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Conserved domains on  [gi|902951550|sp|C0HJN6|]
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RecName: Full=Collagen alpha-2(I) chain; AltName: Full=Alpha-2 type I collagen

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 ...
 314-537 1.12e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.15  E-value: 1.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 314 FPGSPGNIGPAGKEGPVGIPGIDGRPGPTGPAGARniGFPGPKGPTGDNGDKGHAGIAGARGAPGPDGNNGAQGPPqGGK 393
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPA--GPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA-GEK 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 394 GEQGPAGPPGFQGIPGPAGTAGEAGKPGERGIPGEFGIPGPaGPRGERGPPGESGAAGPTGPIGNRGPSGPAGPDGNKGE 473
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP 270

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 902951550 474 PGVVGAPGTAGPSGPSGIPGERGAAGIPGPKGEKGEPGirRDGARGAPGAVGAPGPAGANGDRG 537
Cdd:NF038329 271 DGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG--KDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 639-857 3.31e-23

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: 103.83  E-value: 3.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 639 GRSGETGASGPPGFAGEKTP-GPQGIIGAPGFIGIPGSRGERGIPGVAGSVGEPGPIGIAGPPGARGPPGAVGNPGVNGA 717
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPrGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 718 PGEAGRDGNPGSDGPPG-RGHKGERGYPGAGAPGPQGPVGPTGKHGNRGEPGPAGVVGPTGAVGPRGPSGPQGIRGDKGE 796
Cdd:NF038329 197 RGETGPAGEQGPAGPAGpDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 902951550 797 PGDKGPRGIPGIKGHNGIQGIPGIAG---HHGDQGAPGSVGPAGPRGPAGPSGPVGKDGRTGHP 857
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGkdgQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 85-329 3.67e-19

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: 91.12  E-value: 3.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  85 GFKGIRGHNGIDGIKGQPGAPGVKGEPGAPGARGIPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGP 164
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 165 KGEIGPVGSPGASGPAGPRGEVGIPGVSGPVGPPGNGAAGIPGVAGAPGIPGPRGIPGPVGAAGATGARGIVGEPGPAGs 244
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG- 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 245 KAGPQGIPGPSGEEGKRGSTGEigpagppgppgirgspgsRGIPGADGRAGVMGIPGSRGATGPAGVRGFPGSPGNIGPA 324
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGL------------------PGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337


                 ....*
gi 902951550 325 GKEGP 329
Cdd:NF038329 338 GKPAP 342
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 314-537 1.12e-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: 111.15  E-value: 1.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 314 FPGSPGNIGPAGKEGPVGIPGIDGRPGPTGPAGARniGFPGPKGPTGDNGDKGHAGIAGARGAPGPDGNNGAQGPPqGGK 393
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPA--GPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA-GEK 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 394 GEQGPAGPPGFQGIPGPAGTAGEAGKPGERGIPGEFGIPGPaGPRGERGPPGESGAAGPTGPIGNRGPSGPAGPDGNKGE 473
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP 270

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 902951550 474 PGVVGAPGTAGPSGPSGIPGERGAAGIPGPKGEKGEPGirRDGARGAPGAVGAPGPAGANGDRG 537
Cdd:NF038329 271 DGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG--KDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 262-504 3.20e-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: 109.61  E-value: 3.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 262 GSTGEIGPAGPpgppgirgspgsRGIPGADGRAGVMGIPGSRGATGPAGVRGFPGSPGNIGPAGKEGPVGIPGIDGRPGP 341
Cdd:NF038329 117 GEKGEPGPAGP------------AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 342 TGPAGARniGFPGPKGPTGDNGDKGHAGIAGARGAPGPDGNNGAQGPPqgGKGEQGPAGPPGFQGIPGPAGTAGEAGKPG 421
Cdd:NF038329 185 KGPAGEK--GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPA--GDGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 422 ERGIPGEFGIPGPAGPRGERGPPGESGAAGPTGPIGNRGPSGPAGPDGNKGEPGVVGAPGTAGPSGPSGIPGERGAAGIP 501
Cdd:NF038329 261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340


                 ...
gi 902951550 502 GPK 504
Cdd:NF038329 341 APK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 639-857 3.31e-23

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: 103.83  E-value: 3.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 639 GRSGETGASGPPGFAGEKTP-GPQGIIGAPGFIGIPGSRGERGIPGVAGSVGEPGPIGIAGPPGARGPPGAVGNPGVNGA 717
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPrGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 718 PGEAGRDGNPGSDGPPG-RGHKGERGYPGAGAPGPQGPVGPTGKHGNRGEPGPAGVVGPTGAVGPRGPSGPQGIRGDKGE 796
Cdd:NF038329 197 RGETGPAGEQGPAGPAGpDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 902951550 797 PGDKGPRGIPGIKGHNGIQGIPGIAG---HHGDQGAPGSVGPAGPRGPAGPSGPVGKDGRTGHP 857
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGkdgQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 391-603 1.37e-22

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 101.91  E-value: 1.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 391 GGKGEQGPAGPPGFQGIPGPAGTAGEAGKPGERGIPGEFGIPGPAGPRGERGPPGESGAAGPTGPIGNRGPSGPAGPDGN 470
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 471 KGEPGVVGAPGTAGPSGPSGipgERGAAGIPGPKGEKGEPGIRRDGARGAPGAVGAPGPAGANGDRGEAGPAGPAGPAGP 550
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDG---EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 902951550 551 RGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGTRGDGGPPGATGFPGAAG 603
Cdd:NF038329 274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 237-474 1.27e-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: 98.82  E-value: 1.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 237 GEPGPAGskagPQGIPGPSGEEGKRGSTGEIGPAGPPGPPGIRGSPGSRGIPGADGRAGVMGIPGSRGATGPAGVRGFPG 316
Cdd:NF038329 120 GEPGPAG----PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 317 SPGNIGPAGKEGPVGIPGIDGRPGPTGPAGarnigfPGPKGPTGDNGDKGHAGIAGARGAPGPDGNNGAQGPpqggKGEQ 396
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDG------PAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGP----RGDR 265

