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Conserved domains on  [gi|2462605947|ref|XP_054210189|]
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collagen alpha-1(IX) chain isoform X1 [Homo sapiens]

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 3.02e-62

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


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 208.75  E-value: 3.02e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947   50 GQDDLPGFDLISqfqvdkaaSRRAIQRVVGSATLQVAYKLGNNVDFRIPTRNLYPSGLPEEYSFLTTFRMTGstlKKNWN 129
Cdd:smart00210   1 GQDLLQVFDLPS--------LSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTP---KSRGV 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947  130 IWQIQDSSGKEQVGIKINGQTQSVVFSYKGLDGSLQTAAFSNLsSLFDSQWHKIMIGVERSSATLFVDCNRIESLPIKPR 209
Cdd:smart00210  70 LFAIYDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNL-PLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRP 148

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462605947  210 G--PIDIDGFAVLGKLADNpQVSVPFELQWMLIHCDP 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 ...
 427-727 1.13e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 138.11  E-value: 1.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 427 GMRGHKGAkGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGivgDKGEKGARGLDGEPGPQGLPGAPGDQGQ 506
Cdd:NF038329  109 GLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG---ERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 507 RGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPGtkelskiallmkgepgkpgppgdaglQGLPGVP 586
Cdd:NF038329  185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG--------------------------DGQQGPD 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 587 GIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPGKlgslgspglpglpgp 666
Cdd:NF038329  239 GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGK--------------- 303

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462605947 667 pglpgmKGDRGVVGEPGPKGEQGASGEEgeagergelgdiGLPGPKGSAGNPGEPGLRGPE 727
Cdd:NF038329  304 ------DGQNGKDGLPGKDGKDGQPGKD------------GLPGKDGKDGQPGKPAPKTPE 346
 
Name Accession Description Interval E-value
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 50-244 3.02e-62

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 208.75  E-value: 3.02e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947   50 GQDDLPGFDLISqfqvdkaaSRRAIQRVVGSATLQVAYKLGNNVDFRIPTRNLYPSGLPEEYSFLTTFRMTGstlKKNWN 129
Cdd:smart00210   1 GQDLLQVFDLPS--------LSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTP---KSRGV 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947  130 IWQIQDSSGKEQVGIKINGQTQSVVFSYKGLDGSLQTAAFSNLsSLFDSQWHKIMIGVERSSATLFVDCNRIESLPIKPR 209
Cdd:smart00210  70 LFAIYDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNL-PLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRP 148

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462605947  210 G--PIDIDGFAVLGKLADNpQVSVPFELQWMLIHCDP 244
Cdd:smart00210 149 GqpPIDTDGIEVRGAQAAD-RKPFQGDLQQLKIVCDP 184
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 427-727 1.13e-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: 138.11  E-value: 1.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 427 GMRGHKGAkGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGivgDKGEKGARGLDGEPGPQGLPGAPGDQGQ 506
Cdd:NF038329  109 GLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG---ERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 507 RGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPGtkelskiallmkgepgkpgppgdaglQGLPGVP 586
Cdd:NF038329  185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG--------------------------DGQQGPD 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 587 GIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPGKlgslgspglpglpgp 666
Cdd:NF038329  239 GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGK--------------- 303

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462605947 667 pglpgmKGDRGVVGEPGPKGEQGASGEEgeagergelgdiGLPGPKGSAGNPGEPGLRGPE 727
Cdd:NF038329  304 ------DGQNGKDGLPGKDGKDGQPGKD------------GLPGKDGKDGQPGKPAPKTPE 346
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 396-651 2.55e-28

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 119.24  E-value: 2.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 396 PGPrgtigfhdgdplcpnACPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITG 475
Cdd:NF038329  128 AGP---------------AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 476 IVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGpKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGipgmpgtk 555
Cdd:NF038329  193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG-------- 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 556 elskiallmkgepgkpgppgDAGLQGLPGVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPG 635
Cdd:NF038329  264 --------------------DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                         250
                  ....*....|....*.
gi 2462605947 636 SRGELGPVGSPGLPGK 651
Cdd:NF038329  324 KDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 416-631 9.26e-28

