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Conserved domains on  [gi|226693380|ref|NP_031766|]
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collagen alpha-1(IX) chain isoform 1 precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 50-244 1.20e-55

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 190.26  E-value: 1.20e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380    50 GQDDLPGFDLISqfqiekaaSRRTIQRVVGSTALQVAYKLGSNVDFRIPTRHLYPSGLPEEYSFLTTFRMTGStleKHWN 129
Cdd:smart00210   1 GQDLLQVFDLPS--------LSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPK---SRGV 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380   130 IWQIQDSAGREQVGVKINGQTKSVAFSYKGLDGSLQTAAFLNLPsLFDSRWHKLMIGVERTSATLFIDCIRIESLPIKPR 209
Cdd:smart00210  70 LFAIYDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLP-LADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRP 148

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 226693380   210 GQ--IDADGFAVLGKLVDNpQVSVPFELQWMLIHCDP 244
Cdd:smart00210 149 GQppIDTDGIEVRGAQAAD-RKPFQGDLQQLKIVCDP 184
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 442-702 9.29e-40

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: 153.14  E-value: 9.29e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 442 GRQGHKGEegdqGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGI 521
Cdd:NF038329 109 GLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 522 QGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGlQGLPGVPGIPGAKGVAGEKGNTGAPGKPGQLG 601
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 602 SSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGKlgsvgspglpglpgppglpgmKGDRGVFGEPGPKGEQGAS 681
Cdd:NF038329 264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGK---------------------DGQNGKDGLPGKDGKDGQP 322

                        250       260
                 ....*....|....*....|.
gi 226693380 682 GEEGEAGARGDLGDMGQPGPK 702
Cdd:NF038329 323 GKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 607-881 5.31e-22

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 99.98  E-value: 5.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 607 GQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGKLGsvgspglpglpgppgLPGMKGDRGVFGEPGPKGEQGASGEEGE 686
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPG---------------PQGERGEKGPAGPQGEAGPQGPAGKDGE 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 687 AGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRGLPGVEGPRGPPGPRGM-----QGDQGATGLPGIQGPPGRAPTDqh 761
Cdd:NF038329 182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKD-- 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 762 ikqvcmrvvqehfaemaaslkrpdtgasglpgrpgppgppgppgenGFPGQMGIRGLPGIKGPPGALGLRGPKGDLGEKG 841
Cdd:NF038329 260 ----------------------------------------------GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 226693380 842 ERGPPGR-GPKGLPGAIGLPGDPGPAsyGKNGRDGEQGPPG 881
Cdd:NF038329 294 KDGLPGKdGKDGQNGKDGLPGKDGKD--GQPGKDGLPGKDG 332
 
Name Accession Description Interval E-value
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 50-244 1.20e-55

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 190.26  E-value: 1.20e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380    50 GQDDLPGFDLISqfqiekaaSRRTIQRVVGSTALQVAYKLGSNVDFRIPTRHLYPSGLPEEYSFLTTFRMTGStleKHWN 129
Cdd:smart00210   1 GQDLLQVFDLPS--------LSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPK---SRGV 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380   130 IWQIQDSAGREQVGVKINGQTKSVAFSYKGLDGSLQTAAFLNLPsLFDSRWHKLMIGVERTSATLFIDCIRIESLPIKPR 209
Cdd:smart00210  70 LFAIYDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLP-LADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRP 148

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 226693380   210 GQ--IDADGFAVLGKLVDNpQVSVPFELQWMLIHCDP 244
Cdd:smart00210 149 GQppIDTDGIEVRGAQAAD-RKPFQGDLQQLKIVCDP 184
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 442-702 9.29e-40

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: 153.14  E-value: 9.29e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 442 GRQGHKGEegdqGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGI 521
Cdd:NF038329 109 GLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 522 QGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGlQGLPGVPGIPGAKGVAGEKGNTGAPGKPGQLG 601
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 602 SSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGKlgsvgspglpglpgppglpgmKGDRGVFGEPGPKGEQGAS 681
Cdd:NF038329 264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGK---------------------DGQNGKDGLPGKDGKDGQP 322

