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Conserved domains on  [gi|112363119|ref|NP_034066|]
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collagen alpha-3(IX) chain isoform 2 precursor [Mus musculus]

Protein Classification

collagen-like domain-containing protein( domain architecture ID 1903237)

collagen-like domain-containing protein such as collagens, which are extracellular structural proteins involved in formation of connective tissue structure

PubMed:  21421911|15837519

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 ...
 310-514 4.93e-22

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: 99.59  E-value: 4.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 310 LDGEKGEAGRNGGQGEKGPNGLPGLPGRAGSKGEKGEPGRTGELGEAGPSGEPGIPGDVGVPGERGEAGHRGSVGALGPQ 389
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 390 GPPGAPGIRGFQGQKGSTGDPGLPGPQGL-----------RGDVGDRGPGGATGPKGDQGIAGSDGLPGDKGELGPNGPV 458
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEdgpagpagdgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 112363119 459 GQKGESGSRGELGPKGIQGPNGTSGVQGVPGPPGPLGLQGVQGVPGITGKPGVPGK 514
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 31-349 2.77e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 43.74  E-value: 2.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119  31 GPQGPPGKPGKDGIDGEAGPPGLPGLPGPKGTSGKPGKPGEAGLPGLPGVDGLTGRDGPAGPKGAPGERgslgppgppgl 110
Cdd:NF038329 129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR----------- 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 111 ggkGLPGPPGEAGVSGLPGGIGLRgppgpsglpglpglpgppgppgnpgvlpegatdlqcpaicPPGPPGPPGMPGFKGP 190
Cdd:NF038329 198 ---GETGPAGEQGPAGPAGPDGEA----------------------------------------GPAGEDGPAGPAGDGQ 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 191 TGYKGEQGEVGKDGEKgspgppgppgipgtvglqgprglrglpgplgppgdrgpigfrgppgtpgapgkvGDRGERGPEG 270
Cdd:NF038329 235 QGPDGDPGPTGEDGPQ------------------------------------------------------GPDGPAGKDG 260

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 112363119 271 FRGPKGDLGRPGPKGIPGMAGPGGEPGMPGKDGKDGVPGLDGEKGEAGRNGGQGEKGPNGLPGLPGRAGSKGEKGEPGR 349
Cdd:NF038329 261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 310-514 4.93e-22

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: 99.59  E-value: 4.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 310 LDGEKGEAGRNGGQGEKGPNGLPGLPGRAGSKGEKGEPGRTGELGEAGPSGEPGIPGDVGVPGERGEAGHRGSVGALGPQ 389
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 390 GPPGAPGIRGFQGQKGSTGDPGLPGPQGL-----------RGDVGDRGPGGATGPKGDQGIAGSDGLPGDKGELGPNGPV 458
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEdgpagpagdgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 112363119 459 GQKGESGSRGELGPKGIQGPNGTSGVQGVPGPPGPLGLQGVQGVPGITGKPGVPGK 514
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 400-656 2.01e-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: 85.34  E-value: 2.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 400 FQGQKGSTGDPGLPGPQGLRGDVGDRGPGGATGPKGDQGIAGSDGLPGDKGELGPNGPVGQKGESGSRGELGPKGIQGPN 479
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 480 GTSGVQGVPGPPGPLGLQGVQGVPGITGKPGVPGKEASEQRirelcggmiseqiaqlaahlRKPLAPGSIGRPGPAGPPg 559
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQ--------------------GPDGDPGPTGEDGPQGPD- 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 560 ppgppgsighpgarGPPGYRGPTGELGDPGPRGSQGDRGDkgatgAGLDGPAGDQGYQGPQGVPGisKDGRDGAHGEPGL 639
Cdd:NF038329 254 --------------GPAGKDGPRGDRGEAGPDGPDGKDGE-----RGPVGPAGKDGQNGKDGLPG--KDGKDGQNGKDGL 312

                        250
                 ....*....|....*..
gi 112363119 640 PGDPGLPGAAGAQGTPG 656
Cdd:NF038329 313 PGKDGKDGQPGKDGLPG 329
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 203-480 5.39e-16

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: 80.72  E-value: 5.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 203 DGEKGSPGPpgppgipgtvglqgprglrglpgplgppgdrgpigfrgppgtpgapgkVGDRGERGPEGFRGPKGDLGRPG 282
Cdd:NF038329 116 DGEKGEPGP------------------------------------------------AGPAGPAGEQGPRGDRGETGPAG 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 283 PKGIPGMAGPGGEPGMPGKDGKDGVPGLDGEKGEAGRNGGQGEKGPNGLPGLPGRAGSKGEKGEPGRTGELGEAGPSGEP 362
Cdd:NF038329 148 PAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPA 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 363 GIPGDvGVPGERGEAGHRGSVGALGPqgppgapgiRGFQGQKGSTGDPGLPGPQGLRGDVGDRGPggaTGPKGDQGIAGS 442
Cdd:NF038329 228 GPAGD-GQQGPDGDPGPTGEDGPQGP---------DGPAGKDGPRGDRGEAGPDGPDGKDGERGP---VGPAGKDGQNGK 294

