NCBI Conserved Domain Search

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: 44.02 E-value: 1.68e-06

                          10        20        30
                  ....*....|....*....|....*....|...
gi 110625696   59 QGPAGVPGRDGSPGANGIPGTPGIPGRDGFKGE 91
Cdd:pfam01391  24 PGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56

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: 42.48 E-value: 6.12e-06

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 110625696   60 GPAGVPGRDGSPGANGIPGTPGIPGRDGFKGEKGE 94
Cdd:pfam01391  16 GPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50

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: 41.71 E-value: 1.30e-05

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 110625696   60 GPAGVPGRDGSPGANGIPGTPGIPGRDGFKGEKGE 94
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGP 41

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: 40.17 E-value: 4.88e-05

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 110625696   59 QGPAGVPGRDGSPGANGIPGTPGIPGRDGFKGEKGE 94
Cdd:pfam01391  18 PGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53

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: 39.40 E-value: 7.92e-05

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 110625696   58 LQGPAGVPGRDGSPGANGIPGTPGIPGRDGFKGEKG 93
Cdd:pfam01391   8 PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPG 43

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: 39.01 E-value: 1.12e-04

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 110625696   58 LQGPAGVPGRDGSPGANGIPGTPGIPGRDGFKGEKG 93
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPG 37

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: 38.63 E-value: 1.55e-04

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 110625696   60 GPAGVPGRDGSPGANGIPGTPGIPGRDGFKGEKGE 94
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGP 35

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: 37.09 E-value: 5.68e-04

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 110625696   59 QGPAGVPGRDGSPGANGIPGTPGIPGRDGFKGEKGEC 95
Cdd:pfam01391  21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57