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Conserved domains on  [gi|1984007493|sp|A0A2K5EJU6|]
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RecName: Full=Apolipoprotein A-I; Short=Apo-AI; Short=ApoA-I; AltName: Full=Apolipoprotein A1; Contains: RecName: Full=Proapolipoprotein A-I; Short=ProapoA-I; Contains: RecName: Full=Truncated apolipoprotein A-I; 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 ...
 67-240 4.72e-53

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: 170.14  E-value: 4.72e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984007493  67 KLLDNWDSLTSTVNKLREQLGPVTQEFWDNLEKETEELRQEMSKDLEEVKAQVQPYLDNFQKNWQEEMNLYSQKLEPLRT 146
Cdd:pfam01442   1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984007493 147 ELQEGALQKLQDLQEKLSPLAEQVRDRARAHVNTLRTQLAPYSDELRQRLATRLEALKENSGASLAEYHAKASEHLSALG 226
Cdd:pfam01442  81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160

                         170
                  ....*....|....
gi 1984007493 227 EKAKPALDDLRQGL 240
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 ...
 67-240 4.72e-53

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: 170.14  E-value: 4.72e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984007493  67 KLLDNWDSLTSTVNKLREQLGPVTQEFWDNLEKETEELRQEMSKDLEEVKAQVQPYLDNFQKNWQEEMNLYSQKLEPLRT 146
Cdd:pfam01442   1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984007493 147 ELQEGALQKLQDLQEKLSPLAEQVRDRARAHVNTLRTQLAPYSDELRQRLATRLEALKENSGASLAEYHAKASEHLSALG 226
Cdd:pfam01442  81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160

                         170
                  ....*....|....
gi 1984007493 227 EKAKPALDDLRQGL 240
Cdd:pfam01442 161 EKLEPQAEDLREKL 174
ApoLp-III_like cd13769
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ...
 73-191 3.89e-03

Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.


Pssm-ID: 259842 [Multi-domain]  Cd Length: 158  Bit Score: 36.92  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984007493  73 DSLTSTVNKLREQLGPVTQEFWDNLEKETEELRQEmskdlEEVKAQVQPYLDNFQKNWQEEMNlYSQKLEPLRTELQEGA 152
Cdd:cd13769    53 SSLKEEAKKKQGEVEEAWNEFKTKLSETVPELRKS-----LPVEEKAQELQAKLQSGLQTLVT-ESQKLAKAISENSQKA 126

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1984007493 153 lqklqdlQEKLSPLAEQVRDRARAHVNTLRTQLAPYSDE 191
Cdd:cd13769   127 -------QEELQKATKQAYDIAVEAAQNLQNQLQTATQK 158
 
Name Accession Description Interval E-value
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 67-240 4.72e-53

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: 170.14  E-value: 4.72e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984007493  67 KLLDNWDSLTSTVNKLREQLGPVTQEFWDNLEKETEELRQEMSKDLEEVKAQVQPYLDNFQKNWQEEMNLYSQKLEPLRT 146
Cdd:pfam01442   1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984007493 147 ELQEGALQKLQDLQEKLSPLAEQVRDRARAHVNTLRTQLAPYSDELRQRLATRLEALKENSGASLAEYHAKASEHLSALG 226
Cdd:pfam01442  81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160

                         170
                  ....*....|....
gi 1984007493 227 EKAKPALDDLRQGL 240
Cdd:pfam01442 161 EKLEPQAEDLREKL 174
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 154-264 4.21e-05

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: 43.02  E-value: 4.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984007493 154 QKLQDLQEKLSPLAEQVRDRarahvntlrtqLAPYSDELRQRLATRLEALKENSGASLAEYHAKASEHLSALGEKAKPAL 233
Cdd:pfam01442  11 TYAEELQEQLGPVAQELVDR-----------LEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYT 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1984007493 234 DDLRQGLLPVLESFKVSFLSALEEYTKKLSS 264
Cdd:pfam01442  80 EELRKRLNADAEELQEKLAPYGEELRERLEQ 110
ApoLp-III_like cd13769
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ...
 73-191 3.89e-03

Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.


Pssm-ID: 259842 [Multi-domain]  Cd Length: 158  Bit Score: 36.92  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984007493  73 DSLTSTVNKLREQLGPVTQEFWDNLEKETEELRQEmskdlEEVKAQVQPYLDNFQKNWQEEMNlYSQKLEPLRTELQEGA 152
Cdd:cd13769    53 SSLKEEAKKKQGEVEEAWNEFKTKLSETVPELRKS-----LPVEEKAQELQAKLQSGLQTLVT-ESQKLAKAISENSQKA 126

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1984007493 153 lqklqdlQEKLSPLAEQVRDRARAHVNTLRTQLAPYSDE 191
Cdd:cd13769   127 -------QEELQKATKQAYDIAVEAAQNLQNQLQTATQK 158
 
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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