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 902951550 397 GPAGPPGFQGIPGPAGTAGEAGKPGERgipGEFGIPGPAGPRGERGPPGESGAAGPTGPIGNRGPSGPAGPDGNKGEP 474
Cdd:NF038329 266 GEAGPDGPDGKDGERGPVGPAGKDGQN---GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 85-329 3.67e-19

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: 91.12  E-value: 3.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  85 GFKGIRGHNGIDGIKGQPGAPGVKGEPGAPGARGIPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGP 164
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 165 KGEIGPVGSPGASGPAGPRGEVGIPGVSGPVGPPGNGAAGIPGVAGAPGIPGPRGIPGPVGAAGATGARGIVGEPGPAGs 244
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG- 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 245 KAGPQGIPGPSGEEGKRGSTGEigpagppgppgirgspgsRGIPGADGRAGVMGIPGSRGATGPAGVRGFPGSPGNIGPA 324
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGL------------------PGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337


                 ....*
gi 902951550 325 GKEGP 329
Cdd:NF038329 338 GKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 7-223 7.05e-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: 81.10  E-value: 7.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550   7 GPRGPPGASGAPGPQGFQGPPGEPGEPGQTGPAGARGPPGPPGKAGEDGHPGKPGRSGERGVVGPQGARGFPGTPGIPGF 86
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  87 KGIRGHNGIDGIKGQPGAPGVKGEPGAPGARGIPGeRGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKG 166
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 902951550 167 EIGPVGSPGASGPAGPRGEVGIPGVSGPVGPpgNGAAGIPGVAGAPGIPGPRGIPGP 223
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQ--NGKDGLPGKDGKDGQPGKDGLPGK 330
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 49-262 8.20e-16

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 80.72  E-value: 8.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  49 GKAGEDGHPGKPGRSGERGVVGPQGARGFPGTPGIPGFKGIRGHNGIDGIKGQPGAPGVKGEPGAPGARGIPGERGRVGA 128
Cdd:NF038329 129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGP 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 129 PGPAGARGSDGSVGPVGPAGPIGSaGPPGFPGAPGPKGEIGPVGSPGASGPAGPRGEVGIPGVSGPVGPpgNGAAGIPGV 208
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK--DGERGPVGP 285

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 902951550 209 AGAPGIPGPRGIPGPVGAAGATGARGIVGEPGPAGsKAGPQGIPGPSGEEGKRG 262
Cdd:NF038329 286 AGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDG-QPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1-218 2.12e-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: 79.56  E-value: 2.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550   1 GPMGIMGPRGPPGASGAPGPQGFQGPPGEPGEPGQTGPAGARGPPGPPGKAGEDGHPGKPGRSGERGVVGPQGARGFPGT 80
Cdd:NF038329 129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGP 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  81 PGIPGFKGIRGHNGIDGIKGQPGaPGVKGEPGAPGARGIPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAgppGFPG 160
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER---GPVG 284

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 902951550 161 APGPKGEIGPVGSPGASGPAGPRGEVGIPGVSGPVGPPG-NGAAGIPGVAGAPGIPGPR 218
Cdd:NF038329 285 PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGkDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 534-788 6.27e-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: 78.02  E-value: 6.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 534 GDRGEAGPAGPAGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGTRGDGGPPGATGFPGAAGrtgppgpsgI 613
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG---------P 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 614 SGPPGPPGPAGKEGIRGPRGDQGPVGRSGETGASGPPGFAGEKTPGPQGIIGAPGFIGIPGSRGERGIPGVAGSVGEPGP 693
Cdd:NF038329 188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 694 IGiagppgargPPGAVGNPGVNGAPGEAGRDGNPGSDGPPGRGHKGERgypgAGAPGPQGPVGPTGKHGNRGEPGPAGVV 773
Cdd:NF038329 268 AG---------PDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQ----NGKDGLPGKDGKDGQPGKDGLPGKDGKD 334

                        250
                 ....*....|....*
gi 902951550 774 GPTGAVGPRGPSGPQ 788
Cdd:NF038329 335 GQPGKPAPKTPEVPQ 349
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1-212 1.41e-13

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 73.79  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550   1 GPMGIMGPRGPPGASGAPGPQGFQGPPGEPGEPGQTGPAGARGPPGPPGKAGEDGHPGKPGRSGERGVVGPQGARGFPGT 80
Cdd:NF038329 135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGP 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  81 PGIPGFKGIRGHNGIDGI-----KGQPGAPGVKGEPGAPGARGIPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGP 155
Cdd:NF038329 215 DGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGK 294

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 902951550 156 PGFPGAPGPKGEIGPVGSPGASGPAGPRGEVGIPGVSGPVGPPGNGAAGIPGVAGAP 212
Cdd:NF038329 295 DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKP 351
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 745-861 1.84e-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: 70.32  E-value: 1.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 745 GAGAPGPQGPVGPTGKHGNRGEPGPAGVVGPTGAVGPRGPSGPQGIRGDKGEPGDKGPRGIPGIKGHNGIQGIPGIAGHH 824
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 902951550 825 GDQGAPGSVGPAGPRGPAGPSGPVGKDGRTGHPGAVG 861
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG 231
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 762-867 2.62e-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: 69.93  E-value: 2.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 762 GNRGEPGPAGVVGPTGAVGPRGPSGPQGIRGDKGEPGDKGPRGIPGIKGHNGIQGIPGIAGHHGDQGAPGSVGPAGPRGP 841
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100
                 ....*....|....*....|....*.
gi 902951550 842 AGPSGPVGKDGRTGHPGAVGPAGIRG 867
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAG 222
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
246-503 8.71e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 58.89  E-value: 8.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 246 AGPQGIPGPSGEEGKRGSTGEIGPAGPPGPPGIRGSPGSRGIPGADGRAGVMGIPGSRGATGPAGVRGF---PGSPGNIG 322
Cdd:COG5164   12 SDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGttpAQNQGGTR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 323 PAGKEGPVGIPGIDGRPGPTGPAGArnigfpgpKGPTGDNGDKGHAgiagARGAPGPDGNNGAQGPPQGGKGEQGPAGPP 402
Cdd:COG5164   92 PAGNTGGTTPAGDGGATGPPDDGGA--------TGPPDDGGSTTPP----SGGSTTPPGDGGSTPPGPGSTGPGGSTTPP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 403 GFQGIPGPAGTAGEAGKPGERG--IPGEFGIPGPAGPRGERGPPGESGAAGPTGPIGNRGPSGPAGPDGN-KGEPGVVGA 479
Cdd:COG5164  160 GDGGSTTPPGPGGSTTPPDDGGstTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGpKDQRPKTNP 239