                        250       260
                 ....*....|....*....|.
gi 226693380 682 GEEGEAGARGDLGDMGQPGPK 702
Cdd:NF038329 323 GKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 418-641 1.45e-38

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: 149.67  E-value: 1.45e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 418 GRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGI 497
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 498 PGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGpKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGVPG 577
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226693380 578 IPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGK 641
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 487-755 4.91e-34

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: 136.19  E-value: 4.91e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 487 GFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGD 566
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 567 VGLQGlpgvpgipgakgVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEvGPRGPRGLPGSRGPVGPEGSPGIPGKLGSvg 646
Cdd:NF038329 197 RGETG------------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGP-- 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 647 spglpglpgppglpgmKGDRGVFGEPGPKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRGLPgve 726
Cdd:NF038329 262 ----------------RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP--- 322

                        250       260
                 ....*....|....*....|....*....
gi 226693380 727 gprgppgprgmqGDQGATGLPGIQGPPGR 755
Cdd:NF038329 323 ------------GKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 416-621 5.86e-34

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: 136.19  E-value: 5.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 416 PPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQ 495
Cdd:NF038329 127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQ 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 496 GIPGAAG-----------------DQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEA 558
Cdd:NF038329 207 GPAGPAGpdgeagpagedgpagpaGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPA 286

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226693380 559 GKPGPPGDVGLQGLPGVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPR 621
Cdd:NF038329 287 GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQ 349
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 317-580 4.00e-29

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: 121.55  E-value: 4.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 317 GKPGTPGADGLTGPDGSPGSVGPRGQKGEPGVPGSRgfpgrgipgppgppgttglpgelGRVGPIGdpgkrgppgppgpp 396
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ-----------------------GEAGPQG-------------- 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 397 gpsgtigfhdgdplcpnscPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGiTGI 476
Cdd:NF038329 175 -------------------PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQ 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 477 VGDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKG 556
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG 314

                        250       260
                 ....*....|....*....|....
gi 226693380 557 EAGKPGPPGDVGLQGLPGVPGIPG 580
Cdd:NF038329 315 KDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 553-759 8.71e-23

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 102.29  E-value: 8.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 553 GTKGEAGKPGPPGDVGLQGlpgvpgipgAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGP 632
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQG---------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 633 EGSPGIPGKLGSVGSPGLPGLPGPPGLPGMKGDRGVFGEPGP--KGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGE 710
Cdd:NF038329 188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 226693380 711 PGLRGPEGIRGlpgvegPRGPPGPRGMQGDQGATGLPGIQGPPGRAPTD 759
Cdd:NF038329 268 AGPDGPDGKDG------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD 310
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 607-881 5.31e-22

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 99.98  E-value: 5.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 607 GQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGKLGsvgspglpglpgppgLPGMKGDRGVFGEPGPKGEQGASGEEGE 686
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPG---------------PQGERGEKGPAGPQGEAGPQGPAGKDGE 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 687 AGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRGLPGVEGPRGPPGPRGM-----QGDQGATGLPGIQGPPGRAPTDqh 761
Cdd:NF038329 182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKD-- 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 762 ikqvcmrvvqehfaemaaslkrpdtgasglpgrpgppgppgppgenGFPGQMGIRGLPGIKGPPGALGLRGPKGDLGEKG 841
Cdd:NF038329 260 ----------------------------------------------GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 226693380 842 ERGPPGR-GPKGLPGAIGLPGDPGPAsyGKNGRDGEQGPPG 881
Cdd:NF038329 294 KDGLPGKdGKDGQNGKDGLPGKDGKD--GQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 320-563 5.35e-20

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: 93.82  E-value: 5.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 320 GTPGADGLTGPDGSPGSVGPRGQKGEPGvpgsrgfpgrgipgppgppgttglpgelgrvgpigdpgkrgppgppgppgps 399
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETG---------------------------------------------------- 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 400 gtigfhdgdplcpnscPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGhKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGD 479
Cdd:NF038329 202 ----------------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 480 KGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPgspgpkGDTGLPGVDGRDGIPGMPGTKGEAG 559
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLP------GKDGKDGQPGKDGLPGKDGKDGQPG 338