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 112363119 443 DGLPGDKGELGPNGPVGQKGESGSRGELGPKGIQGPNG 480
Cdd:NF038329 295 DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 192-416 1.20e-13

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: 73.40  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 192 GYKGEQGEVGKDGEKGSPGPPGPPGIPGTVGLQGPRGLRGLPGPLGPPGDRGPIGFRgppgtpgapgkvGDRGERGPEGF 271
Cdd:NF038329 129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK------------GPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 272 RGPKGDLGRPGPKGIPGMAGPGGEPGMPGKDGKDGvPGLDGEKGEAGRNGGQGEKGPNGLPGLPGRAGSKGEKGEPGRTG 351
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 112363119 352 ELGEAGPSGEPGIP---GDVGVPGERGEAGHRGSVGALGPQGPPGAPGIRGFQGQKGSTGDPGLPGPQ 416
Cdd:NF038329 276 KDGERGPVGPAGKDgqnGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 324-378 1.77e-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: 39.78  E-value: 1.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 112363119  324 GEKGPNGLPGLPGRAGSKGEKGEPGRTGELGEAGPSGEPGIPGDVGVPGERGEAG 378
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 31-349 2.77e-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: 2.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119  31 GPQGPPGKPGKDGIDGEAGPPGLPGLPGPKGTSGKPGKPGEAGLPGLPGVDGLTGRDGPAGPKGAPGERgslgppgppgl 110
Cdd:NF038329 129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR----------- 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 111 ggkGLPGPPGEAGVSGLPGGIGLRgppgpsglpglpglpgppgppgnpgvlpegatdlqcpaicPPGPPGPPGMPGFKGP 190
Cdd:NF038329 198 ---GETGPAGEQGPAGPAGPDGEA----------------------------------------GPAGEDGPAGPAGDGQ 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 191 TGYKGEQGEVGKDGEKgspgppgppgipgtvglqgprglrglpgplgppgdrgpigfrgppgtpgapgkvGDRGERGPEG 270
Cdd:NF038329 235 QGPDGDPGPTGEDGPQ------------------------------------------------------GPDGPAGKDG 260

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 112363119 271 FRGPKGDLGRPGPKGIPGMAGPGGEPGMPGKDGKDGVPGLDGEKGEAGRNGGQGEKGPNGLPGLPGRAGSKGEKGEPGR 349
Cdd:NF038329 261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 310-514 4.93e-22

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: 99.59  E-value: 4.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 310 LDGEKGEAGRNGGQGEKGPNGLPGLPGRAGSKGEKGEPGRTGELGEAGPSGEPGIPGDVGVPGERGEAGHRGSVGALGPQ 389
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 390 GPPGAPGIRGFQGQKGSTGDPGLPGPQGL-----------RGDVGDRGPGGATGPKGDQGIAGSDGLPGDKGELGPNGPV 458
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEdgpagpagdgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 112363119 459 GQKGESGSRGELGPKGIQGPNGTSGVQGVPGPPGPLGLQGVQGVPGITGKPGVPGK 514
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 400-656 2.01e-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: 85.34  E-value: 2.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 400 FQGQKGSTGDPGLPGPQGLRGDVGDRGPGGATGPKGDQGIAGSDGLPGDKGELGPNGPVGQKGESGSRGELGPKGIQGPN 479
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 480 GTSGVQGVPGPPGPLGLQGVQGVPGITGKPGVPGKEASEQRirelcggmiseqiaqlaahlRKPLAPGSIGRPGPAGPPg 559
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQ--------------------GPDGDPGPTGEDGPQGPD- 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 560 ppgppgsighpgarGPPGYRGPTGELGDPGPRGSQGDRGDkgatgAGLDGPAGDQGYQGPQGVPGisKDGRDGAHGEPGL 639
Cdd:NF038329 254 --------------GPAGKDGPRGDRGEAGPDGPDGKDGE-----RGPVGPAGKDGQNGKDGLPG--KDGKDGQNGKDGL 312

                        250
                 ....*....|....*..
gi 112363119 640 PGDPGLPGAAGAQGTPG 656
Cdd:NF038329 313 PGKDGKDGQPGKDGLPG 329
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 203-480 5.39e-16

