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Conserved domains on  [gi|1720364129|ref|XP_030101412|]
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EMI domain-containing protein 1 isoform X4 [Mus musculus]

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 ...
 236-285 1.67e-08

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: 50.18  E-value: 1.67e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720364129 236 GHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGE 285
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 104-291 6.17e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 38.35  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364129 104 DGSLQDrLDSWGLPGPTGPKGGTDSQSPVRIRGPPGPQGPPGRPGQTGAAGTPGKMGPPGPPGPPGPPGPPAPVGPPYGQ 183
Cdd:NF038329  107 DEGLQQ-LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364129 184 vslhGDPllsntfTEMGSHWPQGPTGPPGPPGPPGPMGPPGLPGPMGAPGSPGHMGIP--GPSGPKGTSGHPGEKGERGL 261
Cdd:NF038329  186 ----GPA------GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGP 255

                         170       180       190
                  ....*....|....*....|....*....|
gi 1720364129 262 PGEPGPQGLMGVPGEPGPKGDPGEKSHWGE 291
Cdd:NF038329  256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285
 
Name Accession Description Interval E-value
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 236-285 1.67e-08

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: 50.18  E-value: 1.67e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720364129 236 GHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGE 285
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 212-290 6.68e-06

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: 47.59  E-value: 6.68e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364129 212 GPPGPPGPMGPPGLPGPMGAPGSPGHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEKSHWG 290
Cdd:NF038329  141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAG 219
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 104-291 6.17e-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: 38.35  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364129 104 DGSLQDrLDSWGLPGPTGPKGGTDSQSPVRIRGPPGPQGPPGRPGQTGAAGTPGKMGPPGPPGPPGPPGPPAPVGPPYGQ 183
Cdd:NF038329  107 DEGLQQ-LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364129 184 vslhGDPllsntfTEMGSHWPQGPTGPPGPPGPPGPMGPPGLPGPMGAPGSPGHMGIP--GPSGPKGTSGHPGEKGERGL 261
Cdd:NF038329  186 ----GPA------GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGP 255

                         170       180       190
                  ....*....|....*....|....*....|
gi 1720364129 262 PGEPGPQGLMGVPGEPGPKGDPGEKSHWGE 291
Cdd:NF038329  256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 80-291 7.82e-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: 37.96  E-value: 7.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364129  80 PSVPATPEDSALLWGSPAARGSPGDGSLQDRLDSWGLPGPTGPKGGTDSQSPVRIRGPPGPQGPPGRPGQTGAAGTPGKM 159
Cdd:NF038329  124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364129 160 GPPGPPGPPGPPGPPAPVGPPYGQvslhgdpllsntftemgshwpqgptgppgppgppgpmgPPGLPGPMGAPGSPGHMG 239
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPA--------------------------------------GPAGDGQQGPDGDPGPTG 245

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720364129 240 IPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEKSHWGE 291
Cdd:NF038329  246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
 
Name Accession Description Interval E-value
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 236-285 1.67e-08

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: 50.18  E-value: 1.67e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720364129 236 GHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGE 285
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 239-286 8.47e-07

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: 45.56  E-value: 8.47e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720364129 239 GIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEK 286
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 212-290 6.68e-06

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: 47.59  E-value: 6.68e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364129 212 GPPGPPGPMGPPGLPGPMGAPGSPGHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEKSHWG 290
Cdd:NF038329  141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAG 219
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 104-291 6.17e-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: 38.35  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364129 104 DGSLQDrLDSWGLPGPTGPKGGTDSQSPVRIRGPPGPQGPPGRPGQTGAAGTPGKMGPPGPPGPPGPPGPPAPVGPPYGQ 183
Cdd:NF038329  107 DEGLQQ-LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364129 184 vslhGDPllsntfTEMGSHWPQGPTGPPGPPGPPGPMGPPGLPGPMGAPGSPGHMGIP--GPSGPKGTSGHPGEKGERGL 261
Cdd:NF038329  186 ----GPA------GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGP 255

                         170       180       190
                  ....*....|....*....|....*....|
gi 1720364129 262 PGEPGPQGLMGVPGEPGPKGDPGEKSHWGE 291
Cdd:NF038329  256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 80-291 7.82e-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: 37.96  E-value: 7.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364129  80 PSVPATPEDSALLWGSPAARGSPGDGSLQDRLDSWGLPGPTGPKGGTDSQSPVRIRGPPGPQGPPGRPGQTGAAGTPGKM 159
Cdd:NF038329  124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364129 160 GPPGPPGPPGPPGPPAPVGPPYGQvslhgdpllsntftemgshwpqgptgppgppgppgpmgPPGLPGPMGAPGSPGHMG 239
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPA--------------------------------------GPAGDGQQGPDGDPGPTG 245

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720364129 240 IPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEKSHWGE 291
Cdd:NF038329  246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
 
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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