                 ....
gi 226693380 560 KPGP 563
Cdd:NF038329 339 KPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 663-883 1.22e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 83.42  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 663 KGDRGVFGEPGPKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRGlpgvegprgppgprgMQGDQG 742
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG---------------KDGEAG 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 743 ATGLPGIQGPPGRAptdqhikqvcmrvvqehfaemaaslkrpdtgasglpGRPGPPGPPGPPGENGFPGQMGIRGLPGIK 822
Cdd:NF038329 184 AKGPAGEKGPQGPR------------------------------------GETGPAGEQGPAGPAGPDGEAGPAGEDGPA 227

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226693380 823 GPPGAlGLRGPKGDLGEKGERGPPG-RGPKGLPGAIGLPGDPGPAsyGKNGRDGEQGPPGVA 883
Cdd:NF038329 228 GPAGD-GQQGPDGDPGPTGEDGPQGpDGPAGKDGPRGDRGEAGPD--GPDGKDGERGPVGPA 286
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 670-888 9.29e-11

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 64.93  E-value: 9.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 670 GEPGPKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPegirglpgvegprgppgprgmQGDQGATGLPGI 749
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGP---------------------QGEAGPQGPAGK 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 750 QGPPGRaptdqhikqvcmrvvqehfaemaaslkrpdtgasglpgrpgppgppgppgengfpgqmgirglpgiKGPPGALG 829
Cdd:NF038329 179 DGEAGA------------------------------------------------------------------KGPAGEKG 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 830 LRGPKGDLGEKGERGPPG-RGPKGLPGAIGLPGDPGPASYGKNGRDGEQGPPGVAGIPGV 888
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGpAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGP 252
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 492-761 1.10e-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: 52.70  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380  492 PGPQGIPGaagdqGQRGPPGET------------------GPEGDRGIQGSRGIPGSPGP---------KGDTGLPGVDG 544
Cdd:pfam09606 104 PGPGGPMG-----QQMGGPGTAsnllaslgrpqmpmggagFPSQMSRVGRMQPGGQAGGMmqpssgqpgSGTPNQMGPNG 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380  545 RDGIPGMPGTKGEAGKP---GPPGDVGLQGLPGvPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVG----- 616
Cdd:pfam09606 179 GPGQGQAGGMNGGQQGPmggQMPPQMGVPGMPG-PADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGqqsql 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380  617 ----------PRGPRGLPGSRGPVGPEGSPGI-PGKLGSVGSPGLPGLPGPPGLPGMKGDRGVFGEPGPKGEQGAS-GEE 684
Cdd:pfam09606 258 gmginqmqqmPQGVGGGAGQGGPGQPMGPPGQqPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSvGQG 337

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226693380  685 GEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRGlpgVEGPRGPPGPRGMQGDQGATGLPGIQGPPGRAPTDQH 761
Cdd:pfam09606 338 GQVVALGGLNHLETWNPGNFGGLGANPMQRGQPGMMS---SPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQP 411
PHA03169 PHA03169
hypothetical protein; Provisional
 433-616 2.73e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.66  E-value: 2.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 433 GAKGEIGEPGRQGHKGEEGDQGELG---EVGDQGPPGPQGL--RGITGIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQR 507
Cdd:PHA03169  70 ESDTETAEESRHGEKEERGQGGPSGsgsESVGSPTPSPSGSaeELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEP 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 508 GPPGETGPEGDRGIQGSRGIPGSPG---PKGDTGLPGVDGRDGIPGMPGTKGEAG-----KPGPPGDVGLQGLPGVPGIP 579
Cdd:PHA03169 150 APPESHNPSPNQQPSSFLQPSHEDSpeePEPPTSEPEPDSPGPPQSETPTSSPPPqsppdEPGEPQSPTPQQAPSPNTQQ 229

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 226693380 580 GAKGVAGEKGNTG-APGKPGQLGSSGKPGQQGPPGEVG 616
Cdd:PHA03169 230 AVEHEDEPTEPEReGPPFPGHRSHSYTVVGWKPSTRPG 267
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 820-883 3.86e-05

