NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|227116289|ref|NP_031767|]
View 

collagen alpha-2(IX) chain precursor [Mus musculus]

Protein Classification

collagen-like domain-containing protein( domain architecture ID 1903237)

collagen-like domain-containing protein such as collagens, which are extracellular structural proteins involved in formation of connective tissue structure

PubMed:  21421911|15837519

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 240-497 5.24e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 126.56  E-value: 5.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 240 GPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGS 319
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 320 AGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQqglpgvsGPPGKEGEPGPRGEIGPQGIMGQKGDQGERGPVGQPG 399
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 400 PQGRQGPKGEQgppgipgpqglpgikgdkgspGKTGPRGGVGDPGVAGLPGEKGEKGQSGEPGLKGQqgvRGETGYPGPS 479
Cdd:NF038329 270 PDGPDGKDGER---------------------GPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK---DGKDGQPGKD 325

                        250
                 ....*....|....*...
gi 227116289 480 GDAGAPGVQGYPGLPGPR 497
Cdd:NF038329 326 GLPGKDGKDGQPGKPAPK 343
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 35-342 4.25e-14

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: 74.94  E-value: 4.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289  35 GPPGPPGVPGSDGIDGDKGPPGKVGPPGSKGEPGKPGPDGPDGKPGIDGLMGAKGEPGPVGTPGVKGQPGlpgppglpgp 114
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG---------- 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 115 gfagppgppgpvglpgeigtpgpkgdpgpegpsgppgppgkpgrpgtiqglegsadflcptncPAGVKGPQGLQGVKGHP 194
Cdd:NF038329 196 ---------------------------------------------------------------PRGETGPAGEQGPAGPA 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 195 GKRGILGDPGRQGKPGPKGDvgasgeqgipgppgpqgirgypGMAGPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGR 274
Cdd:NF038329 213 GPDGEAGPAGEDGPAGPAGD----------------------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP 270

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 227116289 275 AGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPG 342
Cdd:NF038329 271 DGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 240-497 5.24e-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: 126.56  E-value: 5.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 240 GPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGS 319
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 320 AGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQqglpgvsGPPGKEGEPGPRGEIGPQGIMGQKGDQGERGPVGQPG 399
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 400 PQGRQGPKGEQgppgipgpqglpgikgdkgspGKTGPRGGVGDPGVAGLPGEKGEKGQSGEPGLKGQqgvRGETGYPGPS 479
Cdd:NF038329 270 PDGPDGKDGER---------------------GPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK---DGKDGQPGKD 325

                        250
                 ....*....|....*...
gi 227116289 480 GDAGAPGVQGYPGLPGPR 497
Cdd:NF038329 326 GLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 276-501 6.86e-30

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 123.09  E-value: 6.86e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 276 GEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQ 355
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 356 QGLPGVSGPPGKEGEPGPRGEIGPQGIMGQKGDQGErgpvGQPGPQGRQGPKGEQGPPGIPGPQGLPGIKGDKGSPGKTG 435
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227116289 436 PRGGVGDPGVAGLPGEKGEKGQSGEPGLKGQQGVRGETGYPGPSGDAGAPGVQGYPGLPGPRGLVG 501
Cdd:NF038329 273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 178-401 2.60e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 112.31  E-value: 2.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 178 PAGVKGPQGLQGVKGHPGKRGILGDPGRQGKPGPKGDVGASGEQGIPGPPGPQGIRGYPGMAGPKGEMGPRGYKGMVGSI 257
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 258 GAAGPPGEEGPRGPPGRAGEKGDVGSQGaRGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGV 337
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP 282

