NCBI Conserved Domain Search

NCBI

3D Macromolecular Structures

Conserved Domains

Conserved domains on [gi|194387528|dbj|BAG60128|]

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unnamed protein product [Homo sapiens]

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

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...

90-195

8.32e-10

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: 57.22 E-value: 8.32e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528  90 PGPMGLMGPRGPPGAAGAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPG 169
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                         90       100
                 ....*....|....*....|....*.
gi 194387528 170 TPGLPGFKGIRGHNGLKTSQPRTGIG 195
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAGDG 233

Name

Accession

Description

Interval

E-value

gly_rich_SclB

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...

90-195

8.32e-10

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: 57.22 E-value: 8.32e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528  90 PGPMGLMGPRGPPGAAGAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPG 169
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                         90       100
                 ....*....|....*....|....*.
gi 194387528 170 TPGLPGFKGIRGHNGLKTSQPRTGIG 195
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAGDG 233

gly_rich_SclB

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...

90-204

2.22e-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: 56.07 E-value: 2.22e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528  90 PGPMGLMGPRGPPGAAGAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPG 169
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 194387528 170 TPGLPGFKGIRGHNGLKTSQPRTGIGAPRTRNTSG 204
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQG 236

gly_rich_SclB

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...

32-184

1.69e-08

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: 53.37 E-value: 1.69e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528  32 KGPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPGPPGLGGnfAAQYDGKGVGLGPGPMGLMGPRGPPGAAGAPGPQ 111
Cdd:NF038329 158 RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG--PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQ 235

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194387528 112 GFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNG 184
Cdd:NF038329 236 GPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG 308

gly_rich_SclB

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...

26-184

6.48e-08

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: 6.48e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528  26 QEETVRKGPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPGPPGLGGNFAAqyDGKGVGLGPGPMGLMGPRGPPGAA 105
Cdd:NF038329 167 QGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP--AGEDGPAGPAGDGQQGPDGDPGPT 244

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194387528 106 GAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNG 184
Cdd:NF038329 245 GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

gly_rich_SclB

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...

91-191

1.81e-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: 50.29 E-value: 1.81e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528  91 GPMGLMGPRGPPGAAGAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPGT 170
Cdd:NF038329 138 GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGE 217

                         90       100
                 ....*....|....*....|.
gi 194387528 171 PGLPGFKGIRGHNGLKTSQPR 191
Cdd:NF038329 218 AGPAGEDGPAGPAGDGQQGPD 238

gly_rich_SclB

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...

89-198

2.95e-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: 49.90 E-value: 2.95e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528  89 GPGPMGLMGPRGPPGAAGAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFP 168
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110
                 ....*....|....*....|....*....|
gi 194387528 169 GTPGLPGFKGIRGHNGLKTSQPRTGIGAPR 198
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGED 224

gly_rich_SclB

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...

33-184

4.62e-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: 49.13 E-value: 4.62e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528  33 GPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPGPPGLGGNFAAQydgkgvglgpGPMGLMGPRGPPGAAGAPGPQG 112
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA----------GPQGEAGPQGPAGKDGEAGAKG 186

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194387528 113 FQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGvVGPQGARGFPGTPGLPGFKGIRGHNG 184
Cdd:NF038329 187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAG 257

gly_rich_SclB

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...

32-184

4.98e-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: 49.13 E-value: 4.98e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528  32 KGPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPGPPGLGGNFAAQYDgKGVGLGPGPMGLMGPRGPPGAAGAPGPQ 111
Cdd:NF038329 137 RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP-AGEKGPQGPRGETGPAGEQGPAGPAGPD 215

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194387528 112 GFQGPAGEPGEPG-----QTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNG 184
Cdd:NF038329 216 GEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293

Collagen

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...

118-174

5.83e-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: 44.79 E-value: 5.83e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 194387528  118 GEPGEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPGTPGLP 174
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57

gly_rich_SclB

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...

23-184

1.40e-06

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: 47.98 E-value: 1.40e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528  23 QSLQEETVRKGPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPG--PPGLGGNFAAQYDGKGVGLGPGPMGLMGPRG 100
Cdd:NF038329 131 AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGkdGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528 101 PPGAAGAPGPQGFQGPAGEP--------GEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPGTPG 172
Cdd:NF038329 211 PAGPDGEAGPAGEDGPAGPAgdgqqgpdGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290

                        170
                 ....*....|..
gi 194387528 173 LPGFKGIRGHNG 184
Cdd:NF038329 291 QNGKDGLPGKDG 302

Name

Accession

Description

Interval

E-value

gly_rich_SclB

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...

90-195

8.32e-10

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: 57.22 E-value: 8.32e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528  90 PGPMGLMGPRGPPGAAGAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPG 169
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                         90       100
                 ....*....|....*....|....*.
gi 194387528 170 TPGLPGFKGIRGHNGLKTSQPRTGIG 195
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAGDG 233

gly_rich_SclB

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...

90-204

2.22e-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: 56.07 E-value: 2.22e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528  90 PGPMGLMGPRGPPGAAGAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPG 169
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 194387528 170 TPGLPGFKGIRGHNGLKTSQPRTGIGAPRTRNTSG 204
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQG 236

gly_rich_SclB

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...