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: 47.21  E-value: 3.86e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226693380 820 GIKGPPGALGLRGPKGDLGEKGERGPPG-RGPKGLPGAIGLPGDPGPAsygknGRDGEQGPPGVA 883
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGpAGPAGPPGPQGERGEKGPA-----GPQGEAGPQGPA 176
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
417-587 1.84e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.02  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 417 PGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEV--GDQGPPGPQGLR----GITGIVGDKGEKGARGFDG 490
Cdd:COG5164   87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGGSTppgpGSTGPGGSTTPPGDGGSTT 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 491 EPGPQGIPGAAGDQGQRGPP--GETGPEGDRGIQGSRGiPGSPGPKGDtGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVG 568
Cdd:COG5164  167 PPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQG-PDGPVKKDD-KNGKGNPPDDRGGKTGPKDQRPKTNPIERRG 244

                        170
                 ....*....|....*....
gi 226693380 569 LQGLPGVPGIPGAKGVAGE 587
Cdd:COG5164  245 PERPEAAALPAELTALEAE 263
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
594-883 6.67e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 40.01  E-value: 6.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 594 PGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGKLGSVGSPGLPGLPGPPGLPGMKGDRGVFGEPG 673
Cdd:COG5164    3 LYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 674 PKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGirglpgvegprgppgprgmQGDQGATGLPGIQGPp 753
Cdd:COG5164   83 PAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-------------------PPSGGSTTPPGDGGS- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 754 graptdqhikqvcmrvvqehfaemaaslKRPDTGASGLPGRPGPPGPPGPPGENGFPGQMGIRGLPGIKGPP--GALGLR 831
Cdd:COG5164  143 ----------------------------TPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPnkGETGTD 194

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226693380 832 GPKGDLGEKGERGP-------PGRGPKGLPGAIGLPGDPGPAS--YGKNGRDGEQGPPGVA 883
Cdd:COG5164  195 IPTGGTPRQGPDGPvkkddknGKGNPPDDRGGKTGPKDQRPKTnpIERRGPERPEAAALPA 255
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 816-863 8.17e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.55  E-value: 8.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 226693380  816 RGLPGIKGPPGALGLRGPKGDLGEKGERGPPGR-GPKGLPGAIGLPGDP 863
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPpGPPGPPGAPGAPGPP 57
 
Name Accession Description Interval E-value
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 50-244 1.20e-55

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 190.26  E-value: 1.20e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380    50 GQDDLPGFDLISqfqiekaaSRRTIQRVVGSTALQVAYKLGSNVDFRIPTRHLYPSGLPEEYSFLTTFRMTGStleKHWN 129
Cdd:smart00210   1 GQDLLQVFDLPS--------LSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPK---SRGV 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380   130 IWQIQDSAGREQVGVKINGQTKSVAFSYKGLDGSLQTAAFLNLPsLFDSRWHKLMIGVERTSATLFIDCIRIESLPIKPR 209
Cdd:smart00210  70 LFAIYDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLP-LADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRP 148

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 226693380   210 GQ--IDADGFAVLGKLVDNpQVSVPFELQWMLIHCDP 244
Cdd:smart00210 149 GQppIDTDGIEVRGAQAAD-RKPFQGDLQQLKIVCDP 184
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 442-702 9.29e-40

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: 153.14  E-value: 9.29e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 442 GRQGHKGEegdqGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGI 521
Cdd:NF038329 109 GLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 522 QGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGlQGLPGVPGIPGAKGVAGEKGNTGAPGKPGQLG 601
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 602 SSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGKlgsvgspglpglpgppglpgmKGDRGVFGEPGPKGEQGAS 681
Cdd:NF038329 264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGK---------------------DGQNGKDGLPGKDGKDGQP 322

                        250       260
                 ....*....|....*....|.
gi 226693380 682 GEEGEAGARGDLGDMGQPGPK 702
Cdd:NF038329 323 GKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 418-641 1.45e-38

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: 149.67  E-value: 1.45e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 418 GRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGI 497
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 498 PGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGpKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGVPG 577
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226693380 578 IPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGK 641
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 487-755 4.91e-34

