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Conserved domains on  [gi|35902808|ref|NP_919351|]
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progressive ankylosis protein homolog B [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKH super family cl09432
Progressive ankylosis protein (ANKH); This family consists of several progressive ankylosis ...
 1-345 0e+00

Progressive ankylosis protein (ANKH); This family consists of several progressive ankylosis protein (ANK or ANKH) sequences. The ANK protein spans the outer cell membrane and shuttles inorganic pyrophosphate (PPi), a major inhibitor of physiologic and pathologic calcification, bone mineralization and bone resorption. Mutations in ANK are thought to give rise to Craniometaphyseal dysplasia (CMD) which is a rare skeletal disorder characterized by progressive thickening and increased mineral density of craniofacial bones and abnormally developed metaphyses in long bones. This family shows distant homology to the MOP (TCDB) superfamily of transporters.


The actual alignment was detected with superfamily member pfam07260:

Pssm-ID: 429370  Cd Length: 344  Bit Score: 689.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902808     1 MKEFPALTHYWPLIRFLVPLAITNIAIDLGEQALNRGIAAVKEDAVEMLASYGLAYSLMKFFTGPMSDFKNVGLVFVNSK 80
Cdd:pfam07260   1 MVDFPSLTAYWPLIRFLVPLAITNIAIDFGEQALNRGIAAVKEDAVEMLASYGLAYSLMKFFTGPMSDFKNVGLVFVNSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902808    81 RDRTKAVLCMVVAGTVAIVFHTLIAYTNLGYYIINKLHHVDESVGSKTRKAFLYLAAFPLLDAMAWTHAGILLKHKHSLL 160
Cdd:pfam07260  81 RDRSKAVLCMVVAGAIAAILHTLIAYTDLGYYIINKLHHVDDSVGSKTRKAFLYLAAFPLLDAMAWIHAGILLKHKYSFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902808   161 VGCASISDVVAQIVFVGILLHSHLECVEPMLIPILSLYMGALVRFTIVGLGYYKVIHDNIPESSGPEVGGDATIKKMLSF 240
Cdd:pfam07260 161 VGSASISDVVAQIVFVAILLHSNLECFEPLLIPILSLYMGALVRFTIVGLGYYCNIHDIIPDSSGPDMGGDATIKKMLSF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902808   241 WWPLALILATQRISRPIVNLFVSRDLKGSTAATEAVAVLTATYPVGHMPYGWLTELRAVYPAFDKNNPSNKLiNSGTVVT 320
Cdd:pfam07260 241 WWPLALILATQRISRPIVNLFVSRDLKGSSAATEAVAVLTATYPVGHMPYGWLTELRAVYPAFDKNNPSNKL-NSGSMVT 319

                         330       340
                  ....*....|....*....|....*
gi 35902808   321 KSHIKRFTFFCLALSITLCFMVFWA 345
Cdd:pfam07260 320 KSHIKKFTFCCFALSLTLCFVVFWS 344
MATE_like super family cl09326
Multidrug and toxic compound extrusion family and similar proteins; The integral membrane ...
 327-438 2.65e-03

Multidrug and toxic compound extrusion family and similar proteins; The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. MATE has also been identified as a large multigene family in plants, where the proteins are linked to disease resistance. A number of family members are involved in the synthesis of peptidoglycan components in bacteria.


The actual alignment was detected with superfamily member cd13123:

Pssm-ID: 447704 [Multi-domain]  Cd Length: 420  Bit Score: 40.13  E-value: 2.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902808 327 FTFFCLALSITLCFMVFWAPhisesILVDII--GVDHAFAELCITPLRIFSFFPIPVTIRAHLTGWLMTLKKTFVLAPSS 404
Cdd:cd13123  78 LTLLLLVLLLLTLLGILFAP-----LLVKLLapGFSGDKFELAVALTRIMFPYLLFISLSALLGGILNAHGRFFAPALAP 152

                        90       100       110
                ....*....|....*....|....*....|....*
gi 35902808 405 VLRIIVLISSLIVLPYMGVHGAT-LGVGSLLAGFL 438
Cdd:cd13123 153 VLLNLVIIAGLLLLAPLFDLGIYaLAWGVLLGGVL 187
 
Name Accession Description Interval E-value
ANKH pfam07260
Progressive ankylosis protein (ANKH); This family consists of several progressive ankylosis ...
 1-345 0e+00

Progressive ankylosis protein (ANKH); This family consists of several progressive ankylosis protein (ANK or ANKH) sequences. The ANK protein spans the outer cell membrane and shuttles inorganic pyrophosphate (PPi), a major inhibitor of physiologic and pathologic calcification, bone mineralization and bone resorption. Mutations in ANK are thought to give rise to Craniometaphyseal dysplasia (CMD) which is a rare skeletal disorder characterized by progressive thickening and increased mineral density of craniofacial bones and abnormally developed metaphyses in long bones. This family shows distant homology to the MOP (TCDB) superfamily of transporters.


