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Conserved domains on  [gi|1958777315|ref|XP_038966234|]
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collagen alpha-2(IX) chain isoform X1 [Rattus norvegicus]

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 ...
 21-259 6.41e-33

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: 129.64  E-value: 6.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  21 GPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGS 100
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 101 AGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQqgfpgisGPPGKEGEPGPRGETGPQGIMGEKGDQGERGPVGQPG 180
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958777315 181 PQGRQGPKGEQGSPGIPGPQGLpgiKGDKGSPGKTGPRggvGDPGVAGLPGEKGEKGLSGEPGLKGQQGVRGEPGYPGP 259
Cdd:NF038329  270 PDGPDGKDGERGPVGPAGKDGQ---NGKDGLPGKDGKD---GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 171-442 2.43e-12

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 68.39  E-value: 2.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 171 GERGPVGQPGPQGRQGPKGEQGSPGIPGPQGLPGIKGDKGSPGKTGPRGGVGDPGVAGLPGEKGEKGLSGEPGLKGQQGV 250
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 251 RGEPGYPGPSGDAGAPGVQGYPGLPGPRGLVGDRGvpgqpgrqgvvgraasdqhivdvvlkmiqeqlaevavsakrealg 330
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG--------------------------------------------- 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 331 atgmvglpgppgppgypgkqgpNGHPGPRGIPGIVGAVGQIGNTGPKGKrgekgdqgemgrghpgmpgppgipglpgrpg 410
Cdd:NF038329  232 ----------------------DGQQGPDGDPGPTGEDGPQGPDGPAGK------------------------------- 258

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958777315 411 qaiNGKDGDRGSPGAPGEAGRPGRPGPVGLPG 442
Cdd:NF038329  259 ---DGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 21-259 6.41e-33

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: 129.64  E-value: 6.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  21 GPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGS 100
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 101 AGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQqgfpgisGPPGKEGEPGPRGETGPQGIMGEKGDQGERGPVGQPG 180
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958777315 181 PQGRQGPKGEQGSPGIPGPQGLpgiKGDKGSPGKTGPRggvGDPGVAGLPGEKGEKGLSGEPGLKGQQGVRGEPGYPGP 259
Cdd:NF038329  270 PDGPDGKDGERGPVGPAGKDGQ---NGKDGLPGKDGKD---GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 57-282 1.29e-31

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: 125.79  E-value: 1.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  57 GEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQ 136
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 137 QGFPGISGPPGKEGEPGPRGETGPQGIMGEKGDQGErgpvGQPGPQGRQGPKGEQGSPGIPGPQGLPGIKGDKGSPGKTG 216
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958777315 217 PRGGVGDPGVAGLPGEKGEKGLSGEPGLKGQQGVRGEPGYPGPSGDAGAPGVQGYPGLPGPRGLVG 282
Cdd:NF038329  273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 8-218 1.02e-28

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 117.70  E-value: 1.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315   8 KGPQGIRGYPGMAGPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDG 87
Cdd:NF038329  134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAG 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  88 KDGTPGIPGMKGSAGQVGRpGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGFPGISGPPGKEGEPGPRGETGPQGIMGEK 167
Cdd:NF038329  214 PDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN 292

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958777315 168 GDQGERGPVGQPGPQGRQGPKGEQGSPGIPGPQGLPGIKGDKGSPGKTGPR 218
Cdd:NF038329  293 GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 105-298 2.40e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 110.77  E-value: 2.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 105 GRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGFPGISGPPGKEGEPGPRGETGPQGIMGEKGDQGERGPVGQPGPQGR 184
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 185 QGPKGEQGSPGIPGPQGLPGIKGDKGSPGKTGPRGGvGDPGVAGLPGEKGEKGLSGEPGLKGQQGVRGEPGYPGPSGDAG 264
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1958777315 265 APGVQGYPGLPGPRGLVGDRGVPGQPGRQGVVGR 298
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK 309
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 127-437 3.29e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 95.74  E-value: 3.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 127 GPGDKGEPGQQGFPGISGPPGKEGEPGPRGETGPQGIMGEKGDQGERGPVGQPGPQGRQGPKGEQGSPGIPGPQGLPGIK 206
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 207 GDKGSPGKTGPRGGVGDPGVAGLPGEKGEKGLSGEPGlKGQQGVRGEPGYPGPSGDAGAPGVQGYPGLPGPRGLVGDRGV 286
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 287 PGQPGRQGVVGRAASDqhivdvvlkmiqeqlaevavsakrealgatgmvglpgppgppgypgkqgpnGHPGPRGIPGIVG 366
Cdd:NF038329  274 DGKDGERGPVGPAGKD---------------------------------------------------GQNGKDGLPGKDG 302