                        250       260
                 ....*....|....*....|....
gi 902951550 480 PGTAGPSGPSGIPGERGAAGIPGP 503
Cdd:COG5164  240 IERRGPERPEAAALPAELTALEAE 263
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 433-488 4.03e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.49  E-value: 4.03e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 902951550  433 GPAGPRGERGPPGESGAAGPTGPIGNRGPSGPAGPDGNKGEPGVVGAPGTAGPSGP 488
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
91-355 1.00e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 52.34  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  91 GHNGIDGIKGQPGAPGVKGEPGAPGARGIPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPgpkgeiGP 170
Cdd:COG5164   10 GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGT------TP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 171 VGSPGASGPAGPRGEVGIPGVSGPVGPPGNGAAGIPGVAGAPGIPGPRGIPGPVGAAGATGARGIVGEPGPAGSKAGPQG 250
Cdd:COG5164   84 AQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 251 IPGPSGEEGKRGSTGEIGPAGPPGPPGIRGSPGSRGIPGADGRAGVmGIPGSRGATGPAGVRGfpGSPGNIGPAGKEGPV 330
Cdd:COG5164  164 STTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPV-KKDDKNGKGNPPDDRG--GKTGPKDQRPKTNPI 240

                        250       260
                 ....*....|....*....|....*
gi 902951550 331 GIPGIDGRPGPTGPAGARNIGFPGP 355
Cdd:COG5164  241 ERRGPERPEAAALPAELTALEAENR 265
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
507-789 2.33e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 51.18  E-value: 2.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 507 KGEPGIRRDGARGAPGAVGAPGPAGANGDRGEAGPAGPAGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGT 586
Cdd:COG5164    1 TGLYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 587 RGDGGPPGATGFPGAAGRTgppgpsgisgppgppgpagkegirGPRGDQGPVGRSGETGASGPPGFAGEKTPGPQGIIGA 666
Cdd:COG5164   81 TTPAQNQGGTRPAGNTGGT------------------------TPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTP 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 667 PGFIGIPGSRGERGIPGVAGSVGEPGPIGIAGPPGARGPPGAVGNPGVNGAPGEAGRDGNPGSDGPPGRGHKGERGYPGA 746
Cdd:COG5164  137 PGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNG 216

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 902951550 747 GAPGPQGPVGPTGKHGNRGEPGPAGVVGPTGAVGPRGPSGPQG 789
Cdd:COG5164  217 KGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTA 259
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 104-532 2.09e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.44  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 104 APGVKGEPGAPGARGIPGERG-RVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGEIGPVGSPGASGPAGP 182
Cdd:PRK07764 364 LPSASDDERGLLARLERLERRlGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPS 443

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 183 RGEVGIPGVSGPVGPPGNGAAGIPGVAGAPGIPGPRGIPGPVGAAGAtgargivgePGPAGSKAGPQGIPGPSGEEGKRG 262
Cdd:PRK07764 444 PAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAP---------AAAPAAPAAPAAPAGADDAATLRE 514

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 263 STGEIGPAGPPGPPGIRGSPGSRG-IPGADGRAGVMGIPgsrgaTGPAGVR-GFPGSPGNIGPAGKEGPVGIPGIDGRPG 340
Cdd:PRK07764 515 RWPEILAAVPKRSRKTWAILLPEAtVLGVRGDTLVLGFS-----TGGLARRfASPGNAEVLVTALAEELGGDWQVEAVVG 589

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 341 PTGPAGarniGFPGPKGPTGdngdkghAGIAGARGAPGPDGNNGAQGPPQGGKGEQGPAGPPGFQGIPGPAGTAGEAGKP 420
Cdd:PRK07764 590 PAPGAA----GGEGPPAPAS-------SGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVA 658

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 421 GERGIPGEFGIPGPAGPRGERGPPGESGAAGPTGPIGNRGPSG-PAGPDGNKGEPGVVGAPGTAGPSGPSGIPGERGAAG 499
Cdd:PRK07764 659 VPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPaPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDP 738

                        410       420       430
                 ....*....|....*....|....*....|...
gi 902951550 500 IPGPKGEKGEPGIRRDGARGAPGAVGAPGPAGA 532
Cdd:PRK07764 739 VPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPA 771
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 76-132 2.25e-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: 2.25e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 902951550   76 GFPGTPGIPGFKGIRGHNGIDGIKGQPGAPGVKGEPGAPGARGIPGERGRVGAPGPA 132
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 750-804 4.14e-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: 4.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 902951550  750 GPQGPVGPTGKHGNRGEPGPAGVVGPTGAVGPRGPSGPQGIRGDKGEPGDKGPRG 804
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 109-467 1.79e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  109 GEPGAPGARGIPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGEIGPVGSPGASGPAGPRGEVGI 188
Cdd:PHA03307   38 GSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPP 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  189 PGVSGPVGPPGNGAAGIPGVAGAPGIPGPRG----IPGPVGAAGATGARGIVGEPGPAGSKAGPQGIPGPSGEEGKRGST 264
Cdd:PHA03307  118 PPTPPPASPPPSPAPDLSEMLRPVGSPGPPPaaspPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPST 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  265 GEIGPAGPPGPPGIRGSPGSRGIPGADGRAGVMGIPGSRGATGPAGVRGFPGSPGNIGPAGKEGPV--------GIPGID 336
Cdd:PHA03307  198 PPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPItlptriweASGWNG 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  337 GRPGPTGPAGARNIGFPGPKGPTGDNGDKGHAGIAGARGAPGPDGNNGAQGPPQGGKGEQGPAGPPGFQGIPGPAGTAG- 415
Cdd:PHA03307  278 PSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPp 357

