NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2776325169|ref|WP_367721203|]
View 

DUF4183 domain-containing protein, partial [Bacillus toyonensis]

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
DUF4183 super family cl16407
Domain of unknown function (DUF4183); This domain of unknown function contains a highly ...
 290-355 1.67e-12

Domain of unknown function (DUF4183); This domain of unknown function contains a highly conserved ING motif.


The actual alignment was detected with superfamily member pfam13799:

Pssm-ID: 404653 [Multi-domain]  Cd Length: 74  Bit Score: 62.02  E-value: 1.67e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2776325169 290 KLIYTNADGIAQYGTTNILSPSevSYINLFINGILQPQPFYEVSTGKLTLLDNQPPSQGSSIILQF 355
Cdd:pfam13799  11 ATSFTDDDGAPATGLPGILTPN--SYFNLYINGVLQPSTLYTVTPGALTLTGGDPILAGTPIILEF 74
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 222-274 3.17e-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: 40.94  E-value: 3.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2776325169 222 GVTGATGATGVTGPTGATGPTGVTGATGPTGATGATGVTGITGATGPTGGIGP 274
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
 
Name Accession Description Interval E-value
DUF4183 pfam13799
Domain of unknown function (DUF4183); This domain of unknown function contains a highly ...
 290-355 1.67e-12

Domain of unknown function (DUF4183); This domain of unknown function contains a highly conserved ING motif.


Pssm-ID: 404653 [Multi-domain]  Cd Length: 74  Bit Score: 62.02  E-value: 1.67e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2776325169 290 KLIYTNADGIAQYGTTNILSPSevSYINLFINGILQPQPFYEVSTGKLTLLDNQPPSQGSSIILQF 355
Cdd:pfam13799  11 ATSFTDDDGAPATGLPGILTPN--SYFNLYINGVLQPSTLYTVTPGALTLTGGDPILAGTPIILEF 74
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 222-274 3.17e-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: 40.94  E-value: 3.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2776325169 222 GVTGATGATGVTGPTGATGPTGVTGATGPTGATGATGVTGITGATGPTGGIGP 274
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 219-274 1.19e-04

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: 43.74  E-value: 1.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2776325169 219 GVTGVTGATGATGVTGPTGATGPTGVTGATGPTGATGATGVTGITGATGPTGGIGP 274
Cdd:NF038329  123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK 178
 
Name Accession Description Interval E-value
DUF4183 pfam13799
Domain of unknown function (DUF4183); This domain of unknown function contains a highly ...
 290-355 1.67e-12

Domain of unknown function (DUF4183); This domain of unknown function contains a highly conserved ING motif.


Pssm-ID: 404653 [Multi-domain]  Cd Length: 74  Bit Score: 62.02  E-value: 1.67e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2776325169 290 KLIYTNADGIAQYGTTNILSPSevSYINLFINGILQPQPFYEVSTGKLTLLDNQPPSQGSSIILQF 355
Cdd:pfam13799  11 ATSFTDDDGAPATGLPGILTPN--SYFNLYINGVLQPSTLYTVTPGALTLTGGDPILAGTPIILEF 74
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 222-274 3.17e-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: 40.94  E-value: 3.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2776325169 222 GVTGATGATGVTGPTGATGPTGVTGATGPTGATGATGVTGITGATGPTGGIGP 274
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 219-274 1.19e-04

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: 43.74  E-value: 1.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2776325169 219 GVTGVTGATGATGVTGPTGATGPTGVTGATGPTGATGATGVTGITGATGPTGGIGP 274
Cdd:NF038329  123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK 178
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 225-275 1.18e-03

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: 1.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2776325169 225 GATGATGVTGPTGATGPTGVTGATGPTGATGATGVTGITGATGPTGGIGPI 275
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
 
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