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958777315 367 AVGQIGNTGPKGKRGEkgdqgemgrghpgmpgppgipglpgrpgqaiNGKDGDRGSPGAPGEAGRPGRPGP 437
Cdd:NF038329  303 KDGQNGKDGLPGKDGK-------------------------------DGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 8-204 1.63e-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: 90.73  E-value: 1.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315   8 KGPQGIRGYPGMAGPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGaRGPQGITGPKGTTGPPGIDG 87
Cdd:NF038329  173 QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQG 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  88 KDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGfpgISGPPGKEGEPGPRGETGPQGIMGEK 167
Cdd:NF038329  252 PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG---KDGQNGKDGLPGKDGKDGQPGKDGLP 328

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958777315 168 GDQGERGPVGQPGPQGRQGPKGEQGSPGIPGPQGLPG 204
Cdd:NF038329  329 GKDGKDGQPGKPAPKTPEVPQKPDTAPHTPKTPQIPG 365
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 171-442 2.43e-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: 68.39  E-value: 2.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 171 GERGPVGQPGPQGRQGPKGEQGSPGIPGPQGLPGIKGDKGSPGKTGPRGGVGDPGVAGLPGEKGEKGLSGEPGLKGQQGV 250
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 251 RGEPGYPGPSGDAGAPGVQGYPGLPGPRGLVGDRGvpgqpgrqgvvgraasdqhivdvvlkmiqeqlaevavsakrealg 330
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG--------------------------------------------- 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 331 atgmvglpgppgppgypgkqgpNGHPGPRGIPGIVGAVGQIGNTGPKGKrgekgdqgemgrghpgmpgppgipglpgrpg 410
Cdd:NF038329  232 ----------------------DGQQGPDGDPGPTGEDGPQGPDGPAGK------------------------------- 258

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958777315 411 qaiNGKDGDRGSPGAPGEAGRPGRPGPVGLPG 442
Cdd:NF038329  259 ---DGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 4-123 7.64e-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: 66.85  E-value: 7.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315   4 PLENKGPQGIRGYPGMA-----GPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKG 78
Cdd:NF038329  214 PDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958777315  79 TTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPG 123
Cdd:NF038329  294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
9-242 5.88e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 55.04  E-value: 5.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315   9 GPQGIRGYPGMAGPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGP---QGITGPKGTTGPPGI 85
Cdd:COG5164    22 GSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPaqnQGGTRPAGNTGGTTP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  86 DGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGFPGISGPPGKEGEPGPRGETGPQGIMG 165
Cdd:COG5164   102 AGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGG 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 166 EK--GDQGERGPVGQPGPQGRQGPKGEQGSPG----IPGPQGLPGIKGDKGSPGKTGPRGGVGDPGVAGLPGEKGEKGLS 239
Cdd:COG5164   182 STtpPNKGETGTDIPTGGTPRQGPDGPVKKDDkngkGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTALE 261


                  ...
gi 1958777315 240 GEP 242
Cdd:COG5164   262 AEN 264
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 144-199 4.76e-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: 4.76e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958777315 144 GPPGKEGEPGPRGETGPQGIMGEKGDQGERGPVGQPGPQGRQGPKGEQGSPGIPGP 199
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 240-294 5.14e-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: 40.94  E-value: 5.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958777315 240 GEPGLKGQQGVRGEPGYPGPSGDAGAPGVQGYPGLPGPRGLVGDRGVPGQPGRQG 294
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 81-332 5.54e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 5.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  81 GPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGdkGEPGQQGFPGISGPPGKEGEPGPRGETGP 160
Cdd:PRK07764  589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPA--EASAAPAPGVAAPEHHPKHVAVPDASDGG 666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 161 QGIMGEKGDQGERGPVGQPGPQGRQGPKGEQGSPGIPGPqglpgikgDKGSPGKTGPRGGVGDPGVAGLPGEKGEKGLSG 240
Cdd:PRK07764  667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAP--------AATPPAGQADDPAAQPPQAAQGASAPSPAADDP 738

