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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768023352   34 RNWCSYvvtRTISCHVQNGT--YLQRV----LQNCPWPMSCpgSSYRTVVRPTYKVMYKIVTAREWRCCPGHSG 101
Cdd:pfam07546   1 RNVCAY---KVVSCVVVTGTesYVQPVykpyLTWCAGHRRC--STYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768023352 139 PPTPATPEDPAPLWGPPPAQGSPGDGGLQGLPGAIESVRVPLLPRNDQVGAWGLPGPTGPKGDAGSRGP 207
Cdd:NF038329 187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGP 255

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768023352   34 RNWCSYvvtRTISCHVQNGT--YLQRV----LQNCPWPMSCpgSSYRTVVRPTYKVMYKIVTAREWRCCPGHSG 101
Cdd:pfam07546   1 RNVCAY---KVVSCVVVTGTesYVQPVykpyLTWCAGHRRC--STYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69

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.

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 768023352  324 GHPGEKGERGLRGEPGPQGSAGQRGEPGPKGDPGE 358
Cdd:pfam01391  22 GPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768023352 294 GPPGPPGPTGVPGSPGHIGPPGPTGPKGISGHPGEKGERGLRGEPGPQGSAGQRGEPGPKGDPGEK 359
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768023352   34 RNWCSYvvtRTISCHVQNGT--YLQRV----LQNCPWPMSCpgSSYRTVVRPTYKVMYKIVTAREWRCCPGHSG 101
Cdd:pfam07546   1 RNVCAY---KVVSCVVVTGTesYVQPVykpyLTWCAGHRRC--STYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69

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.

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 768023352  324 GHPGEKGERGLRGEPGPQGSAGQRGEPGPKGDPGE 358
Cdd:pfam01391  22 GPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768023352 294 GPPGPPGPTGVPGSPGHIGPPGPTGPKGISGHPGEKGERGLRGEPGPQGSAGQRGEPGPKGDPGEK 359
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191