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Conserved domains on  [gi|2462583775|ref|XP_054181069|]
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EMI domain-containing protein 1 isoform X10 [Homo sapiens]

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 8.11e-19

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: 80.16  E-value: 8.11e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462583775  34 RNWCSYvvtRTISCHVQNGT--YLQRV----LQNCPWPMSCpgSSYRTVVRPTYKVMYKIVTAREWRCCPGHSG 101
Cdd:pfam07546   1 RNVCAY---KVVSCVVVTGTesYVQPVykpyLTWCAGHRRC--STYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 136-340 5.50e-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: 48.36  E-value: 5.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583775 136 QPVPPTPATPEDPAPLWGPPPAQGSPGDGGLQDQVGAWGLPGPTGPKGDAGSRGPMGMRGPPGPQGPPGSPGRAGAVGTP 215
Cdd:NF038329  121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583775 216 GERGPPGPPgppgppgppapvgppharisqhgdpllsntftetnnhwPQGPTGPPGPPGPMGPPGPPGPTGVPGSPGHIG 295
Cdd:NF038329  201 GPAGEQGPA--------------------------------------GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG 242

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462583775 296 PPGPTGPKGISGHPGEKGERGLRGEPGPQGSAGQRGEPGPKGDPG 340
Cdd:NF038329  243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
 
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 8.11e-19

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: 80.16  E-value: 8.11e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462583775  34 RNWCSYvvtRTISCHVQNGT--YLQRV----LQNCPWPMSCpgSSYRTVVRPTYKVMYKIVTAREWRCCPGHSG 101
Cdd:pfam07546   1 RNVCAY---KVVSCVVVTGTesYVQPVykpyLTWCAGHRRC--STYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 136-340 5.50e-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: 48.36  E-value: 5.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583775 136 QPVPPTPATPEDPAPLWGPPPAQGSPGDGGLQDQVGAWGLPGPTGPKGDAGSRGPMGMRGPPGPQGPPGSPGRAGAVGTP 215
Cdd:NF038329  121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583775 216 GERGPPGPPgppgppgppapvgppharisqhgdpllsntftetnnhwPQGPTGPPGPPGPMGPPGPPGPTGVPGSPGHIG 295
Cdd:NF038329  201 GPAGEQGPA--------------------------------------GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG 242

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462583775 296 PPGPTGPKGISGHPGEKGERGLRGEPGPQGSAGQRGEPGPKGDPG 340
Cdd:NF038329  243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 307-341 2.97e-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: 41.33  E-value: 2.97e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462583775 307 GHPGEKGERGLRGEPGPQGSAGQRGEPGPKGDPGE 341
Cdd:pfam01391  22 GPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 307-347 3.13e-05

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: 46.05  E-value: 3.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2462583775 307 GHPGEKGERGLRGEPGPQGSAGQRGEPGPKGDPGEKSHWGE 347
Cdd:NF038329  186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 277-347 2.31e-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: 43.36  E-value: 2.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462583775 277 GPPGPPGPTGVPGSPGHIGPPGPTGPKGISGHPGEKGERGLRGEPGPQGSAGQRGEPGPKGDPGEKSHWGE 347
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
 
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 8.11e-19

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: 80.16  E-value: 8.11e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462583775  34 RNWCSYvvtRTISCHVQNGT--YLQRV----LQNCPWPMSCpgSSYRTVVRPTYKVMYKIVTAREWRCCPGHSG 101
Cdd:pfam07546   1 RNVCAY---KVVSCVVVTGTesYVQPVykpyLTWCAGHRRC--STYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 136-340 5.50e-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: 48.36  E-value: 5.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583775 136 QPVPPTPATPEDPAPLWGPPPAQGSPGDGGLQDQVGAWGLPGPTGPKGDAGSRGPMGMRGPPGPQGPPGSPGRAGAVGTP 215
Cdd:NF038329  121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583775 216 GERGPPGPPgppgppgppapvgppharisqhgdpllsntftetnnhwPQGPTGPPGPPGPMGPPGPPGPTGVPGSPGHIG 295
Cdd:NF038329  201 GPAGEQGPA--------------------------------------GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG 242

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462583775 296 PPGPTGPKGISGHPGEKGERGLRGEPGPQGSAGQRGEPGPKGDPG 340
Cdd:NF038329  243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 307-341 2.97e-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: 41.33  E-value: 2.97e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462583775 307 GHPGEKGERGLRGEPGPQGSAGQRGEPGPKGDPGE 341
Cdd:pfam01391  22 GPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 307-347 3.13e-05

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: 46.05  E-value: 3.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2462583775 307 GHPGEKGERGLRGEPGPQGSAGQRGEPGPKGDPGEKSHWGE 347
Cdd:NF038329  186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 277-347 2.31e-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: 43.36  E-value: 2.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462583775 277 GPPGPPGPTGVPGSPGHIGPPGPTGPKGISGHPGEKGERGLRGEPGPQGSAGQRGEPGPKGDPGEKSHWGE 347
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 301-342 2.72e-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: 35.93  E-value: 2.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462583775 301 GPKGISGHPGEKGERGLRGEPGPQGSAGQRGEPGPKGDPGEK 342
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 316-347 5.86e-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: 34.78  E-value: 5.86e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462583775 316 GLRGEPGPQGSAGQRGEPGPKGDPGEKSHWGE 347
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGE 32
 
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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