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227116289 338 PGQPGTKGGPGDKGEPGQQGlpgVSGPPGKEGEPGPRGEIGPQGIMGQKGDQGERGPVGQPGPQ 401
Cdd:NF038329 283 VGPAGKDGQNGKDGLPGKDG---KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 192-408 4.35e-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: 111.92  E-value: 4.35e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 192 GHPGKRGILGDPGRQGKPGPKGDVGASGEQGIPGPPGPQGIRGYPGMAGPKGEMGPRGYKGMVGSIGAAGPPGEEGP--- 268
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPqgp 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 269 RGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGI--DGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGG 346
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227116289 347 PGDKGEPGQQGLPGVSGPPGKEGEPGPRGEIGPQGIMGQKGDQGERGPVGQPGPQGRQGPKG 408
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 324-517 2.71e-24

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: 106.53  E-value: 2.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 324 GRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGLPGVSGPPGKEGEPGPRGEIGPQGIMGQKGDQGERGPVGQPGPQGR 403
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 404 QGPKGEQGPPGIPGPQGLPGIKGDKGSPGKTGPRGGvGDPGVAGLPGEKGEKGQSGEPGLKGQQGVRGETGYPGPSGDAG 483
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                        170       180       190
                 ....*....|....*....|....*....|....
gi 227116289 484 APGVQGYPGLPGPRGLVGDRGVPGQPGRQGVVGR 517
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK 309
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 178-380 3.47e-24

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: 106.14  E-value: 3.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 178 PAGVKGPQGLQGVKGHPGKRGILGDPGRQGKPGPKGDVGASGEQGIPGPPGPQGIRGYPGMAGPKGEMGPRGYKGMVGSI 257
Cdd:NF038329 145 PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGED 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 258 GAAGPPG--EEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLA 335
Cdd:NF038329 225 GPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKD 304

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 227116289 336 GVPGQPGTKGGPGDKGEPGQQGLPGVSGPPGKEGEPGPRGEIGPQ 380
Cdd:NF038329 305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQ 349
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 380-661 3.32e-17

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 84.57  E-value: 3.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 380 QGIMGQKGDqGERGPVGQPGPQGRQGPKGEQGPPGIPGPQGLPGIKGDKGSPGKTGPRGGVGDPGVAGLPGEKGEKGQSG 459
Cdd:NF038329 108 EGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 460 EPGLKGQQGVRGETGYPGPSGDAGAPGVQGYPGLPGPRGLVGDRGvPGQPGRQGVVGRAASDqhivdvvlkmiqeqlaev 539
Cdd:NF038329 187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGED------------------ 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 540 avsakrealgaagmvglpgppgppgypgkqgpnGHPGPRGIPGIVGAVGQIGNTGPKGKRGEKGDRGEMGRGHPGMPGPP 619
Cdd:NF038329 248 ---------------------------------GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGK 294

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 227116289 620 GIPGLPgrpgqaiNGKDGDRGSPGAPGEAGRPGRPGPVGLPG 661
Cdd:NF038329 295 DGLPGK-------DGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 35-342 4.25e-14

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: 74.94  E-value: 4.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289  35 GPPGPPGVPGSDGIDGDKGPPGKVGPPGSKGEPGKPGPDGPDGKPGIDGLMGAKGEPGPVGTPGVKGQPGlpgppglpgp 114
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG---------- 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 115 gfagppgppgpvglpgeigtpgpkgdpgpegpsgppgppgkpgrpgtiqglegsadflcptncPAGVKGPQGLQGVKGHP 194
Cdd:NF038329 196 ---------------------------------------------------------------PRGETGPAGEQGPAGPA 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 195 GKRGILGDPGRQGKPGPKGDvgasgeqgipgppgpqgirgypGMAGPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGR 274
Cdd:NF038329 213 GPDGEAGPAGEDGPAGPAGD----------------------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP 270

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 227116289 275 AGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPG 342
Cdd:NF038329 271 DGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
194-461 7.44e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 52.34  E-value: 7.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 194 PGKRGILGDPGRQGKPGPKGDVGASGEQGIPGPPGPQGIRGYPGMAGPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPG 273
Cdd:COG5164    6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 274 RAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPG--IPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKG 351
Cdd:COG5164   86 NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGstTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGST 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 352 EPGQQGLPGVSGPPGKEGEPGPRGEIGPQGIMGQKGDQGERGPVGQPGPQGRQGPKGEQgppgipgpqglPGIKGDKGSP 431
Cdd:COG5164  166 TPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDR-----------GGKTGPKDQR 234