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: 136.19  E-value: 4.91e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 487 GFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGD 566
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 567 VGLQGlpgvpgipgakgVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEvGPRGPRGLPGSRGPVGPEGSPGIPGKLGSvg 646
Cdd:NF038329 197 RGETG------------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGP-- 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 647 spglpglpgppglpgmKGDRGVFGEPGPKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRGLPgve 726
Cdd:NF038329 262 ----------------RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP--- 322

                        250       260
                 ....*....|....*....|....*....
gi 226693380 727 gprgppgprgmqGDQGATGLPGIQGPPGR 755
Cdd:NF038329 323 ------------GKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 416-621 5.86e-34

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: 136.19  E-value: 5.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 416 PPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQ 495
Cdd:NF038329 127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQ 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 496 GIPGAAG-----------------DQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEA 558
Cdd:NF038329 207 GPAGPAGpdgeagpagedgpagpaGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPA 286

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226693380 559 GKPGPPGDVGLQGLPGVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPR 621
Cdd:NF038329 287 GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQ 349
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 317-580 4.00e-29

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: 121.55  E-value: 4.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 317 GKPGTPGADGLTGPDGSPGSVGPRGQKGEPGVPGSRgfpgrgipgppgppgttglpgelGRVGPIGdpgkrgppgppgpp 396
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ-----------------------GEAGPQG-------------- 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 397 gpsgtigfhdgdplcpnscPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRGiTGI 476
Cdd:NF038329 175 -------------------PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQ 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 477 VGDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKG 556
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG 314

                        250       260
                 ....*....|....*....|....
gi 226693380 557 EAGKPGPPGDVGLQGLPGVPGIPG 580
Cdd:NF038329 315 KDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 553-759 8.71e-23

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 102.29  E-value: 8.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 553 GTKGEAGKPGPPGDVGLQGlpgvpgipgAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGP 632
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQG---------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 633 EGSPGIPGKLGSVGSPGLPGLPGPPGLPGMKGDRGVFGEPGP--KGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGE 710
Cdd:NF038329 188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 226693380 711 PGLRGPEGIRGlpgvegPRGPPGPRGMQGDQGATGLPGIQGPPGRAPTD 759
Cdd:NF038329 268 AGPDGPDGKDG------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD 310
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 607-881 5.31e-22

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 99.98  E-value: 5.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 607 GQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGKLGsvgspglpglpgppgLPGMKGDRGVFGEPGPKGEQGASGEEGE 686
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPG---------------PQGERGEKGPAGPQGEAGPQGPAGKDGE 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 687 AGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRGLPGVEGPRGPPGPRGM-----QGDQGATGLPGIQGPPGRAPTDqh 761
Cdd:NF038329 182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKD-- 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 762 ikqvcmrvvqehfaemaaslkrpdtgasglpgrpgppgppgppgenGFPGQMGIRGLPGIKGPPGALGLRGPKGDLGEKG 841
Cdd:NF038329 260 ----------------------------------------------GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 226693380 842 ERGPPGR-GPKGLPGAIGLPGDPGPAsyGKNGRDGEQGPPG 881
Cdd:NF038329 294 KDGLPGKdGKDGQNGKDGLPGKDGKD--GQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 320-563 5.35e-20

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: 93.82  E-value: 5.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 320 GTPGADGLTGPDGSPGSVGPRGQKGEPGvpgsrgfpgrgipgppgppgttglpgelgrvgpigdpgkrgppgppgppgps 399
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETG---------------------------------------------------- 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 400 gtigfhdgdplcpnscPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGhKGEEGDQGELGEVGDQGPPGPQGLRGITGIVGD 479
Cdd:NF038329 202 ----------------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 480 KGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPgspgpkGDTGLPGVDGRDGIPGMPGTKGEAG 559
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLP------GKDGKDGQPGKDGLPGKDGKDGQPG 338


                 ....
gi 226693380 560 KPGP 563
Cdd:NF038329 339 KPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 663-883 1.22e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 83.42  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 663 KGDRGVFGEPGPKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRGlpgvegprgppgprgMQGDQG 742
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG---------------KDGEAG 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 743 ATGLPGIQGPPGRAptdqhikqvcmrvvqehfaemaaslkrpdtgasglpGRPGPPGPPGPPGENGFPGQMGIRGLPGIK 822
Cdd:NF038329 184 AKGPAGEKGPQGPR------------------------------------GETGPAGEQGPAGPAGPDGEAGPAGEDGPA 227

