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Conserved domains on  [gi|1690553922|ref|NP_001357934|]
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EMI domain-containing protein 1 isoform 7 precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
 34-101 1.12e-18

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


:

Pssm-ID: 462204  Cd Length: 69  Bit Score: 79.39  E-value: 1.12e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1690553922  34 RNWCSYvvtRTVSCHVQNGT--YLQRV----LQNCPWPMGCPgnSYRTVVRPLYKVTYKTVTAREWRCCPGHSG 101
Cdd:pfam07546   1 RNVCAY---KVVSCVVVTGTesYVQPVykpyLTWCAGHRRCS--TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 260-309 1.49e-09

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: 53.27  E-value: 1.49e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1690553922 260 GHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGE 309
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 236-365 1.85e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 49.52  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553922 236 GPPGPPGPMGPPGLPGPMGAPGSPGHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEKSHWGE 315
Cdd:NF038329  141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1690553922 316 GLHQLREALKILAERvlileTMIGLYEPDLGSG-AGPDGTGTPSLLRGKRG 365
Cdd:NF038329  221 AGEDGPAGPAGDGQQ-----GPDGDPGPTGEDGpQGPDGPAGKDGPRGDRG 266
 
Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
 34-101 1.12e-18

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


Pssm-ID: 462204  Cd Length: 69  Bit Score: 79.39  E-value: 1.12e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1690553922  34 RNWCSYvvtRTVSCHVQNGT--YLQRV----LQNCPWPMGCPgnSYRTVVRPLYKVTYKTVTAREWRCCPGHSG 101
Cdd:pfam07546   1 RNVCAY---KVVSCVVVTGTesYVQPVykpyLTWCAGHRRCS--TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 260-309 1.49e-09

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: 53.27  E-value: 1.49e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1690553922 260 GHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGE 309
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 236-365 1.85e-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: 49.52  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553922 236 GPPGPPGPMGPPGLPGPMGAPGSPGHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEKSHWGE 315
Cdd:NF038329  141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1690553922 316 GLHQLREALKILAERvlileTMIGLYEPDLGSG-AGPDGTGTPSLLRGKRG 365
Cdd:NF038329  221 AGEDGPAGPAGDGQQ-----GPDGDPGPTGEDGpQGPDGPAGKDGPRGDRG 266
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 235-316 5.78e-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: 38.73  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553922 235 PGPpgppgpmgppglpgpmgapgsPGHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEKSHWG 314
Cdd:NF038329  173 QGP---------------------AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG 231


                  ..
gi 1690553922 315 EG 316
Cdd:NF038329  232 DG 233
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 139-315 6.42e-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: 6.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553922 139 GLPGPTGPKGGTDSQSPvriRGPPGPQGPPGRPGQTGAAGTPGKMGPPGPPGPPGPPGPPAPVGPPYGQvslhGDPllsn 218
Cdd:NF038329  120 GEPGPAGPAGPAGEQGP---RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK----GPA---- 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553922 219 tfTEMGSHWPQGPTGPPGPPGPPGPMGPPGLPGPMGAPGSPGHMGIP--GPSGPKGTSGHPGEKGERGLPGEPGPQGLMG 296
Cdd:NF038329  189 --GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                         170
                  ....*....|....*....
gi 1690553922 297 VPGEPGPKGDPGEKSHWGE 315
Cdd:NF038329  267 EAGPDGPDGKDGERGPVGP 285
 
Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
 34-101 1.12e-18

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


Pssm-ID: 462204  Cd Length: 69  Bit Score: 79.39  E-value: 1.12e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1690553922  34 RNWCSYvvtRTVSCHVQNGT--YLQRV----LQNCPWPMGCPgnSYRTVVRPLYKVTYKTVTAREWRCCPGHSG 101
Cdd:pfam07546   1 RNVCAY---KVVSCVVVTGTesYVQPVykpyLTWCAGHRRCS--TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 260-309 1.49e-09

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: 53.27  E-value: 1.49e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1690553922 260 GHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGE 309
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 263-310 9.78e-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: 48.26  E-value: 9.78e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1690553922 263 GIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEK 310
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 236-365 1.85e-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: 49.52  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553922 236 GPPGPPGPMGPPGLPGPMGAPGSPGHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEKSHWGE 315
Cdd:NF038329  141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1690553922 316 GLHQLREALKILAERvlileTMIGLYEPDLGSG-AGPDGTGTPSLLRGKRG 365
Cdd:NF038329  221 AGEDGPAGPAGDGQQ-----GPDGDPGPTGEDGpQGPDGPAGKDGPRGDRG 266
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 235-316 5.78e-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: 38.73  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553922 235 PGPpgppgpmgppglpgpmgapgsPGHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEKSHWG 314
Cdd:NF038329  173 QGP---------------------AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG 231


                  ..
gi 1690553922 315 EG 316
Cdd:NF038329  232 DG 233
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 139-315 6.42e-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: 6.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553922 139 GLPGPTGPKGGTDSQSPvriRGPPGPQGPPGRPGQTGAAGTPGKMGPPGPPGPPGPPGPPAPVGPPYGQvslhGDPllsn 218
Cdd:NF038329  120 GEPGPAGPAGPAGEQGP---RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK----GPA---- 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690553922 219 tfTEMGSHWPQGPTGPPGPPGPPGPMGPPGLPGPMGAPGSPGHMGIP--GPSGPKGTSGHPGEKGERGLPGEPGPQGLMG 296
Cdd:NF038329  189 --GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                         170
                  ....*....|....*....
gi 1690553922 297 VPGEPGPKGDPGEKSHWGE 315
Cdd:NF038329  267 EAGPDGPDGKDGERGPVGP 285
 
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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