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Conserved domains on  [gi|527504093|sp|P17139|]
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RecName: Full=Collagen alpha-1(IV) chain; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1645-1758 2.42e-62

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


:

Pssm-ID: 128421  Cd Length: 114  Bit Score: 208.01  E-value: 2.42e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093   1645 TQIIAVHSQDTSVPQCPQGWSGMWTGYSFVMHTAaGAEGTGQSLQSPGSCLEEFRAVPFIECHGRGTCNYYATN-HGFWL 1723
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTG-NGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNdYSFWL 79

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 527504093   1724 SIVDQDKQFRKPMSQTLKAGGLKDRVSRCQVCLKN 1758
Cdd:smart00111   80 STIEPSDQFTAPRPMTPKAGDLRPYISRCQVCEKP 114
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1536-1642 1.42e-60

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


:

Pssm-ID: 460201  Cd Length: 110  Bit Score: 202.82  E-value: 1.42e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1536 FTFAKHSQTTAVPQCPPGASQLWEGYSLLYVQGNGRASGQDLGQPGSCLSKFNTMPFMFCNMNSVCHVSSrNDYSFWLST 1615
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 527504093  1616 DE---PMTPMMNPVTGTAIRPYISRCAVCE 1642
Cdd:pfam01413   80 VEeqfRKPMSQTPKAGNELRSYISRCVVCE 109
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 257-478 2.04e-29

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 123.48  E-value: 2.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  257 QGPVGPAGVKGE---KGRDGPVGPPGMLGLDGPPGYPGLKGQKGDLGDAGQRGKRGKDGVPGNYGEKGSQGEQGLGGTPG 333
Cdd:NF038329  122 PGPAGPAGPAGEqgpRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  334 YPGTKGGAGEPGYPGRPGFEGDCGPEGPLGEG-TGEAGPHGAQGFDGVQGGKGLPGHDGLPGPVGPRGPVGAPGAPGQPG 412
Cdd:NF038329  202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527504093  413 IDGMPGytEKGDRGEDGYPGFAGEPGLPGEPGDCGYPGEDGLPGYDiqgppGLDGQSGRDGFPGIP 478
Cdd:NF038329  282 PVGPAG--KDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD-----GLPGKDGKDGQPGKP 340
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 697-947 1.09e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 121.55  E-value: 1.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  697 GYKGERGADGLPGLPGAQGPRGipaplrivnqvagQPGVDGMPGLPGDRGADGLPGLPGPVGPDGYPGTPGERGMDGLPG 776
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRG-------------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  777 FPGLHGEPGMRGQQGEVGFNGIDGDCGEPGLDGYPGAPGAPGAPGETGFGFPGQVGYPGPNGDAGAAGLPGPDGYPGRDG 856
Cdd:NF038329  184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  857 LPGTPGYPGEAGMNGQDGAPGQPGSrgesglvgiDGKKGRDGTPGTRGQDGgpgYSGEAGAPGQNGMDGYPGAPGDQGYP 936
Cdd:NF038329  264 DRGEAGPDGPDGKDGERGPVGPAGK---------DGQNGKDGLPGKDGKDG---QNGKDGLPGKDGKDGQPGKDGLPGKD 331

                         250
                  ....*....|.
gi 527504093  937 GSPGQDGYPGP 947
Cdd:NF038329  332 GKDGQPGKPAP 342
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1167-1429 2.79e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 114.23  E-value: 2.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1167 GIPGENGLPGLRGQDGQPGLKGENGLDGQPGYPGSAGQLGTPGDVGYPGAPGENGDNGNQGRDGQPGLRGESGQPGQPGL 1246
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1247 PGRDgqpgpvgppgddgypgapgqdiyGPPGQAGQDGYPGLDGLPGAPGLNGEPGSPGQygmpglpggpgesglpGYPGE 1326
Cdd:NF038329  197 RGET-----------------------GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------------GQQGP 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1327 RGLPGLDGKRGHDGLPGAPGVPGVEGVPGLEGDCGEDGYPGAPGAPGSNGYPGERGLPGVPGQQGRSGDNGYPGAPGQPG 1406
Cdd:NF038329  238 DGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317

                         250       260
                  ....*....|....*....|...
gi 527504093 1407 IKGPRGDDGFPGRDGLDGLPGRP 1429
Cdd:NF038329  318 KDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 986-1244 3.02e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 108.07  E-value: 3.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  986 LDGVPGYPGEHGTDGLPGLPGADGQPGFVGEAGEPGTPGYRGQPGEPGNLAYPGQPGDVgypgpdgppglpgqdGLPGLN 1065
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKD 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1066 GERGDNGDsypgnPGLSGQPGDAGYDGLDgvpgppgypgitGMPGLKGESGLPGLPGRQGNDGIPGQPGlEGECGEDGFP 1145
Cdd:NF038329  180 GEAGAKGP-----AGEKGPQGPRGETGPA------------GEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDP 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1146 GSPGQPGYPGQQGREGEKGYPGIPGENGLPGLRGQDGQPGLKGENGLDGQPGYPGSAGQLGTPGDVGYPGAPGENGDNGN 1225
Cdd:NF038329  242 GPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321

                         250
                  ....*....|....*....
gi 527504093 1226 QGRDGQPGLRGESGQPGQP 1244
Cdd:NF038329  322 PGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 129-360 5.16e-22

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 101.14  E-value: 5.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  129 DGFPGMPGLAGPPGQSGQNGNPGRPGLSGPPGEGG-VNSQGRKGVKGESGRSGVPGLPGNSGYPGLKGAKGDPGPYGLPG 207
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGpPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  208 FPGVSGLKGRMGvrtsgvkgekGLPGPPGPPGQPGSYPWASKPIEMEVLQGPVGPAGVKGEKGRDGPVGPPGMLGLDGPP 287
Cdd:NF038329  196 PRGETGPAGEQG----------PAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527504093  288 GYPGLKGQKGDLGDAGQRGKRGKDGVPGNYGEKGSQGEQGLGGTPGYPGTKGGAGEPGYPGRPGFEGDCGPEG 360
Cdd:NF038329  266 GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1339-1528 7.26e-21

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 97.67  E-value: 7.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1339 DGLPGAPGVPGVEGVPGLEGDCGEDGYPGAPGAPGSNGYPGERGLPGVPGQQGRSGDNGYPGAPGQPGIKGPRGDDGFPG 1418
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1419 RDGLDGLPGRPGREGLPGPMAMAVRNPPGQPGENGYPGEKGYPGLPGDNGLSGPPGKAGYPGAPGTDGYPGPPGLSGMPG 1498
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190
                  ....*....|....*....|....*....|
gi 527504093 1499 HGGDQGFQGAAGRTGNPGLPGTPGYPGSPG 1528
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDG 305
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 388-637 4.46e-20

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 95.36  E-value: 4.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  388 GHDGLPGPVGPRGPVGAPGapgqpgidgmpgytEKGDRGEDGYPGFAGEPGLPGEPGDCGYPGEDGLPGydIQGPPGLDG 467
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQG--------------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG--PQGPAGKDG 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  468 QSGRDGFPGIPGDIGDPGYSGEKGFPGtgvnKVGPPGMTGLPGEPGMPGRIGVDGyPGPPGNNGERGEDCGYCPDGVPGN 547
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRGETGPAGEQG----PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGP 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  548 AGDPGFPGMNGYPGPPGPNGDHGDCGMPGAPGKPGSAGSDGLSGSPGLPGIPGYPGMKGEAGEivgpmENPAGIPGLKGD 627
Cdd:NF038329  256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGK-----DGQPGKDGLPGK 330