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 241 EPglkgqqgvrgEPGYPGPSGDAGAPGVQGYPGLPGPRGlvgdrgvPGQPGRQGVVGRAASDQHIVDVVLKMIQEQL--- 317
Cdd:PRK07764  739 VP----------LPPEPDDPPDPAGAPAQPPPPPAPAPA-------AAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRrda 801

                         250
                  ....*....|....*
gi 1958777315 318 AEVAVSAKREALGAT 332
Cdd:PRK07764  802 EEVAMELLEEELGAK 816
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 21-259 6.41e-33

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: 129.64  E-value: 6.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  21 GPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGS 100
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 101 AGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQqgfpgisGPPGKEGEPGPRGETGPQGIMGEKGDQGERGPVGQPG 180
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958777315 181 PQGRQGPKGEQGSPGIPGPQGLpgiKGDKGSPGKTGPRggvGDPGVAGLPGEKGEKGLSGEPGLKGQQGVRGEPGYPGP 259
Cdd:NF038329  270 PDGPDGKDGERGPVGPAGKDGQ---NGKDGLPGKDGKD---GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 57-282 1.29e-31

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: 125.79  E-value: 1.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  57 GEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQ 136
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 137 QGFPGISGPPGKEGEPGPRGETGPQGIMGEKGDQGErgpvGQPGPQGRQGPKGEQGSPGIPGPQGLPGIKGDKGSPGKTG 216
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958777315 217 PRGGVGDPGVAGLPGEKGEKGLSGEPGLKGQQGVRGEPGYPGPSGDAGAPGVQGYPGLPGPRGLVG 282
Cdd:NF038329  273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 8-218 1.02e-28

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 117.70  E-value: 1.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315   8 KGPQGIRGYPGMAGPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDG 87
Cdd:NF038329  134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAG 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  88 KDGTPGIPGMKGSAGQVGRpGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGFPGISGPPGKEGEPGPRGETGPQGIMGEK 167
Cdd:NF038329  214 PDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN 292

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958777315 168 GDQGERGPVGQPGPQGRQGPKGEQGSPGIPGPQGLPGIKGDKGSPGKTGPR 218
Cdd:NF038329  293 GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 105-298 2.40e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 110.77  E-value: 2.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 105 GRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGFPGISGPPGKEGEPGPRGETGPQGIMGEKGDQGERGPVGQPGPQGR 184
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 185 QGPKGEQGSPGIPGPQGLPGIKGDKGSPGKTGPRGGvGDPGVAGLPGEKGEKGLSGEPGLKGQQGVRGEPGYPGPSGDAG 264
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1958777315 265 APGVQGYPGLPGPRGLVGDRGVPGQPGRQGVVGR 298
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK 309
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 127-437 3.29e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 95.74  E-value: 3.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 127 GPGDKGEPGQQGFPGISGPPGKEGEPGPRGETGPQGIMGEKGDQGERGPVGQPGPQGRQGPKGEQGSPGIPGPQGLPGIK 206
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 207 GDKGSPGKTGPRGGVGDPGVAGLPGEKGEKGLSGEPGlKGQQGVRGEPGYPGPSGDAGAPGVQGYPGLPGPRGLVGDRGV 286
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 287 PGQPGRQGVVGRAASDqhivdvvlkmiqeqlaevavsakrealgatgmvglpgppgppgypgkqgpnGHPGPRGIPGIVG 366
Cdd:NF038329  274 DGKDGERGPVGPAGKD---------------------------------------------------GQNGKDGLPGKDG 302

