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Conserved domains on  [gi|22096340|sp|P18835|]
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RecName: Full=Cuticle collagen 19; Flags: Precursor

Protein Classification

cuticular collagen family protein( domain architecture ID 18387949)

cuticular collagen family protein is a structural macromolecule of the extracellular matrix containing triple helix domains that form tight interactions and stabilize supramolecular aggregates

Gene Ontology:  GO:0042302|GO:0005581
PubMed:  1916105|21421911

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 77-275 5.67e-17

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: 80.33  E-value: 5.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22096340   77 GARTARQAGFEQCNCGPKSEGCPAGPPGPPGEGGQKGNPGHDGDDGKPGAPGVIVAITHDIPGGcikcppgrpgPKGPSG 156
Cdd:NF038329 135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG----------ETGPAG 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22096340  157 LPGSAGPAGGNGRRGPPGPVGGPGEQGPQG--DAGRPGAAGRPGPAGPRGEPGTEYKPGQPGRPGPQGPRGETGPAGNPG 234
Cdd:NF038329 205 EQGPAGPAGPDGEAGPAGEDGPAGPAGDGQqgPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG 284

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 22096340  235 APGNDGEAGKNGNAGRPGPPGHPGKNGVPGQKGEDAAPGPD 275
Cdd:NF038329 285 PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD 325
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 4-55 7.95e-12

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


:

Pssm-ID: 198156  Cd Length: 53  Bit Score: 59.02  E-value: 7.95e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 22096340      4 LIVVGSCGV-LVCVLASLYTIGNLLNEIEELQVEFQDGMVEFRAITQDTWARM 55
Cdd:smart01088   1 LVAYVAVAVsTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 77-275 5.67e-17

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: 80.33  E-value: 5.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22096340   77 GARTARQAGFEQCNCGPKSEGCPAGPPGPPGEGGQKGNPGHDGDDGKPGAPGVIVAITHDIPGGcikcppgrpgPKGPSG 156
Cdd:NF038329 135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG----------ETGPAG 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22096340  157 LPGSAGPAGGNGRRGPPGPVGGPGEQGPQG--DAGRPGAAGRPGPAGPRGEPGTEYKPGQPGRPGPQGPRGETGPAGNPG 234
Cdd:NF038329 205 EQGPAGPAGPDGEAGPAGEDGPAGPAGDGQqgPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG 284

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 22096340  235 APGNDGEAGKNGNAGRPGPPGHPGKNGVPGQKGEDAAPGPD 275
Cdd:NF038329 285 PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD 325
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 159-275 6.66e-12

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: 65.31  E-value: 6.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22096340  159 GSAGPAGGNGRRGPPGPVGGPGEQGPQGDAGRPGAAGRPGPAGPRGEPGTEYKPGQPGRPGPQGPRGETGPAGNPGAPGN 238
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 22096340  239 DGEAGKNGNAGRPGPPGHPG-----KNGVPGQKGEDAAPGPD 275
Cdd:NF038329 212 AGPDGEAGPAGEDGPAGPAGdgqqgPDGDPGPTGEDGPQGPD 253
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 4-55 7.95e-12

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 198156  Cd Length: 53  Bit Score: 59.02  E-value: 7.95e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 22096340      4 LIVVGSCGV-LVCVLASLYTIGNLLNEIEELQVEFQDGMVEFRAITQDTWARM 55
Cdd:smart01088   1 LVAYVAVAVsTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 6-55 2.30e-11

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens, see pfam01391. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 460226  Cd Length: 50  Bit Score: 57.85  E-value: 2.30e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 22096340     6 VVGSCGVLVCVLASLYTIGNLLNEIEELQVEFQDGMVEFRAITQDTWARM 55
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 159-280 7.63e-11

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: 62.23  E-value: 7.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22096340  159 GSAGPAGGNGRRGPPGPVGGPGEQGPQGDAGRPGAAGRP---GPAGPRGEPGTEYKPGQPGRPGPQGPRGETGPAGNPGA 235
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERgekGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 22096340  236 PGNDGEAGKNGNAGRPGPPGHPGKNGVPG-----QKGEDAAPGPDAGYCP 280
Cdd:NF038329 200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGP 249
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 92-280 8.60e-11

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: 61.84  E-value: 8.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22096340   92 GPKSEGCPAGPPGPPGEGGQKGNPGHDGDDGKPGAPGVIVAITHDIPGGcikcppgrPGPKGPSGLPGSAGPAGGNGRRG 171
Cdd:NF038329 177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG--------PAGPAGDGQQGPDGDPGPTGEDG 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22096340  172 PPGPVGGPGEQGPQGDAGRPGAAGRPGPAGPRGEPGTEYKPGQPGRPGPQGPRGETGPAGNPGAPGNDGEAGKNGnagrp 251
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG----- 323