                        250       260       270
                 ....*....|....*....|....*....|
gi 227116289 432 GKTGPRGGVGDPGVAGLPGEKGEKGQSGEP 461
Cdd:COG5164  235 PKTNPIERRGPERPEAAALPAELTALEAEN 264
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 253-516 1.77e-06

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: 51.16  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289  253 MVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGipGMKGSAGQVGrPGSPGHQ 332
Cdd:pfam09606  98 MMGPMGPGPGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGG--MMQPSSGQPG-SGTPNQM 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289  333 GLAGVPGQPGTKGGPGDKGEPGQQGLPGVSGPPGKEGEPGPRGEIG--PQGIMGQKGDQGERGPVGQPGPQGRQGPKGEQ 410
Cdd:pfam09606 175 GPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGqqAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQ 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289  411 GPPGIPGPQGLPGIKGDKGSPGKTGPRGGVGDPGVAglPGEKGEKGQSGEPGLKGQQGVRGETGYPGPSGDAGAPGVQGY 490
Cdd:pfam09606 255 SQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQ--PGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQ 332

                         250       260
                  ....*....|....*....|....*....
gi 227116289  491 PGLPGPRGLV---GDRGVPGQPGRQGVVG 516
Cdd:pfam09606 333 SVGQGGQVVAlggLNHLETWNPGNFGGLG 361
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 46-317 1.80e-06

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 51.06  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289  46 DGIDGDKGPPGKVGPPGSKGEPGKPGPDGPDGKPGIDGLMGAKGEPGPVGTPGvkgqpglpgppglpgpgfagppgppgp 125
Cdd:NF038329 167 QGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAG--------------------------- 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 126 vglpgeigtpgpkgdpgpegpsgppgppgkpgrpgtiqglegsadflcptncPAGVKGPQGLQGvkghPGKRGILGDPGR 205
Cdd:NF038329 220 ----------------------------------------------------PAGEDGPAGPAG----DGQQGPDGDPGP 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 206 QGKPGPKGDVGASGEQgipgppgpqgirGYPGMAGPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQG 285
Cdd:NF038329 244 TGEDGPQGPDGPAGKD------------GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311

                        250       260       270
                 ....*....|....*....|....*....|..
gi 227116289 286 ARGPQGITGPKGTTGPPGIDGKDGTPGIPGMK 317
Cdd:NF038329 312 LPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
PHA03169 PHA03169
hypothetical protein; Provisional
 255-390 3.14e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.34  E-value: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 255 GSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGL 334
Cdd:PHA03169  90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQP 169

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227116289 335 AG----VPGQPGTKGGPGDKGEPGQQGLPGVSGPPGKEG-EPGPRGEIGPQGIMGQKGDQG 390
Cdd:PHA03169 170 SHedspEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPdEPGEPQSPTPQQAPSPNTQQA 230
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 240-497 5.24e-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: 126.56  E-value: 5.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 240 GPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGS 319
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 320 AGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQqglpgvsGPPGKEGEPGPRGEIGPQGIMGQKGDQGERGPVGQPG 399
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 400 PQGRQGPKGEQgppgipgpqglpgikgdkgspGKTGPRGGVGDPGVAGLPGEKGEKGQSGEPGLKGQqgvRGETGYPGPS 479
Cdd:NF038329 270 PDGPDGKDGER---------------------GPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK---DGKDGQPGKD 325

                        250
                 ....*....|....*...
gi 227116289 480 GDAGAPGVQGYPGLPGPR 497
Cdd:NF038329 326 GLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 276-501 6.86e-30