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958777315 367 AVGQIGNTGPKGKRGEkgdqgemgrghpgmpgppgipglpgrpgqaiNGKDGDRGSPGAPGEAGRPGRPGP 437
Cdd:NF038329  303 KDGQNGKDGLPGKDGK-------------------------------DGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 8-204 1.63e-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: 90.73  E-value: 1.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315   8 KGPQGIRGYPGMAGPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGaRGPQGITGPKGTTGPPGIDG 87
Cdd:NF038329  173 QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQG 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  88 KDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGfpgISGPPGKEGEPGPRGETGPQGIMGEK 167
Cdd:NF038329  252 PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG---KDGQNGKDGLPGKDGKDGQPGKDGLP 328

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958777315 168 GDQGERGPVGQPGPQGRQGPKGEQGSPGIPGPQGLPG 204
Cdd:NF038329  329 GKDGKDGQPGKPAPKTPEVPQKPDTAPHTPKTPQIPG 365
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 171-442 2.43e-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: 68.39  E-value: 2.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 171 GERGPVGQPGPQGRQGPKGEQGSPGIPGPQGLPGIKGDKGSPGKTGPRGGVGDPGVAGLPGEKGEKGLSGEPGLKGQQGV 250
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 251 RGEPGYPGPSGDAGAPGVQGYPGLPGPRGLVGDRGvpgqpgrqgvvgraasdqhivdvvlkmiqeqlaevavsakrealg 330
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG--------------------------------------------- 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 331 atgmvglpgppgppgypgkqgpNGHPGPRGIPGIVGAVGQIGNTGPKGKrgekgdqgemgrghpgmpgppgipglpgrpg 410
Cdd:NF038329  232 ----------------------DGQQGPDGDPGPTGEDGPQGPDGPAGK------------------------------- 258

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958777315 411 qaiNGKDGDRGSPGAPGEAGRPGRPGPVGLPG 442
Cdd:NF038329  259 ---DGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 4-123 7.64e-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: 66.85  E-value: 7.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315   4 PLENKGPQGIRGYPGMA-----GPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKG 78
Cdd:NF038329  214 PDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958777315  79 TTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPG 123
Cdd:NF038329  294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
9-242 5.88e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 55.04  E-value: 5.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315   9 GPQGIRGYPGMAGPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGP---QGITGPKGTTGPPGI 85
Cdd:COG5164    22 GSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPaqnQGGTRPAGNTGGTTP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  86 DGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGFPGISGPPGKEGEPGPRGETGPQGIMG 165
Cdd:COG5164   102 AGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGG 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 166 EK--GDQGERGPVGQPGPQGRQGPKGEQGSPG----IPGPQGLPGIKGDKGSPGKTGPRGGVGDPGVAGLPGEKGEKGLS 239
Cdd:COG5164   182 STtpPNKGETGTDIPTGGTPRQGPDGPVKKDDkngkGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTALE 261


                  ...
gi 1958777315 240 GEP 242
Cdd:COG5164   262 AEN 264
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 144-199 4.76e-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: 4.76e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958777315 144 GPPGKEGEPGPRGETGPQGIMGEKGDQGERGPVGQPGPQGRQGPKGEQGSPGIPGP 199
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 141-195 1.22e-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: 45.56  E-value: 1.22e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958777315 141 GISGPPGKEGEPGPRGETGPQGIMGEKGDQGERGPVGQPGPQGRQGPKGEQGSPG 195
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 150-204 2.07e-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: 2.07e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958777315 150 GEPGPRGETGPQGIMGEKGDQGERGPVGQPGPQGRQGPKGEQGSPGIPGPQGLPG 204
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 42-96 4.72e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 4.72e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958777315  42 GPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPG 96
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 117-173 5.86e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 5.86e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777315 117 GVPGQPGTKGGPGDKGEPGQQGFPGISGPPGKEGEPGPRGETGPQGIMGEKGDQGER 173
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 126-181 1.01e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 1.01e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958777315 126 GGPGDKGEPGQQGFPGISGPPGKEGEPGPRGETGPQGIMGEKGDQGERGPVGQPGP 181
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 48-104 1.02e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 1.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777315  48 GPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQV 104
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 105-160 1.06e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 1.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958777315 105 GRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGFPGISGPPGKEGEPGPRGETGP 160
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 162-218 1.61e-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: 42.10  E-value: 1.61e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777315 162 GIMGEKGDQGERGPVGQPGPQGRQGPKGEQGSPGIPGPQGLPGIKGDKGSPGKTGPR 218
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 34-297 1.67e-05