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 902951550  416 --EAGKPGERGIPGEFGIPGPAGPRGERGPPGESGAAGPTGPIGNRGPSGPAGP 467
Cdd:PHA03307  358 ppADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGR 411
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 314-537 1.12e-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: 111.15  E-value: 1.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 314 FPGSPGNIGPAGKEGPVGIPGIDGRPGPTGPAGARniGFPGPKGPTGDNGDKGHAGIAGARGAPGPDGNNGAQGPPqGGK 393
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPA--GPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA-GEK 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 394 GEQGPAGPPGFQGIPGPAGTAGEAGKPGERGIPGEFGIPGPaGPRGERGPPGESGAAGPTGPIGNRGPSGPAGPDGNKGE 473
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP 270

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 902951550 474 PGVVGAPGTAGPSGPSGIPGERGAAGIPGPKGEKGEPGirRDGARGAPGAVGAPGPAGANGDRG 537
Cdd:NF038329 271 DGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG--KDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 262-504 3.20e-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: 109.61  E-value: 3.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 262 GSTGEIGPAGPpgppgirgspgsRGIPGADGRAGVMGIPGSRGATGPAGVRGFPGSPGNIGPAGKEGPVGIPGIDGRPGP 341
Cdd:NF038329 117 GEKGEPGPAGP------------AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 342 TGPAGARniGFPGPKGPTGDNGDKGHAGIAGARGAPGPDGNNGAQGPPqgGKGEQGPAGPPGFQGIPGPAGTAGEAGKPG 421
Cdd:NF038329 185 KGPAGEK--GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPA--GDGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 422 ERGIPGEFGIPGPAGPRGERGPPGESGAAGPTGPIGNRGPSGPAGPDGNKGEPGVVGAPGTAGPSGPSGIPGERGAAGIP 501
Cdd:NF038329 261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340


                 ...
gi 902951550 502 GPK 504
Cdd:NF038329 341 APK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 639-857 3.31e-23

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: 103.83  E-value: 3.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 639 GRSGETGASGPPGFAGEKTP-GPQGIIGAPGFIGIPGSRGERGIPGVAGSVGEPGPIGIAGPPGARGPPGAVGNPGVNGA 717
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPrGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 718 PGEAGRDGNPGSDGPPG-RGHKGERGYPGAGAPGPQGPVGPTGKHGNRGEPGPAGVVGPTGAVGPRGPSGPQGIRGDKGE 796
Cdd:NF038329 197 RGETGPAGEQGPAGPAGpDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 902951550 797 PGDKGPRGIPGIKGHNGIQGIPGIAG---HHGDQGAPGSVGPAGPRGPAGPSGPVGKDGRTGHP 857
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGkdgQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 391-603 1.37e-22

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 101.91  E-value: 1.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 391 GGKGEQGPAGPPGFQGIPGPAGTAGEAGKPGERGIPGEFGIPGPAGPRGERGPPGESGAAGPTGPIGNRGPSGPAGPDGN 470
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 471 KGEPGVVGAPGTAGPSGPSGipgERGAAGIPGPKGEKGEPGIRRDGARGAPGAVGAPGPAGANGDRGEAGPAGPAGPAGP 550
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDG---EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 902951550 551 RGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGTRGDGGPPGATGFPGAAG 603
Cdd:NF038329 274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 237-474 1.27e-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: 98.82  E-value: 1.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 237 GEPGPAGskagPQGIPGPSGEEGKRGSTGEIGPAGPPGPPGIRGSPGSRGIPGADGRAGVMGIPGSRGATGPAGVRGFPG 316
Cdd:NF038329 120 GEPGPAG----PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 317 SPGNIGPAGKEGPVGIPGIDGRPGPTGPAGarnigfPGPKGPTGDNGDKGHAGIAGARGAPGPDGNNGAQGPpqggKGEQ 396
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDG------PAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGP----RGDR 265

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 902951550 397 GPAGPPGFQGIPGPAGTAGEAGKPGERgipGEFGIPGPAGPRGERGPPGESGAAGPTGPIGNRGPSGPAGPDGNKGEP 474
Cdd:NF038329 266 GEAGPDGPDGKDGERGPVGPAGKDGQN---GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 85-329 3.67e-19

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: 91.12  E-value: 3.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  85 GFKGIRGHNGIDGIKGQPGAPGVKGEPGAPGARGIPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGP 164
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 165 KGEIGPVGSPGASGPAGPRGEVGIPGVSGPVGPPGNGAAGIPGVAGAPGIPGPRGIPGPVGAAGATGARGIVGEPGPAGs 244
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG- 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 245 KAGPQGIPGPSGEEGKRGSTGEigpagppgppgirgspgsRGIPGADGRAGVMGIPGSRGATGPAGVRGFPGSPGNIGPA 324
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGL------------------PGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337


                 ....*
gi 902951550 325 GKEGP 329
Cdd:NF038329 338 GKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 7-223 7.05e-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: 81.10  E-value: 7.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550   7 GPRGPPGASGAPGPQGFQGPPGEPGEPGQTGPAGARGPPGPPGKAGEDGHPGKPGRSGERGVVGPQGARGFPGTPGIPGF 86
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  87 KGIRGHNGIDGIKGQPGAPGVKGEPGAPGARGIPGeRGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKG 166
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 902951550 167 EIGPVGSPGASGPAGPRGEVGIPGVSGPVGPpgNGAAGIPGVAGAPGIPGPRGIPGP 223
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQ--NGKDGLPGKDGKDGQPGKDGLPGK 330
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 49-262 8.20e-16