                         250
                  ....*....|
gi 527504093  628 HGLPGLPGRP 637
Cdd:NF038329  331 DGKDGQPGKP 340
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 42-202 4.11e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 79.95  E-value: 4.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093   42 PGTKGERGNPGFGGEPGHPGAPGQDGPEGAPGAPGMFGAEGDFGDMG--SKGARGDRGLPGSPGHPGLQGLDGLPG---L 116
Cdd:NF038329  182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpaGDGQQGPDGDPGPTGEDGPQGPDGPAGkdgP 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  117 KGEEGIPGCNGTDGFPGMPGLAGPPGQSGQNGNPGRPGLSGPPGEggvnsQGRKGVKGESGRSGVPGLPGNSGYPGLKGA 196
Cdd:NF038329  262 RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQ-----NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336


                  ....*.
gi 527504093  197 KGDPGP 202
Cdd:NF038329  337 PGKPAP 342
 
Name Accession Description Interval E-value
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1645-1758 2.42e-62

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 128421  Cd Length: 114  Bit Score: 208.01  E-value: 2.42e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093   1645 TQIIAVHSQDTSVPQCPQGWSGMWTGYSFVMHTAaGAEGTGQSLQSPGSCLEEFRAVPFIECHGRGTCNYYATN-HGFWL 1723
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTG-NGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNdYSFWL 79

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 527504093   1724 SIVDQDKQFRKPMSQTLKAGGLKDRVSRCQVCLKN 1758
Cdd:smart00111   80 STIEPSDQFTAPRPMTPKAGDLRPYISRCQVCEKP 114
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1646-1757 1.97e-61

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 460201  Cd Length: 110  Bit Score: 205.14  E-value: 1.97e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1646 QIIAVHSQDTSVPQCPQGWSGMWTGYSFVMHTAAGaEGTGQSLQSPGSCLEEFRAVPFIECHGRGTCNYYATNHGFWLSI 1725
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYASNDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|...
gi 527504093  1726 VDQdkQFRKPMSQTLKAGG-LKDRVSRCQVCLK 1757
Cdd:pfam01413   80 VEE--QFRKPMSQTPKAGNeLRSYISRCVVCEA 110
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1536-1642 1.42e-60

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 460201  Cd Length: 110  Bit Score: 202.82  E-value: 1.42e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1536 FTFAKHSQTTAVPQCPPGASQLWEGYSLLYVQGNGRASGQDLGQPGSCLSKFNTMPFMFCNMNSVCHVSSrNDYSFWLST 1615
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 527504093  1616 DE---PMTPMMNPVTGTAIRPYISRCAVCE 1642
Cdd:pfam01413   80 VEeqfRKPMSQTPKAGNELRSYISRCVVCE 109
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1535-1644 2.39e-58

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 128421  Cd Length: 114  Bit Score: 196.46  E-value: 2.39e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093   1535 GFTFAKHSQTTAVPQCPPGASQLWEGYSLLYVQGNGRASGQDLGQPGSCLSKFNTMPFMFCNMNSVCHVSSRNDYSFWLS 1614
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 527504093   1615 TDEP-----MTPMMNPVTGtAIRPYISRCAVCEVP 1644
Cdd:smart00111   81 TIEPsdqftAPRPMTPKAG-DLRPYISRCQVCEKP 114
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 257-478 2.04e-29

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 123.48  E-value: 2.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  257 QGPVGPAGVKGE---KGRDGPVGPPGMLGLDGPPGYPGLKGQKGDLGDAGQRGKRGKDGVPGNYGEKGSQGEQGLGGTPG 333
Cdd:NF038329  122 PGPAGPAGPAGEqgpRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  334 YPGTKGGAGEPGYPGRPGFEGDCGPEGPLGEG-TGEAGPHGAQGFDGVQGGKGLPGHDGLPGPVGPRGPVGAPGAPGQPG 412
Cdd:NF038329  202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527504093  413 IDGMPGytEKGDRGEDGYPGFAGEPGLPGEPGDCGYPGEDGLPGYDiqgppGLDGQSGRDGFPGIP 478
Cdd:NF038329  282 PVGPAG--KDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD-----GLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 267-485 8.02e-29

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 121.94  E-value: 8.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  267 GEKGRDGPVGPPGMLGLDGPPGYPGLKGQKGDLGDAGQRGKRGKDGVPGNYGEKGSQGEQGLGGTPGYPGTKGGAGEPGY 346
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  347 PGRPGFEGDCGPEGPLGEG--TGEAGPHGAQGFDGV--QGGKGLPGHDGLPGPVGPRGPVGAPGAPGQPGIDGMPGYT-E 421
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDgeAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDgK 276

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527504093  422 KGDRGEDGYPGFAGEPGLPGEPGDCGYPGEDGLPGYDiqGPPGLDGQSGRDGFPGIPGDIGDPG 485
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLP--GKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 697-947 1.09e-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: 121.55  E-value: 1.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  697 GYKGERGADGLPGLPGAQGPRGipaplrivnqvagQPGVDGMPGLPGDRGADGLPGLPGPVGPDGYPGTPGERGMDGLPG 776
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRG-------------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  777 FPGLHGEPGMRGQQGEVGFNGIDGDCGEPGLDGYPGAPGAPGAPGETGFGFPGQVGYPGPNGDAGAAGLPGPDGYPGRDG 856
Cdd:NF038329  184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  857 LPGTPGYPGEAGMNGQDGAPGQPGSrgesglvgiDGKKGRDGTPGTRGQDGgpgYSGEAGAPGQNGMDGYPGAPGDQGYP 936
Cdd:NF038329  264 DRGEAGPDGPDGKDGERGPVGPAGK---------DGQNGKDGLPGKDGKDG---QNGKDGLPGKDGKDGQPGKDGLPGKD 331

                         250
                  ....*....|.
gi 527504093  937 GSPGQDGYPGP 947
Cdd:NF038329  332 GKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 748-967 5.26e-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: 119.24  E-value: 5.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  748 DGLPGLPGPVGPDGYPGTPGERGMDGLPGFPGLHGEPGMRGQQGEVGFNGIDGDCGEPGLDGYPGAPGAPGAPGETgfGF 827
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK--GP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  828 PGQVGYPGPNGDAGAAGLPGPDGYPGRDGLPGTPGYP-----GEAGMNGQDGAPGQPGSRGESGLVGIDGKKGRDGTPGT 902
Cdd:NF038329  194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527504093  903 RGQDGGPGYSGEAGAPGQNGMDGYPGAPGDQGYPGSPGQDGYPGPSGIPGEDGLVGFPGLRGEHG 967
Cdd:NF038329  274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1167-1429 2.79e-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: 114.23  E-value: 2.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1167 GIPGENGLPGLRGQDGQPGLKGENGLDGQPGYPGSAGQLGTPGDVGYPGAPGENGDNGNQGRDGQPGLRGESGQPGQPGL 1246
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1247 PGRDgqpgpvgppgddgypgapgqdiyGPPGQAGQDGYPGLDGLPGAPGLNGEPGSPGQygmpglpggpgesglpGYPGE 1326
Cdd:NF038329  197 RGET-----------------------GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------------GQQGP 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1327 RGLPGLDGKRGHDGLPGAPGVPGVEGVPGLEGDCGEDGYPGAPGAPGSNGYPGERGLPGVPGQQGRSGDNGYPGAPGQPG 1406
Cdd:NF038329  238 DGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317