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 47.31  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  34 MVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGipGMKGSAGQVGrPGSPGHQ 113
Cdd:pfam09606  98 MMGPMGPGPGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGG--MMQPSSGQPG-SGTPNQM 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 114 GLAGVPGQPGTKGGPGDKGEPGQQGFPGISGPPGKEGEPGPRGE----TGPQGIMGEKGDQGERGPVGQPGPQGRQGPKG 189
Cdd:pfam09606 175 GPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQmgqqAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQ 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 190 EQGSPGIPGPQGLPGikGDKGSPGKTGPRGGVGDPGVAglPGEKGEKGLSGEPGLKGQQGVRGEPGYPGPSGDAGAPGVQ 269
Cdd:pfam09606 255 SQLGMGINQMQQMPQ--GVGGGAGQGGPGQPMGPPGQQ--PGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQM 330

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958777315 270 GYPGLPGPRGLV---GDRGVPGQPGRQGVVG 297
Cdd:pfam09606 331 NQSVGQGGQVVAlggLNHLETWNPGNFGGLG 361
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 222-278 1.98e-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: 42.10  E-value: 1.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777315 222 GDPGVAGLPGEKGEKGLSGEPGLKGQQGVRGEPGYPGPSGDAGAPGVQGYPGLPGPR 278
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 174-230 2.02e-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: 42.10  E-value: 2.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777315 174 GPVGQPGPQGRQGPKGEQGSPGIPGPQGLPGIKGDKGSPGKTGPRGGVGDPGVAGLP 230
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 183-237 2.19e-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: 2.19e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958777315 183 GRQGPKGEQGSPGIPGPQGLPGIKGDKGSPGKTGPRGGVGDPGVAGLPGEKGEKG 237
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 213-267 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: 41.71  E-value: 2.25e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958777315 213 GKTGPRGGVGDPGVAGLPGEKGEKGLSGEPGLKGQQGVRGEPGYPGPSGDAGAPG 267
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 186-242 3.02e-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: 3.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777315 186 GPKGEQGSPGIPGPQGLPGIKGDKGSPGKTGPRGGVGDPGVAGLPGEKGEKGLSGEP 242
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 93-148 3.47e-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: 3.47e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958777315  93 GIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGFPGISGPPGK 148
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 189-243 3.68e-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: 3.68e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958777315 189 GEQGSPGIPGPQGLPGIKGDKGSPGKTGPRGGVGDPGVAGLPGEKGEKGLSGEPG 243
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 228-284 3.71e-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: 3.71e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777315 228 GLPGEKGEKGLSGEPGLKGQQGVRGEPGYPGPSGDAGAPGVQGYPGLPGPRGLVGDR 284
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 102-157 3.75e-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: 3.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958777315 102 GQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGFPGISGPPGKEGEPGPRGE 157
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 240-294 5.14e-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: 40.94  E-value: 5.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958777315 240 GEPGLKGQQGVRGEPGYPGPSGDAGAPGVQGYPGLPGPRGLVGDRGVPGQPGRQG 294
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 27-83 5.34e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 5.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777315  27 GPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPP 83
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 81-332 5.54e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 5.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  81 GPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGdkGEPGQQGFPGISGPPGKEGEPGPRGETGP 160
Cdd:PRK07764  589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPA--EASAAPAPGVAAPEHHPKHVAVPDASDGG 666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 161 QGIMGEKGDQGERGPVGQPGPQGRQGPKGEQGSPGIPGPqglpgikgDKGSPGKTGPRGGVGDPGVAGLPGEKGEKGLSG 240
Cdd:PRK07764  667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAP--------AATPPAGQADDPAAQPPQAAQGASAPSPAADDP 738