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226693380 823 GPPGAlGLRGPKGDLGEKGERGPPG-RGPKGLPGAIGLPGDPGPAsyGKNGRDGEQGPPGVA 883
Cdd:NF038329 228 GPAGD-GQQGPDGDPGPTGEDGPQGpDGPAGKDGPRGDRGEAGPD--GPDGKDGERGPVGPA 286
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 670-888 9.29e-11

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 64.93  E-value: 9.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 670 GEPGPKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPegirglpgvegprgppgprgmQGDQGATGLPGI 749
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGP---------------------QGEAGPQGPAGK 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 750 QGPPGRaptdqhikqvcmrvvqehfaemaaslkrpdtgasglpgrpgppgppgppgengfpgqmgirglpgiKGPPGALG 829
Cdd:NF038329 179 DGEAGA------------------------------------------------------------------KGPAGEKG 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 830 LRGPKGDLGEKGERGPPG-RGPKGLPGAIGLPGDPGPASYGKNGRDGEQGPPGVAGIPGV 888
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGpAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGP 252
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 492-761 1.10e-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: 52.70  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380  492 PGPQGIPGaagdqGQRGPPGET------------------GPEGDRGIQGSRGIPGSPGP---------KGDTGLPGVDG 544
Cdd:pfam09606 104 PGPGGPMG-----QQMGGPGTAsnllaslgrpqmpmggagFPSQMSRVGRMQPGGQAGGMmqpssgqpgSGTPNQMGPNG 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380  545 RDGIPGMPGTKGEAGKP---GPPGDVGLQGLPGvPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVG----- 616
Cdd:pfam09606 179 GPGQGQAGGMNGGQQGPmggQMPPQMGVPGMPG-PADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGqqsql 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380  617 ----------PRGPRGLPGSRGPVGPEGSPGI-PGKLGSVGSPGLPGLPGPPGLPGMKGDRGVFGEPGPKGEQGAS-GEE 684
Cdd:pfam09606 258 gmginqmqqmPQGVGGGAGQGGPGQPMGPPGQqPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSvGQG 337

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226693380  685 GEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRGlpgVEGPRGPPGPRGMQGDQGATGLPGIQGPPGRAPTDQH 761
Cdd:pfam09606 338 GQVVALGGLNHLETWNPGNFGGLGANPMQRGQPGMMS---SPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQP 411
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 583-637 2.42e-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: 2.42e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 226693380  583 GVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPG 637
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 496-552 3.45e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.79  E-value: 3.45e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 226693380  496 GIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMP 552
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 457-512 3.88e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.79  E-value: 3.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 226693380  457 GEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGE 512
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 505-561 6.73e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.02  E-value: 6.73e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 226693380  505 GQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKP 561
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 487-541 9.96e-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: 9.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 226693380  487 GFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPG 541
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 526-581 1.13e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 1.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 226693380  526 GIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGVPGIPGA 581
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 541-597 1.19e-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: 43.64  E-value: 1.19e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 226693380  541 GVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGVPGIPGAKGVAGEKGNTGAPGKP 597
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 580-636 2.66e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 2.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 226693380  580 GAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSP 636
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 433-616 2.73e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.66  E-value: 2.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 433 GAKGEIGEPGRQGHKGEEGDQGELG---EVGDQGPPGPQGL--RGITGIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQR 507
Cdd:PHA03169  70 ESDTETAEESRHGEKEERGQGGPSGsgsESVGSPTPSPSGSaeELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEP 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 508 GPPGETGPEGDRGIQGSRGIPGSPG---PKGDTGLPGVDGRDGIPGMPGTKGEAG-----KPGPPGDVGLQGLPGVPGIP 579
Cdd:PHA03169 150 APPESHNPSPNQQPSSFLQPSHEDSpeePEPPTSEPEPDSPGPPQSETPTSSPPPqsppdEPGEPQSPTPQQAPSPNTQQ 229