                         250       260
                  ....*....|....*....|...
gi 527504093 1407 IKGPRGDDGFPGRDGLDGLPGRP 1429
Cdd:NF038329  318 KDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1135-1384 1.47e-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: 111.92  E-value: 1.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1135 LEGECGEDGFPGSPGQPGYPGQQGREGEKGYPGIPGENGLPGLRGQDGQPGLKGENGLDGQPGYPGSAGQLGTPGDVGYP 1214
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1215 GAPGENGDNGNQGRDGQPGLRGESGQPGQPGLPGRDGQPGPVGPpgddgypGAPGQDiyGPPGQAGQDGYPGLDGLPGAP 1294
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD-------GDPGPT--GEDGPQGPDGPAGKDGPRGDR 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1295 GLNGEPGSPGQygmpglpggpgesglPGYPGERGLPGLDGKRGHDGLPGAPGVPGVEGVPGLEGDCGEDGYPGAPGAPGS 1374
Cdd:NF038329  266 GEAGPDGPDGK---------------DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330

                         250
                  ....*....|
gi 527504093 1375 NGYPGERGLP 1384
Cdd:NF038329  331 DGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 339-605 3.10e-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: 111.15  E-value: 3.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  339 GGAGEPGYPGRPGFEGDCGPEGPLGEgTGEAGPHGAQGFDGVQGGKGLPGHDGLPGPVGPRGPVGAPGAPGQPGIDGmpg 418
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGE-TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG--- 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  419 ytEKGDRGEDGYPGFAGEPGLPGEPGDCGYPGEDGLPGYDIQGPPGLDGQSGRDGFPGIPGDIGDPGysgekgfpgtgvn 498
Cdd:NF038329  193 --PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAG------------- 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  499 KVGPPGMTGLPGEPGMPGRIGVDGYPGPPGNNGERGedcgycPDGVPGNAGDPGfpgmngypgppgpngDHGDCGMPGAP 578
Cdd:NF038329  258 KDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG------KDGLPGKDGKDG---------------QNGKDGLPGKD 316

                         250       260
                  ....*....|....*....|....*..
gi 527504093  579 GKPGSAGSDGLSGSPGLPGIPGYPGMK 605
Cdd:NF038329  317 GKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 986-1244 3.02e-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: 108.07  E-value: 3.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  986 LDGVPGYPGEHGTDGLPGLPGADGQPGFVGEAGEPGTPGYRGQPGEPGNLAYPGQPGDVgypgpdgppglpgqdGLPGLN 1065
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKD 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1066 GERGDNGDsypgnPGLSGQPGDAGYDGLDgvpgppgypgitGMPGLKGESGLPGLPGRQGNDGIPGQPGlEGECGEDGFP 1145
Cdd:NF038329  180 GEAGAKGP-----AGEKGPQGPRGETGPA------------GEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDP 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1146 GSPGQPGYPGQQGREGEKGYPGIPGENGLPGLRGQDGQPGLKGENGLDGQPGYPGSAGQLGTPGDVGYPGAPGENGDNGN 1225
Cdd:NF038329  242 GPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321

                         250
                  ....*....|....*....
gi 527504093 1226 QGRDGQPGLRGESGQPGQP 1244
Cdd:NF038329  322 PGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1325-1528 3.28e-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: 108.07  E-value: 3.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1325 GERGLPGLDGKRGHDGLPGAPGVPGVEGVPGLEGDCGEDGYPGAPGAPGSNGYPGERGLPGVPGQQGRSGDNGYPGAPGQ 1404
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1405 PGIKGPRGDDGFPGRDGLDGLPGRPGREGLPGPMAMAVRNPPGQPGENGYPGEKGYPGLPGD---NGLSGPPGKAGYPGA 1481
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKdgpRGDRGEAGPDGPDGK 276

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 527504093 1482 PGTDGYPGPPGLSGMPGHGGDQGFQGAAGRTGNPGLPGTPGYPGSPG 1528
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 129-360 5.16e-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: 101.14  E-value: 5.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  129 DGFPGMPGLAGPPGQSGQNGNPGRPGLSGPPGEGG-VNSQGRKGVKGESGRSGVPGLPGNSGYPGLKGAKGDPGPYGLPG 207
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGpPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  208 FPGVSGLKGRMGvrtsgvkgekGLPGPPGPPGQPGSYPWASKPIEMEVLQGPVGPAGVKGEKGRDGPVGPPGMLGLDGPP 287
Cdd:NF038329  196 PRGETGPAGEQG----------PAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527504093  288 GYPGLKGQKGDLGDAGQRGKRGKDGVPGNYGEKGSQGEQGLGGTPGYPGTKGGAGEPGYPGRPGFEGDCGPEG 360
Cdd:NF038329  266 GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 940-1200 6.63e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 97.67  E-value: 6.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  940 GQDGYPGPSGIPGEDGLVGFPGLRGEHGDNGlpglegECGEEGSRGLDGVPGYPGEHGTDGLPGLPGADGQPGFVGEAGE 1019
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAG------PAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1020 PGTPGYRGQPGEPGNLAYPGQPGdvgypgpdgppglpgQDGLPGLNGERGDNGDSYPGNPGLSGQPGDAGYDGLdgvpgp 1099
Cdd:NF038329  191 KGPQGPRGETGPAGEQGPAGPAG---------------PDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGP------ 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1100 pgypgitgmpglKGESGLPGLPGRQGNDGIPGQPGLEGECGEDGFPGSPGQPGYPGQQGREGEKGYPGIPGENGLPGLRG 1179
Cdd:NF038329  250 ------------QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317

                         250       260
                  ....*....|....*....|.
gi 527504093 1180 QDGQPGLKGENGLDGQPGYPG 1200
Cdd:NF038329  318 KDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1339-1528 7.26e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 97.67  E-value: 7.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1339 DGLPGAPGVPGVEGVPGLEGDCGEDGYPGAPGAPGSNGYPGERGLPGVPGQQGRSGDNGYPGAPGQPGIKGPRGDDGFPG 1418
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1419 RDGLDGLPGRPGREGLPGPMAMAVRNPPGQPGENGYPGEKGYPGLPGDNGLSGPPGKAGYPGAPGTDGYPGPPGLSGMPG 1498
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190
                  ....*....|....*....|....*....|
gi 527504093 1499 HGGDQGFQGAAGRTGNPGLPGTPGYPGSPG 1528
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDG 305
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 388-637 4.46e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 95.36  E-value: 4.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  388 GHDGLPGPVGPRGPVGAPGapgqpgidgmpgytEKGDRGEDGYPGFAGEPGLPGEPGDCGYPGEDGLPGydIQGPPGLDG 467
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQG--------------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG--PQGPAGKDG 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  468 QSGRDGFPGIPGDIGDPGYSGEKGFPGtgvnKVGPPGMTGLPGEPGMPGRIGVDGyPGPPGNNGERGEDCGYCPDGVPGN 547
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRGETGPAGEQG----PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGP 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  548 AGDPGFPGMNGYPGPPGPNGDHGDCGMPGAPGKPGSAGSDGLSGSPGLPGIPGYPGMKGEAGEivgpmENPAGIPGLKGD 627
Cdd:NF038329  256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGK-----DGQPGKDGLPGK 330

                         250
                  ....*....|
gi 527504093  628 HGLPGLPGRP 637
Cdd:NF038329  331 DGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 438-696 8.68e-18