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 117.70  E-value: 9.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 416 PPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGIVGDKGEKGARGLDGEPGPQ 495
Cdd:NF038329  145 PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGED 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 496 GLPGAPGDqGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPGtkelskiallMKGEPGKPGPPG 575
Cdd:NF038329  225 GPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG----------PVGPAGKDGQNG 293

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462605947 576 DAGLQGLPGVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQ 631
Cdd:NF038329  294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQ 349
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 289-607 7.05e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 108.84  E-value: 7.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 289 DGIDGDRGPKGPPGPPgpagepgkpgapGKPGTPGADGLTGPDGSPGSIGSKGQKGEPGVPGSRgfpgrgipgppgppgt 368
Cdd:NF038329  116 DGEKGEPGPAGPAGPA------------GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ---------------- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 369 aglpgelGRVGPVGdpgrrgppgppgppgprgtigfhdgdplcpnacPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKG 448
Cdd:NF038329  168 -------GEAGPQG---------------------------------PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 449 EEGDQGELGEVGAQGPPGAQGLRGiTGIVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIP 528
Cdd:NF038329  208 PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPA 286

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462605947 529 GLPGPKGDTGLPGVDGRDGIPGMPgtkelskiallmkgepgkpgppgdaGLQGLPGVPGIPGAKGVAGEKGSTGAPGKP 607
Cdd:NF038329  287 GKDGQNGKDGLPGKDGKDGQNGKD-------------------------GLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 442-805 3.33e-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: 100.75  E-value: 3.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 442 GRQGHKGEegdqGELGEVGAQGPPGAQGLRGITGIVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGA 521
Cdd:NF038329  109 GLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 522 EGARGIPGLPGPKGDTGLPGVDGRDGIPGmpgtkelskiallmkgepgkpgppgdaglqglpgvpgipgAKGVAGEKGST 601
Cdd:NF038329  185 KGPAGEKGPQGPRGETGPAGEQGPAGPAG----------------------------------------PDGEAGPAGED 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 602 GAPGKPGQmGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPGKLGSLgspglpglpgppglpgmkGDRGVVGE 681
Cdd:NF038329  225 GPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD------------------GERGPVGP 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 682 PGPKGEQGasgeegeagergelgDIGLPGPKGSAGNPGEPGLRGPEGSRGLPgvegprgppgprgvqGEQGATGLPGVQG 761
Cdd:NF038329  286 AGKDGQNG---------------KDGLPGKDGKDGQNGKDGLPGKDGKDGQP---------------GKDGLPGKDGKDG 335

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2462605947 762 PPGRaptdqhikqvcmrviqehfaemaaslkrpdsgatglpgrP 805
Cdd:NF038329  336 QPGK---------------------------------------P 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 576-891 2.75e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 91.89  E-value: 2.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 576 DAGLQGLPGVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSpglpgklgsl 655
Cdd:NF038329  121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE---------- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 656 gspglpglpgppglpgmKGDRGVVGEPGPKGEQGASgeegeagergelgdiGLPGPKGSAGNPGEPGLRGPEGsrglpgv 735
Cdd:NF038329  191 -----------------KGPQGPRGETGPAGEQGPA---------------GPAGPDGEAGPAGEDGPAGPAG------- 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 736 egprgpPGPRGVQGEQGATGLPGVQGPPGRAPTDqhikqvcmrviqehfaemaaslkrpdsgatglpgrpgppgppgppg 815
Cdd:NF038329  232 ------DGQQGPDGDPGPTGEDGPQGPDGPAGKD---------------------------------------------- 259