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 123.09  E-value: 6.86e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 276 GEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQ 355
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 356 QGLPGVSGPPGKEGEPGPRGEIGPQGIMGQKGDQGErgpvGQPGPQGRQGPKGEQGPPGIPGPQGLPGIKGDKGSPGKTG 435
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227116289 436 PRGGVGDPGVAGLPGEKGEKGQSGEPGLKGQQGVRGETGYPGPSGDAGAPGVQGYPGLPGPRGLVG 501
Cdd:NF038329 273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 178-401 2.60e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 112.31  E-value: 2.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 178 PAGVKGPQGLQGVKGHPGKRGILGDPGRQGKPGPKGDVGASGEQGIPGPPGPQGIRGYPGMAGPKGEMGPRGYKGMVGSI 257
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 258 GAAGPPGEEGPRGPPGRAGEKGDVGSQGaRGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGV 337
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP 282

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227116289 338 PGQPGTKGGPGDKGEPGQQGlpgVSGPPGKEGEPGPRGEIGPQGIMGQKGDQGERGPVGQPGPQ 401
Cdd:NF038329 283 VGPAGKDGQNGKDGLPGKDG---KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 192-408 4.35e-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: 111.92  E-value: 4.35e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 192 GHPGKRGILGDPGRQGKPGPKGDVGASGEQGIPGPPGPQGIRGYPGMAGPKGEMGPRGYKGMVGSIGAAGPPGEEGP--- 268
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPqgp 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 269 RGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGI--DGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGG 346
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227116289 347 PGDKGEPGQQGLPGVSGPPGKEGEPGPRGEIGPQGIMGQKGDQGERGPVGQPGPQGRQGPKG 408
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 324-517 2.71e-24

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: 106.53  E-value: 2.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 324 GRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGLPGVSGPPGKEGEPGPRGEIGPQGIMGQKGDQGERGPVGQPGPQGR 403
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 404 QGPKGEQGPPGIPGPQGLPGIKGDKGSPGKTGPRGGvGDPGVAGLPGEKGEKGQSGEPGLKGQQGVRGETGYPGPSGDAG 483
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                        170       180       190
                 ....*....|....*....|....*....|....
gi 227116289 484 APGVQGYPGLPGPRGLVGDRGVPGQPGRQGVVGR 517
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK 309
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 178-380 3.47e-24

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: 106.14  E-value: 3.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 178 PAGVKGPQGLQGVKGHPGKRGILGDPGRQGKPGPKGDVGASGEQGIPGPPGPQGIRGYPGMAGPKGEMGPRGYKGMVGSI 257
Cdd:NF038329 145 PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGED 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 258 GAAGPPG--EEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLA 335
Cdd:NF038329 225 GPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKD 304

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 227116289 336 GVPGQPGTKGGPGDKGEPGQQGLPGVSGPPGKEGEPGPRGEIGPQ 380
Cdd:NF038329 305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQ 349
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 380-661 3.32e-17

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 84.57  E-value: 3.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 380 QGIMGQKGDqGERGPVGQPGPQGRQGPKGEQGPPGIPGPQGLPGIKGDKGSPGKTGPRGGVGDPGVAGLPGEKGEKGQSG 459
Cdd:NF038329 108 EGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 460 EPGLKGQQGVRGETGYPGPSGDAGAPGVQGYPGLPGPRGLVGDRGvPGQPGRQGVVGRAASDqhivdvvlkmiqeqlaev 539
Cdd:NF038329 187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGED------------------ 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 540 avsakrealgaagmvglpgppgppgypgkqgpnGHPGPRGIPGIVGAVGQIGNTGPKGKRGEKGDRGEMGRGHPGMPGPP 619
Cdd:NF038329 248 ---------------------------------GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGK 294

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 227116289 620 GIPGLPgrpgqaiNGKDGDRGSPGAPGEAGRPGRPGPVGLPG 661
Cdd:NF038329 295 DGLPGK-------DGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 35-342 4.25e-14