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: 88.42  E-value: 8.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  438 GLPGEPGDCGYPGEDGLPGydIQGPPGLDGQSGRDGFPGIPGDIGDPGYSGEKGFPGtgvnKVGPPGMTGLPGEPGMPGR 517
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQG--PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG----PQGPAGKDGEAGAKGPAGE 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  518 IGVDGYPGPPGNNGERGEDCGYCPDGVPGNAGDPGfPGMNGYPGPPGPNGDHGDCGMPGAPGKPGSAGSDGLSGSPGLPG 597
Cdd:NF038329  191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG-PAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  598 IPGYPGMKGEAGEIvgpmeNPAGIPGLKGDHGLPGLPGRPGSDGLpgypggpgqngfPGLQGEPGLAGIDGKRGRQGSLG 677
Cdd:NF038329  270 PDGPDGKDGERGPV-----GPAGKDGQNGKDGLPGKDGKDGQNGK------------DGLPGKDGKDGQPGKDGLPGKDG 332

                         250
                  ....*....|....*....
gi 527504093  678 IPGLQGPPGDSFPGQPGTP 696
Cdd:NF038329  333 KDGQPGKPAPKTPEVPQKP 351
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 42-202 4.11e-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: 79.95  E-value: 4.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093   42 PGTKGERGNPGFGGEPGHPGAPGQDGPEGAPGAPGMFGAEGDFGDMG--SKGARGDRGLPGSPGHPGLQGLDGLPG---L 116
Cdd:NF038329  182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpaGDGQQGPDGDPGPTGEDGPQGPDGPAGkdgP 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  117 KGEEGIPGCNGTDGFPGMPGLAGPPGQSGQNGNPGRPGLSGPPGEggvnsQGRKGVKGESGRSGVPGLPGNSGYPGLKGA 196
Cdd:NF038329  262 RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQ-----NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336


                  ....*.
gi 527504093  197 KGDPGP 202
Cdd:NF038329  337 PGKPAP 342
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 1020-1522 2.01e-06

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 52.64  E-value: 2.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1020 PGTPGYRGQPGEPGNLAYPGQPGDVGYPGPDGPPGLPGQDGLPGLNGERGDNGDSYPGNPGLSGQPGDAGYDGLDGVPGP 1099
Cdd:pfam03157  128 PQRPGQGQQPGQGQQWYYPTSPQQPGQWQQPGQGQQGYYPTSPQQSGQRQQPGQGQQLRQGQQGQQSGQGQPGYYPTSSQ 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1100 PGYPGITGMPGLKGESGLPGLPGRQGNDGIPGQPGLEGEcgedgfpgSPGQPGYPGQQGREGEKGYPGIPGENGLPGLRG 1179
Cdd:pfam03157  208 QPGQLQQTGQGQQGQQPERGQQGQQPGQGQQPGQGQQGQ--------QPGQPQQLGQGQQGYYPISPQQPRQWQQSGQGQ 279

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1180 QDGQPGLKGENGLDGQPGYPGSAGQLGTPGDVGYPGAPGENGDNGNQGRDGQPGLRGESGQPGQPGLPGRDGQP------ 1253
Cdd:pfam03157  280 QGYYPTSLQQPGQGQSGYYPTSQQQAGQLQQEQQLGQEQQDQQPGQGRQGQQPGQGQQGQQPAQGQQPGQGQPGyyptsp 359

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1254 GPVGPPGDDGYPGAPGQDIYGPPGQAGQDGYPGLDGLPGAPGLNGEPGSPGQYGMPGLPGGPGESGLPGYPGERGLPGLD 1333
Cdd:pfam03157  360 QQPGQGQPGYYPTSQQQPQQGQQPEQGQQGQQQGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSPQQSGQ 439

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1334 GKRGHDGLPGAPGVPGVEGVPGLEGDCGEDGYPGAPGAPG---------SNGYPGERGLPGVPGQQGRSGDNGYPGAPGQ 1404
Cdd:pfam03157  440 GQQPGQGQQPGQEQPGQGQQPGQGQQGQQPGQPEQGQQPGqgqpgyyptSPQQSGQGQQLGQWQQQGQGQPGYYPTSPLQ 519

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1405 PGIKGPRGDDGFPGRDGLDGLPGRpgregLPGPMAMAVRNPPGQPGENGYPGEKGYPGLPGDNGLSGPPGKAGYPGAPGT 1484
Cdd:pfam03157  520 PGQGQPGYYPTSPQQPGQGQQLGQ-----LQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQGQP 594

                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 527504093  1485 DGYPGPPGLSGMPGHGGDQGFQGAAGRTGNPGLPGTPG 1522
Cdd:pfam03157  595 GYYPTSPQQSGQGQQPGQWQQPGQGQPGYYPTSSLQLG 632
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 827-1305 7.12e-06

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 51.10  E-value: 7.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093   827 FPGQVGYPGPNGDAGAAGLPGPDGYPGRDGLPGTPGYPGEAGMNGQDGAPGQPGsRGESGLVGIDGKKGRDGTPGTRGQD 906
Cdd:pfam03157  202 YPTSSQQPGQLQQTGQGQQGQQPERGQQGQQPGQGQQPGQGQQGQQPGQPQQLG-QGQQGYYPISPQQPRQWQQSGQGQQ 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093   907 GGpgYSGEAGAPGQNGMDGYPGAPGDQGYPGSPGQDGYPGPSGIPGEDGLVGFPGLR--------GEHGDNGLPGLEGEC 978
Cdd:pfam03157  281 GY--YPTSLQQPGQGQSGYYPTSQQQAGQLQQEQQLGQEQQDQQPGQGRQGQQPGQGqqgqqpaqGQQPGQGQPGYYPTS 358

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093   979 GEEGSRGLDGVpgYPGEHGTDGLPGLPGADGQPGFVGEAGEPGTPGYRGQPGEPGNLAYPGQPGDVGYPGPDGPPGLPGQ 1058
Cdd:pfam03157  359 PQQPGQGQPGY--YPTSQQQPQQGQQPEQGQQGQQQGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSPQQ 436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1059 DGLPGLNGERGDNGDSYPGNPGLSGQPGDAGYDGLDGVPGppgypgitgMPGLKGESGLPGLPGRQGNDGIPGQPGLEGE 1138
Cdd:pfam03157  437 SGQGQQPGQGQQPGQEQPGQGQQPGQGQQGQQPGQPEQGQ---------QPGQGQPGYYPTSPQQSGQGQQLGQWQQQGQ 507

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1139 CGEDGFPGSPGQPG------YPGQQGREGEKGYPGIPGENGLPGLRGQDGQPGLKGENGLDGQPGYPGSAGQLGTPGDVG 1212
Cdd:pfam03157  508 GQPGYYPTSPLQPGqgqpgyYPTSPQQPGQGQQLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPGQGQQGQQPGQGQ 587

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1213 YPGAPGENGDNGNQGRDGQPGLRGESGQPGQPGLPGRDGQPGPVGPPGDDGYPGAPGQDIYGP-PGQAGQDGYPGLDGLP 1291
Cdd:pfam03157  588 QPGQGQPGYYPTSPQQSGQGQQPGQWQQPGQGQPGYYPTSSLQLGQGQQGYYPTSPQQPGQGQqPGQWQQSGQGQQGYYP 667

                          490
                   ....*....|....
gi 527504093  1292 GAPGLNGEPGSPGQ 1305
Cdd:pfam03157  668 TSPQQSGQAQQPGQ 681
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1471-1527 2.67e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 2.67e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093  1471 GPPGKAGYPGAPGTDGYPGPPGLSGMPGHGGDQGFQGAAGRTGNPGLPGTPGYPGSP 1527
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 394-451 6.47e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 6.47e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 527504093   394 GPVGPRGPVGAPGAPGQPGIDGMPGytEKGDRGEDGYPGFAGEPGLPGEPGDCGYPGE 451
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPG--PPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 100-154 3.91e-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: 3.91e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 527504093   100 GSPGHPGLQGLDGLPGLKGEEGIPGCNGTDGFPGMPGLAGPPGQSGQNGNPGRPG 154
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 898-953 4.03e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 4.03e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 527504093   898 GTPGTRGQDGGPGYSGEAGAPGQNGMDGYPGAPGDQGYPGSPGQDGYPGPSGIPGE 953
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 1424-1571 6.88e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 44.29  E-value: 6.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1424 GLPGRPGREGLPGPMA--MAVRNPPGQPGENGYPGEKGYP---GLPGdnglSGPPGKAGYPGAPGTDGYPGPPGLSGMPg 1498
Cdd:PRK14959  376 GGASAPSGSAAEGPASggAATIPTPGTQGPQGTAPAAGMTpssAAPA----TPAPSAAPSPRVPWDDAPPAPPRSGIPP- 450

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527504093 1499 hggdqgfqgaagrTGNPGLPGTPGYPGSPGGWAPSRGfTFAKHSQTTAVPQCPPGASQLWEGYSLLYVQGNGR 1571
Cdd:PRK14959  451 -------------RPAPRMPEASPVPGAPDSVASASD-APPTLGDPSDTAEHTPSGPRTWDGFLEFCQGRNGQ 509
PHA03169 PHA03169
hypothetical protein; Provisional
 781-943 2.00e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.65  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  781 HGEPGMRGQQGEVGFNGIDGDCGEPGLDGYPGAPGAPGAPGETGFGfpgqvgypGPNGDAGAAGLPGPDGYPGrdglpgt 860
Cdd:PHA03169   81 HGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGS--------SPESPASHSPPPSPPSHPG------- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  861 PGYPGEAGMNGQDGAPGQPGSRGESGLVGIDGKKGRDGTPGTRGQDGGPGYSGEAGAPGQNGMD--GYPGAPGDQGYPGS 938
Cdd:PHA03169  146 PHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDepGEPQSPTPQQAPSP 225


                  ....*
gi 527504093  939 PGQDG 943
Cdd:PHA03169  226 NTQQA 230
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
71-344 7.61e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 40.78  E-value: 7.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093   71 APGAPGMFGAEGDFGDMGSKGARGDRGLPGSPGHPGLQGLDGLPGLKGEEGIPGCNGTDGFPGMPGLAGPPGQSGQNGNP 150
Cdd:COG5164     5 GPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  151 GRPGLSGPPGeggvnSQGRKGVKGESGRSGVPGLPGNSGYPGLKGAKGdpgpyglPGFPGVSGLKGRMGVRTSGVKGEKG 230
Cdd:COG5164    85 QNQGGTRPAG-----NTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-------PPSGGSTTPPGDGGSTPPGPGSTGP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  231 LPGPPGPPGQPGSYPWASKPIEMEVLQGPVGPAGVKGEKGRDGPVGPPGMLGLDGPPGYPGLKGQKGDLGDAGqrGKRGK 310
Cdd:COG5164   153 GGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGP 230

                         250       260       270
                  ....*....|....*....|....*....|....
gi 527504093  311 DGVPGNYGEKGSQGEQGLGGTPGYPGTKGGAGEP 344
Cdd:COG5164   231 KDQRPKTNPIERRGPERPEAAALPAELTALEAEN 264
PHA03169 PHA03169
hypothetical protein; Provisional
 889-1030 9.36e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.34  E-value: 9.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  889 GIDGKKGRDGTPGTRGQDGGPGYSGEAGAPGQNGMDGYPGAPGDQGYPGSPGQDGYPGPSGIPGEDGLVGFPGLRGEHGD 968
Cdd:PHA03169   90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQP 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527504093  969 NGLPGLEGECGEEGSRGLDGVPGYPGEHGTDGLPGLPGADgqpgfvgEAGEPGTPGYRGQPG 1030
Cdd:PHA03169  170 SHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPD-------EPGEPQSPTPQQAPS 224
 
Name Accession Description Interval E-value
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1645-1758 2.42e-62

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 128421  Cd Length: 114  Bit Score: 208.01  E-value: 2.42e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093   1645 TQIIAVHSQDTSVPQCPQGWSGMWTGYSFVMHTAaGAEGTGQSLQSPGSCLEEFRAVPFIECHGRGTCNYYATN-HGFWL 1723
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTG-NGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNdYSFWL 79

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 527504093   1724 SIVDQDKQFRKPMSQTLKAGGLKDRVSRCQVCLKN 1758
Cdd:smart00111   80 STIEPSDQFTAPRPMTPKAGDLRPYISRCQVCEKP 114
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1646-1757 1.97e-61

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 460201  Cd Length: 110  Bit Score: 205.14  E-value: 1.97e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1646 QIIAVHSQDTSVPQCPQGWSGMWTGYSFVMHTAAGaEGTGQSLQSPGSCLEEFRAVPFIECHGRGTCNYYATNHGFWLSI 1725
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYASNDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|...
gi 527504093  1726 VDQdkQFRKPMSQTLKAGG-LKDRVSRCQVCLK 1757
Cdd:pfam01413   80 VEE--QFRKPMSQTPKAGNeLRSYISRCVVCEA 110
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1536-1642 1.42e-60

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 460201  Cd Length: 110  Bit Score: 202.82  E-value: 1.42e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1536 FTFAKHSQTTAVPQCPPGASQLWEGYSLLYVQGNGRASGQDLGQPGSCLSKFNTMPFMFCNMNSVCHVSSrNDYSFWLST 1615
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 527504093  1616 DE---PMTPMMNPVTGTAIRPYISRCAVCE 1642
Cdd:pfam01413   80 VEeqfRKPMSQTPKAGNELRSYISRCVVCE 109
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1535-1644 2.39e-58

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 128421  Cd Length: 114  Bit Score: 196.46  E-value: 2.39e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093   1535 GFTFAKHSQTTAVPQCPPGASQLWEGYSLLYVQGNGRASGQDLGQPGSCLSKFNTMPFMFCNMNSVCHVSSRNDYSFWLS 1614
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 527504093   1615 TDEP-----MTPMMNPVTGtAIRPYISRCAVCEVP 1644
Cdd:smart00111   81 TIEPsdqftAPRPMTPKAG-DLRPYISRCQVCEKP 114
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 257-478 2.04e-29

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 123.48  E-value: 2.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  257 QGPVGPAGVKGE---KGRDGPVGPPGMLGLDGPPGYPGLKGQKGDLGDAGQRGKRGKDGVPGNYGEKGSQGEQGLGGTPG 333
Cdd:NF038329  122 PGPAGPAGPAGEqgpRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  334 YPGTKGGAGEPGYPGRPGFEGDCGPEGPLGEG-TGEAGPHGAQGFDGVQGGKGLPGHDGLPGPVGPRGPVGAPGAPGQPG 412
Cdd:NF038329  202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527504093  413 IDGMPGytEKGDRGEDGYPGFAGEPGLPGEPGDCGYPGEDGLPGYDiqgppGLDGQSGRDGFPGIP 478
Cdd:NF038329  282 PVGPAG--KDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD-----GLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 267-485 8.02e-29

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 121.94  E-value: 8.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  267 GEKGRDGPVGPPGMLGLDGPPGYPGLKGQKGDLGDAGQRGKRGKDGVPGNYGEKGSQGEQGLGGTPGYPGTKGGAGEPGY 346
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  347 PGRPGFEGDCGPEGPLGEG--TGEAGPHGAQGFDGV--QGGKGLPGHDGLPGPVGPRGPVGAPGAPGQPGIDGMPGYT-E 421
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDgeAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDgK 276

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527504093  422 KGDRGEDGYPGFAGEPGLPGEPGDCGYPGEDGLPGYDiqGPPGLDGQSGRDGFPGIPGDIGDPG 485
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLP--GKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 697-947 1.09e-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: 121.55  E-value: 1.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  697 GYKGERGADGLPGLPGAQGPRGipaplrivnqvagQPGVDGMPGLPGDRGADGLPGLPGPVGPDGYPGTPGERGMDGLPG 776
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRG-------------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  777 FPGLHGEPGMRGQQGEVGFNGIDGDCGEPGLDGYPGAPGAPGAPGETGFGFPGQVGYPGPNGDAGAAGLPGPDGYPGRDG 856
Cdd:NF038329  184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  857 LPGTPGYPGEAGMNGQDGAPGQPGSrgesglvgiDGKKGRDGTPGTRGQDGgpgYSGEAGAPGQNGMDGYPGAPGDQGYP 936
Cdd:NF038329  264 DRGEAGPDGPDGKDGERGPVGPAGK---------DGQNGKDGLPGKDGKDG---QNGKDGLPGKDGKDGQPGKDGLPGKD 331

                         250
                  ....*....|.
gi 527504093  937 GSPGQDGYPGP 947
Cdd:NF038329  332 GKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 748-967 5.26e-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: 119.24  E-value: 5.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  748 DGLPGLPGPVGPDGYPGTPGERGMDGLPGFPGLHGEPGMRGQQGEVGFNGIDGDCGEPGLDGYPGAPGAPGAPGETgfGF 827
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK--GP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  828 PGQVGYPGPNGDAGAAGLPGPDGYPGRDGLPGTPGYP-----GEAGMNGQDGAPGQPGSRGESGLVGIDGKKGRDGTPGT 902
Cdd:NF038329  194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527504093  903 RGQDGGPGYSGEAGAPGQNGMDGYPGAPGDQGYPGSPGQDGYPGPSGIPGEDGLVGFPGLRGEHG 967
Cdd:NF038329  274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1167-1429 2.79e-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: 114.23  E-value: 2.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1167 GIPGENGLPGLRGQDGQPGLKGENGLDGQPGYPGSAGQLGTPGDVGYPGAPGENGDNGNQGRDGQPGLRGESGQPGQPGL 1246
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1247 PGRDgqpgpvgppgddgypgapgqdiyGPPGQAGQDGYPGLDGLPGAPGLNGEPGSPGQygmpglpggpgesglpGYPGE 1326
Cdd:NF038329  197 RGET-----------------------GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------------GQQGP 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1327 RGLPGLDGKRGHDGLPGAPGVPGVEGVPGLEGDCGEDGYPGAPGAPGSNGYPGERGLPGVPGQQGRSGDNGYPGAPGQPG 1406
Cdd:NF038329  238 DGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317

                         250       260
                  ....*....|....*....|...
gi 527504093 1407 IKGPRGDDGFPGRDGLDGLPGRP 1429
Cdd:NF038329  318 KDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1135-1384 1.47e-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: 111.92  E-value: 1.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1135 LEGECGEDGFPGSPGQPGYPGQQGREGEKGYPGIPGENGLPGLRGQDGQPGLKGENGLDGQPGYPGSAGQLGTPGDVGYP 1214
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1215 GAPGENGDNGNQGRDGQPGLRGESGQPGQPGLPGRDGQPGPVGPpgddgypGAPGQDiyGPPGQAGQDGYPGLDGLPGAP 1294
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD-------GDPGPT--GEDGPQGPDGPAGKDGPRGDR 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1295 GLNGEPGSPGQygmpglpggpgesglPGYPGERGLPGLDGKRGHDGLPGAPGVPGVEGVPGLEGDCGEDGYPGAPGAPGS 1374
Cdd:NF038329  266 GEAGPDGPDGK---------------DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330

                         250
                  ....*....|
gi 527504093 1375 NGYPGERGLP 1384
Cdd:NF038329  331 DGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 339-605 3.10e-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: 111.15  E-value: 3.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  339 GGAGEPGYPGRPGFEGDCGPEGPLGEgTGEAGPHGAQGFDGVQGGKGLPGHDGLPGPVGPRGPVGAPGAPGQPGIDGmpg 418
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGE-TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG--- 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  419 ytEKGDRGEDGYPGFAGEPGLPGEPGDCGYPGEDGLPGYDIQGPPGLDGQSGRDGFPGIPGDIGDPGysgekgfpgtgvn 498
Cdd:NF038329  193 --PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAG------------- 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  499 KVGPPGMTGLPGEPGMPGRIGVDGYPGPPGNNGERGedcgycPDGVPGNAGDPGfpgmngypgppgpngDHGDCGMPGAP 578
Cdd:NF038329  258 KDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG------KDGLPGKDGKDG---------------QNGKDGLPGKD 316

                         250       260
                  ....*....|....*....|....*..
gi 527504093  579 GKPGSAGSDGLSGSPGLPGIPGYPGMK 605
Cdd:NF038329  317 GKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 986-1244 3.02e-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: 108.07  E-value: 3.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  986 LDGVPGYPGEHGTDGLPGLPGADGQPGFVGEAGEPGTPGYRGQPGEPGNLAYPGQPGDVgypgpdgppglpgqdGLPGLN 1065
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKD 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1066 GERGDNGDsypgnPGLSGQPGDAGYDGLDgvpgppgypgitGMPGLKGESGLPGLPGRQGNDGIPGQPGlEGECGEDGFP 1145
Cdd:NF038329  180 GEAGAKGP-----AGEKGPQGPRGETGPA------------GEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDP 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1146 GSPGQPGYPGQQGREGEKGYPGIPGENGLPGLRGQDGQPGLKGENGLDGQPGYPGSAGQLGTPGDVGYPGAPGENGDNGN 1225
Cdd:NF038329  242 GPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321

                         250
                  ....*....|....*....
gi 527504093 1226 QGRDGQPGLRGESGQPGQP 1244
Cdd:NF038329  322 PGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1325-1528 3.28e-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: 108.07  E-value: 3.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1325 GERGLPGLDGKRGHDGLPGAPGVPGVEGVPGLEGDCGEDGYPGAPGAPGSNGYPGERGLPGVPGQQGRSGDNGYPGAPGQ 1404
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1405 PGIKGPRGDDGFPGRDGLDGLPGRPGREGLPGPMAMAVRNPPGQPGENGYPGEKGYPGLPGD---NGLSGPPGKAGYPGA 1481
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKdgpRGDRGEAGPDGPDGK 276

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 527504093 1482 PGTDGYPGPPGLSGMPGHGGDQGFQGAAGRTGNPGLPGTPGYPGSPG 1528
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 129-360 5.16e-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: 101.14  E-value: 5.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  129 DGFPGMPGLAGPPGQSGQNGNPGRPGLSGPPGEGG-VNSQGRKGVKGESGRSGVPGLPGNSGYPGLKGAKGDPGPYGLPG 207
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGpPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  208 FPGVSGLKGRMGvrtsgvkgekGLPGPPGPPGQPGSYPWASKPIEMEVLQGPVGPAGVKGEKGRDGPVGPPGMLGLDGPP 287
Cdd:NF038329  196 PRGETGPAGEQG----------PAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527504093  288 GYPGLKGQKGDLGDAGQRGKRGKDGVPGNYGEKGSQGEQGLGGTPGYPGTKGGAGEPGYPGRPGFEGDCGPEG 360
Cdd:NF038329  266 GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 940-1200 6.63e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 97.67  E-value: 6.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  940 GQDGYPGPSGIPGEDGLVGFPGLRGEHGDNGlpglegECGEEGSRGLDGVPGYPGEHGTDGLPGLPGADGQPGFVGEAGE 1019
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAG------PAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1020 PGTPGYRGQPGEPGNLAYPGQPGdvgypgpdgppglpgQDGLPGLNGERGDNGDSYPGNPGLSGQPGDAGYDGLdgvpgp 1099
Cdd:NF038329  191 KGPQGPRGETGPAGEQGPAGPAG---------------PDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGP------ 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1100 pgypgitgmpglKGESGLPGLPGRQGNDGIPGQPGLEGECGEDGFPGSPGQPGYPGQQGREGEKGYPGIPGENGLPGLRG 1179
Cdd:NF038329  250 ------------QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317

                         250       260
                  ....*....|....*....|.
gi 527504093 1180 QDGQPGLKGENGLDGQPGYPG 1200
Cdd:NF038329  318 KDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1339-1528 7.26e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 97.67  E-value: 7.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1339 DGLPGAPGVPGVEGVPGLEGDCGEDGYPGAPGAPGSNGYPGERGLPGVPGQQGRSGDNGYPGAPGQPGIKGPRGDDGFPG 1418
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1419 RDGLDGLPGRPGREGLPGPMAMAVRNPPGQPGENGYPGEKGYPGLPGDNGLSGPPGKAGYPGAPGTDGYPGPPGLSGMPG 1498
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190
                  ....*....|....*....|....*....|
gi 527504093 1499 HGGDQGFQGAAGRTGNPGLPGTPGYPGSPG 1528
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDG 305
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 388-637 4.46e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 95.36  E-value: 4.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  388 GHDGLPGPVGPRGPVGAPGapgqpgidgmpgytEKGDRGEDGYPGFAGEPGLPGEPGDCGYPGEDGLPGydIQGPPGLDG 467
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQG--------------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG--PQGPAGKDG 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  468 QSGRDGFPGIPGDIGDPGYSGEKGFPGtgvnKVGPPGMTGLPGEPGMPGRIGVDGyPGPPGNNGERGEDCGYCPDGVPGN 547
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRGETGPAGEQG----PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGP 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  548 AGDPGFPGMNGYPGPPGPNGDHGDCGMPGAPGKPGSAGSDGLSGSPGLPGIPGYPGMKGEAGEivgpmENPAGIPGLKGD 627
Cdd:NF038329  256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGK-----DGQPGKDGLPGK 330

                         250
                  ....*....|
gi 527504093  628 HGLPGLPGRP 637
Cdd:NF038329  331 DGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 438-696 8.68e-18

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: 88.42  E-value: 8.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  438 GLPGEPGDCGYPGEDGLPGydIQGPPGLDGQSGRDGFPGIPGDIGDPGYSGEKGFPGtgvnKVGPPGMTGLPGEPGMPGR 517
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQG--PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG----PQGPAGKDGEAGAKGPAGE 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  518 IGVDGYPGPPGNNGERGEDCGYCPDGVPGNAGDPGfPGMNGYPGPPGPNGDHGDCGMPGAPGKPGSAGSDGLSGSPGLPG 597
Cdd:NF038329  191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG-PAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  598 IPGYPGMKGEAGEIvgpmeNPAGIPGLKGDHGLPGLPGRPGSDGLpgypggpgqngfPGLQGEPGLAGIDGKRGRQGSLG 677
Cdd:NF038329  270 PDGPDGKDGERGPV-----GPAGKDGQNGKDGLPGKDGKDGQNGK------------DGLPGKDGKDGQPGKDGLPGKDG 332

                         250
                  ....*....|....*....
gi 527504093  678 IPGLQGPPGDSFPGQPGTP 696
Cdd:NF038329  333 KDGQPGKPAPKTPEVPQKP 351
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 42-202 4.11e-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: 79.95  E-value: 4.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093   42 PGTKGERGNPGFGGEPGHPGAPGQDGPEGAPGAPGMFGAEGDFGDMG--SKGARGDRGLPGSPGHPGLQGLDGLPG---L 116
Cdd:NF038329  182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpaGDGQQGPDGDPGPTGEDGPQGPDGPAGkdgP 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  117 KGEEGIPGCNGTDGFPGMPGLAGPPGQSGQNGNPGRPGLSGPPGEggvnsQGRKGVKGESGRSGVPGLPGNSGYPGLKGA 196
Cdd:NF038329  262 RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQ-----NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336


                  ....*.
gi 527504093  197 KGDPGP 202
Cdd:NF038329  337 PGKPAP 342
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 1020-1522 2.01e-06

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 52.64  E-value: 2.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1020 PGTPGYRGQPGEPGNLAYPGQPGDVGYPGPDGPPGLPGQDGLPGLNGERGDNGDSYPGNPGLSGQPGDAGYDGLDGVPGP 1099
Cdd:pfam03157  128 PQRPGQGQQPGQGQQWYYPTSPQQPGQWQQPGQGQQGYYPTSPQQSGQRQQPGQGQQLRQGQQGQQSGQGQPGYYPTSSQ 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1100 PGYPGITGMPGLKGESGLPGLPGRQGNDGIPGQPGLEGEcgedgfpgSPGQPGYPGQQGREGEKGYPGIPGENGLPGLRG 1179
Cdd:pfam03157  208 QPGQLQQTGQGQQGQQPERGQQGQQPGQGQQPGQGQQGQ--------QPGQPQQLGQGQQGYYPISPQQPRQWQQSGQGQ 279

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1180 QDGQPGLKGENGLDGQPGYPGSAGQLGTPGDVGYPGAPGENGDNGNQGRDGQPGLRGESGQPGQPGLPGRDGQP------ 1253
Cdd:pfam03157  280 QGYYPTSLQQPGQGQSGYYPTSQQQAGQLQQEQQLGQEQQDQQPGQGRQGQQPGQGQQGQQPAQGQQPGQGQPGyyptsp 359

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1254 GPVGPPGDDGYPGAPGQDIYGPPGQAGQDGYPGLDGLPGAPGLNGEPGSPGQYGMPGLPGGPGESGLPGYPGERGLPGLD 1333
Cdd:pfam03157  360 QQPGQGQPGYYPTSQQQPQQGQQPEQGQQGQQQGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSPQQSGQ 439

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1334 GKRGHDGLPGAPGVPGVEGVPGLEGDCGEDGYPGAPGAPG---------SNGYPGERGLPGVPGQQGRSGDNGYPGAPGQ 1404
Cdd:pfam03157  440 GQQPGQGQQPGQEQPGQGQQPGQGQQGQQPGQPEQGQQPGqgqpgyyptSPQQSGQGQQLGQWQQQGQGQPGYYPTSPLQ 519

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1405 PGIKGPRGDDGFPGRDGLDGLPGRpgregLPGPMAMAVRNPPGQPGENGYPGEKGYPGLPGDNGLSGPPGKAGYPGAPGT 1484
Cdd:pfam03157  520 PGQGQPGYYPTSPQQPGQGQQLGQ-----LQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQGQP 594

                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 527504093  1485 DGYPGPPGLSGMPGHGGDQGFQGAAGRTGNPGLPGTPG 1522
Cdd:pfam03157  595 GYYPTSPQQSGQGQQPGQWQQPGQGQPGYYPTSSLQLG 632
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 827-1305 7.12e-06