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 80.72  E-value: 8.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  49 GKAGEDGHPGKPGRSGERGVVGPQGARGFPGTPGIPGFKGIRGHNGIDGIKGQPGAPGVKGEPGAPGARGIPGERGRVGA 128
Cdd:NF038329 129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGP 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 129 PGPAGARGSDGSVGPVGPAGPIGSaGPPGFPGAPGPKGEIGPVGSPGASGPAGPRGEVGIPGVSGPVGPpgNGAAGIPGV 208
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK--DGERGPVGP 285

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 902951550 209 AGAPGIPGPRGIPGPVGAAGATGARGIVGEPGPAGsKAGPQGIPGPSGEEGKRG 262
Cdd:NF038329 286 AGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDG-QPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1-218 2.12e-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: 79.56  E-value: 2.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550   1 GPMGIMGPRGPPGASGAPGPQGFQGPPGEPGEPGQTGPAGARGPPGPPGKAGEDGHPGKPGRSGERGVVGPQGARGFPGT 80
Cdd:NF038329 129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGP 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  81 PGIPGFKGIRGHNGIDGIKGQPGaPGVKGEPGAPGARGIPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAgppGFPG 160
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER---GPVG 284

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 902951550 161 APGPKGEIGPVGSPGASGPAGPRGEVGIPGVSGPVGPPG-NGAAGIPGVAGAPGIPGPR 218
Cdd:NF038329 285 PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGkDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 534-788 6.27e-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: 78.02  E-value: 6.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 534 GDRGEAGPAGPAGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGTRGDGGPPGATGFPGAAGrtgppgpsgI 613
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG---------P 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 614 SGPPGPPGPAGKEGIRGPRGDQGPVGRSGETGASGPPGFAGEKTPGPQGIIGAPGFIGIPGSRGERGIPGVAGSVGEPGP 693
Cdd:NF038329 188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 694 IGiagppgargPPGAVGNPGVNGAPGEAGRDGNPGSDGPPGRGHKGERgypgAGAPGPQGPVGPTGKHGNRGEPGPAGVV 773
Cdd:NF038329 268 AG---------PDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQ----NGKDGLPGKDGKDGQPGKDGLPGKDGKD 334

                        250
                 ....*....|....*
gi 902951550 774 GPTGAVGPRGPSGPQ 788
Cdd:NF038329 335 GQPGKPAPKTPEVPQ 349
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1-212 1.41e-13

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 73.79  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550   1 GPMGIMGPRGPPGASGAPGPQGFQGPPGEPGEPGQTGPAGARGPPGPPGKAGEDGHPGKPGRSGERGVVGPQGARGFPGT 80
Cdd:NF038329 135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGP 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  81 PGIPGFKGIRGHNGIDGI-----KGQPGAPGVKGEPGAPGARGIPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGP 155
Cdd:NF038329 215 DGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGK 294

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 902951550 156 PGFPGAPGPKGEIGPVGSPGASGPAGPRGEVGIPGVSGPVGPPGNGAAGIPGVAGAP 212
Cdd:NF038329 295 DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKP 351
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 745-861 1.84e-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: 70.32  E-value: 1.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 745 GAGAPGPQGPVGPTGKHGNRGEPGPAGVVGPTGAVGPRGPSGPQGIRGDKGEPGDKGPRGIPGIKGHNGIQGIPGIAGHH 824
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 902951550 825 GDQGAPGSVGPAGPRGPAGPSGPVGKDGRTGHPGAVG 861
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG 231
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 762-867 2.62e-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: 69.93  E-value: 2.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 762 GNRGEPGPAGVVGPTGAVGPRGPSGPQGIRGDKGEPGDKGPRGIPGIKGHNGIQGIPGIAGHHGDQGAPGSVGPAGPRGP 841
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100
                 ....*....|....*....|....*.
gi 902951550 842 AGPSGPVGKDGRTGHPGAVGPAGIRG 867
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAG 222
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
246-503 8.71e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 58.89  E-value: 8.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 246 AGPQGIPGPSGEEGKRGSTGEIGPAGPPGPPGIRGSPGSRGIPGADGRAGVMGIPGSRGATGPAGVRGF---PGSPGNIG 322
Cdd:COG5164   12 SDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGttpAQNQGGTR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 323 PAGKEGPVGIPGIDGRPGPTGPAGArnigfpgpKGPTGDNGDKGHAgiagARGAPGPDGNNGAQGPPQGGKGEQGPAGPP 402
Cdd:COG5164   92 PAGNTGGTTPAGDGGATGPPDDGGA--------TGPPDDGGSTTPP----SGGSTTPPGDGGSTPPGPGSTGPGGSTTPP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 403 GFQGIPGPAGTAGEAGKPGERG--IPGEFGIPGPAGPRGERGPPGESGAAGPTGPIGNRGPSGPAGPDGN-KGEPGVVGA 479
Cdd:COG5164  160 GDGGSTTPPGPGGSTTPPDDGGstTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGpKDQRPKTNP 239

                        250       260
                 ....*....|....*....|....
gi 902951550 480 PGTAGPSGPSGIPGERGAAGIPGP 503
Cdd:COG5164  240 IERRGPERPEAAALPAELTALEAE 263
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
388-654 1.01e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 55.42  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 388 PPQGGKGEQGPAGPPGFQGIPGPAGTAGEAGKPGERGIPGEFGIPGPAGPRGERGPPGESGAagpTGPIGNRGPSGPAGP 467
Cdd:COG5164   10 GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGA---TGPAQNQGGTTPAQN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 468 DGNKGEPGVVGAPGTAGPSGPSGIPGERGAAGIPGPKGEKGEPGIRRDGARGAPGAV----GAPGPAGANGDRGEAGPAG 543
Cdd:COG5164   87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTppgpGSTGPGGSTTPPGDGGSTT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 544 PAGPAGPRGSPGERGEVGPAGPngfagpagaagqpgakGERGTRGDGGPPGATGFPGAAGRTgppgpSGISGPPGPPGPA 623
Cdd:COG5164  167 PPGPGGSTTPPDDGGSTTPPNK----------------GETGTDIPTGGTPRQGPDGPVKKD-----DKNGKGNPPDDRG 225

