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Conserved domains on  [gi|22035642|ref|NP_085147|]
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apolipoprotein L3 isoform 2 [Homo sapiens]

Protein Classification

ApoL domain-containing protein( domain architecture ID 10527210)

ApoL domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ApoL pfam05461
Apolipoprotein L; Apo L belongs to the high density lipoprotein family that plays a central ...
 29-320 2.68e-162

Apolipoprotein L; Apo L belongs to the high density lipoprotein family that plays a central role in cholesterol transport. The cholesterol content of membranes is important in cellular processes such as modulating gene transcription and signal transduction both in the adult brain and during neurodevelopment. There are six apo L genes located in close proximity to each other on chromosome 22q12 in humans. 22q12 is a confirmed high-susceptibility locus for schizophrenia and close to the region associated with velocardiofacial syndrome that includes symptoms of schizophrenia.


:

Pssm-ID: 461657  Cd Length: 298  Bit Score: 454.42  E-value: 2.68e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22035642    29 LTNNEAWKRFVTAAELPRDEADALYEALKKLRTYAAIEDEYVQQKDEQFREWFLKEFPQVKRKIQESIEKLRALANGIEE 108
Cdd:pfam05461   1 LTEDEAWERFVAEAELSRDEADALREALNELTTLMAIEDKDMLQKDQQERERFLKEFPQVKRELEENIRKLHALADEVDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22035642   109 VHRGCTISNVVSSSTGAASGIMSLAGLVLAPFTAGTSLALTAAGVGLGAASAVTGITTSIVEHSYTSSAEAEASRLTATS 188
Cdd:pfam05461  81 VHRGCTISNVVASSTGAVSGILTILGLALAPVTAGGSLVLSATGLGLGAAAAVTGVSTSIVEHSSNSSAEAEASRLVSTS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22035642   189 IDRLKVFKEVMRDITPNLLSLLNNYYEATQTIGSEIRAIRQARARARL------PVTTWRISAGSGGQAERTIAGTTRAV 262
Cdd:pfam05461 161 TDKLKVVAEVLGGITPKVLSLALDCIQVLKGIGKNIRAIRLAKANPRLvasakrFMTTGRISAQSGKQVQRAFGGTALAM 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 22035642   263 SRGARILSATTSGIFLALDVVNLVYESKHLHEGAKSASAEELRRQAQELEENLMELTQ 320
Cdd:pfam05461 241 SKGARIMGAATAGVFLLLDVVSLVKESKHLHEGAKSESAEELRQQAQELEEKLEELTQ 298
 
Name Accession Description Interval E-value
ApoL pfam05461
Apolipoprotein L; Apo L belongs to the high density lipoprotein family that plays a central ...
 29-320 2.68e-162

Apolipoprotein L; Apo L belongs to the high density lipoprotein family that plays a central role in cholesterol transport. The cholesterol content of membranes is important in cellular processes such as modulating gene transcription and signal transduction both in the adult brain and during neurodevelopment. There are six apo L genes located in close proximity to each other on chromosome 22q12 in humans. 22q12 is a confirmed high-susceptibility locus for schizophrenia and close to the region associated with velocardiofacial syndrome that includes symptoms of schizophrenia.


Pssm-ID: 461657  Cd Length: 298  Bit Score: 454.42  E-value: 2.68e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22035642    29 LTNNEAWKRFVTAAELPRDEADALYEALKKLRTYAAIEDEYVQQKDEQFREWFLKEFPQVKRKIQESIEKLRALANGIEE 108
Cdd:pfam05461   1 LTEDEAWERFVAEAELSRDEADALREALNELTTLMAIEDKDMLQKDQQERERFLKEFPQVKRELEENIRKLHALADEVDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22035642   109 VHRGCTISNVVSSSTGAASGIMSLAGLVLAPFTAGTSLALTAAGVGLGAASAVTGITTSIVEHSYTSSAEAEASRLTATS 188
Cdd:pfam05461  81 VHRGCTISNVVASSTGAVSGILTILGLALAPVTAGGSLVLSATGLGLGAAAAVTGVSTSIVEHSSNSSAEAEASRLVSTS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22035642   189 IDRLKVFKEVMRDITPNLLSLLNNYYEATQTIGSEIRAIRQARARARL------PVTTWRISAGSGGQAERTIAGTTRAV 262
Cdd:pfam05461 161 TDKLKVVAEVLGGITPKVLSLALDCIQVLKGIGKNIRAIRLAKANPRLvasakrFMTTGRISAQSGKQVQRAFGGTALAM 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 22035642   263 SRGARILSATTSGIFLALDVVNLVYESKHLHEGAKSASAEELRRQAQELEENLMELTQ 320
Cdd:pfam05461 241 SKGARIMGAATAGVFLLLDVVSLVKESKHLHEGAKSESAEELRQQAQELEEKLEELTQ 298
ClyA_AhlB-like cd22652
Aeromonas hydrophila hemolytic component B (AhlB), and similar proteins; This model includes ...
 112-169 3.74e-03

