWSFSEWWQEVRDFEKGFYGWLCNKLGLEDCSPYEVVELLDSD 131
 
Name Accession Description Interval E-value
TMEM169 pfam15052
TMEM169 protein family; This domain is thought to be structured transmembrane helices and ...
 147-277 2.96e-89

TMEM169 protein family; This domain is thought to be structured transmembrane helices and includes the intermediary cytoplasmic domain. It is found in eukaryotes, and is approximately 130 amino acids in length.


Pssm-ID: 464471  Cd Length: 131  Bit Score: 261.85  E-value: 2.96e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795612028  147 RMACQVGADRGPHVVLWTLVCLPVVFILSFVVSFYYGTITWYNIFLVYNEERTFWHKISYCPCLILFYPVLIMAMASSLG 226
Cdd:pfam15052   1 KDICRCGLDRGPHIFLWSLICLPFVFVLSFVYSFYYGTLTWYNIFLVYNEERSFLHKITVCPLLILFYPFLIVLFTLGLG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 795612028  227 LYAAVVQLSWSWGAWWQAARDMEKGFCGWLCSKLGLEDCSPYSIVELLESD 277
Cdd:pfam15052  81 LYAAVVQLSWSFSEWWQEVRDFEKGFYGWLCNKLGLEDCSPYEVVELLDSD 131
PT_UbiA cd13956
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ...
 160-245 8.00e-03

UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


Pssm-ID: 260119 [Multi-domain]  Cd Length: 271  Bit Score: 37.33  E-value: 8.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795612028 160 VVLWTLVCLPVVFILSFVVSFYYGTITWYNIFL--VYNeertFWHKISYcPCLILFYPVLIMAMAssLGLYAAVVQLSWS 237
Cdd:cd13956   79 ALAFAAALLLVGLALALALGPLALLLLLAGLLLglAYS----LGLKRLK-LGGWGVLGYATGLAL--LPGLGAVAAGGLV 151


                 ....*...
gi 795612028 238 WGAWWQAA 245
Cdd:cd13956  152 PLALLLAL 159
 
Name Accession Description Interval E-value
TMEM169 pfam15052
TMEM169 protein family; This domain is thought to be structured transmembrane helices and ...
 147-277 2.96e-89

TMEM169 protein family; This domain is thought to be structured transmembrane helices and includes the intermediary cytoplasmic domain. It is found in eukaryotes, and is approximately 130 amino acids in length.


Pssm-ID: 464471  Cd Length: 131  Bit Score: 261.85  E-value: 2.96e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795612028  147 RMACQVGADRGPHVVLWTLVCLPVVFILSFVVSFYYGTITWYNIFLVYNEERTFWHKISYCPCLILFYPVLIMAMASSLG 226
Cdd:pfam15052   1 KDICRCGLDRGPHIFLWSLICLPFVFVLSFVYSFYYGTLTWYNIFLVYNEERSFLHKITVCPLLILFYPFLIVLFTLGLG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 795612028  227 LYAAVVQLSWSWGAWWQAARDMEKGFCGWLCSKLGLEDCSPYSIVELLESD 277
Cdd:pfam15052  81 LYAAVVQLSWSFSEWWQEVRDFEKGFYGWLCNKLGLEDCSPYEVVELLDSD 131
PT_UbiA cd13956
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ...
 160-245 8.00e-03

UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


Pssm-ID: 260119 [Multi-domain]  Cd Length: 271  Bit Score: 37.33  E-value: 8.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795612028 160 VVLWTLVCLPVVFILSFVVSFYYGTITWYNIFL--VYNeertFWHKISYcPCLILFYPVLIMAMAssLGLYAAVVQLSWS 237
Cdd:cd13956   79 ALAFAAALLLVGLALALALGPLALLLLLAGLLLglAYS----LGLKRLK-LGGWGVLGYATGLAL--LPGLGAVAAGGLV 151


                 ....*...
gi 795612028 238 WGAWWQAA 245
Cdd:cd13956  152 PLALLLAL 159
 
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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