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605947 816 enGFPGQMGIRGLPGIKGPPGALGLRGPKGDLGEKGERGPPGR-GPNGLPGAIGLPGDPGPAsyGRNGRDGERGPPG 891
Cdd:NF038329  260 --GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKdGKDGQNGKDGLPGKDGKD--GQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 261-555 3.85e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 81.88  E-value: 3.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 261 PSQTTDERGPPGEQGPPGPPGPPGVPGIDGIDGDRGPKGPPGPPgpagepgkpgapGKPGTPGADGLTGPDGSPGSIGSK 340
Cdd:NF038329  133 EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA------------GKDGEAGAKGPAGEKGPQGPRGET 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 341 GQKGEPGVPGsrgfpgrgipgppgppgtaglpgelgrvgpvgdpgrrgppgppgppgprgtigfhdgdplcpnacPPGRS 420
Cdd:NF038329  201 GPAGEQGPAG-----------------------------------------------------------------PAGPD 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 421 GYPGLPGMRGHKGAKGeigepgrQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGIVGDKGEKGARGLDGEPGPQGLPGA 500
Cdd:NF038329  216 GEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK 288

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462605947 501 PGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPGTK 555
Cdd:NF038329  289 DGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 617-893 2.20e-15

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 79.56  E-value: 2.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 617 GQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPGKLGSlgspglpglpgppglpgmKGDRGVVGEPGPKGEQGASgeege 696
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGP------------------QGERGEKGPAGPQGEAGPQ----- 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 697 agergelgdiGLPGPKGSAGNPGEPGLRGPEGSRGLPGVEGPRGPPGPRGVQGEQGATGLPGVQGPPGRaptdqhikqvc 776
Cdd:NF038329  174 ----------GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------- 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 777 mrviqehfaemaaslkrpdsgatglpgrpgppgppgppgengfpGQMGIRGLPGIKGPPGALGLRGPKGDLGEKGERGPP 856
Cdd:NF038329  233 --------------------------------------------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2462605947 857 GR-GPNGLPGAIGLPGDPGpasygrngRDGERGPPGVA 893
Cdd:NF038329  269 GPdGPDGKDGERGPVGPAG--------KDGQNGKDGLP 298
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 487-541 3.95e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.49  E-value: 3.95e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462605947 487 GLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPG 541
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
376-650 1.34e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.41  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 376 GRVGPVGDPGRRGPPGPPGPPGPRGTigfhdgdplcpnacpPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGE 455
Cdd:COG5164    25 GSTKPAQNQGSTRPAGNTGGTRPAQN---------------QGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 456 LGEVGAQGPPGAQGLRGITGIVGDKGEKGARGLDGEPGP--QGLPGAPGDQGQRGP-PGEAGPKGDRGAEGARGIPGLPG 532
Cdd:COG5164    90 TRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPpsGGSTTPPGDGGSTPPgPGSTGPGGSTTPPGDGGSTTPPG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 533 PKGDTGLPGVDGRDGIPGmpgtkelskiallmkgepgkpgppgdaglqglPGVPGIPGAKGVAGEKGSTGAPGKPGQMGN 612
Cdd:COG5164   170 PGGSTTPPDDGGSTTPPN--------------------------------KGETGTDIPTGGTPRQGPDGPVKKDDKNGK 217

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2462605947 613 SGKPGQQGppGEVGPRGPQGLPGSRGELGPVGSPGLPG 650
Cdd:COG5164   218 GNPPDDRG--GKTGPKDQRPKTNPIERRGPERPEAAAL 253
PHA03169 PHA03169
hypothetical protein; Provisional
 433-626 8.44e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.57  E-value: 8.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 433 GAKGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGIVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGE 512
Cdd:PHA03169   70 ESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEP 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 513 AGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPGTKELSKIALLMKGEPGKPGPPGDAGLQGLPGVPGIPGAK 592
Cdd:PHA03169  150 APPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQ 229

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462605947 593 GVAGEKGSTG----APGKPGQMGNSGKPGQQGPPGEVG 626
Cdd:PHA03169  230 AVEHEDEPTEpereGPPFPGHRSHSYTVVGWKPSTRPG 267
 