Pssm-ID: 429370  Cd Length: 344  Bit Score: 689.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902808     1 MKEFPALTHYWPLIRFLVPLAITNIAIDLGEQALNRGIAAVKEDAVEMLASYGLAYSLMKFFTGPMSDFKNVGLVFVNSK 80
Cdd:pfam07260   1 MVDFPSLTAYWPLIRFLVPLAITNIAIDFGEQALNRGIAAVKEDAVEMLASYGLAYSLMKFFTGPMSDFKNVGLVFVNSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902808    81 RDRTKAVLCMVVAGTVAIVFHTLIAYTNLGYYIINKLHHVDESVGSKTRKAFLYLAAFPLLDAMAWTHAGILLKHKHSLL 160
Cdd:pfam07260  81 RDRSKAVLCMVVAGAIAAILHTLIAYTDLGYYIINKLHHVDDSVGSKTRKAFLYLAAFPLLDAMAWIHAGILLKHKYSFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902808   161 VGCASISDVVAQIVFVGILLHSHLECVEPMLIPILSLYMGALVRFTIVGLGYYKVIHDNIPESSGPEVGGDATIKKMLSF 240
Cdd:pfam07260 161 VGSASISDVVAQIVFVAILLHSNLECFEPLLIPILSLYMGALVRFTIVGLGYYCNIHDIIPDSSGPDMGGDATIKKMLSF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902808   241 WWPLALILATQRISRPIVNLFVSRDLKGSTAATEAVAVLTATYPVGHMPYGWLTELRAVYPAFDKNNPSNKLiNSGTVVT 320
Cdd:pfam07260 241 WWPLALILATQRISRPIVNLFVSRDLKGSSAATEAVAVLTATYPVGHMPYGWLTELRAVYPAFDKNNPSNKL-NSGSMVT 319

                         330       340
                  ....*....|....*....|....*
gi 35902808   321 KSHIKRFTFFCLALSITLCFMVFWA 345
Cdd:pfam07260 320 KSHIKKFTFCCFALSLTLCFVVFWS 344
MATE_MurJ_like cd13123
MurJ/MviN, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins; ...
 327-438 2.65e-03

MurJ/MviN, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins; Escherichia coli MurJ (MviN) has been identified as essential for murein biosynthesis. It has been suggested that MurJ functions as the peptidoglycan lipid II flippase which is involved in translocation of lipid-anchored peptidoglycan precursors across the cytoplasmic membrane, though results obtained in Bacillus subtilis seem to indicate that its MurJ homologs are not essential for growth. Some MviN family members (e.g. in Mycobacterium tuberculosis) possess an extended C-terminal region that contains an intracellular pseudo-kinase domain and an extracellular domain resembling carbohydrate-binding proteins. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are often responsible for multidrug resistance (MDR).


Pssm-ID: 240528 [Multi-domain]  Cd Length: 420  Bit Score: 40.13  E-value: 2.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902808 327 FTFFCLALSITLCFMVFWAPhisesILVDII--GVDHAFAELCITPLRIFSFFPIPVTIRAHLTGWLMTLKKTFVLAPSS 404
Cdd:cd13123  78 LTLLLLVLLLLTLLGILFAP-----LLVKLLapGFSGDKFELAVALTRIMFPYLLFISLSALLGGILNAHGRFFAPALAP 152

                        90       100       110
                ....*....|....*....|....*....|....*
gi 35902808 405 VLRIIVLISSLIVLPYMGVHGAT-LGVGSLLAGFL 438
Cdd:cd13123 153 VLLNLVIIAGLLLLAPLFDLGIYaLAWGVLLGGVL 187
 
