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Conserved domains on  [gi|397529602|ref|NP_001257613|]
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apolipoprotein E precursor [Rattus norvegicus]

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 ...
73-258 1.77e-38

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: 133.93  E-value: 1.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602   73 LMEDTMTEVKAYKKELEEQLGPVAEETRARLAKEVQAAQARLGADMEDLRNRLGQYRNEVNTMLGQSTEELRSRLSTHLR 152
Cdd:pfam01442   1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602  153 KMRKRLMRDADDLQKRLAVYKAGAQEGAERGVSAIRERLGPLVEQGRQRtanlgagaaqpLRDRAQALSDRIRGRLEEVG 232
Cdd:pfam01442  81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQK-----------LAERLEELKESLAPYAEEVQ 149
                         170       180
                  ....*....|....*....|....*.
gi 397529602  233 NQARDRLEEVREQMEEVRSKMEEQTQ 258
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 ...
73-258 1.77e-38

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: 133.93  E-value: 1.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602   73 LMEDTMTEVKAYKKELEEQLGPVAEETRARLAKEVQAAQARLGADMEDLRNRLGQYRNEVNTMLGQSTEELRSRLSTHLR 152
Cdd:pfam01442   1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602  153 KMRKRLMRDADDLQKRLAVYKAGAQEGAERGVSAIRERLGPLVEQGRQRtanlgagaaqpLRDRAQALSDRIRGRLEEVG 232
Cdd:pfam01442  81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQK-----------LAERLEELKESLAPYAEEVQ 149
                         170       180
                  ....*....|....*....|....*.
gi 397529602  233 NQARDRLEEVREQMEEVRSKMEEQTQ 258
Cdd:pfam01442 150 AQLSQRLQELREKLEPQAEDLREKLD 175
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
56-267 1.10e-04

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: 43.89  E-value: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602    56 QVQEELQSSQVTQELTVLMEDTMTEVKAYKKELEEQLGPVAEETRARLAK--EVQAAQARLGADMEDLRNRLGQYRNEVN 133
Cdd:TIGR02168  734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEieELEAQIEQLKEELKALREALDELRAELT 813
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602   134 TmLGQSTEELRSRLSTHLRKMRkRLMRDADDLQKRLAVYK------AGAQEGAERGVSAIRERLGPLVEQGRQRTANLGA 207
Cdd:TIGR02168  814 L-LNEEAANLRERLESLERRIA-ATERRLEDLEEQIEELSedieslAAEIEELEELIEELESELEALLNERASLEEALAL 891
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602   208 gaaqpLRDRAQALSDRIRgRLEEVGNQARDRLEEVREQMEEVRSKMEEQTQQIRLQAEIF 267
Cdd:TIGR02168  892 -----LRSELEELSEELR-ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
65-261 1.76e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602   65 QVTQELTVLmEDTMTEVKAYKKELEEQLGPVAEETRARLAKEVQAAQARLGADMEDLRNRLGQYRNEVNTMLGQSTEELR 144
Cdd:COG4913   266 AARERLAEL-EYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLE 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602  145 SRLStHLRKMRKRLMRDADDLQKRLAVYKAGAQEGAERGVSairerlgpLVEQGRQRTANLGAgaaqpLRDRAQALSDRI 224
Cdd:COG4913   345 REIE-RLERELEERERRRARLEALLAALGLPLPASAEEFAA--------LRAEAAALLEALEE-----ELEALEEALAEA 410
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 397529602  225 RGRLEEVgNQARDRLEEVREQMEEVRSKMEEQTQQIR 261
Cdd:COG4913   411 EAALRDL-RRELRELEAEIASLERRKSNIPARLLALR 446
PRK08475 PRK08475
F0F1 ATP synthase subunit B; Validated
209-291 4.31e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 236272 [Multi-domain]  Cd Length: 167  Bit Score: 37.30  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602 209 AAQPLRDRAQALSDRIRGRLEEVgnqaRDRLEEVREQMEEVRSKMEEQTQQIRL-------QAEIFQARIKGWFEPLVED 281
Cdd:PRK08475  43 AAKPLKNFYKSRINKISKRLEEI----QEKLKESKEKKEDALKKLEEAKEKAELivetakkEAYILTQKIEKQTKDDIEN 118
                         90
                 ....*....|
gi 397529602 282 MQRQWANLME 291
Cdd:PRK08475 119 LIKSFEELME 128
 
Name Accession Description Interval E-value
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
73-258 1.77e-38

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: 133.93  E-value: 1.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602   73 LMEDTMTEVKAYKKELEEQLGPVAEETRARLAKEVQAAQARLGADMEDLRNRLGQYRNEVNTMLGQSTEELRSRLSTHLR 152
Cdd:pfam01442   1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602  153 KMRKRLMRDADDLQKRLAVYKAGAQEGAERGVSAIRERLGPLVEQGRQRtanlgagaaqpLRDRAQALSDRIRGRLEEVG 232
Cdd:pfam01442  81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQK-----------LAERLEELKESLAPYAEEVQ 149
                         170       180
                  ....*....|....*....|....*.
gi 397529602  233 NQARDRLEEVREQMEEVRSKMEEQTQ 258
Cdd:pfam01442 150 AQLSQRLQELREKLEPQAEDLREKLD 175
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
51-202 3.19e-09

