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Conserved domains on  [gi|755534011|ref|XP_011241629|]
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collagen alpha-1(XIII) chain isoform X6 [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 ...
 471-701 5.34e-28

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: 117.70  E-value: 5.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 471 EIGLPGPPGHDGDKGPRGKPGDmgpagpqgppgkdgppgmKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRP 550
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGE------------------TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 551 GATGLPGPIGLPGFTGEKGEAGEKGDPGaevPGPPGPEGPPGPPGLQGFPGPKGEAGLEGSKGEKGSQGEKGDRGPLGLP 630
Cdd:NF038329 183 GAKGPAGEKGPQGPRGETGPAGEQGPAG---PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKD 259

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755534011 631 GTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPGLDGLDAP 701
Cdd:NF038329 260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 338-581 9.38e-21

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: 95.74  E-value: 9.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 338 GTKGEKGAAGSPGLLGQKGEKGDAGNAigGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPK 417
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGET--GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 418 GAKGEPGKGEMVDYNGsinealqeirtLALMGPPGLPGQTGPPGPPGTPGQRGEIGLPGPPGHDGDKGPRGKPGDMGPAG 497
Cdd:NF038329 195 GPRGETGPAGEQGPAG-----------PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 498 PQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEAGEKGDP 577
Cdd:NF038329 264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343


                 ....
gi 755534011 578 GAEV 581
Cdd:NF038329 344 TPEV 347
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 144-425 2.35e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 69.55  E-value: 2.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 144 GIKGQPGEKGAPGDAGmsivgprgppgQPGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQKGEKGQCGEy 223
Cdd:NF038329 117 GEKGEPGPAGPAGPAG-----------EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA- 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 224 phrllpllnsvrlapppvikrrtfQGEQSQTGIQGPPGPPGPPGPSGPLGHPGLPGPIGPPGLPGPPGPKGDPGiQGYHG 303
Cdd:NF038329 185 ------------------------KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ-QGPDG 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 304 RKGERGMPGMPGKHGAKGVPGiaVAGMKGEPGTPGTKGEKGAAGSPGLLGQKGEKGDAGNAigggrgepgppglpgppgp 383
Cdd:NF038329 240 DPGPTGEDGPQGPDGPAGKDG--PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLP------------------- 298

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 755534011 384 kGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPKGAKGEPGK 425
Cdd:NF038329 299 -GKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 471-701 5.34e-28

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: 117.70  E-value: 5.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 471 EIGLPGPPGHDGDKGPRGKPGDmgpagpqgppgkdgppgmKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRP 550
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGE------------------TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 551 GATGLPGPIGLPGFTGEKGEAGEKGDPGaevPGPPGPEGPPGPPGLQGFPGPKGEAGLEGSKGEKGSQGEKGDRGPLGLP 630
Cdd:NF038329 183 GAKGPAGEKGPQGPRGETGPAGEQGPAG---PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKD 259

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755534011 631 GTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPGLDGLDAP 701
Cdd:NF038329 260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 338-581 9.38e-21

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: 95.74  E-value: 9.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 338 GTKGEKGAAGSPGLLGQKGEKGDAGNAigGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPK 417
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGET--GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 418 GAKGEPGKGEMVDYNGsinealqeirtLALMGPPGLPGQTGPPGPPGTPGQRGEIGLPGPPGHDGDKGPRGKPGDMGPAG 497
Cdd:NF038329 195 GPRGETGPAGEQGPAG-----------PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 498 PQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEAGEKGDP 577
Cdd:NF038329 264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343


                 ....
gi 755534011 578 GAEV 581
Cdd:NF038329 344 TPEV 347
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 391-651 1.50e-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: 82.65  E-value: 1.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 391 GQAGPPGQQGDKGQPGAAGEQGPSGPKGAKGEPGKgemvdyngsinealqeirtlalmgppglpgqtgppgppgtPGQRG 470
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE----------------------------------------KGPAG 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 471 EIGLPGPPGHDGDKGPRGKPGDMGPAGPQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGLDGPtGEKGEPGDEGRP 550
Cdd:NF038329 166 PQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPT 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 551 GATGLPGPIGLPGFTGEKGEAGEKGDPGAEvpGPPGPEGPPGPPGLQGFPGPKGEAGLEGSKGEKGSQGEKGDRGPLGLP 630
Cdd:NF038329 245 GEDGPQGPDGPAGKDGPRGDRGEAGPDGPD--GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                        250       260
                 ....*....|....*....|.
gi 755534011 631 GTPGPIGVPGPAGPKGERGSK 651
Cdd:NF038329 323 GKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 144-425 2.35e-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: 69.55  E-value: 2.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 144 GIKGQPGEKGAPGDAGmsivgprgppgQPGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQKGEKGQCGEy 223
Cdd:NF038329 117 GEKGEPGPAGPAGPAG-----------EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA- 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 224 phrllpllnsvrlapppvikrrtfQGEQSQTGIQGPPGPPGPPGPSGPLGHPGLPGPIGPPGLPGPPGPKGDPGiQGYHG 303
Cdd:NF038329 185 ------------------------KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ-QGPDG 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 304 RKGERGMPGMPGKHGAKGVPGiaVAGMKGEPGTPGTKGEKGAAGSPGLLGQKGEKGDAGNAigggrgepgppglpgppgp 383
Cdd:NF038329 240 DPGPTGEDGPQGPDGPAGKDG--PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLP------------------- 298