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 226693380 580 GAKGVAGEKGNTG-APGKPGQLGSSGKPGQQGPPGEVG 616
Cdd:PHA03169 230 AVEHEDEPTEPEReGPPFPGHRSHSYTVVGWKPSTRPG 267
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 481-535 3.24e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 3.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 226693380  481 GEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKG 535
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 592-644 3.30e-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: 3.30e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 226693380  592 GAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGKLGS 644
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 556-612 3.54e-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: 3.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 226693380  556 GEAGKPGPPGDVGLQGLPGVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPP 612
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 571-627 3.72e-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: 3.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 226693380  571 GLPGVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSR 627
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 820-883 3.86e-05

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: 47.21  E-value: 3.86e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226693380 820 GIKGPPGALGLRGPKGDLGEKGERGPPG-RGPKGLPGAIGLPGDPGPAsygknGRDGEQGPPGVA 883
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGpAGPAGPPGPQGERGEKGPA-----GPQGEAGPQGPA 176
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 559-621 4.89e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 4.89e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226693380  559 GKPGPPGdvglqgLPGVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPR 621
Cdd:pfam01391   1 GPPGPPG------PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 478-533 5.67e-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: 5.67e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 226693380  478 GDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGP 533
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 478-640 8.71e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.52  E-value: 8.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 478 GDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGE 557
Cdd:PRK07764 599 GPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAP 678

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 558 AGKPGPPGDVglqglPGVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPG 637
Cdd:PRK07764 679 AAPPPAPAPA-----APAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAG 753


                 ...
gi 226693380 638 IPG 640
Cdd:PRK07764 754 APA 756
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 502-558 1.08e-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: 40.94  E-value: 1.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 226693380  502 GDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEA 558
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 416-621 1.25e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 416 PPGRSGYPGLPGMRGHKGAKGEIGEPGRQGhkGEEGDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQ 495
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPA--APAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 496 GIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGV 575
Cdd:PRK07764 668 GWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD 747

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 226693380 576 PGIPGakgvagekgntGAPGKPGQLGSSGKPGQQGPPGEVGPRGPR 621
Cdd:PRK07764 748 PPDPA-----------GAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 475-531 1.52e-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: 1.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 226693380  475 GIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPEGDRGIQGSRGIPGSP 531
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
417-587 1.84e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.02  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 417 PGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEV--GDQGPPGPQGLR----GITGIVGDKGEKGARGFDG 490
Cdd:COG5164   87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGGSTppgpGSTGPGGSTTPPGDGGSTT 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 491 EPGPQGIPGAAGDQGQRGPP--GETGPEGDRGIQGSRGiPGSPGPKGDtGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVG 568
Cdd:COG5164  167 PPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQG-PDGPVKKDD-KNGKGNPPDDRGGKTGPKDQRPKTNPIERRG 244

                        170
                 ....*....|....*....
gi 226693380 569 LQGLPGVPGIPGAKGVAGE 587
Cdd:COG5164  245 PERPEAAALPAELTALEAE 263
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 487-613 2.28e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 45.06  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 487 GFDGEPGPQGIPG-AAGDQGQRGPPGETGPEGD---RGIQGSRGIPGSPGPkGDTGLPGVDGrDGIPGMPGTKGEAGKPG 562
Cdd:PRK14959 376 GGASAPSGSAAEGpASGGAATIPTPGTQGPQGTapaAGMTPSSAAPATPAP-SAAPSPRVPW-DDAPPAPPRSGIPPRPA 453

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 226693380 563 ppgdvglqglpgvPGIPGAKGVAGEKGNTG-APGKPGQLGSSGKPGQQGPPG 613
Cdd:PRK14959 454 -------------PRMPEASPVPGAPDSVAsASDAPPTLGDPSDTAEHTPSG 492
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 505-622 2.30e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 45.06  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 505 GQRGPPGETGPEGD-RGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGtKGEAGKPGPPGDvGLQGLPGVPGIPgAKG 583
Cdd:PRK14959 376 GGASAPSGSAAEGPaSGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPA-PSAAPSPRVPWD-DAPPAPPRSGIP-PRP 452

