NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1370477576|ref|XP_024308637|]
View 

formiminotransferase N-terminal subdomain-containing protein isoform X15 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
FTCD_N super family cl47991
Formiminotransferase domain, N-terminal subdomain; The formiminotransferase (FT) domain of ...
10-72 5.01e-16

Formiminotransferase domain, N-terminal subdomain; The formiminotransferase (FT) domain of formiminotransferase- cyclodeaminase (FTCD) forms a homodimer, and each protomer comprises two subdomains. The N-terminal subdomain is made up of a six-stranded mixed beta-pleated sheet and five alpha helices, which are arranged on the external surface of the beta sheet. This, in turn, faces the beta-sheet of the C-terminal subdomain to form a double beta-sheet layer. The two subdomains are separated by a short linker sequence, which is not thought to be any more flexible than the remainder of the molecule. The substrate is predicted to form a number of contacts with residues found in both the N-terminal and C-terminal subdomains.


The actual alignment was detected with superfamily member pfam07837:

Pssm-ID: 462283  Cd Length: 176  Bit Score: 67.88  E-value: 5.01e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370477576  10 LAACLLNVSEAGRKYIVENIAKAAlldkngKKHPQVSVLNIFSDQDYKRSVITIATSVDKLVD 72
Cdd:pfam07837   1 LVECVPNFSEGRDKEVIEAIARAA------RSVPGVKLLDVFSDADHNRTVVTLVGEPEAVVE 57
 
Name Accession Description Interval E-value
FTCD_N pfam07837
Formiminotransferase domain, N-terminal subdomain; The formiminotransferase (FT) domain of ...
10-72 5.01e-16

Formiminotransferase domain, N-terminal subdomain; The formiminotransferase (FT) domain of formiminotransferase- cyclodeaminase (FTCD) forms a homodimer, and each protomer comprises two subdomains. The N-terminal subdomain is made up of a six-stranded mixed beta-pleated sheet and five alpha helices, which are arranged on the external surface of the beta sheet. This, in turn, faces the beta-sheet of the C-terminal subdomain to form a double beta-sheet layer. The two subdomains are separated by a short linker sequence, which is not thought to be any more flexible than the remainder of the molecule. The substrate is predicted to form a number of contacts with residues found in both the N-terminal and C-terminal subdomains.


Pssm-ID: 462283  Cd Length: 176  Bit Score: 67.88  E-value: 5.01e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370477576  10 LAACLLNVSEAGRKYIVENIAKAAlldkngKKHPQVSVLNIFSDQDYKRSVITIATSVDKLVD 72
Cdd:pfam07837   1 LVECVPNFSEGRDKEVIEAIARAA------RSVPGVKLLDVFSDADHNRTVVTLVGEPEAVVE 57
 
Name Accession Description Interval E-value
FTCD_N pfam07837
Formiminotransferase domain, N-terminal subdomain; The formiminotransferase (FT) domain of ...
10-72 5.01e-16

Formiminotransferase domain, N-terminal subdomain; The formiminotransferase (FT) domain of formiminotransferase- cyclodeaminase (FTCD) forms a homodimer, and each protomer comprises two subdomains. The N-terminal subdomain is made up of a six-stranded mixed beta-pleated sheet and five alpha helices, which are arranged on the external surface of the beta sheet. This, in turn, faces the beta-sheet of the C-terminal subdomain to form a double beta-sheet layer. The two subdomains are separated by a short linker sequence, which is not thought to be any more flexible than the remainder of the molecule. The substrate is predicted to form a number of contacts with residues found in both the N-terminal and C-terminal subdomains.


Pssm-ID: 462283  Cd Length: 176  Bit Score: 67.88  E-value: 5.01e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370477576  10 LAACLLNVSEAGRKYIVENIAKAAlldkngKKHPQVSVLNIFSDQDYKRSVITIATSVDKLVD 72
Cdd:pfam07837   1 LVECVPNFSEGRDKEVIEAIARAA------RSVPGVKLLDVFSDADHNRTVVTLVGEPEAVVE 57
 
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