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Conserved domains on  [gi|160333304|ref|NP_033822|]
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apolipoprotein A-I preproprotein [Mus musculus]

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 ...
 71-240 3.12e-50

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: 162.82  E-value: 3.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333304   71 ENWDTLGSTVSQLQERLGPLTRDFWDNLEKETDWVRQEMNKDLEEVKQKVQPYLDEFQKKWKEDVELYRQKVAPLGAELQ 150
Cdd:pfam01442   4 DSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333304  151 ESARQKLQELQGRLSPVAEEFRDRMRTHVDSLRTQLAPHSEQMRESLAQRLAELKSN--PTLNEYHTRAKTHLKTLGEKA 228
Cdd:pfam01442  84 KRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESlaPYAEEVQAQLSQRLQELREKL 163

                         170
                  ....*....|..
gi 160333304  229 RPALEDLRHSLM 240
Cdd:pfam01442 164 EPQAEDLREKLD 175
 
Name Accession Description Interval E-value
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 71-240 3.12e-50

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: 162.82  E-value: 3.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333304   71 ENWDTLGSTVSQLQERLGPLTRDFWDNLEKETDWVRQEMNKDLEEVKQKVQPYLDEFQKKWKEDVELYRQKVAPLGAELQ 150
Cdd:pfam01442   4 DSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333304  151 ESARQKLQELQGRLSPVAEEFRDRMRTHVDSLRTQLAPHSEQMRESLAQRLAELKSN--PTLNEYHTRAKTHLKTLGEKA 228
Cdd:pfam01442  84 KRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESlaPYAEEVQAQLSQRLQELREKL 163

                         170
                  ....*....|..
gi 160333304  229 RPALEDLRHSLM 240
Cdd:pfam01442 164 EPQAEDLREKLD 175
 
Name Accession Description Interval E-value
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 71-240 3.12e-50

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: 162.82  E-value: 3.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333304   71 ENWDTLGSTVSQLQERLGPLTRDFWDNLEKETDWVRQEMNKDLEEVKQKVQPYLDEFQKKWKEDVELYRQKVAPLGAELQ 150
Cdd:pfam01442   4 DSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333304  151 ESARQKLQELQGRLSPVAEEFRDRMRTHVDSLRTQLAPHSEQMRESLAQRLAELKSN--PTLNEYHTRAKTHLKTLGEKA 228
Cdd:pfam01442  84 KRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESlaPYAEEVQAQLSQRLQELREKL 163

                         170
                  ....*....|..
gi 160333304  229 RPALEDLRHSLM 240
Cdd:pfam01442 164 EPQAEDLREKLD 175
SWI-SNF_Ssr4_C pfam20497
SWI/SNF and RSC complexes subunit Ssr4 C-terminal; This entry represents the C-temrinal domain ...
 144-212 6.74e-04

SWI/SNF and RSC complexes subunit Ssr4 C-terminal; This entry represents the C-temrinal domain of Ssr4 (SWI/SNF and RSC complexes subunit ssr4), an essential component of the chromatin-remodelling SWI/SNF and RSC (remodelling the structure of chromatin) complexes only found in S. pombe. This domain contains a conserved RYxxxHEWMEEI/V motif. RSC is involved in transcription regulation and nucleosome positioning which controls, particularly, membrane and organelle development genes. The ATP-dependent chromatin remodelling complex SWI/SNF is required for the positive and negative regulation of gene expression of a large number of genes through the regulation of nucleosome remodelling.


Pssm-ID: 466646  Cd Length: 458  Bit Score: 40.52  E-value: 6.74e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333304  144 PLGAELQESARQKLQElqGRLSP-VAEEFRDRMRTHVDSLRTQLaphsEQMRESLAQRLAELKSNPTLNE 212
Cdd:pfam20497  68 AQGGEAKKEVPKKPYV--GKLDPgKADEFRKRVAKKVADTNAEI----EKMKARHAKRLAKFKRGSLLKD 131
 
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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