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Conserved domains on  [gi|381140059|ref|NP_001244202|]
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E3 SUMO-protein ligase ZNF451 isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LAP2alpha super family cl13075
Lamina-associated polypeptide 2 alpha; LAPs are components of the nuclear lamina which ...
 358-498 2.38e-05

Lamina-associated polypeptide 2 alpha; LAPs are components of the nuclear lamina which supports the nuclear envelope.LAP2alpha is a non-membrane-associated member of the LAP family which is unique. This family of proteins is the C terminal domain of LAP2alpha which consists of residues 459-693 and constitutes a dimeric structure with an antiparallel coiled coil. LAP2alpha is involved in cell-cycle regulation and chromatin organization and preferentially binds to lamin A/C.


The actual alignment was detected with superfamily member pfam11560:

Pssm-ID: 371604  Cd Length: 234  Bit Score: 45.84  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381140059  358 GNTTSPLDSTSKEMEVMGCRFYHAASIAARAASYMAYMTQ-YQRKLWEDMEDLVHDPEfDRGKARCIISDGMDAGLWQLC 436
Cdd:pfam11560  93 AIQAASTESCDKHLDLALCRAYEAAASALQIAAHTAFVAKaLQADISQAAQIINSDPS-DAHQALGILNKTYDAASYICD 171

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 381140059  437 TTRDIMDSVVRVMAMAIDYRRQAWLRLTSLTKKTQEKISHLPFDGTSLFGQDVKAVVAEDNN 498
Cdd:pfam11560 172 AAFDEVKMAACAMGNATVGRRYLWLKDCKINLASKNKLASAPFKGGTLFGGEVCKVIKKRGN 233
 
Name Accession Description Interval E-value
LAP2alpha pfam11560
Lamina-associated polypeptide 2 alpha; LAPs are components of the nuclear lamina which ...
 358-498 2.38e-05

Lamina-associated polypeptide 2 alpha; LAPs are components of the nuclear lamina which supports the nuclear envelope.LAP2alpha is a non-membrane-associated member of the LAP family which is unique. This family of proteins is the C terminal domain of LAP2alpha which consists of residues 459-693 and constitutes a dimeric structure with an antiparallel coiled coil. LAP2alpha is involved in cell-cycle regulation and chromatin organization and preferentially binds to lamin A/C.


Pssm-ID: 371604  Cd Length: 234  Bit Score: 45.84  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381140059  358 GNTTSPLDSTSKEMEVMGCRFYHAASIAARAASYMAYMTQ-YQRKLWEDMEDLVHDPEfDRGKARCIISDGMDAGLWQLC 436
Cdd:pfam11560  93 AIQAASTESCDKHLDLALCRAYEAAASALQIAAHTAFVAKaLQADISQAAQIINSDPS-DAHQALGILNKTYDAASYICD 171

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 381140059  437 TTRDIMDSVVRVMAMAIDYRRQAWLRLTSLTKKTQEKISHLPFDGTSLFGQDVKAVVAEDNN 498
Cdd:pfam11560 172 AAFDEVKMAACAMGNATVGRRYLWLKDCKINLASKNKLASAPFKGGTLFGGEVCKVIKKRGN 233
 
Name Accession Description Interval E-value
LAP2alpha pfam11560
Lamina-associated polypeptide 2 alpha; LAPs are components of the nuclear lamina which ...
 358-498 2.38e-05

Lamina-associated polypeptide 2 alpha; LAPs are components of the nuclear lamina which supports the nuclear envelope.LAP2alpha is a non-membrane-associated member of the LAP family which is unique. This family of proteins is the C terminal domain of LAP2alpha which consists of residues 459-693 and constitutes a dimeric structure with an antiparallel coiled coil. LAP2alpha is involved in cell-cycle regulation and chromatin organization and preferentially binds to lamin A/C.


Pssm-ID: 371604  Cd Length: 234  Bit Score: 45.84  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381140059  358 GNTTSPLDSTSKEMEVMGCRFYHAASIAARAASYMAYMTQ-YQRKLWEDMEDLVHDPEfDRGKARCIISDGMDAGLWQLC 436
Cdd:pfam11560  93 AIQAASTESCDKHLDLALCRAYEAAASALQIAAHTAFVAKaLQADISQAAQIINSDPS-DAHQALGILNKTYDAASYICD 171

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 381140059  437 TTRDIMDSVVRVMAMAIDYRRQAWLRLTSLTKKTQEKISHLPFDGTSLFGQDVKAVVAEDNN 498
Cdd:pfam11560 172 AAFDEVKMAACAMGNATVGRRYLWLKDCKINLASKNKLASAPFKGGTLFGGEVCKVIKKRGN 233
 
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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