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Conserved domains on  [gi|2462560692|ref|XP_054174712|]
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centrosomal protein of 192 kDa isoform X21 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Plk4BD_Cep192 cd21856
Plk4-binding domain found in centrosomal protein of 192 kDa (Cep192) and similar proteins; ...
 201-251 2.87e-17

Plk4-binding domain found in centrosomal protein of 192 kDa (Cep192) and similar proteins; Cep192, also called SPD-2, plays a critical role in mitotic centrosome maturation and bipolar spindle assembly. It appears to be a major regulator of pericentriolar material (PCM) recruitment and centriole duplication. It is a centrosome-specific activating scaffold for Aurora kinase A (AURKA) and polo-like kinase 1 (Plk1). Cep192 also plays a key role in centrosome recruitment of both Cep152 and Polo-like kinase 4 (Plk4). This model corresponds to a conserved region in Cep192 that is responsible for binding to the cryptic polo box (CPB) of Plk4.


:

Pssm-ID: 439317  Cd Length: 51  Bit Score: 77.50  E-value: 2.87e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462560692  201 EKLILPTSLEDSSDDDIDDEMFYDDHLEAYFEQLAIPGMIYEDLEGPEPPE 251
Cdd:cd21856      1 EKLLSLASLEDSTDDDIDDEEFYDDHLEAYFEQLAPPGMQRGDIEGQELPE 51
ASH super family cl48275
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
 1322-1385 4.51e-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: 4.51e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462560692 1322 KVASSRKQHLPLKNAGNIEVYLDI-KVPEQGSHFSVDPKNLLLKPGEEHEVIVSFTPKDPEACEE 1385
Cdd:pfam15780   20 PVGTSAERLLTVVNPSEEPAEVKVsKVPAPTKGFSVSPLEFTVQPGESQTLTVTWTPTEEGAVRE 84
 
Name Accession Description Interval E-value
Plk4BD_Cep192 cd21856
Plk4-binding domain found in centrosomal protein of 192 kDa (Cep192) and similar proteins; ...
 201-251 2.87e-17

Plk4-binding domain found in centrosomal protein of 192 kDa (Cep192) and similar proteins; Cep192, also called SPD-2, plays a critical role in mitotic centrosome maturation and bipolar spindle assembly. It appears to be a major regulator of pericentriolar material (PCM) recruitment and centriole duplication. It is a centrosome-specific activating scaffold for Aurora kinase A (AURKA) and polo-like kinase 1 (Plk1). Cep192 also plays a key role in centrosome recruitment of both Cep152 and Polo-like kinase 4 (Plk4). This model corresponds to a conserved region in Cep192 that is responsible for binding to the cryptic polo box (CPB) of Plk4.


Pssm-ID: 439317  Cd Length: 51  Bit Score: 77.50  E-value: 2.87e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462560692  201 EKLILPTSLEDSSDDDIDDEMFYDDHLEAYFEQLAIPGMIYEDLEGPEPPE 251
Cdd:cd21856      1 EKLLSLASLEDSTDDDIDDEEFYDDHLEAYFEQLAPPGMQRGDIEGQELPE 51
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
 1322-1385 4.51e-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: 4.51e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462560692 1322 KVASSRKQHLPLKNAGNIEVYLDI-KVPEQGSHFSVDPKNLLLKPGEEHEVIVSFTPKDPEACEE 1385
Cdd:pfam15780   20 PVGTSAERLLTVVNPSEEPAEVKVsKVPAPTKGFSVSPLEFTVQPGESQTLTVTWTPTEEGAVRE 84
 
Name Accession Description Interval E-value
Plk4BD_Cep192 cd21856
Plk4-binding domain found in centrosomal protein of 192 kDa (Cep192) and similar proteins; ...
 201-251 2.87e-17

Plk4-binding domain found in centrosomal protein of 192 kDa (Cep192) and similar proteins; Cep192, also called SPD-2, plays a critical role in mitotic centrosome maturation and bipolar spindle assembly. It appears to be a major regulator of pericentriolar material (PCM) recruitment and centriole duplication. It is a centrosome-specific activating scaffold for Aurora kinase A (AURKA) and polo-like kinase 1 (Plk1). Cep192 also plays a key role in centrosome recruitment of both Cep152 and Polo-like kinase 4 (Plk4). This model corresponds to a conserved region in Cep192 that is responsible for binding to the cryptic polo box (CPB) of Plk4.


Pssm-ID: 439317  Cd Length: 51  Bit Score: 77.50  E-value: 2.87e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462560692  201 EKLILPTSLEDSSDDDIDDEMFYDDHLEAYFEQLAIPGMIYEDLEGPEPPE 251
Cdd:cd21856      1 EKLLSLASLEDSTDDDIDDEEFYDDHLEAYFEQLAPPGMQRGDIEGQELPE 51
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
 1322-1385 4.51e-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: 4.51e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462560692 1322 KVASSRKQHLPLKNAGNIEVYLDI-KVPEQGSHFSVDPKNLLLKPGEEHEVIVSFTPKDPEACEE 1385
Cdd:pfam15780   20 PVGTSAERLLTVVNPSEEPAEVKVsKVPAPTKGFSVSPLEFTVQPGESQTLTVTWTPTEEGAVRE 84
TRAPPC9-Trs120 pfam08626
Transport protein Trs120 or TRAPPC9, TRAPP II complex subunit; This region is found at the N ...
 1338-1428 5.17e-03

Transport protein Trs120 or TRAPPC9, TRAPP II complex subunit; This region is found at the N terminal of Saccharomyces cerevisiae Trs120 protein. Trs120 is a subunit of the multiprotein complex TRAPP (transport particle protein) which functions in ER to Golgi traffic. Trs120 is specific to the larger TRAPP complex, TRAPP II, along with Trs65p and Trs130p(TRAPPC10). It is suggested that Trs120p is required for the stability of the Trs130p subunit, suggesting that these two proteins might interact in some way. It is likely that there is a complex function for TRAPP II in multiple pathways.


Pssm-ID: 430114  Cd Length: 1221  Bit Score: 42.24  E-value: 5.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560692 1338 NIEVYlDIKVPEQGSHFSVDPKNLLLKPGEEHEVIVSFTPKDPEA------------CEERILKIFVQPFGPQYEVVLKG 1405
Cdd:pfam08626  706 EVEIE-SLSLETEGVEFEALKESFVIGPYSTQTITLPGKPTESGTlkitgcnikvrgCRERRFPIFDKEWKPKKEKKIKR 784

                           90       100
                   ....*....|....*....|...
gi 2462560692 1406 EVISSgSKPLSPGPCldIPSILS 1428
Cdd:pfam08626  785 TGLAA-LEEASERPP--ETKSLS 804
 
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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