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Conserved domains on  [gi|827342893]
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Chain A, Apolipoprotein A-I

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 ...
4-177 1.42e-54

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: 171.29  E-value: 1.42e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827342893    4 KLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRA 83
Cdd:pfam01442   1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827342893   84 ELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLS 163
Cdd:pfam01442  81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160
                         170
                  ....*....|....
gi 827342893  164 EKAKPALEDLRQGL 177
Cdd:pfam01442 161 EKLEPQAEDLREKL 174
 
Name Accession Description Interval E-value
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
4-177 1.42e-54

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: 171.29  E-value: 1.42e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827342893    4 KLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRA 83
Cdd:pfam01442   1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827342893   84 ELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLS 163
Cdd:pfam01442  81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160
                         170
                  ....*....|....
gi 827342893  164 EKAKPALEDLRQGL 177
Cdd:pfam01442 161 EKLEPQAEDLREKL 174
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
20-142 1.50e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827342893  20 REQLGPVTQEFwDNLEKETEGLRQEMSKDLEEVKAKVQPYlDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEK 99
Cdd:PRK00409 508 KKLIGEDKEKL-NELIASLEELERELEQKAEEAEALLKEA-EKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKE 585
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 827342893 100 LSPLGEEMRDRARAHVDALRTHLApysDELRQRLAARLEALKE 142
Cdd:PRK00409 586 ADEIIKELRQLQKGGYASVKAHEL---IEARKRLNKANEKKEK 625
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
34-117 2.47e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.14  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827342893  34 LEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYrQKVEPLRAELqEGARQKLHELQEKLSPLGEEMRDRA-- 111
Cdd:COG0542  430 LKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELI-EEIQELKEEL-EQRYGKIPELEKELAELEEELAELApl 507

                 ....*..
gi 827342893 112 -RAHVDA 117
Cdd:COG0542  508 lREEVTE 514
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
32-175 4.69e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 37.35  E-value: 4.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827342893    32 DNLEKETEGLRqemsKDLEEVKAKVQPYLDDFQKKwQEEMELYRQKVEPLRAELQEgARQKLHELQEKLSPLGEEMrdra 111
Cdd:TIGR02169  332 DKLLAEIEELE----REIEEERKRRDKLTEEYAEL-KEELEDLRAELEEVDKEFAE-TRDELKDYREKLEKLKREI---- 401
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827342893   112 rahvDALRTHLAPYSDELRQRLAARLEAlkENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQ 175
Cdd:TIGR02169  402 ----NELKRELDRLQEELQRLSEELADL--NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
 
Name Accession Description Interval E-value
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
4-177 1.42e-54

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: 171.29  E-value: 1.42e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827342893    4 KLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRA 83
Cdd:pfam01442   1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827342893   84 ELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLS 163
Cdd:pfam01442  81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160
                         170
                  ....*....|....
gi 827342893  164 EKAKPALEDLRQGL 177
Cdd:pfam01442 161 EKLEPQAEDLREKL 174
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
20-142 1.50e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827342893  20 REQLGPVTQEFwDNLEKETEGLRQEMSKDLEEVKAKVQPYlDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEK 99
Cdd:PRK00409 508 KKLIGEDKEKL-NELIASLEELERELEQKAEEAEALLKEA-EKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKE 585
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 827342893 100 LSPLGEEMRDRARAHVDALRTHLApysDELRQRLAARLEALKE 142
Cdd:PRK00409 586 ADEIIKELRQLQKGGYASVKAHEL---IEARKRLNKANEKKEK 625
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
34-117 2.47e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.14  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827342893  34 LEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYrQKVEPLRAELqEGARQKLHELQEKLSPLGEEMRDRA-- 111
Cdd:COG0542  430 LKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELI-EEIQELKEEL-EQRYGKIPELEKELAELEEELAELApl 507

                 ....*..
gi 827342893 112 -RAHVDA 117
Cdd:COG0542  508 lREEVTE 514
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
32-175 4.69e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 37.35  E-value: 4.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827342893    32 DNLEKETEGLRqemsKDLEEVKAKVQPYLDDFQKKwQEEMELYRQKVEPLRAELQEgARQKLHELQEKLSPLGEEMrdra 111
Cdd:TIGR02169  332 DKLLAEIEELE----REIEEERKRRDKLTEEYAEL-KEELEDLRAELEEVDKEFAE-TRDELKDYREKLEKLKREI---- 401
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827342893   112 rahvDALRTHLAPYSDELRQRLAARLEAlkENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQ 175
Cdd:TIGR02169  402 ----NELKRELDRLQEELQRLSEELADL--NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
28-150 5.13e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 37.20  E-value: 5.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827342893   28 QEFWDNLEketeGLRQEMSKDLEEVKA--KVQPYLDDFQKKWQEEMELYRQKvEPLRAElqeGARQKLHELQEKLSPLGE 105
Cdd:COG4913   231 VEHFDDLE----RAHEALEDAREQIELlePIRELAERYAAARERLAELEYLR-AALRLW---FAQRRLELLEAELEELRA 302
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 827342893  106 EmRDRARAHVDALRTHLapysDELRQRLAARLEALKENGGARLAE 150
Cdd:COG4913   303 E-LARLEAELERLEARL----DALREELDELEAQIRGNGGDRLEQ 342
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
68-175 8.48e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 36.47  E-value: 8.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827342893   68 QEEMELYRQKVEPL--RAELQEGARQKLHELQEKLsplgEEMRDRARAHVDALRTHLAPYS---DELRQRLAARLEALKE 142
Cdd:COG3096   346 QEKIERYQEDLEELteRLEEQEEVVEEAAEQLAEA----EARLEAAEEEVDSLKSQLADYQqalDVQQTRAIQYQQAVQA 421
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 827342893  143 NGGAR----LAEYHAK-ATEHLSTLSEKAKPALEDLRQ 175
Cdd:COG3096   422 LEKARalcgLPDLTPEnAEDYLAAFRAKEQQATEEVLE 459
 
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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