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Conserved domains on  [gi|595582082|ref|NP_001277620|]
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collagen alpha-1(IX) chain isoform 2 precursor [Mus musculus]

Protein Classification

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 ...
 216-461 2.66e-30

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: 124.25  E-value: 2.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 216 GEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGD 295
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 296 TGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLP--GVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGE 373
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 374 VGPRGPRGLPGSRGPVGPEGSPGIPGKlgsvgspglpglpgppglpgmKGDRGVFGEPGPKGEQGASGEEGEAGARGDLG 453
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGK---------------------DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335


                 ....*...
gi 595582082 454 DMGQPGPK 461
Cdd:NF038329 336 QPGKPAPK 343
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 366-624 3.12e-15

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: 78.41  E-value: 3.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 366 GQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGKLGsvgspglpglpgppgLPGMKGDRGVFGEPGPKGEQGASGEEGE 445
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPG---------------PQGERGEKGPAGPQGEAGPQGPAGKDGE 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 446 AGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRGLPGVEGPRGPPGPRGmQGDQGATGLPGIQGPPGRAPTDqhikqvc 525
Cdd:NF038329 182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPD------- 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 526 mrvvqehfAEMAASLKRPDTGASGLPGRPGPPGPPGPPGENGFPGQMGIRGLPGIKGPPGALGLRGPKGDLGEKGERGPp 605
Cdd:NF038329 254 --------GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK- 324

                        250
                 ....*....|....*....
gi 595582082 606 gRGPKGLPGAIGLPGDPGP 624
Cdd:NF038329 325 -DGLPGKDGKDGQPGKPAP 342
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 177-231 6.54e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


:

Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 6.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 595582082  177 GRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRG 231
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 216-461 2.66e-30

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: 124.25  E-value: 2.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 216 GEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGD 295
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 296 TGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLP--GVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGE 373
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 374 VGPRGPRGLPGSRGPVGPEGSPGIPGKlgsvgspglpglpgppglpgmKGDRGVFGEPGPKGEQGASGEEGEAGARGDLG 453
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGK---------------------DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335


                 ....*...
gi 595582082 454 DMGQPGPK 461
Cdd:NF038329 336 QPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 177-400 3.33e-30

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: 124.25  E-value: 3.33e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 177 GRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGI 256
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 257 PGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGpKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGVPG 336
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 595582082 337 IPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGK 400
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 175-380 2.19e-26

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: 112.69  E-value: 2.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 175 PPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQ 254
Cdd:NF038329 145 PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGED 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 255 GIPGAAGDqGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGV 334
Cdd:NF038329 225 GPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGK 303

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 595582082 335 PGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPR 380
Cdd:NF038329 304 DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQ 349
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 264-481 1.67e-25

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: 109.99  E-value: 1.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 264 GQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGVPGIPGAKGV 343
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 344 AGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGP-----RGPRGLPGSRGPVGPEGSPGIPGKLGSvgspglpglpgppgl 418
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGPDGPAGKDGP--------------- 261

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 595582082 419 pgmKGDRGVFGEPGPKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRGL 481
Cdd:NF038329 262 ---RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 76-339 7.36e-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: 7.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082  76 GKPGTPGADGLTGPDGSPGSVGPRGQKGEPGVPGSRgfpgrgipgppgppgttglpgelGRVGPIGdpgkrgppgppgpp 155
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ-----------------------GEAGPQG-------------- 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 156 gpsgtigfhdgdplcpnscPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGiTGI 235
Cdd:NF038329 175 -------------------PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQ 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 236 VGDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKG 315
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG 314

                        250       260
                 ....*....|....*....|....
gi 595582082 316 EAGKPGPPGDVGLQGLPGVPGIPG 339
Cdd:NF038329 315 KDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 321-518 2.87e-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: 84.96  E-value: 2.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 321 GPPGDVGLQGLPGVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGK 400
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 401 LGSVGSPGLPGLPGPPGLPGMKGDRGVFGEPGP--KGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGI 478
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 595582082 479 RGlpgvegPRGPPGPRGMQGDQGATGLPGIQGPPGRAPTD 518
Cdd:NF038329 277 DG------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD 310
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 366-624 3.12e-15