                        250       260       270
                 ....*....|....*....|....*....|.
gi 902951550 624 GKEGIRGPRGDQGPVGRSGETGASGPPGFAG 654
Cdd:COG5164  226 GKTGPKDQRPKTNPIERRGPERPEAAALPAE 256
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 433-488 4.03e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.49  E-value: 4.03e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 902951550  433 GPAGPRGERGPPGESGAAGPTGPIGNRGPSGPAGPDGNKGEPGVVGAPGTAGPSGP 488
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 394-450 6.15e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.10  E-value: 6.15e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 902951550  394 GEQGPAGPPGFQGIPGPAGTAGEAGKPGERGIPGEFGIPGPAGPRGERGPPGESGAA 450
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 427-481 7.12e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.72  E-value: 7.12e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 902951550  427 GEFGIPGPAGPRGERGPPGESGAAGPTGPIGNRGPSGPAGPDGNKGEPGVVGAPG 481
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
91-355 1.00e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 52.34  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  91 GHNGIDGIKGQPGAPGVKGEPGAPGARGIPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPgpkgeiGP 170
Cdd:COG5164   10 GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGT------TP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 171 VGSPGASGPAGPRGEVGIPGVSGPVGPPGNGAAGIPGVAGAPGIPGPRGIPGPVGAAGATGARGIVGEPGPAGSKAGPQG 250
Cdd:COG5164   84 AQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 251 IPGPSGEEGKRGSTGEIGPAGPPGPPGIRGSPGSRGIPGADGRAGVmGIPGSRGATGPAGVRGfpGSPGNIGPAGKEGPV 330
Cdd:COG5164  164 STTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPV-KKDDKNGKGNPPDDRG--GKTGPKDQRPKTNPI 240

                        250       260
                 ....*....|....*....|....*
gi 902951550 331 GIPGIDGRPGPTGPAGARNIGFPGP 355
Cdd:COG5164  241 ERRGPERPEAAALPAELTALEAENR 265
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 430-485 1.16e-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: 46.33  E-value: 1.16e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 902951550  430 GIPGPAGPRGERGPPGESGAAGPTGPIGNRGPSGPAGPDGNKGEPGVVGAPGTAGP 485
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 409-465 1.33e-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: 45.95  E-value: 1.33e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 902951550  409 GPAGTAGEAGKPGERGIPGEFGIPGPAGPRGERGPPGESGAAGPTGPIGNRGPSGPA 465
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 457-511 1.37e-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: 45.95  E-value: 1.37e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 902951550  457 GNRGPSGPAGPDGNKGEPGVVGAPGTAGPSGPSGIPGERGAAGIPGPKGEKGEPG 511
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
507-789 2.33e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 51.18  E-value: 2.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 507 KGEPGIRRDGARGAPGAVGAPGPAGANGDRGEAGPAGPAGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGT 586
Cdd:COG5164    1 TGLYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 587 RGDGGPPGATGFPGAAGRTgppgpsgisgppgppgpagkegirGPRGDQGPVGRSGETGASGPPGFAGEKTPGPQGIIGA 666
Cdd:COG5164   81 TTPAQNQGGTRPAGNTGGT------------------------TPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTP 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 667 PGFIGIPGSRGERGIPGVAGSVGEPGPIGIAGPPGARGPPGAVGNPGVNGAPGEAGRDGNPGSDGPPGRGHKGERGYPGA 746
Cdd:COG5164  137 PGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNG 216

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 902951550 747 GAPGPQGPVGPTGKHGNRGEPGPAGVVGPTGAVGPRGPSGPQG 789
Cdd:COG5164  217 KGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTA 259
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 418-474 3.52e-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: 44.79  E-value: 3.52e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 902951550  418 GKPGERGIPGEFGIPGPAGPRGERGPPGESGAAGPTGPIGNRGPSGPAGPDGNKGEP 474
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 415-469 3.74e-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: 44.79  E-value: 3.74e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 902951550  415 GEAGKPGERGIPGEFGIPGPAGPRGERGPPGESGAAGPTGPIGNRGPSGPAGPDG 469
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 397-455 4.08e-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: 44.79  E-value: 4.08e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 902951550  397 GPAGPPGFQGIPGPAGTAGEAGKPGERGIPGEfgiPGPAGPRGERGPPGESGAAGPTGP 455
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGE---PGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 445-499 4.97e-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: 44.41  E-value: 4.97e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 902951550  445 GESGAAGPTGPIGNRGPSGPAGPDGNKGEPGVVGAPGTAGPSGPSGIPGERGAAG 499
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 391-446 1.12e-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: 43.64  E-value: 1.12e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 902951550  391 GGKGEQGPAGPPGFQGIPGPAGTAGEAGKPGERGIPGEFGIPGPAGPRGERGPPGE 446
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 424-480 1.57e-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: 43.25  E-value: 1.57e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 902951550  424 GIPGEFGIPGPAGPRGERGPPGESGAAGPTGPIGNRGPSGPAGPDGNKGEPGVVGAP 480
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 104-532 2.09e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.44  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 104 APGVKGEPGAPGARGIPGERG-RVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGEIGPVGSPGASGPAGP 182
Cdd:PRK07764 364 LPSASDDERGLLARLERLERRlGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPS 443

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 183 RGEVGIPGVSGPVGPPGNGAAGIPGVAGAPGIPGPRGIPGPVGAAGAtgargivgePGPAGSKAGPQGIPGPSGEEGKRG 262
Cdd:PRK07764 444 PAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAP---------AAAPAAPAAPAAPAGADDAATLRE 514