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: 80.72  E-value: 5.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 203 DGEKGSPGPpgppgipgtvglqgprglrglpgplgppgdrgpigfrgppgtpgapgkVGDRGERGPEGFRGPKGDLGRPG 282
Cdd:NF038329 116 DGEKGEPGP------------------------------------------------AGPAGPAGEQGPRGDRGETGPAG 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 283 PKGIPGMAGPGGEPGMPGKDGKDGVPGLDGEKGEAGRNGGQGEKGPNGLPGLPGRAGSKGEKGEPGRTGELGEAGPSGEP 362
Cdd:NF038329 148 PAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPA 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 363 GIPGDvGVPGERGEAGHRGSVGALGPqgppgapgiRGFQGQKGSTGDPGLPGPQGLRGDVGDRGPggaTGPKGDQGIAGS 442
Cdd:NF038329 228 GPAGD-GQQGPDGDPGPTGEDGPQGP---------DGPAGKDGPRGDRGEAGPDGPDGKDGERGP---VGPAGKDGQNGK 294

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 112363119 443 DGLPGDKGELGPNGPVGQKGESGSRGELGPKGIQGPNG 480
Cdd:NF038329 295 DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 192-416 1.20e-13

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: 73.40  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 192 GYKGEQGEVGKDGEKGSPGPPGPPGIPGTVGLQGPRGLRGLPGPLGPPGDRGPIGFRgppgtpgapgkvGDRGERGPEGF 271
Cdd:NF038329 129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK------------GPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 272 RGPKGDLGRPGPKGIPGMAGPGGEPGMPGKDGKDGvPGLDGEKGEAGRNGGQGEKGPNGLPGLPGRAGSKGEKGEPGRTG 351
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 112363119 352 ELGEAGPSGEPGIP---GDVGVPGERGEAGHRGSVGALGPQGPPGAPGIRGFQGQKGSTGDPGLPGPQ 416
Cdd:NF038329 276 KDGERGPVGPAGKDgqnGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 324-378 1.77e-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: 39.78  E-value: 1.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 112363119  324 GEKGPNGLPGLPGRAGSKGEKGEPGRTGELGEAGPSGEPGIPGDVGVPGERGEAG 378
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 31-349 2.77e-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: 2.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119  31 GPQGPPGKPGKDGIDGEAGPPGLPGLPGPKGTSGKPGKPGEAGLPGLPGVDGLTGRDGPAGPKGAPGERgslgppgppgl 110
Cdd:NF038329 129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR----------- 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 111 ggkGLPGPPGEAGVSGLPGGIGLRgppgpsglpglpglpgppgppgnpgvlpegatdlqcpaicPPGPPGPPGMPGFKGP 190
Cdd:NF038329 198 ---GETGPAGEQGPAGPAGPDGEA----------------------------------------GPAGEDGPAGPAGDGQ 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363119 191 TGYKGEQGEVGKDGEKgspgppgppgipgtvglqgprglrglpgplgppgdrgpigfrgppgtpgapgkvGDRGERGPEG 270
Cdd:NF038329 235 QGPDGDPGPTGEDGPQ------------------------------------------------------GPDGPAGKDG 260

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 112363119 271 FRGPKGDLGRPGPKGIPGMAGPGGEPGMPGKDGKDGVPGLDGEKGEAGRNGGQGEKGPNGLPGLPGRAGSKGEKGEPGR 349
Cdd:NF038329 261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 423-479 3.25e-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: 3.25e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 112363119  423 GDRGPGGATGPKGDQGIAGSDGLPGDKGELGPNGPVGQKGESGSRGELGPKGIQGPN 479
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 318-374 3.88e-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: 38.63  E-value: 3.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 112363119  318 GRNGGQGEKGPNGLPGLPGRAGSKGEKGEPGRTGELGEAGPSGEPGIPGDVGVPGER 374
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 405-460 1.16e-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: 37.47  E-value: 1.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 112363119  405 GSTGDPGLPGPQGLRGDVGDRGPGGATGPKGDQGIAGSDGLPGDKGELGPNGPVGQ 460
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 402-458 1.25e-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: 37.47  E-value: 1.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 112363119  402 GQKGSTGDPGLPGPQGLRGDVGDRGPGGATGPKGDQGIAGSDGLPGDKGELGPNGPV 458
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 321-377 1.53e-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: 37.09  E-value: 1.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 112363119  321 GGQGEKGPNGLPGLPGRAGSKGEKGEPGRTGELGEAGPSGEPGIPGDVGVPGERGEA 377
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 408-463 3.81e-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: 3.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 112363119  408 GDPGLPGPQGLRGDVGDRGPGGATGPKGDQGIAGSDGLPGDKGELGPNGPVGQKGE 463
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 309-363 5.33e-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: 35.55  E-value: 5.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 112363119  309 GLDGEKGEAGRNGGQGEKGPNGLPGLPGRAGSKGEKGEPGRTGELGEAGPSGEPG 363
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
 
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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