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: 78.41  E-value: 3.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 366 GQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGKLGsvgspglpglpgppgLPGMKGDRGVFGEPGPKGEQGASGEEGE 445
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPG---------------PQGERGEKGPAGPQGEAGPQGPAGKDGE 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 446 AGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRGLPGVEGPRGPPGPRGmQGDQGATGLPGIQGPPGRAPTDqhikqvc 525
Cdd:NF038329 182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPD------- 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 526 mrvvqehfAEMAASLKRPDTGASGLPGRPGPPGPPGPPGENGFPGQMGIRGLPGIKGPPGALGLRGPKGDLGEKGERGPp 605
Cdd:NF038329 254 --------GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK- 324

                        250
                 ....*....|....*....
gi 595582082 606 gRGPKGLPGAIGLPGDPGP 624
Cdd:NF038329 325 -DGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 79-322 5.44e-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: 71.47  E-value: 5.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082  79 GTPGADGLTGPDGSPGSVGPRGQKGEPGvpgsrgfpgrgipgppgppgttglpgelgrvgpigdpgkrgppgppgppgps 158
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETG---------------------------------------------------- 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 159 gtigfhdgdplcpnscPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGhKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGD 238
Cdd:NF038329 202 ----------------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 239 KGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPgspgpkGDTGLPGVDGRDGIPGMPGTKGEAG 318
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLP------GKDGKDGQPGKDGLPGKDGKDGQPG 338


                 ....
gi 595582082 319 KPGP 322
Cdd:NF038329 339 KPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 422-642 1.07e-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: 64.16  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 422 KGDRGVFGEPGPKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRGLPGVEGPRGPPGPRGMQGDQG 501
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 502 ATGLPGIQGPPGRAPTDqhikqvcmrvvqehfaemaaslkrpdtgasglpgrpgppgppgppgengfpGQMGIRGLPGIK 581
Cdd:NF038329 199 ETGPAGEQGPAGPAGPD---------------------------------------------------GEAGPAGEDGPA 227

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 595582082 582 GPPGAlGLRGPKGDLGEKGERGPPG-RGPKGLPGAIGLPGDPGPAsyGKNGRDGEQGPPGVA 642
Cdd:NF038329 228 GPAGD-GQQGPDGDPGPTGEDGPQGpDGPAGKDGPRGDRGEAGPD--GPDGKDGERGPVGPA 286
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 342-396 4.75e-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: 44.02  E-value: 4.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 595582082  342 GVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPG 396
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 541-653 1.97e-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: 44.51  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 541 KRPDTGASGLPGRPGPPGPPGPPGENGFPGQMGIRGLPGIKGPPGALGLRGPKGDLGEKGERGPPG-RGPKGLPGAIGLP 619
Cdd:NF038329 139 DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGeQGPAGPAGPDGEA 218

                         90       100       110
                 ....*....|....*....|....*....|....
gi 595582082 620 GDPGPASYGKNGRDGEQGPPGVAGIPGVPGPPGP 653
Cdd:NF038329 219 GPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGP 252
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 177-231 6.54e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 6.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 595582082  177 GRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRG 231
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 237-399 1.01e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 237 GDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGE 316
Cdd:PRK07764 599 GPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAP 678

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 317 AGKPGPPGDVglqglPGVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPG 396
Cdd:PRK07764 679 AAPPPAPAPA-----APAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAG 753


                 ...
gi 595582082 397 IPG 399
Cdd:PRK07764 754 APA 756
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 216-461 2.66e-30

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: 124.25  E-value: 2.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 216 GEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGD 295
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 296 TGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLP--GVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGE 373
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 374 VGPRGPRGLPGSRGPVGPEGSPGIPGKlgsvgspglpglpgppglpgmKGDRGVFGEPGPKGEQGASGEEGEAGARGDLG 453
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGK---------------------DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335


                 ....*...
gi 595582082 454 DMGQPGPK 461
Cdd:NF038329 336 QPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 177-400 3.33e-30

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: 124.25  E-value: 3.33e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 177 GRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGI 256
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 257 PGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGpKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGVPG 336
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 595582082 337 IPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGK 400
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 175-380 2.19e-26

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: 112.69  E-value: 2.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 175 PPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQ 254
Cdd:NF038329 145 PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGED 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 255 GIPGAAGDqGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGV 334
Cdd:NF038329 225 GPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGK 303

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 595582082 335 PGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPR 380
Cdd:NF038329 304 DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQ 349
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 264-481 1.67e-25

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: 109.99  E-value: 1.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 264 GQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGVPGIPGAKGV 343
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 344 AGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGP-----RGPRGLPGSRGPVGPEGSPGIPGKLGSvgspglpglpgppgl 418
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGPDGPAGKDGP--------------- 261