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 263 STGEIGPAGPPGPPGIRGSPGSRG-IPGADGRAGVMGIPgsrgaTGPAGVR-GFPGSPGNIGPAGKEGPVGIPGIDGRPG 340
Cdd:PRK07764 515 RWPEILAAVPKRSRKTWAILLPEAtVLGVRGDTLVLGFS-----TGGLARRfASPGNAEVLVTALAEELGGDWQVEAVVG 589

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 341 PTGPAGarniGFPGPKGPTGdngdkghAGIAGARGAPGPDGNNGAQGPPQGGKGEQGPAGPPGFQGIPGPAGTAGEAGKP 420
Cdd:PRK07764 590 PAPGAA----GGEGPPAPAS-------SGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVA 658

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 421 GERGIPGEFGIPGPAGPRGERGPPGESGAAGPTGPIGNRGPSG-PAGPDGNKGEPGVVGAPGTAGPSGPSGIPGERGAAG 499
Cdd:PRK07764 659 VPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPaPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDP 738

                        410       420       430
                 ....*....|....*....|....*....|...
gi 902951550 500 IPGPKGEKGEPGIRRDGARGAPGAVGAPGPAGA 532
Cdd:PRK07764 739 VPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPA 771
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 76-132 2.25e-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: 2.25e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 902951550   76 GFPGTPGIPGFKGIRGHNGIDGIKGQPGAPGVKGEPGAPGARGIPGERGRVGAPGPA 132
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 750-804 4.14e-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: 4.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 902951550  750 GPQGPVGPTGKHGNRGEPGPAGVVGPTGAVGPRGPSGPQGIRGDKGEPGDKGPRG 804
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 94-149 5.90e-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: 5.90e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 902951550   94 GIDGIKGQPGAPGVKGEPGAPGARGIPGERGRVGAPGPAGARGSDGSVGPVGPAGP 149
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 746-798 6.77e-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: 41.33  E-value: 6.77e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 902951550  746 AGAPGPQGPVGPTGKHGNRGEPGPAGVVGPTGAVGPRGPSGPQGIRGDKGEPG 798
Cdd:pfam01391   3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
7-265 7.30e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 46.18  E-value: 7.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550   7 GPRGPPGASGAPGPQGFQGPPGEPGEPGQTGPAGARgppgppgkagedGHPGKPGRSGERGVVGPQGARGFPGTPGIPGF 86
Cdd:COG5164    7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNT------------GGTRPAQNQGSTTPAGNTGGTRPAGNQGATGP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  87 KGIRGHNGIDGIKGQPGAPGVKGEPGAPGARGIPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKG 166
Cdd:COG5164   75 AQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 167 EIGPVGSPGASGPAGPRGEVGIPGVSGPVGPPGNGAAGIP---GVAGAPGIPGPRGIPGPVGAAGATGARGIVGEPGPAG 243
Cdd:COG5164  155 STTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDiptGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQR 234

                        250       260
                 ....*....|....*....|..
gi 902951550 244 SKAGPQGIPGPSGEEGKRGSTG 265
Cdd:COG5164  235 PKTNPIERRGPERPEAAALPAE 256
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 100-153 7.47e-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: 7.47e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 902951550  100 GQPGAPGVKGEPGAPGARGIPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSA 153
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 301-494 9.45e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 9.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 301 GSRGATGPAGVRGFPGSPGNIG---PAGKEGPVGIPGIDGRPGPTGPAGARNIGFPGPKGPTgdnGDKGHAGIAGARGAP 377
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEaarPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPE---HHPKHVAVPDASDGG 666

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 378 GPDGNNGAQGPPQGGKGEQGPAGPPGFQGIPGPAGTAGEAGKPGERGIPGEFGIPgPAGPRGERGPPGESGAAGPTGPIG 457
Cdd:PRK07764 667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQP-PQAAQGASAPSPAADDPVPLPPEP 745

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 902951550 458 NRGPSGPAGPDGNKGEPGVVGAPGTAGPSGPSGIPGE 494
Cdd:PRK07764 746 DDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 481-538 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
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 902951550  481 GTAGPSGPSGIPGERGAAGIPGPKGEKGEPGIRrdGARGAPGAVGAPGPAGANGDRGE 538
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEP--GPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 451-506 1.69e-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: 40.17  E-value: 1.69e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 902951550  451 GPTGPIGNRGPSGPAGPDGNKGEPGVVGAPGTAGPSGPSGIPGERGAAGIPGPKGE 506
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 765-819 1.79e-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: 40.17  E-value: 1.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 902951550  765 GEPGPAGVVGPTGAVGPRGPSGPQGIRGDKGEPGDKGPRGIPGIKGHNGIQGIPG 819
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 384-441 3.57e-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: 3.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 902951550  384 GAQGPPqGGKGEQGPAGPPGFQGIPGPAGTAGEAGKPGERGIPGEFGIPGPAGPRGER 441
Cdd:pfam01391   1 GPPGPP-GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
314-526 4.12e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 44.07  E-value: 4.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 314 FPGSPGNIGPAGKEGPVGIPGIDGRPGPTGPAGARNIGFPGPKGPTGDNGDKGHAGIAGARGAPGPDGNNGAQGPPQGGK 393
Cdd:PRK07003 358 FEPAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATAD 437

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 394 GEQGPAGPPGFQGIPGPAGTAGEAGkpgergipgefgiPGPAGPRGERGPPGESGAAGPTGPIGNRGPSGPAGPDGNKGE 473
Cdd:PRK07003 438 RGDDAADGDAPVPAKANARASADSR-------------CDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATP 504

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 902951550 474 PGVVGAPGTAGPSGPSgipgERGAAGIPGPKGEKGEPGIRRDGARgAPGAVGA 526
Cdd:PRK07003 505 AAVPDARAPAAASRED----APAAAAPPAPEARPPTPAAAAPAAR-AGGAAAA 552
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 79-135 6.64e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 6.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 902951550   79 GTPGIPGFKGIRGHNGIDGIKGQPGAPGVKGEPGAPGARGIPGERGRVGAPGPAGAR 135
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 366-490 9.40e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 42.74  E-value: 9.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 366 GHAGIAGARGAPGPDGNNGAQGPPQGGKGEQGPAGPPGFQGIPGPAGTAGEAGKPGERgIPGEfgiPGPAGPRGERGPPG 445
Cdd:PRK14959 376 GGASAPSGSAAEGPASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPAPSAAPSPR-VPWD---DAPPAPPRSGIPPR 451