32-184

1.69e-08

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: 53.37 E-value: 1.69e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528  32 KGPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPGPPGLGGnfAAQYDGKGVGLGPGPMGLMGPRGPPGAAGAPGPQ 111
Cdd:NF038329 158 RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG--PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQ 235

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194387528 112 GFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNG 184
Cdd:NF038329 236 GPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG 308

gly_rich_SclB

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...

26-184

6.48e-08

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: 6.48e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528  26 QEETVRKGPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPGPPGLGGNFAAqyDGKGVGLGPGPMGLMGPRGPPGAA 105
Cdd:NF038329 167 QGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP--AGEDGPAGPAGDGQQGPDGDPGPT 244

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194387528 106 GAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNG 184
Cdd:NF038329 245 GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

gly_rich_SclB

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...

91-191

1.81e-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: 50.29 E-value: 1.81e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528  91 GPMGLMGPRGPPGAAGAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPGT 170
Cdd:NF038329 138 GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGE 217

                         90       100
                 ....*....|....*....|.
gi 194387528 171 PGLPGFKGIRGHNGLKTSQPR 191
Cdd:NF038329 218 AGPAGEDGPAGPAGDGQQGPD 238

gly_rich_SclB

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...

89-198

2.95e-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: 49.90 E-value: 2.95e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528  89 GPGPMGLMGPRGPPGAAGAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFP 168
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110
                 ....*....|....*....|....*....|
gi 194387528 169 GTPGLPGFKGIRGHNGLKTSQPRTGIGAPR 198
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGED 224

gly_rich_SclB

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...

33-184

4.62e-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: 49.13 E-value: 4.62e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528  33 GPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPGPPGLGGNFAAQydgkgvglgpGPMGLMGPRGPPGAAGAPGPQG 112
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA----------GPQGEAGPQGPAGKDGEAGAKG 186

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194387528 113 FQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGvVGPQGARGFPGTPGLPGFKGIRGHNG 184
Cdd:NF038329 187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAG 257

gly_rich_SclB

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...

32-184

4.98e-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: 49.13 E-value: 4.98e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528  32 KGPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPGPPGLGGNFAAQYDgKGVGLGPGPMGLMGPRGPPGAAGAPGPQ 111
Cdd:NF038329 137 RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP-AGEKGPQGPRGETGPAGEQGPAGPAGPD 215

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194387528 112 GFQGPAGEPGEPG-----QTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNG 184
Cdd:NF038329 216 GEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293

Collagen

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...

118-174

5.83e-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: 44.79 E-value: 5.83e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 194387528  118 GEPGEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPGTPGLP 174
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57

gly_rich_SclB

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...

23-184

1.40e-06

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: 47.98 E-value: 1.40e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528  23 QSLQEETVRKGPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPG--PPGLGGNFAAQYDGKGVGLGPGPMGLMGPRG 100
Cdd:NF038329 131 AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGkdGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387528 101 PPGAAGAPGPQGFQGPAGEP--------GEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPGTPG 172
Cdd:NF038329 211 PAGPDGEAGPAGEDGPAGPAgdgqqgpdGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290

                        170
                 ....*....|..
gi 194387528 173 LPGFKGIRGHNG 184
Cdd:NF038329 291 QNGKDGLPGKDG 302

Collagen

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...

127-181

2.79e-06

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: 43.25 E-value: 2.79e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 194387528  127 GPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRG 181
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

Collagen

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...

121-175

7.25e-06

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: 42.10 E-value: 7.25e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 194387528  121 GEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPGTPGLPG 175
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

Collagen

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...

111-157

2.23e-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: 37.86 E-value: 2.23e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 194387528  111 QGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDSHPGKPGRPGERG 157
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

Collagen

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...

130-184

7.13e-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: 36.32 E-value: 7.13e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 194387528  130 GARGPAGPPGKAGEDSHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNG 184
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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of the residues that compose this conserved feature have been mapped to the query sequence.

Click on the triangle to view details about the feature, including a multiple sequence alignment of your query sequence and the protein sequences used to curate the domain model, where hash marks (#) above the aligned sequences show the location of the conserved feature residues.

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Functional characterization of the conserved domain architecture found on the query. Click here to see more details.

This image shows a graphical summary of conserved domains identified on the query sequence. The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits (labeled illustration) or all hits (labeled illustration).
Domains are color coded according to superfamilies to which they have been assigned. Hits with scores that pass a domain-specific threshold (specific hits) are drawn in bright colors. Others (non-specific hits) and superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features), they are mapped to the query sequence and indicated through sets of triangles with the same color and shade of the domain or superfamily that provides the annotation.
Mouse over the colored bars or triangles to see descriptions of the domains and features. click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.

The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores. Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.

To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page, or click on the triangles, if present, that represent functional sites (conserved features) mapped to the query sequence.

Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence. (labeled illustration)
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Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance. (labeled illustration)
Four types of hits can be shown, as available, for each region on the query sequence:

specific hits meet or exceed a domain-specific e-value threshold (illustrated example) and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains

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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool (CDART).

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