Name Accession Description Interval E-value
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 50-244 3.02e-62

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 208.75  E-value: 3.02e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947   50 GQDDLPGFDLISqfqvdkaaSRRAIQRVVGSATLQVAYKLGNNVDFRIPTRNLYPSGLPEEYSFLTTFRMTGstlKKNWN 129
Cdd:smart00210   1 GQDLLQVFDLPS--------LSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTP---KSRGV 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947  130 IWQIQDSSGKEQVGIKINGQTQSVVFSYKGLDGSLQTAAFSNLsSLFDSQWHKIMIGVERSSATLFVDCNRIESLPIKPR 209
Cdd:smart00210  70 LFAIYDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNL-PLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRP 148

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462605947  210 G--PIDIDGFAVLGKLADNpQVSVPFELQWMLIHCDP 244
Cdd:smart00210 149 GqpPIDTDGIEVRGAQAAD-RKPFQGDLQQLKIVCDP 184
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 427-727 1.13e-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: 138.11  E-value: 1.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 427 GMRGHKGAkGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGivgDKGEKGARGLDGEPGPQGLPGAPGDQGQ 506
Cdd:NF038329  109 GLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG---ERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 507 RGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPGtkelskiallmkgepgkpgppgdaglQGLPGVP 586
Cdd:NF038329  185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG--------------------------DGQQGPD 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 587 GIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPGKlgslgspglpglpgp 666
Cdd:NF038329  239 GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGK--------------- 303

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462605947 667 pglpgmKGDRGVVGEPGPKGEQGASGEEgeagergelgdiGLPGPKGSAGNPGEPGLRGPE 727
Cdd:NF038329  304 ------DGQNGKDGLPGKDGKDGQPGKD------------GLPGKDGKDGQPGKPAPKTPE 346
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 396-651 2.55e-28

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 119.24  E-value: 2.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 396 PGPrgtigfhdgdplcpnACPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITG 475
Cdd:NF038329  128 AGP---------------AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 476 IVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGpKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGipgmpgtk 555
Cdd:NF038329  193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG-------- 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 556 elskiallmkgepgkpgppgDAGLQGLPGVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPG 635
Cdd:NF038329  264 --------------------DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                         250
                  ....*....|....*.
gi 2462605947 636 SRGELGPVGSPGLPGK 651
Cdd:NF038329  324 KDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 416-631 9.26e-28

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 117.70  E-value: 9.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 416 PPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGIVGDKGEKGARGLDGEPGPQ 495
Cdd:NF038329  145 PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGED 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 496 GLPGAPGDqGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPGtkelskiallMKGEPGKPGPPG 575
Cdd:NF038329  225 GPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG----------PVGPAGKDGQNG 293

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462605947 576 DAGLQGLPGVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQ 631
Cdd:NF038329  294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQ 349
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 289-607 7.05e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 108.84  E-value: 7.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 289 DGIDGDRGPKGPPGPPgpagepgkpgapGKPGTPGADGLTGPDGSPGSIGSKGQKGEPGVPGSRgfpgrgipgppgppgt 368
Cdd:NF038329  116 DGEKGEPGPAGPAGPA------------GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ---------------- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 369 aglpgelGRVGPVGdpgrrgppgppgppgprgtigfhdgdplcpnacPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKG 448
Cdd:NF038329  168 -------GEAGPQG---------------------------------PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 449 EEGDQGELGEVGAQGPPGAQGLRGiTGIVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIP 528
Cdd:NF038329  208 PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPA 286