                        170       180
                 ....*....|....*....|....*....
gi 22096340  252 gppghpgKNGVPGQKGEDAAPGPDAGYCP 280
Cdd:NF038329 324 -------KDGLPGKDGKDGQPGKPAPKTP 345
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 189-248 3.07e-07

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: 46.33  E-value: 3.07e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22096340   189 GRPGAAGRPGPAGPRGEPGteyKPGQPGRPGPQGPRGETGPAGNPGAPGNDGEAGKNGNA 248
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPG---PPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 77-275 5.67e-17

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: 80.33  E-value: 5.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22096340   77 GARTARQAGFEQCNCGPKSEGCPAGPPGPPGEGGQKGNPGHDGDDGKPGAPGVIVAITHDIPGGcikcppgrpgPKGPSG 156
Cdd:NF038329 135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG----------ETGPAG 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22096340  157 LPGSAGPAGGNGRRGPPGPVGGPGEQGPQG--DAGRPGAAGRPGPAGPRGEPGTEYKPGQPGRPGPQGPRGETGPAGNPG 234
Cdd:NF038329 205 EQGPAGPAGPDGEAGPAGEDGPAGPAGDGQqgPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG 284

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 22096340  235 APGNDGEAGKNGNAGRPGPPGHPGKNGVPGQKGEDAAPGPD 275
Cdd:NF038329 285 PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD 325
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 159-275 6.66e-12

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: 65.31  E-value: 6.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22096340  159 GSAGPAGGNGRRGPPGPVGGPGEQGPQGDAGRPGAAGRPGPAGPRGEPGTEYKPGQPGRPGPQGPRGETGPAGNPGAPGN 238
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 22096340  239 DGEAGKNGNAGRPGPPGHPG-----KNGVPGQKGEDAAPGPD 275
Cdd:NF038329 212 AGPDGEAGPAGEDGPAGPAGdgqqgPDGDPGPTGEDGPQGPD 253
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 4-55 7.95e-12

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 198156  Cd Length: 53  Bit Score: 59.02  E-value: 7.95e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 22096340      4 LIVVGSCGV-LVCVLASLYTIGNLLNEIEELQVEFQDGMVEFRAITQDTWARM 55
Cdd:smart01088   1 LVAYVAVAVsTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 6-55 2.30e-11

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens, see pfam01391. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 460226  Cd Length: 50  Bit Score: 57.85  E-value: 2.30e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 22096340     6 VVGSCGVLVCVLASLYTIGNLLNEIEELQVEFQDGMVEFRAITQDTWARM 55
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 159-280 7.63e-11

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: 62.23  E-value: 7.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22096340  159 GSAGPAGGNGRRGPPGPVGGPGEQGPQGDAGRPGAAGRP---GPAGPRGEPGTEYKPGQPGRPGPQGPRGETGPAGNPGA 235
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERgekGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 22096340  236 PGNDGEAGKNGNAGRPGPPGHPGKNGVPG-----QKGEDAAPGPDAGYCP 280
Cdd:NF038329 200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGP 249
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 92-280 8.60e-11

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: 61.84  E-value: 8.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22096340   92 GPKSEGCPAGPPGPPGEGGQKGNPGHDGDDGKPGAPGVIVAITHDIPGGcikcppgrPGPKGPSGLPGSAGPAGGNGRRG 171
Cdd:NF038329 177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG--------PAGPAGDGQQGPDGDPGPTGEDG 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22096340  172 PPGPVGGPGEQGPQGDAGRPGAAGRPGPAGPRGEPGTEYKPGQPGRPGPQGPRGETGPAGNPGAPGNDGEAGKNGnagrp 251
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG----- 323

                        170       180
                 ....*....|....*....|....*....
gi 22096340  252 gppghpgKNGVPGQKGEDAAPGPDAGYCP 280
Cdd:NF038329 324 -------KDGLPGKDGKDGQPGKPAPKTP 345
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 189-248 3.07e-07

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: 46.33  E-value: 3.07e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22096340   189 GRPGAAGRPGPAGPRGEPGteyKPGQPGRPGPQGPRGETGPAGNPGAPGNDGEAGKNGNA 248
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPG---PPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 188-242 2.22e-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: 2.22e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 22096340   188 AGRPGAAGRPGPAGPRGEPGteyKPGQPGRPGPQGPRGETGPAGNPGAPGNDGEA 242
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPG---PPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 219-274 1.54e-04

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: 1.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 22096340   219 GPQGPRGETGPAGNPGAPGNDGEAGKNGNAGRPGPPGHPGKNGVPGQKGEDAAPGP 274
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 187-233 1.44e-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: 36.32  E-value: 1.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 22096340   187 DAGRPGAAGRPGPAGPRGEPGteyKPGQPGRPGPQGPRGETGPAGNP 233
Cdd:pfam01391  14 PPGPPGPPGPPGPPGPPGEPG---PPGPPGPPGPPGPPGAPGAPGPP 57
 
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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