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: 55.35  E-value: 3.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602   51 QTLSDQVQEELQssQVTQELTVLMEDTMTEVKAYKKELEEQLGPVAEETRARLAKEVQAAQARLGADMEDLRNRLGQYRN 130
Cdd:pfam01442  25 QELVDRLEKETE--ALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRKRLNADAEELQEKLAPYGE 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 397529602  131 EVNTMLGQSTEELRSRLSTHLRKMRKRLMRDADDLQKRLAVYKAGAQEGAERGVSAIRERLGPLVEQGRQRT 202
Cdd:pfam01442 103 ELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELREKLEPQAEDLREKL 174
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
56-267 1.10e-04

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: 43.89  E-value: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602    56 QVQEELQSSQVTQELTVLMEDTMTEVKAYKKELEEQLGPVAEETRARLAK--EVQAAQARLGADMEDLRNRLGQYRNEVN 133
Cdd:TIGR02168  734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEieELEAQIEQLKEELKALREALDELRAELT 813
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602   134 TmLGQSTEELRSRLSTHLRKMRkRLMRDADDLQKRLAVYK------AGAQEGAERGVSAIRERLGPLVEQGRQRTANLGA 207
Cdd:TIGR02168  814 L-LNEEAANLRERLESLERRIA-ATERRLEDLEEQIEELSedieslAAEIEELEELIEELESELEALLNERASLEEALAL 891
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602   208 gaaqpLRDRAQALSDRIRgRLEEVGNQARDRLEEVREQMEEVRSKMEEQTQQIRLQAEIF 267
Cdd:TIGR02168  892 -----LRSELEELSEELR-ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
65-261 1.76e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602   65 QVTQELTVLmEDTMTEVKAYKKELEEQLGPVAEETRARLAKEVQAAQARLGADMEDLRNRLGQYRNEVNTMLGQSTEELR 144
Cdd:COG4913   266 AARERLAEL-EYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLE 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602  145 SRLStHLRKMRKRLMRDADDLQKRLAVYKAGAQEGAERGVSairerlgpLVEQGRQRTANLGAgaaqpLRDRAQALSDRI 224
Cdd:COG4913   345 REIE-RLERELEERERRRARLEALLAALGLPLPASAEEFAA--------LRAEAAALLEALEE-----ELEALEEALAEA 410
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 397529602  225 RGRLEEVgNQARDRLEEVREQMEEVRSKMEEQTQQIR 261
Cdd:COG4913   411 EAALRDL-RRELRELEAEIASLERRKSNIPARLLALR 446
PRK08475 PRK08475
F0F1 ATP synthase subunit B; Validated
209-291 4.31e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 236272 [Multi-domain]  Cd Length: 167  Bit Score: 37.30  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602 209 AAQPLRDRAQALSDRIRGRLEEVgnqaRDRLEEVREQMEEVRSKMEEQTQQIRL-------QAEIFQARIKGWFEPLVED 281
Cdd:PRK08475  43 AAKPLKNFYKSRINKISKRLEEI----QEKLKESKEKKEDALKKLEEAKEKAELivetakkEAYILTQKIEKQTKDDIEN 118
                         90
                 ....*....|
gi 397529602 282 MQRQWANLME 291
Cdd:PRK08475 119 LIKSFEELME 128
ElaB COG4575
Membrane-anchored ribosome-binding protein ElaB, inhibits growth in stationary phase, YqjD ...
176-252 5.61e-03

Membrane-anchored ribosome-binding protein ElaB, inhibits growth in stationary phase, YqjD/DUF883 family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 443632 [Multi-domain]  Cd Length: 108  Bit Score: 36.07  E-value: 5.61e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 397529602 176 AQEGAERGVSAIRERLGPLVEQgrqrTANLGAGAAQPLRDRAQALSDRIRGRLEEVGNQARDRLEEVREQMEE-VRSK 252
Cdd:COG4575   13 SKEDLEADLKALVDDLEELLKS----TADDAGEKAAELREKAEAALDEARERLSEAEDAAVERAREAADAADDyVHEN 86
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
81-268 5.70e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.46  E-value: 5.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602  81 VKAYKKELEEQLGPVAEETRARLAKEVQAAQARLgadmEDLRNRLGQYRNEVN--------TMLGQSTEELRSRLSThLR 152
Cdd:COG3206  158 AEAYLEQNLELRREEARKALEFLEEQLPELRKEL----EEAEAALEEFRQKNGlvdlseeaKLLLQQLSELESQLAE-AR 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397529602 153 KMRKRLMRDADDLQKRLAVYKAGAQE-GAERGVSAIRERLGPLVEQGRQRTANLGAG--AAQPLRDRAQALSDRIRGRLE 229
Cdd:COG3206  233 AELAEAEARLAALRAQLGSGPDALPElLQSPVIQQLRAQLAELEAELAELSARYTPNhpDVIALRAQIAALRAQLQQEAQ 312
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 397529602 230 EVGNQARDRLEEVREQMEEVRSKMEEQTQQIRLQAEIFQ 268
Cdd:COG3206  313 RILASLEAELEALQAREASLQAQLAQLEARLAELPELEA 351
 
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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