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462605947 529 GLPGPKGDTGLPGVDGRDGIPGMPgtkelskiallmkgepgkpgppgdaGLQGLPGVPGIPGAKGVAGEKGSTGAPGKP 607
Cdd:NF038329  287 GKDGQNGKDGLPGKDGKDGQNGKD-------------------------GLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 442-805 3.33e-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: 100.75  E-value: 3.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 442 GRQGHKGEegdqGELGEVGAQGPPGAQGLRGITGIVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGA 521
Cdd:NF038329  109 GLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 522 EGARGIPGLPGPKGDTGLPGVDGRDGIPGmpgtkelskiallmkgepgkpgppgdaglqglpgvpgipgAKGVAGEKGST 601
Cdd:NF038329  185 KGPAGEKGPQGPRGETGPAGEQGPAGPAG----------------------------------------PDGEAGPAGED 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 602 GAPGKPGQmGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPGKLGSLgspglpglpgppglpgmkGDRGVVGE 681
Cdd:NF038329  225 GPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD------------------GERGPVGP 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 682 PGPKGEQGasgeegeagergelgDIGLPGPKGSAGNPGEPGLRGPEGSRGLPgvegprgppgprgvqGEQGATGLPGVQG 761
Cdd:NF038329  286 AGKDGQNG---------------KDGLPGKDGKDGQNGKDGLPGKDGKDGQP---------------GKDGLPGKDGKDG 335

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2462605947 762 PPGRaptdqhikqvcmrviqehfaemaaslkrpdsgatglpgrP 805
Cdd:NF038329  336 QPGK---------------------------------------P 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 576-891 2.75e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 91.89  E-value: 2.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 576 DAGLQGLPGVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSpglpgklgsl 655
Cdd:NF038329  121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE---------- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 656 gspglpglpgppglpgmKGDRGVVGEPGPKGEQGASgeegeagergelgdiGLPGPKGSAGNPGEPGLRGPEGsrglpgv 735
Cdd:NF038329  191 -----------------KGPQGPRGETGPAGEQGPA---------------GPAGPDGEAGPAGEDGPAGPAG------- 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 736 egprgpPGPRGVQGEQGATGLPGVQGPPGRAPTDqhikqvcmrviqehfaemaaslkrpdsgatglpgrpgppgppgppg 815
Cdd:NF038329  232 ------DGQQGPDGDPGPTGEDGPQGPDGPAGKD---------------------------------------------- 259

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605947 816 enGFPGQMGIRGLPGIKGPPGALGLRGPKGDLGEKGERGPPGR-GPNGLPGAIGLPGDPGPAsyGRNGRDGERGPPG 891
Cdd:NF038329  260 --GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKdGKDGQNGKDGLPGKDGKD--GQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 261-555 3.85e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 81.88  E-value: 3.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 261 PSQTTDERGPPGEQGPPGPPGPPGVPGIDGIDGDRGPKGPPGPPgpagepgkpgapGKPGTPGADGLTGPDGSPGSIGSK 340
Cdd:NF038329  133 EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA------------GKDGEAGAKGPAGEKGPQGPRGET 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 341 GQKGEPGVPGsrgfpgrgipgppgppgtaglpgelgrvgpvgdpgrrgppgppgppgprgtigfhdgdplcpnacPPGRS 420
Cdd:NF038329  201 GPAGEQGPAG-----------------------------------------------------------------PAGPD 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 421 GYPGLPGMRGHKGAKGeigepgrQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGIVGDKGEKGARGLDGEPGPQGLPGA 500
Cdd:NF038329  216 GEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK 288

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462605947 501 PGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPGTK 555
Cdd:NF038329  289 DGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 617-893 2.20e-15