Aeromonas hydrophila hemolytic component B (AhlB), and similar proteins; This model includes Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). It consists of three proteins, AhlA, AhlB and AhlC, encoded by one operon containing the three genes. Functional and mutagenic studies support a model of pore assembly where the soluble tetrameric form of AhlC first disassociates into monomers, binds a single membrane leaflet, and then recruits AhlB to promote soluble to pore transition; AhlA then binds to form the active hydrophilic lined pore. The structure of AhlB shows an elongated, almost entirely alpha-helical protein, including a hydrophobic beta-hairpin known as a beta-tongue to shield membrane inserting hydrophobic residues. The head domain of AhlB undergoes a large conformational change involving the beta tongue becoming an extended alpha helix, and the tail domain helices sliding relative to one another as AhlB assembles into a hydrophobic pore.


Pssm-ID: 439150 [Multi-domain]  Cd Length: 332  Bit Score: 38.74  E-value: 3.74e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 22035642 112 GCTISNVVSSSTGAASGIMSLAGLVLAPFTAGTSLALTAAGVGLGAASAVTGITTSIV 169
Cdd:cd22652 170 GAIAGIVLSGLAIIGGVFMIAVGAVASFVTAGTSTPLVIGGVAVVAAGAGGEAASAIA 227
 
Name Accession Description Interval E-value
ApoL pfam05461
Apolipoprotein L; Apo L belongs to the high density lipoprotein family that plays a central ...
 29-320 2.68e-162

Apolipoprotein L; Apo L belongs to the high density lipoprotein family that plays a central role in cholesterol transport. The cholesterol content of membranes is important in cellular processes such as modulating gene transcription and signal transduction both in the adult brain and during neurodevelopment. There are six apo L genes located in close proximity to each other on chromosome 22q12 in humans. 22q12 is a confirmed high-susceptibility locus for schizophrenia and close to the region associated with velocardiofacial syndrome that includes symptoms of schizophrenia.


Pssm-ID: 461657  Cd Length: 298  Bit Score: 454.42  E-value: 2.68e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22035642    29 LTNNEAWKRFVTAAELPRDEADALYEALKKLRTYAAIEDEYVQQKDEQFREWFLKEFPQVKRKIQESIEKLRALANGIEE 108
Cdd:pfam05461   1 LTEDEAWERFVAEAELSRDEADALREALNELTTLMAIEDKDMLQKDQQERERFLKEFPQVKRELEENIRKLHALADEVDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22035642   109 VHRGCTISNVVSSSTGAASGIMSLAGLVLAPFTAGTSLALTAAGVGLGAASAVTGITTSIVEHSYTSSAEAEASRLTATS 188
Cdd:pfam05461  81 VHRGCTISNVVASSTGAVSGILTILGLALAPVTAGGSLVLSATGLGLGAAAAVTGVSTSIVEHSSNSSAEAEASRLVSTS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22035642   189 IDRLKVFKEVMRDITPNLLSLLNNYYEATQTIGSEIRAIRQARARARL------PVTTWRISAGSGGQAERTIAGTTRAV 262
Cdd:pfam05461 161 TDKLKVVAEVLGGITPKVLSLALDCIQVLKGIGKNIRAIRLAKANPRLvasakrFMTTGRISAQSGKQVQRAFGGTALAM 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 22035642   263 SRGARILSATTSGIFLALDVVNLVYESKHLHEGAKSASAEELRRQAQELEENLMELTQ 320
Cdd:pfam05461 241 SKGARIMGAATAGVFLLLDVVSLVKESKHLHEGAKSESAEELRQQAQELEEKLEELTQ 298
ClyA_AhlB-like cd22652
Aeromonas hydrophila hemolytic component B (AhlB), and similar proteins; This model includes ...
 112-169 3.74e-03

Aeromonas hydrophila hemolytic component B (AhlB), and similar proteins; This model includes Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). It consists of three proteins, AhlA, AhlB and AhlC, encoded by one operon containing the three genes. Functional and mutagenic studies support a model of pore assembly where the soluble tetrameric form of AhlC first disassociates into monomers, binds a single membrane leaflet, and then recruits AhlB to promote soluble to pore transition; AhlA then binds to form the active hydrophilic lined pore. The structure of AhlB shows an elongated, almost entirely alpha-helical protein, including a hydrophobic beta-hairpin known as a beta-tongue to shield membrane inserting hydrophobic residues. The head domain of AhlB undergoes a large conformational change involving the beta tongue becoming an extended alpha helix, and the tail domain helices sliding relative to one another as AhlB assembles into a hydrophobic pore.


Pssm-ID: 439150 [Multi-domain]  Cd Length: 332  Bit Score: 38.74  E-value: 3.74e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 22035642 112 GCTISNVVSSSTGAASGIMSLAGLVLAPFTAGTSLALTAAGVGLGAASAVTGITTSIV 169
Cdd:cd22652 170 GAIAGIVLSGLAIIGGVFMIAVGAVASFVTAGTSTPLVIGGVAVVAAGAGGEAASAIA 227
 
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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