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 226693380 584 VAGEKGNTGAPGKPGQLGS-SGKPGQQGPPGEVGPRGPRG 622
Cdd:PRK14959 453 APRMPEASPVPGAPDSVASaSDAPPTLGDPSDTAEHTPSG 492
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 418-472 3.71e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 3.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 226693380  418 GRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGDQGPPGPQGLRG 472
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 562-624 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: 39.01  E-value: 4.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226693380  562 GPPGDVGLQGLPGVPGIPGAKGVAGEKGNTGAPGKPGQlgssgkPGQQGPPGEVGPRGPRGLP 624
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGP------PGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 670-721 4.26e-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: 4.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 226693380  670 GEPGPKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRG 721
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 664-712 2.14e-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: 2.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 226693380  664 GDRGVFGEPGPKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPG 712
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 498-711 2.27e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 498 PGAAGDQGQRGPPGETGPEgdrgiQGSRgiPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDvglqglpgvpg 577
Cdd:PRK07764 592 PGAAGGEGPPAPASSGPPE-----EAAR--PAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHH----------- 653

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 578 ipgAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGKLGSVGSPGLPGLPGPP 657
Cdd:PRK07764 654 ---PKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASA 730

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 226693380 658 GLPGmkGDRGVFGEPGPKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEP 711
Cdd:PRK07764 731 PSPA--ADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 515-644 2.35e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 41.59  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 515 PEGDRGIQGSRGI--PGSPGPKGDTGLPGvdgrdgipGMPGTKGEAGKPGPPGDVGLQGLPGVPGIPGAKGVAGEKGNtG 592
Cdd:COG5180  311 PPATRPVRPPGGArdPGTPRPGQPTERPA--------GVPEAASDAGQPPSAYPPAEEAVPGKPLEQGAPRPGSSGGD-G 381

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 226693380 593 APGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGKLGS 644
Cdd:COG5180  382 APFQPPNGAPQPGLGRRGAPGPPMGAGDLVQAALDGGGRETASLGGAAGGAG 433
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 667-721 2.76e-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: 2.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 226693380  667 GVFGEPGPKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRG 721
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 451-507 3.08e-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: 3.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 226693380  451 GDQGELGEVGDQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQR 507
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 529-645 6.23e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 40.43  E-value: 6.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 529 GSPGPKGDTGLPGvdgrdgipgmPGTKGEAGKPgPPGDVGLQGlpgvpgipgAKGVAGEKGNTGAPGKPGqlgSSGKPGQ 608
Cdd:PRK14959 376 GGASAPSGSAAEG----------PASGGAATIP-TPGTQGPQG---------TAPAAGMTPSSAAPATPA---PSAAPSP 432

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 226693380 609 QGPPGEVGPRGPR-GLPGSRGPVGPEGSPgIPGKLGSV 645
Cdd:PRK14959 433 RVPWDDAPPAPPRsGIPPRPAPRMPEASP-VPGAPDSV 469
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
594-883 6.67e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 40.01  E-value: 6.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 594 PGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGKLGSVGSPGLPGLPGPPGLPGMKGDRGVFGEPG 673
Cdd:COG5164    3 LYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 674 PKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGirglpgvegprgppgprgmQGDQGATGLPGIQGPp 753
Cdd:COG5164   83 PAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-------------------PPSGGSTTPPGDGGS- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693380 754 graptdqhikqvcmrvvqehfaemaaslKRPDTGASGLPGRPGPPGPPGPPGENGFPGQMGIRGLPGIKGPP--GALGLR 831
Cdd:COG5164  143 ----------------------------TPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPnkGETGTD 194

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226693380 832 GPKGDLGEKGERGP-------PGRGPKGLPGAIGLPGDPGPAS--YGKNGRDGEQGPPGVA 883
Cdd:COG5164  195 IPTGGTPRQGPDGPvkkddknGKGNPPDDRGGKTGPKDQRPKTnpIERRGPERPEAAALPA 255
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 816-863 8.17e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.55  E-value: 8.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 226693380  816 RGLPGIKGPPGALGLRGPKGDLGEKGERGPPGR-GPKGLPGAIGLPGDP 863
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPpGPPGPPGAPGAPGPP 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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