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: 74.94  E-value: 4.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289  35 GPPGPPGVPGSDGIDGDKGPPGKVGPPGSKGEPGKPGPDGPDGKPGIDGLMGAKGEPGPVGTPGVKGQPGlpgppglpgp 114
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG---------- 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 115 gfagppgppgpvglpgeigtpgpkgdpgpegpsgppgppgkpgrpgtiqglegsadflcptncPAGVKGPQGLQGVKGHP 194
Cdd:NF038329 196 ---------------------------------------------------------------PRGETGPAGEQGPAGPA 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 195 GKRGILGDPGRQGKPGPKGDvgasgeqgipgppgpqgirgypGMAGPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGR 274
Cdd:NF038329 213 GPDGEAGPAGEDGPAGPAGD----------------------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP 270

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 227116289 275 AGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPG 342
Cdd:NF038329 271 DGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
194-461 7.44e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 52.34  E-value: 7.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 194 PGKRGILGDPGRQGKPGPKGDVGASGEQGIPGPPGPQGIRGYPGMAGPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPG 273
Cdd:COG5164    6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 274 RAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPG--IPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKG 351
Cdd:COG5164   86 NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGstTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGST 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 352 EPGQQGLPGVSGPPGKEGEPGPRGEIGPQGIMGQKGDQGERGPVGQPGPQGRQGPKGEQgppgipgpqglPGIKGDKGSP 431
Cdd:COG5164  166 TPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDR-----------GGKTGPKDQR 234

                        250       260       270
                 ....*....|....*....|....*....|
gi 227116289 432 GKTGPRGGVGDPGVAGLPGEKGEKGQSGEP 461
Cdd:COG5164  235 PKTNPIERRGPERPEAAALPAELTALEAEN 264
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 253-516 1.77e-06

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: 51.16  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289  253 MVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGipGMKGSAGQVGrPGSPGHQ 332
Cdd:pfam09606  98 MMGPMGPGPGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGG--MMQPSSGQPG-SGTPNQM 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289  333 GLAGVPGQPGTKGGPGDKGEPGQQGLPGVSGPPGKEGEPGPRGEIG--PQGIMGQKGDQGERGPVGQPGPQGRQGPKGEQ 410
Cdd:pfam09606 175 GPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGqqAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQ 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289  411 GPPGIPGPQGLPGIKGDKGSPGKTGPRGGVGDPGVAglPGEKGEKGQSGEPGLKGQQGVRGETGYPGPSGDAGAPGVQGY 490
Cdd:pfam09606 255 SQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQ--PGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQ 332

                         250       260
                  ....*....|....*....|....*....
gi 227116289  491 PGLPGPRGLV---GDRGVPGQPGRQGVVG 516
Cdd:pfam09606 333 SVGQGGQVVAlggLNHLETWNPGNFGGLG 361
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 46-317 1.80e-06

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 51.06  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289  46 DGIDGDKGPPGKVGPPGSKGEPGKPGPDGPDGKPGIDGLMGAKGEPGPVGTPGvkgqpglpgppglpgpgfagppgppgp 125
Cdd:NF038329 167 QGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAG--------------------------- 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 126 vglpgeigtpgpkgdpgpegpsgppgppgkpgrpgtiqglegsadflcptncPAGVKGPQGLQGvkghPGKRGILGDPGR 205
Cdd:NF038329 220 ----------------------------------------------------PAGEDGPAGPAG----DGQQGPDGDPGP 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 206 QGKPGPKGDVGASGEQgipgppgpqgirGYPGMAGPKGEMGPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQG 285
Cdd:NF038329 244 TGEDGPQGPDGPAGKD------------GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311

