NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|160395564|sp|Q9P2B7|]
View 

RecName: Full=Cilia- and flagella-associated protein 97

Protein Classification

CFAP97 domain-containing protein( domain architecture ID 10620683)

CFAP97 domain-containing protein similar to vertebrate cilia- and flagella-associated protein 97 (CFAP97)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Hmw_CFAP97 pfam13879
Hemingway/CFA97; Drosophila Hemingway (Hmw) is required for motile cilia function and sperm ...
346-447 7.29e-19

Hemingway/CFA97; Drosophila Hemingway (Hmw) is required for motile cilia function and sperm flagella assembly. The human orthologue, known as cilia- and flagella-associated protein 97 (CFAP97) or KIAA1430, localizes to the primary cilium. Another member of this family is the uncharacterized protein CFAP97D1/2 (CFAP97 domain-containing protein 1/2).


:

Pssm-ID: 464014  Cd Length: 100  Bit Score: 81.63  E-value: 7.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160395564  346 LNHLLKAFLQLDKKGPQKHHFDQpsvapgKNYSFTREEVRQIDRENQRLLKELSRQAEKPGSKSTIPRSAD------HPP 419
Cdd:pfam13879   1 LNKLKNAKPTVDNKAPPHLSLKL------KKLQFEEERLAEIERENQILLEKISRIMRRKGKVDKNSLSTQsyssktRPK 74
                          90       100
                  ....*....|....*....|....*...
gi 160395564  420 KLYhsALNRQKEQQRIERENLALLKRLE 447
Cdd:pfam13879  75 SLN--AENRKRELLRIEEENQKLLKRLQ 100
 
Name Accession Description Interval E-value
Hmw_CFAP97 pfam13879
Hemingway/CFA97; Drosophila Hemingway (Hmw) is required for motile cilia function and sperm ...
346-447 7.29e-19

Hemingway/CFA97; Drosophila Hemingway (Hmw) is required for motile cilia function and sperm flagella assembly. The human orthologue, known as cilia- and flagella-associated protein 97 (CFAP97) or KIAA1430, localizes to the primary cilium. Another member of this family is the uncharacterized protein CFAP97D1/2 (CFAP97 domain-containing protein 1/2).


Pssm-ID: 464014  Cd Length: 100  Bit Score: 81.63  E-value: 7.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160395564  346 LNHLLKAFLQLDKKGPQKHHFDQpsvapgKNYSFTREEVRQIDRENQRLLKELSRQAEKPGSKSTIPRSAD------HPP 419
Cdd:pfam13879   1 LNKLKNAKPTVDNKAPPHLSLKL------KKLQFEEERLAEIERENQILLEKISRIMRRKGKVDKNSLSTQsyssktRPK 74
                          90       100
                  ....*....|....*....|....*...
gi 160395564  420 KLYhsALNRQKEQQRIERENLALLKRLE 447
Cdd:pfam13879  75 SLN--AENRKRELLRIEEENQKLLKRLQ 100
GINS_A_psf1 cd11710
Alpha-helical domain of GINS complex protein Psf1; Psf1 is a component of the GINS tetrameric ...
382-484 2.51e-03

Alpha-helical domain of GINS complex protein Psf1; Psf1 is a component of the GINS tetrameric protein complex. Psf1 is mainly expressed in highly proliferative tissues, such as blastocysts, adult bone marrow, and testis, in which the stem cell system is active. Loss of Psf1 causes embryonic lethality. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits are homologous and homologs are also found in the archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3.


Pssm-ID: 212548  Cd Length: 129  Bit Score: 38.00  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160395564 382 EEVRQIDRENQRLLKELSRQAEKPGSKSTIprsadhppKLYHSALNRQKeqqrieRENLALLkrleavkptvgMKRSEQL 461
Cdd:cd11710   32 EEIRDLYEENQALLEEAQEEEEDPGLIPGL--------LVRHLSILRNK------RCLLAYL-----------YERLDRI 86
                         90       100
                 ....*....|....*....|...
gi 160395564 462 MDYHRNmgylNSSPLSRRARSTL 484
Cdd:cd11710   87 RELRWE----NGSVLPEDIKENL 105
 
Name Accession Description Interval E-value
Hmw_CFAP97 pfam13879
Hemingway/CFA97; Drosophila Hemingway (Hmw) is required for motile cilia function and sperm ...
346-447 7.29e-19

Hemingway/CFA97; Drosophila Hemingway (Hmw) is required for motile cilia function and sperm flagella assembly. The human orthologue, known as cilia- and flagella-associated protein 97 (CFAP97) or KIAA1430, localizes to the primary cilium. Another member of this family is the uncharacterized protein CFAP97D1/2 (CFAP97 domain-containing protein 1/2).


Pssm-ID: 464014  Cd Length: 100  Bit Score: 81.63  E-value: 7.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160395564  346 LNHLLKAFLQLDKKGPQKHHFDQpsvapgKNYSFTREEVRQIDRENQRLLKELSRQAEKPGSKSTIPRSAD------HPP 419
Cdd:pfam13879   1 LNKLKNAKPTVDNKAPPHLSLKL------KKLQFEEERLAEIERENQILLEKISRIMRRKGKVDKNSLSTQsyssktRPK 74
                          90       100
                  ....*....|....*....|....*...
gi 160395564  420 KLYhsALNRQKEQQRIERENLALLKRLE 447
Cdd:pfam13879  75 SLN--AENRKRELLRIEEENQKLLKRLQ 100
GINS_A_psf1 cd11710
Alpha-helical domain of GINS complex protein Psf1; Psf1 is a component of the GINS tetrameric ...
382-484 2.51e-03

Alpha-helical domain of GINS complex protein Psf1; Psf1 is a component of the GINS tetrameric protein complex. Psf1 is mainly expressed in highly proliferative tissues, such as blastocysts, adult bone marrow, and testis, in which the stem cell system is active. Loss of Psf1 causes embryonic lethality. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits are homologous and homologs are also found in the archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3.


Pssm-ID: 212548  Cd Length: 129  Bit Score: 38.00  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160395564 382 EEVRQIDRENQRLLKELSRQAEKPGSKSTIprsadhppKLYHSALNRQKeqqrieRENLALLkrleavkptvgMKRSEQL 461
Cdd:cd11710   32 EEIRDLYEENQALLEEAQEEEEDPGLIPGL--------LVRHLSILRNK------RCLLAYL-----------YERLDRI 86
                         90       100
                 ....*....|....*....|...
gi 160395564 462 MDYHRNmgylNSSPLSRRARSTL 484
Cdd:cd11710   87 RELRWE----NGSVLPEDIKENL 105
 
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