NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|966751413|ref|NP_001304947|]
View 

apolipoprotein A-I isoform 1 preproprotein [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
69-242 1.12e-56

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: 179.38  E-value: 1.12e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966751413   69 KLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRA 148
Cdd:pfam01442   1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966751413  149 ELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLS 228
Cdd:pfam01442  81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160
                         170
                  ....*....|....
gi 966751413  229 EKAKPALEDLRQGL 242
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 ...
69-242 1.12e-56

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: 179.38  E-value: 1.12e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966751413   69 KLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRA 148
Cdd:pfam01442   1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966751413  149 ELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLS 228
Cdd:pfam01442  81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160
                         170
                  ....*....|....
gi 966751413  229 EKAKPALEDLRQGL 242
Cdd:pfam01442 161 EKLEPQAEDLREKL 174
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
85-207 1.12e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966751413  85 REQLGPVTQEFwDNLEKETEGLRQEMSKDLEEVKAKVQPYlDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEK 164
Cdd:PRK00409 508 KKLIGEDKEKL-NELIASLEELERELEQKAEEAEALLKEA-EKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKE 585
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 966751413 165 LSPLGEEMRDRARAHVDALRTHLApysDELRQRLAARLEALKE 207
Cdd:PRK00409 586 ADEIIKELRQLQKGGYASVKAHEL---IEARKRLNKANEKKEK 625
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
97-240 6.43e-04

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: 40.82  E-value: 6.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966751413    97 DNLEKETEGLRqemsKDLEEVKAKVQPYLDDFQKKwQEEMELYRQKVEPLRAELQEgARQKLHELQEKLSPLGEEMrdra 176
Cdd:TIGR02169  332 DKLLAEIEELE----REIEEERKRRDKLTEEYAEL-KEELEDLRAELEEVDKEFAE-TRDELKDYREKLEKLKREI---- 401
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966751413   177 rahvDALRTHLAPYSDELRQRLAARLEAlkENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQ 240
Cdd:TIGR02169  402 ----NELKRELDRLQEELQRLSEELADL--NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
99-182 2.43e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.91  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966751413  99 LEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYrQKVEPLRAELqEGARQKLHELQEKLSPLGEEMRDRA-- 176
Cdd:COG0542  430 LKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELI-EEIQELKEEL-EQRYGKIPELEKELAELEEELAELApl 507

                 ....*..
gi 966751413 177 -RAHVDA 182
Cdd:COG0542  508 lREEVTE 514
 
Name Accession Description Interval E-value
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
69-242 1.12e-56

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: 179.38  E-value: 1.12e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966751413   69 KLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRA 148
Cdd:pfam01442   1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966751413  149 ELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLS 228
Cdd:pfam01442  81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160
                         170
                  ....*....|....
gi 966751413  229 EKAKPALEDLRQGL 242
Cdd:pfam01442 161 EKLEPQAEDLREKL 174
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
85-207 1.12e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966751413  85 REQLGPVTQEFwDNLEKETEGLRQEMSKDLEEVKAKVQPYlDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEK 164
Cdd:PRK00409 508 KKLIGEDKEKL-NELIASLEELERELEQKAEEAEALLKEA-EKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKE 585
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 966751413 165 LSPLGEEMRDRARAHVDALRTHLApysDELRQRLAARLEALKE 207
Cdd:PRK00409 586 ADEIIKELRQLQKGGYASVKAHEL---IEARKRLNKANEKKEK 625
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
97-240 6.43e-04

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: 40.82  E-value: 6.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966751413    97 DNLEKETEGLRqemsKDLEEVKAKVQPYLDDFQKKwQEEMELYRQKVEPLRAELQEgARQKLHELQEKLSPLGEEMrdra 176
Cdd:TIGR02169  332 DKLLAEIEELE----REIEEERKRRDKLTEEYAEL-KEELEDLRAELEEVDKEFAE-TRDELKDYREKLEKLKREI---- 401
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966751413   177 rahvDALRTHLAPYSDELRQRLAARLEAlkENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQ 240
Cdd:TIGR02169  402 ----NELKRELDRLQEELQRLSEELADL--NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
99-182 2.43e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.91  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966751413  99 LEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYrQKVEPLRAELqEGARQKLHELQEKLSPLGEEMRDRA-- 176
Cdd:COG0542  430 LKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELI-EEIQELKEEL-EQRYGKIPELEKELAELEEELAELApl 507

                 ....*..
gi 966751413 177 -RAHVDA 182
Cdd:COG0542  508 lREEVTE 514
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
93-215 2.88e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966751413   93 QEFWDNLEketeGLRQEMSKDLEEVKA--KVQPYLDDFQKKWQEEMELYRQKvEPLRAElqeGARQKLHELQEKLSPLGE 170
Cdd:COG4913   231 VEHFDDLE----RAHEALEDAREQIELlePIRELAERYAAARERLAELEYLR-AALRLW---FAQRRLELLEAELEELRA 302
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 966751413  171 EmRDRARAHVDALRTHLapysDELRQRLAARLEALKENGGARLAE 215
Cdd:COG4913   303 E-LARLEAELERLEARL----DALREELDELEAQIRGNGGDRLEQ 342
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
133-240 6.38e-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: 38.01  E-value: 6.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966751413  133 QEEMELYRQKVEPL--RAELQEGARQKLHELQEKLsplgEEMRDRARAHVDALRTHLAPYS---DELRQRLAARLEALKE 207
Cdd:COG3096   346 QEKIERYQEDLEELteRLEEQEEVVEEAAEQLAEA----EARLEAAEEEVDSLKSQLADYQqalDVQQTRAIQYQQAVQA 421
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 966751413  208 NGGAR----LAEYHAK-ATEHLSTLSEKAKPALEDLRQ 240
Cdd:COG3096   422 LEKARalcgLPDLTPEnAEDYLAAFRAKEQQATEEVLE 459
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
73-240 9.44e-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: 37.34  E-value: 9.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966751413    73 NWDSVTSTFSKLREQLGpVTQEFWDNLEKETEglrqEMSKDLEEVKAKVQPYLDDFqKKWQEEMELYRQKVEPLRAELQE 152
Cdd:TIGR02168  289 ELYALANEISRLEQQKQ-ILRERLANLERQLE----ELEAQLEELESKLDELAEEL-AELEEKLEELKEELESLEAELEE 362
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966751413   153 gARQKLHELQEKLSPLGEEMRDRARA------HVDALRTHLAPYSDELrQRLAARLEALKENGGARLAEYHAKATEHLST 226
Cdd:TIGR02168  363 -LEAELEELESRLEELEEQLETLRSKvaqlelQIASLNNEIERLEARL-ERLEDRRERLQQEIEELLKKLEEAELKELQA 440
                          170
                   ....*....|....
gi 966751413   227 LSEKAKPALEDLRQ 240
Cdd:TIGR02168  441 ELEELEEELEELQE 454
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH