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Conserved domains on  [gi|30084|emb|CAA38276|]
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unnamed protein product [Homo sapiens]

Protein Classification

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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 2.79e-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: 2.79e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084        50 GQDDLPGFDLISqfqvdkaaSRRAIQRVVGSATLQVAYKLGNNVDFRIPTRNLYPSGLPEEYSFLTTFRMTGstlKKNWN 129
Cdd:smart00210   1 GQDLLQVFDLPS--------LSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTP---KSRGV 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084       130 IWQIQDSSGKEQVGIKINGQTQSVVFSYKGLDGSLQTAAFSNLsSLFDSQWHKIMIGVERSSATLFVDCNRIESLPIKPR 209
Cdd:smart00210  70 LFAIYDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNL-PLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRP 148

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 30084       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 ...
 427-717 1.84e-36

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: 143.51  E-value: 1.84e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     427 GMRGHKGAkGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGlvgDKGEKGARGLDGEPGPQGLPGAPGDQGQ 506
Cdd:NF038329 109 GLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG---ERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     507 RGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPGtkgepgkpgppgdaglQGLPGVPGIPGAKGVAG 586
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------DGQQGPDGDPGPTGEDG 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     587 EKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPGKlgslgspglpglpgppglpgmKGDR 666
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGK---------------------DGQN 307

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30084     667 GVVGEPGPKGEQGASGEEgeagergelgdiGLPGPKGSAGNPGEPGLRGPE 717
Cdd:NF038329 308 GKDGLPGKDGKDGQPGKD------------GLPGKDGKDGQPGKPAPKTPE 346
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 816-863 6.72e-03

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


:

Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.55  E-value: 6.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 30084      816 RGLPGIKGPPGALGLRGPKGDLGEKGERGPPGR-GPNGLPGAIGLPGDP 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 2.79e-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: 2.79e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084        50 GQDDLPGFDLISqfqvdkaaSRRAIQRVVGSATLQVAYKLGNNVDFRIPTRNLYPSGLPEEYSFLTTFRMTGstlKKNWN 129
Cdd:smart00210   1 GQDLLQVFDLPS--------LSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTP---KSRGV 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084       130 IWQIQDSSGKEQVGIKINGQTQSVVFSYKGLDGSLQTAAFSNLsSLFDSQWHKIMIGVERSSATLFVDCNRIESLPIKPR 209
Cdd:smart00210  70 LFAIYDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNL-PLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRP 148

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 30084       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 ...
 427-717 1.84e-36

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: 143.51  E-value: 1.84e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     427 GMRGHKGAkGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGlvgDKGEKGARGLDGEPGPQGLPGAPGDQGQ 506
Cdd:NF038329 109 GLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG---ERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     507 RGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPGtkgepgkpgppgdaglQGLPGVPGIPGAKGVAG 586
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------DGQQGPDGDPGPTGEDG 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     587 EKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPGKlgslgspglpglpgppglpgmKGDR 666
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGK---------------------DGQN 307

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30084     667 GVVGEPGPKGEQGASGEEgeagergelgdiGLPGPKGSAGNPGEPGLRGPE 717
Cdd:NF038329 308 GKDGLPGKDGKDGQPGKD------------GLPGKDGKDGQPGKPAPKTPE 346
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 416-625 9.92e-32

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 129.25  E-value: 9.92e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     416 PPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGLVGDKGEKGARGLDGEPGPQ 495
Cdd:NF038329 145 PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGED 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     496 GLPGAPGDqGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGmpgtkgepgkpgppgDAGLQGLPGV 575
Cdd:NF038329 225 GPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG---------------ERGPVGPAGK 288

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 30084     576 PGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPG 625
Cdd:NF038329 289 DGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 289-597 1.54e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 113.85  E-value: 1.54e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     289 DGIDGDRGPKGPPGPPgpagepgkpgapGKPGTPGADGLTGPDGSPGSIGSKGQKGEPGVPGSRgfpgrgipgppgppgt 368
Cdd:NF038329 116 DGEKGEPGPAGPAGPA------------GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ---------------- 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     369 aglpgelGRVGPVGdpgrrgppgppgppgprgtigfhdgdplcpnacPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKG 448
Cdd:NF038329 168 -------GEAGPQG---------------------------------PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     449 EEGDQGELGEVGAQGPPGAQGLRGiTGLVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIP 528
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPA 286

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30084     529 GLPGPKGDTGLPGVDGRDGIPGMPgtkgepgkpgppgdaGLQGLPGVPGIPGAKGVAGEKGSTGAPGKP 597
Cdd:NF038329 287 GKDGQNGKDGLPGKDGKDGQNGKD---------------GLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 442-795 6.60e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 105.76  E-value: 6.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     442 GRQGHKGEegdqGELGEVGAQGPPGAQGLRGITGLVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGA 521
Cdd:NF038329 109 GLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     522 EGARGIPGLPGPKGDTGLPGVDGRDGIPGmpgtkgepgkpgppgdaglqglpgvpgipgAKGVAGEKGSTGAPGKPGQmG 601
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGEQGPAGPAG------------------------------PDGEAGPAGEDGPAGPAGD-G 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     602 NSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPGKLGSLgspglpglpgppglpgmkGDRGVVGEPGPKGEQGas 681
Cdd:NF038329 234 QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD------------------GERGPVGPAGKDGQNG-- 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     682 geegeagergelgDIGLPGPKGSAGNPGEPGLRGPEGSRGLPgvegprgppgprgvqGEQGATGLPGVQGPPGRaptdqh 761
Cdd:NF038329 294 -------------KDGLPGKDGKDGQNGKDGLPGKDGKDGQP---------------GKDGLPGKDGKDGQPGK------ 339

                        330       340       350
                 ....*....|....*....|....*....|....
gi 30084     762 ikqvcmrviqehfaemaaslkrpdsgatglpgrP 795
Cdd:NF038329 340 ---------------------------------P 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 566-881 1.09e-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: 93.05  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     566 DAGLQGLPGVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSpglpgklgsl 645
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE---------- 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     646 gspglpglpgppglpgmKGDRGVVGEPGPKGEQGASgeegeagergelgdiGLPGPKGSAGNPGEPGLRGPEGsrglpgv 725
Cdd:NF038329 191 -----------------KGPQGPRGETGPAGEQGPA---------------GPAGPDGEAGPAGEDGPAGPAG------- 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     726 egprgpPGPRGVQGEQGATGLPGVQGPPGRAPTDqhikqvcmrviqehfaemaaslkrpdsgatglpgrpgppgppgppg 805
Cdd:NF038329 232 ------DGQQGPDGDPGPTGEDGPQGPDGPAGKD---------------------------------------------- 259

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30084     806 enGFPGQMGIRGLPGIKGPPGALGLRGPKGDLGEKGERGPPGR-GPNGLPGAIGLPGDPGPAsyGKNGRDGERGPPG 881
Cdd:NF038329 260 --GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKdGKDGQNGKDGLPGKDGKD--GQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 261-552 2.87e-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: 82.26  E-value: 2.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     261 PSQTTDERGPPGEQGPPGASGPPGVPGIDGIDGDRGPKGPPGPPgpagepgkpgapGKPGTPGADGLTGPDGSPGSIGSK 340
Cdd:NF038329 133 EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA------------GKDGEAGAKGPAGEKGPQGPRGET 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     341 GQKGEPGVPGsrgfpgrgipgppgppgtaglpgelgrvgpvgdpgrrgppgppgppgprgtigfhdgdplcpnacPPGRS 420
Cdd:NF038329 201 GPAGEQGPAG-----------------------------------------------------------------PAGPD 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     421 GYPGLPGMRGHKGAKGeigepgrQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGLVGDKGEKGARGLDGEPGPQGLPGA 500
Cdd:NF038329 216 GEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK 288

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30084     501 PGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMP 552
Cdd:NF038329 289 DGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 607-883 3.92e-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: 3.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     607 GQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPGKLGSlgspglpglpgppglpgmKGDRGVVGEPGPKGEQGASgeege 686
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGP------------------QGERGEKGPAGPQGEAGPQ----- 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     687 agergelgdiGLPGPKGSAGNPGEPGLRGPEGSRGLPGVEGPRGPPGPRGVQGEQGATGLPGVQGPPGRaptdqhikqvc 766
Cdd:NF038329 174 ----------GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------- 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     767 mrviqehfaemaaslkrpdsgatglpgrpgppgppgppgengfpGQMGIRGLPGIKGPPGALGLRGPKGDLGEKGERGPP 846
Cdd:NF038329 233 --------------------------------------------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 30084     847 GR-GPNGLPGAIGLPGDPGpasygkngRDGERGPPGLA 883
Cdd:NF038329 269 GPdGPDGKDGERGPVGPAG--------KDGQNGKDGLP 298
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 496-552 2.09e-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: 48.26  E-value: 2.09e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 30084      496 GLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMP 552
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
376-640 5.19e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 50.03  E-value: 5.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084    376 GRVGPVGDPGRRGPPGPPgppgprgtigfhdgdplcpnacppGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQge 455
Cdd:COG5164  25 GSTKPAQNQGSTRPAGNT------------------------GGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQ-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084    456 lgevGAQGPPGAQGLRGITGLVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPP--GEAGPKGDRGAEGARgiPGLPGP 533
Cdd:COG5164  79 ----GGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGGSTPPG--PGSTGP 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084    534 KGDTGLPGVDGRDGIPGMPGTKGEPGKPGppgdAGLQGLPGVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGppG 613
Cdd:COG5164 153 GGSTTPPGDGGSTTPPGPGGSTTPPDDGG----STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--G 226

                       250       260
                ....*....|....*....|....*..
gi 30084    614 EVGPRGPQGLPGSRGELGPVGSPGLPG 640
Cdd:COG5164 227 KTGPKDQRPKTNPIERRGPERPEAAAL 253
PHA03169 PHA03169
hypothetical protein; Provisional
 433-625 1.85e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 44.96  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     433 GAKGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGLVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGE 512
Cdd:PHA03169  70 ESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEP 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     513 AGPKGDRGAEGARGIPGLPG--------PKGDTGLPGVDGRDGIPGMPGTKGEPGKPGPPGDAGLQGlPGVPGIPGAKGv 584
Cdd:PHA03169 150 APPESHNPSPNQQPSSFLQPshedspeePEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQS-PTPQQAPSPNT- 227

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 30084     585 aGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPG 625
Cdd:PHA03169 228 -QQAVEHEDEPTEPEREGPPFPGHRSHSYTVVGWKPSTRPG 267
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 816-863 6.72e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.55  E-value: 6.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 30084      816 RGLPGIKGPPGALGLRGPKGDLGEKGERGPPGR-GPNGLPGAIGLPGDP 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 2.79e-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: 2.79e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084        50 GQDDLPGFDLISqfqvdkaaSRRAIQRVVGSATLQVAYKLGNNVDFRIPTRNLYPSGLPEEYSFLTTFRMTGstlKKNWN 129
Cdd:smart00210   1 GQDLLQVFDLPS--------LSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTP---KSRGV 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084       130 IWQIQDSSGKEQVGIKINGQTQSVVFSYKGLDGSLQTAAFSNLsSLFDSQWHKIMIGVERSSATLFVDCNRIESLPIKPR 209
Cdd:smart00210  70 LFAIYDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNL-PLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRP 148

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 30084       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 ...
 427-717 1.84e-36

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: 143.51  E-value: 1.84e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     427 GMRGHKGAkGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGlvgDKGEKGARGLDGEPGPQGLPGAPGDQGQ 506
Cdd:NF038329 109 GLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG---ERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     507 RGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPGtkgepgkpgppgdaglQGLPGVPGIPGAKGVAG 586
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------DGQQGPDGDPGPTGEDG 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     587 EKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPGKlgslgspglpglpgppglpgmKGDR 666
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGK---------------------DGQN 307

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30084     667 GVVGEPGPKGEQGASGEEgeagergelgdiGLPGPKGSAGNPGEPGLRGPE 717
Cdd:NF038329 308 GKDGLPGKDGKDGQPGKD------------GLPGKDGKDGQPGKPAPKTPE 346
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 416-625 9.92e-32

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 129.25  E-value: 9.92e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     416 PPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGLVGDKGEKGARGLDGEPGPQ 495
Cdd:NF038329 145 PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGED 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     496 GLPGAPGDqGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGmpgtkgepgkpgppgDAGLQGLPGV 575
Cdd:NF038329 225 GPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG---------------ERGPVGPAGK 288

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 30084     576 PGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPG 625
Cdd:NF038329 289 DGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 289-597 1.54e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 113.85  E-value: 1.54e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     289 DGIDGDRGPKGPPGPPgpagepgkpgapGKPGTPGADGLTGPDGSPGSIGSKGQKGEPGVPGSRgfpgrgipgppgppgt 368
Cdd:NF038329 116 DGEKGEPGPAGPAGPA------------GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ---------------- 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     369 aglpgelGRVGPVGdpgrrgppgppgppgprgtigfhdgdplcpnacPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKG 448
Cdd:NF038329 168 -------GEAGPQG---------------------------------PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     449 EEGDQGELGEVGAQGPPGAQGLRGiTGLVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIP 528
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPA 286

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30084     529 GLPGPKGDTGLPGVDGRDGIPGMPgtkgepgkpgppgdaGLQGLPGVPGIPGAKGVAGEKGSTGAPGKP 597
Cdd:NF038329 287 GKDGQNGKDGLPGKDGKDGQNGKD---------------GLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 442-795 6.60e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 105.76  E-value: 6.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     442 GRQGHKGEegdqGELGEVGAQGPPGAQGLRGITGLVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGA 521
Cdd:NF038329 109 GLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     522 EGARGIPGLPGPKGDTGLPGVDGRDGIPGmpgtkgepgkpgppgdaglqglpgvpgipgAKGVAGEKGSTGAPGKPGQmG 601
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGEQGPAGPAG------------------------------PDGEAGPAGEDGPAGPAGD-G 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     602 NSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPGKLGSLgspglpglpgppglpgmkGDRGVVGEPGPKGEQGas 681
Cdd:NF038329 234 QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD------------------GERGPVGPAGKDGQNG-- 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     682 geegeagergelgDIGLPGPKGSAGNPGEPGLRGPEGSRGLPgvegprgppgprgvqGEQGATGLPGVQGPPGRaptdqh 761
Cdd:NF038329 294 -------------KDGLPGKDGKDGQNGKDGLPGKDGKDGQP---------------GKDGLPGKDGKDGQPGK------ 339

                        330       340       350
                 ....*....|....*....|....*....|....
gi 30084     762 ikqvcmrviqehfaemaaslkrpdsgatglpgrP 795
Cdd:NF038329 340 ---------------------------------P 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 566-881 1.09e-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: 93.05  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     566 DAGLQGLPGVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSpglpgklgsl 645
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE---------- 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     646 gspglpglpgppglpgmKGDRGVVGEPGPKGEQGASgeegeagergelgdiGLPGPKGSAGNPGEPGLRGPEGsrglpgv 725
Cdd:NF038329 191 -----------------KGPQGPRGETGPAGEQGPA---------------GPAGPDGEAGPAGEDGPAGPAG------- 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     726 egprgpPGPRGVQGEQGATGLPGVQGPPGRAPTDqhikqvcmrviqehfaemaaslkrpdsgatglpgrpgppgppgppg 805
Cdd:NF038329 232 ------DGQQGPDGDPGPTGEDGPQGPDGPAGKD---------------------------------------------- 259

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30084     806 enGFPGQMGIRGLPGIKGPPGALGLRGPKGDLGEKGERGPPGR-GPNGLPGAIGLPGDPGPAsyGKNGRDGERGPPG 881
Cdd:NF038329 260 --GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKdGKDGQNGKDGLPGKDGKD--GQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 261-552 2.87e-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: 82.26  E-value: 2.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     261 PSQTTDERGPPGEQGPPGASGPPGVPGIDGIDGDRGPKGPPGPPgpagepgkpgapGKPGTPGADGLTGPDGSPGSIGSK 340
Cdd:NF038329 133 EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA------------GKDGEAGAKGPAGEKGPQGPRGET 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     341 GQKGEPGVPGsrgfpgrgipgppgppgtaglpgelgrvgpvgdpgrrgppgppgppgprgtigfhdgdplcpnacPPGRS 420
Cdd:NF038329 201 GPAGEQGPAG-----------------------------------------------------------------PAGPD 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     421 GYPGLPGMRGHKGAKGeigepgrQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGLVGDKGEKGARGLDGEPGPQGLPGA 500
Cdd:NF038329 216 GEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK 288

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30084     501 PGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMP 552
Cdd:NF038329 289 DGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 607-883 3.92e-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: 3.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     607 GQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPGKLGSlgspglpglpgppglpgmKGDRGVVGEPGPKGEQGASgeege 686
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGP------------------QGERGEKGPAGPQGEAGPQ----- 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     687 agergelgdiGLPGPKGSAGNPGEPGLRGPEGSRGLPGVEGPRGPPGPRGVQGEQGATGLPGVQGPPGRaptdqhikqvc 766
Cdd:NF038329 174 ----------GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------- 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     767 mrviqehfaemaaslkrpdsgatglpgrpgppgppgppgengfpGQMGIRGLPGIKGPPGALGLRGPKGDLGEKGERGPP 846
Cdd:NF038329 233 --------------------------------------------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 30084     847 GR-GPNGLPGAIGLPGDPGpasygkngRDGERGPPGLA 883
Cdd:NF038329 269 GPdGPDGKDGERGPVGPAG--------KDGQNGKDGLP 298
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 496-552 2.09e-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: 48.26  E-value: 2.09e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 30084      496 GLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMP 552
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 487-541 2.15e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.26  E-value: 2.15e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30084      487 GLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPG 541
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 583-639 6.21e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.10  E-value: 6.21e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 30084      583 GVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLP 639
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 457-513 1.94e-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: 45.56  E-value: 1.94e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 30084      457 GEVGAQGPPGAQGLRGITGLVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEA 513
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 481-535 2.31e-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: 2.31e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30084      481 GEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKG 535
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 484-540 4.73e-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: 44.79  E-value: 4.73e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 30084      484 GARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLP 540
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 463-519 4.82e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.41  E-value: 4.82e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 30084      463 GPPGAQGLRGITGLVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDR 519
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
376-640 5.19e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 50.03  E-value: 5.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084    376 GRVGPVGDPGRRGPPGPPgppgprgtigfhdgdplcpnacppGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQge 455
Cdd:COG5164  25 GSTKPAQNQGSTRPAGNT------------------------GGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQ-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084    456 lgevGAQGPPGAQGLRGITGLVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPP--GEAGPKGDRGAEGARgiPGLPGP 533
Cdd:COG5164  79 ----GGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGGSTPPG--PGSTGP 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084    534 KGDTGLPGVDGRDGIPGMPGTKGEPGKPGppgdAGLQGLPGVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGppG 613
Cdd:COG5164 153 GGSTTPPGDGGSTTPPGPGGSTTPPDDGG----STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--G 226

                       250       260
                ....*....|....*....|....*..
gi 30084    614 EVGPRGPQGLPGSRGELGPVGSPGLPG 640
Cdd:COG5164 227 KTGPKDQRPKTNPIERRGPERPEAAAL 253
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 475-531 5.37e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.41  E-value: 5.37e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 30084      475 GLVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIPGLP 531
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 460-515 7.65e-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: 7.65e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 30084      460 GAQGPPGAQGLRGITGLVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGP 515
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 478-533 7.96e-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: 44.02  E-value: 7.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 30084      478 GDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGP 533
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 574-629 2.74e-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: 2.74e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 30084      574 GVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGE 629
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 571-627 2.83e-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: 2.83e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 30084      571 GLPGVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSR 627
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 505-553 4.27e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 4.27e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 30084      505 GQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPG 553
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 418-472 1.79e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 1.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30084      418 GRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRG 472
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 433-625 1.85e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 44.96  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     433 GAKGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGLVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGE 512
Cdd:PHA03169  70 ESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEP 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     513 AGPKGDRGAEGARGIPGLPG--------PKGDTGLPGVDGRDGIPGMPGTKGEPGKPGPPGDAGLQGlPGVPGIPGAKGv 584
Cdd:PHA03169 150 APPESHNPSPNQQPSSFLQPshedspeePEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQS-PTPQQAPSPNT- 227

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 30084     585 aGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPG 625
Cdd:PHA03169 228 -QQAVEHEDEPTEPEREGPPFPGHRSHSYTVVGWKPSTRPG 267
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 592-640 1.98e-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: 1.98e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 30084      592 GAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPG 640
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 454-510 3.40e-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: 3.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 30084      454 GELGEVGAQGPPGAQGLRGITGLVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPP 510
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 502-553 3.43e-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: 3.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 30084      502 GDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPG 553
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 451-507 4.18e-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: 4.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 30084      451 GDQGELGEVGAQGPPGAQGLRGITGLVGDKGEKGARGLDGEPGPQGLPGAPGDQGQR 507
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 567-618 4.66e-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: 4.66e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 30084      567 AGLQGLPGVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPR 618
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 501-622 8.99e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 43.13  E-value: 8.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     501 PGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPGTKGEPGKPGPPGDAglQGLPGVPGIPg 580
Cdd:PRK14959 373 PSGGGASAPSGSAAEGPASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPAPSAAPSPRVPWDDA--PPAPPRSGIP- 449

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 30084     581 AKGVAGEKGSTGAPGKPGQMGN-SGKPGQQGPPGEVGPRGPQG 622
Cdd:PRK14959 450 PRPAPRMPEASPVPGAPDSVASaSDAPPTLGDPSDTAEHTPSG 492
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 492-760 4.75e-03

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: 40.76  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084      492 PGPQGLPGapgdqGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPGTKGEPGKPGPPGDAGLQG 571
Cdd:pfam09606 104 PGPGGPMG-----QQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNG 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084      572 LPGVPGIPGAKGVAG------EKGSTGAPGKPGQMGNSGKPGQQGPPGevGPRGPQGLPGSRGELGPVGSPGLPGKLGSL 645
Cdd:pfam09606 179 GPGQGQAGGMNGGQQgpmggqMPPQMGVPGMPGPADAGAQMGQQAQAN--GGMNPQQMGGAPNQVAMQQQQPQQQGQQSQ 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084      646 GSPGLPGLPGPPGLPGMKGDRGVVGEPGPKGEQGASGEEGEAGERGELGDIGLP--------GPKGSAGNPGEPGLRGPE 717
Cdd:pfam09606 257 LGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQtrqqqqqqGGNHPAAHQQQMNQSVGQ 336

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 30084      718 GSRGLPGVEGPRGPPGPRGVQGEQGATglPGVQGPPGRAPTDQ 760
Cdd:pfam09606 337 GGQVVALGGLNHLETWNPGNFGGLGAN--PMQRGQPGMMSSPS 377
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 816-863 6.72e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.55  E-value: 6.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 30084      816 RGLPGIKGPPGALGLRGPKGDLGEKGERGPPGR-GPNGLPGAIGLPGDP 863
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPpGPPGPPGAPGAPGPP 57
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 487-613 8.87e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 39.66  E-value: 8.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30084     487 GLDGEPGPQGLPG-APGDQGQRGPPGEAGPKGDRGAEG---ARGIPGLPGPkGDTGLPGVDGRDGIPGMPGTKGEPGkpg 562
Cdd:PRK14959 376 GGASAPSGSAAEGpASGGAATIPTPGTQGPQGTAPAAGmtpSSAAPATPAP-SAAPSPRVPWDDAPPAPPRSGIPPR--- 451

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30084     563 ppgdaglqglpGVPGIPGAKGVAGEKGSTG-APGKPGQMGNSGKPGQQGPPG 613
Cdd:PRK14959 452 -----------PAPRMPEASPVPGAPDSVAsASDAPPTLGDPSDTAEHTPSG 492
 
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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