                        250       260       270
                 ....*....|....*....|....*....|..
gi 227116289 286 ARGPQGITGPKGTTGPPGIDGKDGTPGIPGMK 317
Cdd:NF038329 312 LPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 261-315 6.99e-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: 6.99e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 227116289  261 GPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPG 315
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 267-323 1.50e-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: 1.50e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 227116289  267 GPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQV 323
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 321-376 1.69e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 1.69e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 227116289  321 GQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGLPGVSGPPGKEGEPGPRGE 376
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 318-374 4.38e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 4.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 227116289  318 GSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGLPGVSGPPGKEGEPGPR 374
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 324-379 4.38e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 4.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 227116289  324 GRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGLPGVSGPPGKEGEPGPRGEIGP 379
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 441-497 6.00e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 6.00e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 227116289  441 GDPGVAGLPGEKGEKGQSGEPGLKGQQGVRGETGYPGPSGDAGAPGVQGYPGLPGPR 497
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 447-503 6.50e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 6.50e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 227116289  447 GLPGEKGEKGQSGEPGLKGQQGVRGETGYPGPSGDAGAPGVQGYPGLPGPRGLVGDR 503
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 246-302 7.91e-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: 7.91e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 227116289  246 GPRGYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPP 302
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 294-348 1.00e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 1.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 227116289  294 GPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPG 348
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 255-311 1.02e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 1.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 227116289  255 GSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTP 311
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 432-486 1.16e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 1.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 227116289  432 GKTGPRGGVGDPGVAGLPGEKGEKGQSGEPGLKGQQGVRGETGYPGPSGDAGAPG 486
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 459-513 2.55e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 2.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 227116289  459 GEPGLKGQQGVRGETGYPGPSGDAGAPGVQGYPGLPGPRGLVGDRGVPGQPGRQG 513
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 291-347 3.81e-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: 3.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 227116289  291 GITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGP 347
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 306-360 4.05e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 4.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 227116289  306 GKDGTPGIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGLPG 360
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 426-482 4.51e-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: 4.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 227116289  426 GDKGSPGKTGPRGGVGDPGVAGLPGEKGEKGQSGEPGLKGQQGVRGETGYPGPSGDA 482
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 252-307 8.81e-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: 8.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 227116289  252 GMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGK 307
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 249-303 9.16e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 9.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 227116289  249 GYKGMVGSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPG 303
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 363-413 1.82e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 1.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 227116289  363 GPPGKEGEPGPRGEIGPQGIMGQKGDQGERGPVGQPGPQGRQGPKGEQGPP 413
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
PHA03169 PHA03169
hypothetical protein; Provisional
 255-390 3.14e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.34  E-value: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 255 GSIGAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTPGIPGMKGSAGQVGRPGSPGHQGL 334
Cdd:PHA03169  90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQP 169

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227116289 335 AG----VPGQPGTKGGPGDKGEPGQQGLPGVSGPPGKEG-EPGPRGEIGPQGIMGQKGDQG 390
Cdd:PHA03169 170 SHedspEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPdEPGEPQSPTPQQAPSPNTQQA 230
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 333-387 3.20e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 3.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 227116289  333 GLAGVPGQPGTKGGPGDKGEPGQQGLPGVSGPPGKEGEPGPRGEIGPQGIMGQKG 387
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 465-518 3.46e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 3.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 227116289  465 GQQGVRGETGYPGPSGDAGAPGVQGYPGLPGPRGLVGDRGVPGQPGRQGVVGRA 518
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 243-410 9.32e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 39.12  E-value: 9.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 243 GEMGPRGYKGM-----VGSI------GAAGPPGEEGPRGPPGRAGEKGDVGSQGARGPQGITGPKGTTGPPGIDGKDGTP 311
Cdd:PRK12678  36 KQLGIKGTSGMrkgelIAAIkearggGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227116289 312 GIPGMKGSAGQVGRPGSPGHQGLAGVPGQPGTKGGPGDKGEPGQQGLPGVSGPPGKEGEPGPRGEIGPQGIMGQKGDQGE 391
Cdd:PRK12678 116 AEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREE 195

                        170
                 ....*....|....*....
gi 227116289 392 RGPVGQPGPQGRQGPKGEQ 410
Cdd:PRK12678 196 RGRDGDDRDRRDRREQGDR 214
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH