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Conserved domains on  [gi|119631226|gb|EAX10821|]
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C1q and tumor necrosis factor related protein 3, isoform CRA_c [Homo sapiens]

Protein Classification

collagen-like protein( domain architecture ID 10476057)

collagen-like protein similar to collagen, a structural macromolecule of the extracellular matrix containing triple helix domains that form tight interactions and stabilize supramolecular aggregates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 214-253 3.60e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


:

Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 3.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 119631226  214 NGATGHEGAKGEKGDKGDLGPRGERGQHGPKGEKGYPGIP 253
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48
 
Name Accession Description Interval E-value
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 214-253 3.60e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 3.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 119631226  214 NGATGHEGAKGEKGDKGDLGPRGERGQHGPKGEKGYPGIP 253
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 217-251 1.52e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 39.50  E-value: 1.52e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 119631226 217 TGHEGAKGEKGDKGDLGPRGERGQHGPKGEKGYPG 251
Cdd:NF038329 256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290
 
Name Accession Description Interval E-value
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 214-253 3.60e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 3.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 119631226  214 NGATGHEGAKGEKGDKGDLGPRGERGQHGPKGEKGYPGIP 253
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 223-253 8.70e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.70  E-value: 8.70e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 119631226  223 KGEKGDKGDLGPRGERGQHGPKGEKGYPGIP 253
Cdd:pfam01391  24 PGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 217-251 1.52e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 39.50  E-value: 1.52e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 119631226 217 TGHEGAKGEKGDKGDLGPRGERGQHGPKGEKGYPG 251
Cdd:NF038329 256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290
 
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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