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 595582082 419 pgmKGDRGVFGEPGPKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRGL 481
Cdd:NF038329 262 ---RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 76-339 7.36e-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: 7.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082  76 GKPGTPGADGLTGPDGSPGSVGPRGQKGEPGVPGSRgfpgrgipgppgppgttglpgelGRVGPIGdpgkrgppgppgpp 155
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ-----------------------GEAGPQG-------------- 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 156 gpsgtigfhdgdplcpnscPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGiTGI 235
Cdd:NF038329 175 -------------------PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQ 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 236 VGDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKG 315
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG 314

                        250       260
                 ....*....|....*....|....
gi 595582082 316 EAGKPGPPGDVGLQGLPGVPGIPG 339
Cdd:NF038329 315 KDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 321-518 2.87e-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: 84.96  E-value: 2.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 321 GPPGDVGLQGLPGVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGK 400
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 401 LGSVGSPGLPGLPGPPGLPGMKGDRGVFGEPGP--KGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGI 478
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 595582082 479 RGlpgvegPRGPPGPRGMQGDQGATGLPGIQGPPGRAPTD 518
Cdd:NF038329 277 DG------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD 310
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 366-624 3.12e-15

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: 78.41  E-value: 3.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 366 GQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGKLGsvgspglpglpgppgLPGMKGDRGVFGEPGPKGEQGASGEEGE 445
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPG---------------PQGERGEKGPAGPQGEAGPQGPAGKDGE 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 446 AGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRGLPGVEGPRGPPGPRGmQGDQGATGLPGIQGPPGRAPTDqhikqvc 525
Cdd:NF038329 182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPD------- 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 526 mrvvqehfAEMAASLKRPDTGASGLPGRPGPPGPPGPPGENGFPGQMGIRGLPGIKGPPGALGLRGPKGDLGEKGERGPp 605
Cdd:NF038329 254 --------GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK- 324

                        250
                 ....*....|....*....
gi 595582082 606 gRGPKGLPGAIGLPGDPGP 624
Cdd:NF038329 325 -DGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 79-322 5.44e-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: 71.47  E-value: 5.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082  79 GTPGADGLTGPDGSPGSVGPRGQKGEPGvpgsrgfpgrgipgppgppgttglpgelgrvgpigdpgkrgppgppgppgps 158
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETG---------------------------------------------------- 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 159 gtigfhdgdplcpnscPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGhKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGD 238
Cdd:NF038329 202 ----------------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 239 KGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPgspgpkGDTGLPGVDGRDGIPGMPGTKGEAG 318
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLP------GKDGKDGQPGKDGLPGKDGKDGQPG 338


                 ....
gi 595582082 319 KPGP 322
Cdd:NF038329 339 KPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 422-642 1.07e-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: 64.16  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 422 KGDRGVFGEPGPKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRGLPGVEGPRGPPGPRGMQGDQG 501
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 502 ATGLPGIQGPPGRAPTDqhikqvcmrvvqehfaemaaslkrpdtgasglpgrpgppgppgppgengfpGQMGIRGLPGIK 581
Cdd:NF038329 199 ETGPAGEQGPAGPAGPD---------------------------------------------------GEAGPAGEDGPA 227