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 902951550 446 ESGAAGPTGPIgnrgPSGPAGPDGNKGEPGVVGAPGTAGPSGPSG 490
Cdd:PRK14959 452 PAPRMPEASPV----PGAPDSVASASDAPPTLGDPSDTAEHTPSG 492
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 409-596 9.74e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 9.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 409 GPAGTAGEAGKPGERGIPGEFGIPGPAGPRGERGPPGESGAAGPTGPignRGPSGPAGPDGNKGEPGVVGAPGTAGPSGP 488
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAP---AEASAAPAPGVAAPEHHPKHVAVPDASDGG 666

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 489 SGIPGERGAAGiPGPKGEKGEPGIRRDGARGAPGAVGAPGPAGANGDRGEAGPAGPAGPAGPRGSPGERGEVGPAGPNGF 568
Cdd:PRK07764 667 DGWPAKAGGAA-PAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEP 745

                        170       180
                 ....*....|....*....|....*...
gi 902951550 569 AGPAGAAGQPGAKGERGTRGDGGPPGAT 596
Cdd:PRK07764 746 DDPPDPAGAPAQPPPPPAPAPAAAPAAA 773
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 813-867 9.93e-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: 9.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 902951550  813 GIQGIPGIAGHHGDQGAPGSVGPAGPRGPAGPSGPVGKDGRTGHPGAVGPAGIRG 867
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 423-591 1.01e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.97  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 423 RGIPGEFGIPGPAGPR-GE--------RGPPGESGAAGPTGPIGNRGPSGPAGPDGNKGEPGVVGAPGTAGPSGPSGIPG 493
Cdd:PRK12678  32 RALAKQLGIKGTSGMRkGEliaaikeaRGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 494 ERGAAGIPGPKGEKGEPGIRRDGARGAPGAVGAPGPAGANGDRGEAGPAGPAGPAGPRGSPGERGEVGPAGPNGFAGPAG 573
Cdd:PRK12678 112 AAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERG 191

                        170
                 ....*....|....*...
gi 902951550 574 AAGQPGAKGERGTRGDGG 591
Cdd:PRK12678 192 RREERGRDGDDRDRRDRR 209
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 293-538 1.38e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 293 RAGVMGIPGSRGATGPAGVRGFPGSPGNIGPAGKEGPVGIPGIDGRPGPTGPAGARNIGFPGPKGPTGDngdKGHAGIAG 372
Cdd:PRK07764 585 EAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHH---PKHVAVPD 661

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 373 ARGAPGPDGNNGAQGPPQGGKGEQGPAGPPGFQGIPGPAGTAGEAGKPgeRGIPGEFGIPGPAGPRGERGPPGESGAAGP 452
Cdd:PRK07764 662 ASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATP--PAGQADDPAAQPPQAAQGASAPSPAADDPV 739

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 453 TGPIGNRGPSGPAGPDGNKGEPGVVGAPGTAGPSGPSGIPGErgaagipgpkgekgepgirrdgargAPGAVGAPGPAGA 532
Cdd:PRK07764 740 PLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSE-------------------------EEEMAEDDAPSMD 794


                 ....*.
gi 902951550 533 NGDRGE 538
Cdd:PRK07764 795 DEDRRD 800
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 109-467 1.79e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  109 GEPGAPGARGIPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGEIGPVGSPGASGPAGPRGEVGI 188
Cdd:PHA03307   38 GSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPP 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  189 PGVSGPVGPPGNGAAGIPGVAGAPGIPGPRG----IPGPVGAAGATGARGIVGEPGPAGSKAGPQGIPGPSGEEGKRGST 264
Cdd:PHA03307  118 PPTPPPASPPPSPAPDLSEMLRPVGSPGPPPaaspPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPST 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  265 GEIGPAGPPGPPGIRGSPGSRGIPGADGRAGVMGIPGSRGATGPAGVRGFPGSPGNIGPAGKEGPV--------GIPGID 336
Cdd:PHA03307  198 PPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPItlptriweASGWNG 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550  337 GRPGPTGPAGARNIGFPGPKGPTGDNGDKGHAGIAGARGAPGPDGNNGAQGPPQGGKGEQGPAGPPGFQGIPGPAGTAG- 415
Cdd:PHA03307  278 PSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPp 357

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 902951550  416 --EAGKPGERGIPGEFGIPGPAGPRGERGPPGESGAAGPTGPIGNRGPSGPAGP 467
Cdd:PHA03307  358 ppADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGR 411
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 340-402 1.87e-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: 1.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 902951550  340 GPTGPAGARniGFPGPKGPTGDNGDKGHAGIAGARGAPGPDGNNGAQGPPqggkGEQGPAGPP 402
Cdd:pfam01391   1 GPPGPPGPP--GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP----GAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 102-258 2.28e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902951550 102 PGAPGVKGEPGAPGARGIPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGEIGPVGSPGASGPAG 181
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 902951550 182 PRGEVGIPGVSGPVGPPGNGAAGIPGVAGAPGIPGPRGIPGPVGAAGATGARGIVGEPGPAGSKAGPQGIPGPSGEE 258
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD 746
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 286-334 4.44e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 4.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 902951550  286 GIPGADGRAGVMGIPGSRGATGPAGVRGFPGSPGNIGPAGKEGPVGIPG 334
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 298-358 6.33e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.55  E-value: 6.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 902951550  298 GIPGSRGATGPAGVRGFPGSPGNIGPAGKEGPVGIPGIDGRPGPTGPAGArnigfPGPKGP 358
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA-----PGAPGP 56
 
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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