Name Accession Description Interval E-value
ANKH pfam07260
Progressive ankylosis protein (ANKH); This family consists of several progressive ankylosis ...
 1-345 0e+00

Progressive ankylosis protein (ANKH); This family consists of several progressive ankylosis protein (ANK or ANKH) sequences. The ANK protein spans the outer cell membrane and shuttles inorganic pyrophosphate (PPi), a major inhibitor of physiologic and pathologic calcification, bone mineralization and bone resorption. Mutations in ANK are thought to give rise to Craniometaphyseal dysplasia (CMD) which is a rare skeletal disorder characterized by progressive thickening and increased mineral density of craniofacial bones and abnormally developed metaphyses in long bones. This family shows distant homology to the MOP (TCDB) superfamily of transporters.


Pssm-ID: 429370  Cd Length: 344  Bit Score: 689.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902808     1 MKEFPALTHYWPLIRFLVPLAITNIAIDLGEQALNRGIAAVKEDAVEMLASYGLAYSLMKFFTGPMSDFKNVGLVFVNSK 80
Cdd:pfam07260   1 MVDFPSLTAYWPLIRFLVPLAITNIAIDFGEQALNRGIAAVKEDAVEMLASYGLAYSLMKFFTGPMSDFKNVGLVFVNSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902808    81 RDRTKAVLCMVVAGTVAIVFHTLIAYTNLGYYIINKLHHVDESVGSKTRKAFLYLAAFPLLDAMAWTHAGILLKHKHSLL 160
Cdd:pfam07260  81 RDRSKAVLCMVVAGAIAAILHTLIAYTDLGYYIINKLHHVDDSVGSKTRKAFLYLAAFPLLDAMAWIHAGILLKHKYSFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902808   161 VGCASISDVVAQIVFVGILLHSHLECVEPMLIPILSLYMGALVRFTIVGLGYYKVIHDNIPESSGPEVGGDATIKKMLSF 240
Cdd:pfam07260 161 VGSASISDVVAQIVFVAILLHSNLECFEPLLIPILSLYMGALVRFTIVGLGYYCNIHDIIPDSSGPDMGGDATIKKMLSF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902808   241 WWPLALILATQRISRPIVNLFVSRDLKGSTAATEAVAVLTATYPVGHMPYGWLTELRAVYPAFDKNNPSNKLiNSGTVVT 320
Cdd:pfam07260 241 WWPLALILATQRISRPIVNLFVSRDLKGSSAATEAVAVLTATYPVGHMPYGWLTELRAVYPAFDKNNPSNKL-NSGSMVT 319

                         330       340
                  ....*....|....*....|....*
gi 35902808   321 KSHIKRFTFFCLALSITLCFMVFWA 345
Cdd:pfam07260 320 KSHIKKFTFCCFALSLTLCFVVFWS 344
MATE_MurJ_like cd13123
MurJ/MviN, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins; ...
 327-438 2.65e-03

MurJ/MviN, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins; Escherichia coli MurJ (MviN) has been identified as essential for murein biosynthesis. It has been suggested that MurJ functions as the peptidoglycan lipid II flippase which is involved in translocation of lipid-anchored peptidoglycan precursors across the cytoplasmic membrane, though results obtained in Bacillus subtilis seem to indicate that its MurJ homologs are not essential for growth. Some MviN family members (e.g. in Mycobacterium tuberculosis) possess an extended C-terminal region that contains an intracellular pseudo-kinase domain and an extracellular domain resembling carbohydrate-binding proteins. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are often responsible for multidrug resistance (MDR).


Pssm-ID: 240528 [Multi-domain]  Cd Length: 420  Bit Score: 40.13  E-value: 2.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35902808 327 FTFFCLALSITLCFMVFWAPhisesILVDII--GVDHAFAELCITPLRIFSFFPIPVTIRAHLTGWLMTLKKTFVLAPSS 404
Cdd:cd13123  78 LTLLLLVLLLLTLLGILFAP-----LLVKLLapGFSGDKFELAVALTRIMFPYLLFISLSALLGGILNAHGRFFAPALAP 152

                        90       100       110
                ....*....|....*....|....*....|....*
gi 35902808 405 VLRIIVLISSLIVLPYMGVHGAT-LGVGSLLAGFL 438
Cdd:cd13123 153 VLLNLVIIAGLLLLAPLFDLGIYaLAWGVLLGGVL 187
 
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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