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Conserved domains on  [gi|1958799976|ref|XP_038938632|]
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deleted in lung and esophageal cancer protein 1 homolog isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASH super family cl48275
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
 608-713 3.88e-03

Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function.


The actual alignment was detected with superfamily member pfam15780:

Pssm-ID: 464865 [Multi-domain]  Cd Length: 98  Bit Score: 38.41  E-value: 3.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958799976  608 LKDLTAQYFIRFEPENVQSIARKQLIIRNathvelafhwqimkpnlqplmPGETHSLDSIKCHPDRETAFSIIPEKGILQ 687
Cdd:pfam15780    5 LAPFSRQPFVCFGDVPVGTSAERLLTVVN---------------------PSEEPAEVKVSKVPAPTKGFSVSPLEFTVQ 63

                           90       100
                   ....*....|....*....|....*.
gi 1958799976  688 AHSDHEFILSFSPYELKCFHSVLQMV 713
Cdd:pfam15780   64 PGESQTLTVTWTPTEEGAVRETLQFT 89
 
Name Accession Description Interval E-value
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
 608-713 3.88e-03

Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function.


Pssm-ID: 464865 [Multi-domain]  Cd Length: 98  Bit Score: 38.41  E-value: 3.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958799976  608 LKDLTAQYFIRFEPENVQSIARKQLIIRNathvelafhwqimkpnlqplmPGETHSLDSIKCHPDRETAFSIIPEKGILQ 687
Cdd:pfam15780    5 LAPFSRQPFVCFGDVPVGTSAERLLTVVN---------------------PSEEPAEVKVSKVPAPTKGFSVSPLEFTVQ 63

                           90       100
                   ....*....|....*....|....*.
gi 1958799976  688 AHSDHEFILSFSPYELKCFHSVLQMV 713
Cdd:pfam15780   64 PGESQTLTVTWTPTEEGAVRETLQFT 89
 
Name Accession Description Interval E-value
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
 608-713 3.88e-03

Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function.


Pssm-ID: 464865 [Multi-domain]  Cd Length: 98  Bit Score: 38.41  E-value: 3.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958799976  608 LKDLTAQYFIRFEPENVQSIARKQLIIRNathvelafhwqimkpnlqplmPGETHSLDSIKCHPDRETAFSIIPEKGILQ 687
Cdd:pfam15780    5 LAPFSRQPFVCFGDVPVGTSAERLLTVVN---------------------PSEEPAEVKVSKVPAPTKGFSVSPLEFTVQ 63

                           90       100
                   ....*....|....*....|....*.
gi 1958799976  688 AHSDHEFILSFSPYELKCFHSVLQMV 713
Cdd:pfam15780   64 PGESQTLTVTWTPTEEGAVRETLQFT 89
 
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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