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Conserved domains on  [gi|22748979|ref|NP_689677|]
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transmembrane protein 199 [Homo sapiens]

Protein Classification

TMEM199/VMA12 family protein( domain architecture ID 10569530)

TMEM199/VMA12 family protein similar to fungal vacuolar ATPase assembly integral membrane protein VPH2 (also called protein VMA12) and mammalian transmembrane protein 199 (TMEM199), which are accessory components required for assembly of the proton-transporting vacuolar (V)-ATPase protein pump

Gene Ontology:  GO:0070072

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Vma12 pfam11712
Endoplasmic reticulum-based factor for assembly of V-ATPase; The yeast vacuolar ...
 78-201 2.54e-29

Endoplasmic reticulum-based factor for assembly of V-ATPase; The yeast vacuolar proton-translocating ATPase (V-ATPase) is the best characterized member of the V-ATPase family. A total of thirteen genes are required for encoding the subunits of the enzyme complex itself and an additional three for providing factors necessary for the assembly of the whole. Vma12 is one of these latter, all three of which are localized to the endoplasmic reticulum.


:

Pssm-ID: 463329  Cd Length: 139  Bit Score: 106.17  E-value: 2.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748979    78 ELLEGSEIYLPE-VVKPPRNPELVARLEKIKIQLANEEYKRITRN----VTCQDTRHGGTLSDLG--KQVRSLKALVITI 150
Cdd:pfam11712   1 SLLRGSKVYIPPpPPKPEPSPEYKALMARLRAEQEEREYQRMTNPtsrkRTPGDTIDQPPPADDSdnVTPAQVKRQLSLI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 22748979   151 FNFIVTVVAAFVCTYLGSQYIFT-EMASRVLAALIVASVVGLAELYVMVRAM 201
Cdd:pfam11712  81 LNILVSVVAVAFAVWYAARSWVGpSTPARVLLSLFGALLVAVAEVVVYAGYL 132
 
Name Accession Description Interval E-value
Vma12 pfam11712
Endoplasmic reticulum-based factor for assembly of V-ATPase; The yeast vacuolar ...
 78-201 2.54e-29

Endoplasmic reticulum-based factor for assembly of V-ATPase; The yeast vacuolar proton-translocating ATPase (V-ATPase) is the best characterized member of the V-ATPase family. A total of thirteen genes are required for encoding the subunits of the enzyme complex itself and an additional three for providing factors necessary for the assembly of the whole. Vma12 is one of these latter, all three of which are localized to the endoplasmic reticulum.


Pssm-ID: 463329  Cd Length: 139  Bit Score: 106.17  E-value: 2.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748979    78 ELLEGSEIYLPE-VVKPPRNPELVARLEKIKIQLANEEYKRITRN----VTCQDTRHGGTLSDLG--KQVRSLKALVITI 150
Cdd:pfam11712   1 SLLRGSKVYIPPpPPKPEPSPEYKALMARLRAEQEEREYQRMTNPtsrkRTPGDTIDQPPPADDSdnVTPAQVKRQLSLI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 22748979   151 FNFIVTVVAAFVCTYLGSQYIFT-EMASRVLAALIVASVVGLAELYVMVRAM 201
Cdd:pfam11712  81 LNILVSVVAVAFAVWYAARSWVGpSTPARVLLSLFGALLVAVAEVVVYAGYL 132
 
Name Accession Description Interval E-value
Vma12 pfam11712
Endoplasmic reticulum-based factor for assembly of V-ATPase; The yeast vacuolar ...
 78-201 2.54e-29

Endoplasmic reticulum-based factor for assembly of V-ATPase; The yeast vacuolar proton-translocating ATPase (V-ATPase) is the best characterized member of the V-ATPase family. A total of thirteen genes are required for encoding the subunits of the enzyme complex itself and an additional three for providing factors necessary for the assembly of the whole. Vma12 is one of these latter, all three of which are localized to the endoplasmic reticulum.


Pssm-ID: 463329  Cd Length: 139  Bit Score: 106.17  E-value: 2.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22748979    78 ELLEGSEIYLPE-VVKPPRNPELVARLEKIKIQLANEEYKRITRN----VTCQDTRHGGTLSDLG--KQVRSLKALVITI 150
Cdd:pfam11712   1 SLLRGSKVYIPPpPPKPEPSPEYKALMARLRAEQEEREYQRMTNPtsrkRTPGDTIDQPPPADDSdnVTPAQVKRQLSLI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 22748979   151 FNFIVTVVAAFVCTYLGSQYIFT-EMASRVLAALIVASVVGLAELYVMVRAM 201
Cdd:pfam11712  81 LNILVSVVAVAFAVWYAARSWVGpSTPARVLLSLFGALLVAVAEVVVYAGYL 132
 
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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