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 241 EPglkgqqgvrgEPGYPGPSGDAGAPGVQGYPGLPGPRGlvgdrgvPGQPGRQGVVGRAASDQHIVDVVLKMIQEQL--- 317
Cdd:PRK07764  739 VP----------LPPEPDDPPDPAGAPAQPPPPPAPAPA-------AAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRrda 801

                         250
                  ....*....|....*
gi 1958777315 318 AEVAVSAKREALGAT 332
Cdd:PRK07764  802 EEVAMELLEEELGAK 816
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 75-129 6.76e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 6.76e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958777315  75 GPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPG 129
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 36-92 6.90e-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: 40.55  E-value: 6.90e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777315  36 GSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTP 92
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 210-266 7.04e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 7.04e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777315 210 GSPGKTGPRGGVGDPGVAGLPGEKGEKGLSGEPGLKGQQGVRGEPGYPGPSGDAGAP 266
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 207-263 9.27e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 9.27e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777315 207 GDKGSPGKTGPRGGVGDPGVAGLPGEKGEKGLSGEPGLKGQQGVRGEPGYPGPSGDA 263
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 168-224 1.29e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 1.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777315 168 GDQGERGPVGQPGPQGRQGPKGEQGSPGIPGPQGLPGIKGDKGSPGKTGPRGGVGDP 224
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 39-228 2.32e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  39 GAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGV 118
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 119 PGQPGTKGGPGDKGEPGQQGFPGISGPPGKEGEPGPRGETGPQgimgekgdQGERGPVGQPGPQGRQGPKGEQGSPGIPG 198
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAG--------QADDPAAQPPQAAQGASAPSPAADDPVPL 741

                         170       180       190
                  ....*....|....*....|....*....|
gi 1958777315 199 PQGLPGIKGDKGSPGKTGPRGGVGDPGVAG 228
Cdd:PRK07764  742 PPEPDDPPDPAGAPAQPPPPPAPAPAAAPA 771
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 72-128 2.58e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 2.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777315  72 GITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGP 128
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 87-141 2.84e-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: 2.84e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958777315  87 GKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGFPG 141
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 15-70 3.82e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 3.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958777315  15 GYPGMAGPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGP 70
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 33-88 5.95e-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: 5.95e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958777315  33 GMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGK 88
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 30-84 6.19e-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: 6.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958777315  30 GYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPG 84
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 246-299 8.73e-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: 37.47  E-value: 8.73e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958777315 246 GQQGVRGEPGYPGPSGDAGAPGVQGYPGLPGPRGLVGDRGVPGQPGRQGVVGRA 299
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 20-200 9.86e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 9.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  20 AGPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITG------PKGTTGPPGIDGKDGTPG 93
Cdd:PRK07764  592 PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVaapehhPKHVAVPDASDGGDGWPA 671

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  94 IPGMKGSAGQVGRPGSPGHQGLAGVPG-QPGTKGGPGDKGEPGQQGFPGISGPPGKEGEPGPRGETGPQGIMGEKGDQGE 172
Cdd:PRK07764  672 KAGGAAPAAPPPAPAPAAPAAPAGAAPaQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDP 751

                         170       180
                  ....*....|....*....|....*...
gi 1958777315 173 RGPVGQPGPQGRQGPKGEQGSPGIPGPQ 200
Cdd:PRK07764  752 AGAPAQPPPPPAPAPAAAPAAAPPPSPP 779
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 198-254 1.58e-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: 36.70  E-value: 1.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777315 198 GPQGLPGIKGDKGSPGKTGPRGGVGDPGVAGLPGEKGEKGLSGEPGLKGQQGVRGEP 254
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 24-193 1.72e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 41.04  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  24 GEMGPRGYKGM-----VGSI----GAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITG--PKGTTGPPGIDGKDGTP 92
Cdd:PRK12678   36 KQLGIKGTSGMrkgelIAAIkearGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEaaAAKAEAAPAARAAAAAA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  93 GIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGFPGISGPPGKEGEPGPRGETGPQGIMGEKGDQGE 172
Cdd:PRK12678  116 AEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREE 195

