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Conserved domains on  [gi|1027923590|sp|P0DO95|]
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RecName: Full=Apolipoprotein E; Short=Apo-E; Flags: Precursor

Protein Classification

apolipoprotein A1/A4/E family protein( domain architecture ID 12019813)

apolipoprotein A1/A4/E family protein associates with lipid particles and may function in lipoprotein-mediated lipid transport

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
81-266 7.91e-36

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


:

Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 127.38  E-value: 7.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027923590  81 LMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRGEVQAMLGQSTEELRARLASHLR 160
Cdd:pfam01442   1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027923590 161 KLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRvraatvgslagQPLQERAQAWGERLRARMEEVG 240
Cdd:pfam01442  81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELR-----------QKLAERLEELKESLAPYAEEVQ 149
                         170       180
                  ....*....|....*....|....*.
gi 1027923590 241 SRTRDRLDEVKEQVAEVRAKLEEQAQ 266
Cdd:pfam01442 150 AQLSQRLQELREKLEPQAEDLREKLD 175
 
Name Accession Description Interval E-value
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
81-266 7.91e-36

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 127.38  E-value: 7.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027923590  81 LMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRGEVQAMLGQSTEELRARLASHLR 160
Cdd:pfam01442   1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027923590 161 KLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRvraatvgslagQPLQERAQAWGERLRARMEEVG 240
Cdd:pfam01442  81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELR-----------QKLAERLEELKESLAPYAEEVQ 149
                         170       180
                  ....*....|....*....|....*.
gi 1027923590 241 SRTRDRLDEVKEQVAEVRAKLEEQAQ 266
Cdd:pfam01442 150 AQLSQRLQELREKLEPQAEDLREKLD 175
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
61-288 9.27e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 37.73  E-value: 9.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027923590   61 LSEQVQEELLSSQVTQELTTLMDETMKELKAYKSELEEQLSPVAEETRARLSK--ELQAAQARLGADMEDVRSRLVQYRG 138
Cdd:TIGR02168  731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEieELEAQIEQLKEELKALREALDELRA 810
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027923590  139 EVQAmLGQSTEELRARLASHLRKLRKRLLRdADDLQKRLAVYQ------AGAREGAERGVSAIRERLGPLVEQGRVRAAt 212
Cdd:TIGR02168  811 ELTL-LNEEAANLRERLESLERRIAATERR-LEDLEEQIEELSedieslAAEIEELEELIEELESELEALLNERASLEE- 887
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1027923590  213 vgslAGQPLQERAQAWGERLRArMEEVGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVE 288
Cdd:TIGR02168  888 ----ALALLRSELEELSEELRE-LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
 
Name Accession Description Interval E-value
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
81-266 7.91e-36

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 127.38  E-value: 7.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027923590  81 LMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRGEVQAMLGQSTEELRARLASHLR 160
Cdd:pfam01442   1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027923590 161 KLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRvraatvgslagQPLQERAQAWGERLRARMEEVG 240
Cdd:pfam01442  81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELR-----------QKLAERLEELKESLAPYAEEVQ 149
                         170       180
                  ....*....|....*....|....*.
gi 1027923590 241 SRTRDRLDEVKEQVAEVRAKLEEQAQ 266
Cdd:pfam01442 150 AQLSQRLQELREKLEPQAEDLREKLD 175
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
58-177 9.74e-08

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 51.11  E-value: 9.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027923590  58 VQTLSEQVQEELlsSQVTQELTTLMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYR 137
Cdd:pfam01442  57 LEELQAKLGQNV--EELRQRLEPYTEELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERL 134
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1027923590 138 GEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRL 177
Cdd:pfam01442 135 EELKESLAPYAEEVQAQLSQRLQELREKLEPQAEDLREKL 174
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
61-288 9.27e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 37.73  E-value: 9.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027923590   61 LSEQVQEELLSSQVTQELTTLMDETMKELKAYKSELEEQLSPVAEETRARLSK--ELQAAQARLGADMEDVRSRLVQYRG 138
Cdd:TIGR02168  731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEieELEAQIEQLKEELKALREALDELRA 810
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027923590  139 EVQAmLGQSTEELRARLASHLRKLRKRLLRdADDLQKRLAVYQ------AGAREGAERGVSAIRERLGPLVEQGRVRAAt 212
Cdd:TIGR02168  811 ELTL-LNEEAANLRERLESLERRIAATERR-LEDLEEQIEELSedieslAAEIEELEELIEELESELEALLNERASLEE- 887
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1027923590  213 vgslAGQPLQERAQAWGERLRArMEEVGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVE 288
Cdd:TIGR02168  888 ----ALALLRSELEELSEELRE-LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
 
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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