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 595582082 582 GPPGAlGLRGPKGDLGEKGERGPPG-RGPKGLPGAIGLPGDPGPAsyGKNGRDGEQGPPGVA 642
Cdd:NF038329 228 GPAGD-GQQGPDGDPGPTGEDGPQGpDGPAGKDGPRGDRGEAGPD--GPDGKDGERGPVGPA 286
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 342-396 4.75e-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: 44.02  E-value: 4.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 595582082  342 GVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPG 396
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 255-311 6.26e-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: 44.02  E-value: 6.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 595582082  255 GIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMP 311
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 216-271 7.18e-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: 43.64  E-value: 7.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 595582082  216 GEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGE 271
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 264-320 1.32e-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: 1.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 595582082  264 GQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKP 320
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 246-300 1.97e-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: 1.97e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 595582082  246 GFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPG 300
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 285-340 2.09e-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: 2.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 595582082  285 GIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGVPGIPGA 340
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 300-356 2.24e-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: 2.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 595582082  300 GVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGVPGIPGAKGVAGEKGNTGAPGKP 356
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 339-395 4.78e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 4.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 595582082  339 GAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSP 395
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 240-294 5.93e-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: 40.94  E-value: 5.93e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 595582082  240 GEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKG 294
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 351-403 6.11e-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: 40.94  E-value: 6.11e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 595582082  351 GAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGKLGS 403
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 315-371 6.36e-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: 40.94  E-value: 6.36e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 595582082  315 GEAGKPGPPGDVGLQGLPGVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPP 371
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 330-386 6.81e-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: 40.94  E-value: 6.81e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 595582082  330 GLPGVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSR 386
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 237-292 1.01e-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: 1.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 595582082  237 GDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGP 292
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 318-380 1.05e-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: 1.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 595582082  318 GKPGPPGdvglqgLPGVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPR 380
Cdd:pfam01391   1 GPPGPPG------PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 261-317 1.89e-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: 39.78  E-value: 1.89e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 595582082  261 GDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEA 317
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 541-653 1.97e-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: 44.51  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 541 KRPDTGASGLPGRPGPPGPPGPPGENGFPGQMGIRGLPGIKGPPGALGLRGPKGDLGEKGERGPPG-RGPKGLPGAIGLP 619
Cdd:NF038329 139 DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGeQGPAGPAGPDGEA 218

                         90       100       110
                 ....*....|....*....|....*....|....
gi 595582082 620 GDPGPASYGKNGRDGEQGPPGVAGIPGVPGPPGP 653
Cdd:NF038329 219 GPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGP 252
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 234-290 2.62e-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: 2.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 595582082  234 GIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSP 290
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 177-231 6.54e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 6.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 595582082  177 GRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRG 231
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 429-480 7.43e-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: 7.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 595582082  429 GEPGPKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRG 480
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 321-383 7.89e-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: 37.86  E-value: 7.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 595582082  321 GPPGDVGLQGLPGVPGIPGAKGVAGEKGNTGAPGKPGQlgssgkPGQQGPPGEVGPRGPRGLP 383
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGP------PGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 237-399 1.01e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 237 GDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGE 316
Cdd:PRK07764 599 GPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAP 678

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 317 AGKPGPPGDVglqglPGVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPG 396
Cdd:PRK07764 679 AAPPPAPAPA-----APAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAG 753


                 ...
gi 595582082 397 IPG 399
Cdd:PRK07764 754 APA 756
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 264-381 1.62e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 41.59  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 264 GQRGPPGETGPEGD-RGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGtKGEAGKPGPPGDvGLQGLPGVPGIPgAKG 342
Cdd:PRK14959 376 GGASAPSGSAAEGPaSGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPA-PSAAPSPRVPWD-DAPPAPPRSGIP-PRP 452

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 595582082 343 VAGEKGNTGAPGKPGQLGS-SGKPGQQGPPGEVGPRGPRG 381
Cdd:PRK14959 453 APRMPEASPVPGAPDSVASaSDAPPTLGDPSDTAEHTPSG 492
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 175-380 2.10e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 175 PPGRSGYPGLPGMRGHKGAKGEIGEPGRQGhkGEEGDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQ 254
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPA--APAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 255 GIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGV 334
Cdd:PRK07764 668 GWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD 747

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 595582082 335 PGIPGakgvagekgntGAPGKPGQLGSSGKPGQQGPPGEVGPRGPR 380
Cdd:PRK07764 748 PPDPA-----------GAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 246-372 2.52e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 41.20  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582082 246 GFDGEPGPQGIPG-AAGDQGQRGPPGETGPEGD---RGIQGSRGIPGSPGPkGDTGLPGVDGrDGIPGMPGTKGEAGKPG 321
Cdd:PRK14959 376 GGASAPSGSAAEGpASGGAATIPTPGTQGPQGTapaAGMTPSSAAPATPAP-SAAPSPRVPW-DDAPPAPPRSGIPPRPA 453

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 595582082 322 ppgdvglqglpgvPGIPGAKGVAGEKGNTG-APGKPGQLGSSGKPGQQGPPG 372
Cdd:PRK14959 454 -------------PRMPEASPVPGAPDSVAsASDAPPTLGDPSDTAEHTPSG 492
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 423-471 3.49e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 3.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 595582082  423 GDRGVFGEPGPKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPG 471
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 426-480 4.51e-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: 4.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 595582082  426 GVFGEPGPKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRG 480
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 210-266 5.18e-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: 5.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 595582082  210 GDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQR 266
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 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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