                         170       180
                  ....*....|....*....|.
gi 1958777315 173 RGPVGQPGPQGRQGPKGEQGS 193
Cdd:PRK12678  196 RGRDGDDRDRRDRREQGDRRE 216
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 9-68 2.43e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.93  E-value: 2.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315   9 GPQGIRGYPGMAGPKGEMGPRGYKGMVGsigAAGPPGEEGPRGPPGRAGEKGDVGSQGAR 68
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPG---PPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 8-58 2.71e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.93  E-value: 2.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958777315   8 KGPQGIRGYPGMAGPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGE 58
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
dnaA PRK14086
chromosomal replication initiator protein DnaA;
45-232 2.74e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 40.19  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  45 GEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGS-PGHQGLAGVPGQPG 123
Cdd:PRK14086   93 GEPAPPPPHARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQDQLPTARPAYPAYQQRPEPGAwPRAADDYGWQQQRL 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 124 TKGGPGDKGEPGQQgfpgisgPPGKEGEPGPRGETGPQGIMGEKGDQGERGPVGQPGPQGRQGPKGEQGS----PGIPGP 199
Cdd:PRK14086  173 GFPPRAPYASPASY-------APEQERDREPYDAGRPEYDQRRRDYDHPRPDWDRPRRDRTDRPEPPPGAghvhRGGPGP 245

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958777315 200 QGLPGIKGDKGSPGKTGPRGgvGDPGVAGLPGE 232
Cdd:PRK14086  246 PERDDAPVVPIRPSAPGPLA--AQPAPAPGPGE 276
PHA03169 PHA03169
hypothetical protein; Provisional
 46-210 3.82e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.57  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  46 EEGPRGPPGRAGEKGDVGSqgargpqgitGPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTK 125
Cdd:PHA03169   77 EESRHGEKEERGQGGPSGS----------GSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGP 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 126 GGPGDKGEPGQQGFPGISGPPGKEGEPGPRGETGPQGIMGEKGDQGERGPVGQPGPQGRQGPKgEQGSPGIPGPQGLPGI 205
Cdd:PHA03169  147 HEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPD-EPGEPQSPTPQQAPSP 225


                  ....*
gi 1958777315 206 KGDKG 210
Cdd:PHA03169  226 NTQQA 230
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 3-133 4.29e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 39.66  E-value: 4.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315   3 VPLENKGPQGirgypGMAGPKGEMGPRGykGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPK--GTT 80
Cdd:PRK14959  366 MPVESLRPSG-----GGASAPSGSAAEG--PASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPAPSAAPSPRvpWDD 438

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958777315  81 GPPGIDGKDGTP-GIPGMKGSAGQVGRPGSpghqgLAGVPGQPGTKGGPGDKGE 133
Cdd:PRK14959  439 APPAPPRSGIPPrPAPRMPEASPVPGAPDS-----VASASDAPPTLGDPSDTAE 487
PHA03169 PHA03169
hypothetical protein; Provisional
 96-276 4.39e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.18  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  96 GMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGFPGISGPPGKEGEPGPRGETGPqgimGEKGDQGERGP 175
Cdd:PHA03169   82 GEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGP----HEPAPPESHNP 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315 176 VGQPGPQGRQGPKGEQGSPGIPGPQGLPGIKGDKGSPGKTGPRGGVGDPGvAGLPGEKGEKGLSGEPGLKGQQGV----- 250
Cdd:PHA03169  158 SPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSP-PDEPGEPQSPTPQQAPSPNTQQAVehede 236

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1958777315 251 -----RGEPGYPGPSGDAGAPGVQGYPGLPG 276
Cdd:PHA03169  237 ptepeREGPPFPGHRSHSYTVVGWKPSTRPG 267
PHA03169 PHA03169
hypothetical protein; Provisional
 36-171 6.11e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 38.80  E-value: 6.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777315  36 GSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGL 115
Cdd:PHA03169   90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQP 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958777315 116 AG----VPGQPGTKGGPGDKGEPGQQGFPGISGPPGKEG-EPGPRGETGPQGIMGEKGDQG 171
Cdd:PHA03169  170 SHedspEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPdEPGEPQSPTPQQAPSPNTQQA 230
 
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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