NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|755536216|ref|XP_011241965|]
View 

EMI domain-containing protein 1 isoform X2 [Mus musculus]

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
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
 34-101 5.62e-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: 77.46  E-value: 5.62e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755536216   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 ...
 321-370 8.95e-10

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: 54.04  E-value: 8.95e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 755536216  321 GHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGE 370
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 189-370 3.19e-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: 39.50  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536216 189 DGSLQDRLDSW--GLPGPTGPKGGTDSQSPvriRGPPGPQGPPGRPGQTGAAGTPGKMGPPGPPGPPGPPGPPAPVGPPY 266
Cdd:NF038329 107 DEGLQQLKGDGekGEPGPAGPAGPAGEQGP---RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536216 267 GQvslhGDPllsntfTEMGSHWPQGPTGPPGPPGPPGPMGPPGLPGPMGAPGSPGHMGIP--GPSGPKGTSGHPGEKGER 344
Cdd:NF038329 184 AK----GPA------GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPD 253

                        170       180
                 ....*....|....*....|....*.
gi 755536216 345 GLPGEPGPQGLMGVPGEPGPKGDPGE 370
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDGE 279
 
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 5.62e-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: 77.46  E-value: 5.62e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755536216   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 ...
 321-370 8.95e-10

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: 54.04  E-value: 8.95e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 755536216  321 GHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGE 370
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 320-383 1.02e-09

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: 59.92  E-value: 1.02e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755536216 320 PGHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEKSHWAPHSPRDPR 383
Cdd:NF038329 140 RGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 297-382 3.91e-07

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: 51.83  E-value: 3.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536216 297 GPPGPPGPMGPPGLPGPMGAPGSPGHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEKSHWAP 376
Cdd:NF038329 141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220


                 ....*.
gi 755536216 377 HSPRDP 382
Cdd:NF038329 221 AGEDGP 226
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 300-382 1.33e-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: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536216 300 GPPGPMGPPGLPGPMGAPGSPGHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEP-----GPKGDPGEKSHW 374
Cdd:NF038329 168 GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGED 247


                 ....*...
gi 755536216 375 APHSPRDP 382
Cdd:NF038329 248 GPQGPDGP 255
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 297-383 1.45e-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: 40.66  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536216 297 GPPGPPGPMGPPGLPGPMGAPGSPGHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPG------- 369
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPApktpevp 348

                         90
                 ....*....|....
gi 755536216 370 EKSHWAPHSPRDPR 383
Cdd:NF038329 349 QKPDTAPHTPKTPQ 362
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 189-370 3.19e-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: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536216 189 DGSLQDRLDSW--GLPGPTGPKGGTDSQSPvriRGPPGPQGPPGRPGQTGAAGTPGKMGPPGPPGPPGPPGPPAPVGPPY 266
Cdd:NF038329 107 DEGLQQLKGDGekGEPGPAGPAGPAGEQGP---RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536216 267 GQvslhGDPllsntfTEMGSHWPQGPTGPPGPPGPPGPMGPPGLPGPMGAPGSPGHMGIP--GPSGPKGTSGHPGEKGER 344
Cdd:NF038329 184 AK----GPA------GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPD 253

                        170       180
                 ....*....|....*....|....*.
gi 755536216 345 GLPGEPGPQGLMGVPGEPGPKGDPGE 370
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDGE 279
 
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 5.62e-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: 77.46  E-value: 5.62e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755536216   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 ...
 321-370 8.95e-10

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: 54.04  E-value: 8.95e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 755536216  321 GHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGE 370
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 320-383 1.02e-09

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: 59.92  E-value: 1.02e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755536216 320 PGHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEKSHWAPHSPRDPR 383
Cdd:NF038329 140 RGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 324-371 5.93e-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: 49.03  E-value: 5.93e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 755536216  324 GIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEK 371
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 297-382 3.91e-07

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: 51.83  E-value: 3.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536216 297 GPPGPPGPMGPPGLPGPMGAPGSPGHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEKSHWAP 376
Cdd:NF038329 141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220


                 ....*.
gi 755536216 377 HSPRDP 382
Cdd:NF038329 221 AGEDGP 226
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 300-382 1.33e-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: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536216 300 GPPGPMGPPGLPGPMGAPGSPGHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEP-----GPKGDPGEKSHW 374
Cdd:NF038329 168 GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGED 247


                 ....*...
gi 755536216 375 APHSPRDP 382
Cdd:NF038329 248 GPQGPDGP 255
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 297-383 1.45e-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: 40.66  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536216 297 GPPGPPGPMGPPGLPGPMGAPGSPGHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPG------- 369
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPApktpevp 348

                         90
                 ....*....|....
gi 755536216 370 EKSHWAPHSPRDPR 383
Cdd:NF038329 349 QKPDTAPHTPKTPQ 362
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 189-370 3.19e-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: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536216 189 DGSLQDRLDSW--GLPGPTGPKGGTDSQSPvriRGPPGPQGPPGRPGQTGAAGTPGKMGPPGPPGPPGPPGPPAPVGPPY 266
Cdd:NF038329 107 DEGLQQLKGDGekGEPGPAGPAGPAGEQGP---RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536216 267 GQvslhGDPllsntfTEMGSHWPQGPTGPPGPPGPPGPMGPPGLPGPMGAPGSPGHMGIP--GPSGPKGTSGHPGEKGER 344
Cdd:NF038329 184 AK----GPA------GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPD 253

                        170       180
                 ....*....|....*....|....*.
gi 755536216 345 GLPGEPGPQGLMGVPGEPGPKGDPGE 370
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDGE 279
 
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