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 79.56  E-value: 2.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 617 GQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPGKLGSlgspglpglpgppglpgmKGDRGVVGEPGPKGEQGASgeege 696
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGP------------------QGERGEKGPAGPQGEAGPQ----- 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 697 agergelgdiGLPGPKGSAGNPGEPGLRGPEGSRGLPGVEGPRGPPGPRGVQGEQGATGLPGVQGPPGRaptdqhikqvc 776
Cdd:NF038329  174 ----------GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------- 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 777 mrviqehfaemaaslkrpdsgatglpgrpgppgppgppgengfpGQMGIRGLPGIKGPPGALGLRGPKGDLGEKGERGPP 856
Cdd:NF038329  233 --------------------------------------------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2462605947 857 GR-GPNGLPGAIGLPGDPGpasygrngRDGERGPPGVA 893
Cdd:NF038329  269 GPdGPDGKDGERGPVGPAG--------KDGQNGKDGLP 298
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 487-541 3.95e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.49  E-value: 3.95e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462605947 487 GLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPG 541
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 496-552 4.03e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.49  E-value: 4.03e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605947 496 GLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMP 552
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 593-649 1.09e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.33  E-value: 1.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605947 593 GVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLP 649
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 457-513 2.76e-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: 45.18  E-value: 2.76e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605947 457 GEVGAQGPPGAQGLRGITGIVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEA 513
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 481-535 4.08e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.79  E-value: 4.08e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462605947 481 GEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKG 535
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 463-519 6.94e-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: 6.94e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605947 463 GPPGAQGLRGITGIVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDR 519
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 484-540 8.04e-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: 8.04e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605947 484 GARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLP 540
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 478-533 1.38e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 1.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462605947 478 GDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGP 533
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 475-531 2.19e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 2.19e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605947 475 GIVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIPGLP 531
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 584-639 4.66e-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: 41.71  E-value: 4.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462605947 584 GVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGE 639
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 581-637 4.76e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 4.76e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605947 581 GLPGVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSR 637
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 505-553 7.12e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 7.12e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2462605947 505 GQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPG 553
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 466-521 1.05e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 1.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462605947 466 GAQGLRGITGIVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGA 521
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
376-650 1.34e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.41  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 376 GRVGPVGDPGRRGPPGPPGPPGPRGTigfhdgdplcpnacpPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGE 455
Cdd:COG5164    25 GSTKPAQNQGSTRPAGNTGGTRPAQN---------------QGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 456 LGEVGAQGPPGAQGLRGITGIVGDKGEKGARGLDGEPGP--QGLPGAPGDQGQRGP-PGEAGPKGDRGAEGARGIPGLPG 532
Cdd:COG5164    90 TRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPpsGGSTTPPGDGGSTPPgPGSTGPGGSTTPPGDGGSTTPPG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 533 PKGDTGLPGVDGRDGIPGmpgtkelskiallmkgepgkpgppgdaglqglPGVPGIPGAKGVAGEKGSTGAPGKPGQMGN 612
Cdd:COG5164   170 PGGSTTPPDDGGSTTPPN--------------------------------KGETGTDIPTGGTPRQGPDGPVKKDDKNGK 217

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2462605947 613 SGKPGQQGppGEVGPRGPQGLPGSRGELGPVGSPGLPG 650
Cdd:COG5164   218 GNPPDDRG--GKTGPKDQRPKTNPIERRGPERPEAAAL 253
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 418-472 2.90e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 2.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462605947 418 GRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRG 472
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 602-650 3.11e-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: 3.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2462605947 602 GAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPG 650
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 454-510 4.70e-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: 4.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605947 454 GELGEVGAQGPPGAQGLRGITGIVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPP 510
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 451-507 6.07e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 6.07e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605947 451 GDQGELGEVGAQGPPGAQGLRGITGIVGDKGEKGARGLDGEPGPQGLPGAPGDQGQR 507
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 577-628 7.77e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 7.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462605947 577 AGLQGLPGVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPR 628
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 433-626 8.44e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.57  E-value: 8.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 433 GAKGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGIVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGE 512
Cdd:PHA03169   70 ESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEP 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605947 513 AGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPGTKELSKIALLMKGEPGKPGPPGDAGLQGLPGVPGIPGAK 592
Cdd:PHA03169  150 APPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQ 229

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462605947 593 GVAGEKGSTG----APGKPGQMGNSGKPGQQGPPGEVG 626
Cdd:PHA03169  230 AVEHEDEPTEpereGPPFPGHRSHSYTVVGWKPSTRPG 267
 
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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