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 755534011 384 kGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPKGAKGEPGK 425
Cdd:NF038329 299 -GKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 512-563 1.60e-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: 42.87  E-value: 1.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755534011  512 GEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPG 563
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 134-222 5.39e-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: 42.97  E-value: 5.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 134 KGAIGMPGRVGIKGQPGEKGAPGDAGMSIVGPRGPPGQPGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQ 213
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK 288


                 ....*....
gi 755534011 214 KGEKGQCGE 222
Cdd:NF038329 289 DGQNGKDGL 297
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 175-220 6.81e-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: 35.55  E-value: 6.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 755534011  175 RGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQKGEKGQC 220
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 471-701 5.34e-28

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: 117.70  E-value: 5.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 471 EIGLPGPPGHDGDKGPRGKPGDmgpagpqgppgkdgppgmKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRP 550
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGE------------------TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 551 GATGLPGPIGLPGFTGEKGEAGEKGDPGaevPGPPGPEGPPGPPGLQGFPGPKGEAGLEGSKGEKGSQGEKGDRGPLGLP 630
Cdd:NF038329 183 GAKGPAGEKGPQGPRGETGPAGEQGPAG---PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKD 259

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755534011 631 GTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPGLDGLDAP 701
Cdd:NF038329 260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 338-581 9.38e-21

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: 95.74  E-value: 9.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 338 GTKGEKGAAGSPGLLGQKGEKGDAGNAigGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPK 417
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGET--GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 418 GAKGEPGKGEMVDYNGsinealqeirtLALMGPPGLPGQTGPPGPPGTPGQRGEIGLPGPPGHDGDKGPRGKPGDMGPAG 497
Cdd:NF038329 195 GPRGETGPAGEQGPAG-----------PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 498 PQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEAGEKGDP 577
Cdd:NF038329 264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343


                 ....
gi 755534011 578 GAEV 581
Cdd:NF038329 344 TPEV 347
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 391-651 1.50e-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: 82.65  E-value: 1.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 391 GQAGPPGQQGDKGQPGAAGEQGPSGPKGAKGEPGKgemvdyngsinealqeirtlalmgppglpgqtgppgppgtPGQRG 470
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE----------------------------------------KGPAG 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 471 EIGLPGPPGHDGDKGPRGKPGDMGPAGPQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGLDGPtGEKGEPGDEGRP 550
Cdd:NF038329 166 PQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPT 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 551 GATGLPGPIGLPGFTGEKGEAGEKGDPGAEvpGPPGPEGPPGPPGLQGFPGPKGEAGLEGSKGEKGSQGEKGDRGPLGLP 630
Cdd:NF038329 245 GEDGPQGPDGPAGKDGPRGDRGEAGPDGPD--GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                        250       260
                 ....*....|....*....|.
gi 755534011 631 GTPGPIGVPGPAGPKGERGSK 651
Cdd:NF038329 323 GKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 144-425 2.35e-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: 69.55  E-value: 2.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 144 GIKGQPGEKGAPGDAGmsivgprgppgQPGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQKGEKGQCGEy 223
Cdd:NF038329 117 GEKGEPGPAGPAGPAG-----------EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA- 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 224 phrllpllnsvrlapppvikrrtfQGEQSQTGIQGPPGPPGPPGPSGPLGHPGLPGPIGPPGLPGPPGPKGDPGiQGYHG 303
Cdd:NF038329 185 ------------------------KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ-QGPDG 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 304 RKGERGMPGMPGKHGAKGVPGiaVAGMKGEPGTPGTKGEKGAAGSPGLLGQKGEKGDAGNAigggrgepgppglpgppgp 383
Cdd:NF038329 240 DPGPTGEDGPQGPDGPAGKDG--PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLP------------------- 298

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 755534011 384 kGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPKGAKGEPGK 425
Cdd:NF038329 299 -GKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 512-563 1.60e-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: 42.87  E-value: 1.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755534011  512 GEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPG 563
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 515-571 1.84e-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: 42.48  E-value: 1.84e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755534011  515 GPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEA 571
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 619-673 2.13e-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: 42.48  E-value: 2.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755534011  619 GEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPG 673
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 640-694 3.77e-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: 41.71  E-value: 3.77e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755534011  640 GPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPG 694
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 625-679 1.03e-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: 40.55  E-value: 1.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755534011  625 GPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRG 679
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 610-666 2.89e-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: 39.40  E-value: 2.89e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755534011  610 GSKGEKGSQGEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLP 666
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 134-222 5.39e-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: 42.97  E-value: 5.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534011 134 KGAIGMPGRVGIKGQPGEKGAPGDAGMSIVGPRGPPGQPGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQ 213
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK 288


                 ....*....
gi 755534011 214 KGEKGQCGE 222
Cdd:NF038329 289 DGQNGKDGL 297
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 649-697 1.85e-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: 1.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 755534011  649 GSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPGLDG 697
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 606-654 1.99e-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: 1.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 755534011  606 AGLEGSKGEKGSQGEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDP 654
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 175-220 6.81e-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: 35.55  E-value: 6.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 755534011  175 RGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQKGEKGQC 220
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 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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