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 51.10  E-value: 7.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093   827 FPGQVGYPGPNGDAGAAGLPGPDGYPGRDGLPGTPGYPGEAGMNGQDGAPGQPGsRGESGLVGIDGKKGRDGTPGTRGQD 906
Cdd:pfam03157  202 YPTSSQQPGQLQQTGQGQQGQQPERGQQGQQPGQGQQPGQGQQGQQPGQPQQLG-QGQQGYYPISPQQPRQWQQSGQGQQ 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093   907 GGpgYSGEAGAPGQNGMDGYPGAPGDQGYPGSPGQDGYPGPSGIPGEDGLVGFPGLR--------GEHGDNGLPGLEGEC 978
Cdd:pfam03157  281 GY--YPTSLQQPGQGQSGYYPTSQQQAGQLQQEQQLGQEQQDQQPGQGRQGQQPGQGqqgqqpaqGQQPGQGQPGYYPTS 358

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093   979 GEEGSRGLDGVpgYPGEHGTDGLPGLPGADGQPGFVGEAGEPGTPGYRGQPGEPGNLAYPGQPGDVGYPGPDGPPGLPGQ 1058
Cdd:pfam03157  359 PQQPGQGQPGY--YPTSQQQPQQGQQPEQGQQGQQQGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSPQQ 436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1059 DGLPGLNGERGDNGDSYPGNPGLSGQPGDAGYDGLDGVPGppgypgitgMPGLKGESGLPGLPGRQGNDGIPGQPGLEGE 1138
Cdd:pfam03157  437 SGQGQQPGQGQQPGQEQPGQGQQPGQGQQGQQPGQPEQGQ---------QPGQGQPGYYPTSPQQSGQGQQLGQWQQQGQ 507

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1139 CGEDGFPGSPGQPG------YPGQQGREGEKGYPGIPGENGLPGLRGQDGQPGLKGENGLDGQPGYPGSAGQLGTPGDVG 1212
Cdd:pfam03157  508 GQPGYYPTSPLQPGqgqpgyYPTSPQQPGQGQQLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPGQGQQGQQPGQGQ 587

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1213 YPGAPGENGDNGNQGRDGQPGLRGESGQPGQPGLPGRDGQPGPVGPPGDDGYPGAPGQDIYGP-PGQAGQDGYPGLDGLP 1291
Cdd:pfam03157  588 QPGQGQPGYYPTSPQQSGQGQQPGQWQQPGQGQPGYYPTSSLQLGQGQQGYYPTSPQQPGQGQqPGQWQQSGQGQQGYYP 667

                          490
                   ....*....|....
gi 527504093  1292 GAPGLNGEPGSPGQ 1305
Cdd:pfam03157  668 TSPQQSGQAQQPGQ 681
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1382-1437 1.18e-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: 44.41  E-value: 1.18e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 527504093  1382 GLPGVPGQQGRSGDNGYPGAPGQPGIKGPRGDDGFPGRDGLDGLPGRPGREGLPGP 1437
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1471-1527 2.67e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 2.67e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093  1471 GPPGKAGYPGAPGTDGYPGPPGLSGMPGHGGDQGFQGAAGRTGNPGLPGTPGYPGSP 1527
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 1130-1581 3.11e-05

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 48.79  E-value: 3.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1130 PGQPGLEGECGEDGFPGSPGQPGYPGQQGREGEKGYPGIPGENGLPGLRGQDGQP--GLKGENGLDGQPGYPGSAGQlgT 1207
Cdd:pfam03157  131 PGQGQQPGQGQQWYYPTSPQQPGQWQQPGQGQQGYYPTSPQQSGQRQQPGQGQQLrqGQQGQQSGQGQPGYYPTSSQ--Q 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1208 PGDVGYPGAPGENGDNGNQGRDGQPGLRGESGQPGQPGLPGRDGQPGPVGPPGDDGYPGAPGQdiYGPPGQAGQDGYPGL 1287
Cdd:pfam03157  209 PGQLQQTGQGQQGQQPERGQQGQQPGQGQQPGQGQQGQQPGQPQQLGQGQQGYYPISPQQPRQ--WQQSGQGQQGYYPTS 286

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1288 DGLPGAPGLNGEPGSPGQYGMPGLPGGPGESGLPGYPGERGLPGLDGKRGHDGLPGAPGVPG------VEGVPGLEGDCG 1361
Cdd:pfam03157  287 LQQPGQGQSGYYPTSQQQAGQLQQEQQLGQEQQDQQPGQGRQGQQPGQGQQGQQPAQGQQPGqgqpgyYPTSPQQPGQGQ 366

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1362 EDGYPGAPGAPGSNGYP--GERGLPGVPGQQGRSGDNGYPGAPGQPGIKGPRGDDGFPGRDG-LDGLPGRPGREGLPGPM 1438
Cdd:pfam03157  367 PGYYPTSQQQPQQGQQPeqGQQGQQQGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGyYPTSPQQSGQGQQPGQG 446

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  1439 AMAVRNPPGQPGENGYPGEKGYPGLPGDNGLSGPPGKAGYPGAPGTDGYPGPPGLSGMPGHgGDQGFQGAAGRTGNPGLP 1518
Cdd:pfam03157  447 QQPGQEQPGQGQQPGQGQQGQQPGQPEQGQQPGQGQPGYYPTSPQQSGQGQQLGQWQQQGQ-GQPGYYPTSPLQPGQGQP 525

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527504093  1519 GTpgYPGSPGgwAPSRGFTFAKHSQTTAVPQCPPGASQLWEGYSLLYVQGNGRASGQDLGQPG 1581
Cdd:pfam03157  526 GY--YPTSPQ--QPGQGQQLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPGQGQQGQQPG 584
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 394-451 6.47e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 6.47e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 527504093   394 GPVGPRGPVGAPGAPGQPGIDGMPGytEKGDRGEDGYPGFAGEPGLPGEPGDCGYPGE 451
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPG--PPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1364-1418 7.80e-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: 7.80e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 527504093  1364 GYPGAPGAPGSNGYPGERGLPGVPGQQGRSGDNGYPGAPGQPGIKGPRGDDGFPG 1418
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1370-1426 8.95e-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: 8.95e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093  1370 GAPGSNGYPGERGLPGVPGQQGRSGDNGYPGAPGQPGIKGPRGDDGFPGRDGLDGLP 1426
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1140-1196 2.59e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 2.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093  1140 GEDGFPGSPGQPGYPGQQGREGEKGYPGIPGENGLPGLRGQDGQPGLKGENGLDGQP 1196
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1361-1415 3.03e-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: 3.03e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 527504093  1361 GEDGYPGAPGAPGSNGYPGERGLPGVPGQQGRSGDNGYPGAPGQPGIKGPRGDDG 1415
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1445-1492 3.21e-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: 3.21e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 527504093  1445 PPGQPGENGYPGEKGYPGLPGDNGLSGPPGKAGYPGAPGTDGYPGPPG 1492
Cdd:pfam01391    8 PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1110-1166 3.69e-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: 3.69e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093  1110 GLKGESGLPGLPGRQGNDGIPGQPGLEGECGEDGFPGSPGQPGYPGQQGREGEKGYP 1166
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 100-154 3.91e-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: 3.91e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 527504093   100 GSPGHPGLQGLDGLPGLKGEEGIPGCNGTDGFPGMPGLAGPPGQSGQNGNPGRPG 154
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 898-953 4.03e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 4.03e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 527504093   898 GTPGTRGQDGGPGYSGEAGAPGQNGMDGYPGAPGDQGYPGSPGQDGYPGPSGIPGE 953
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1445-1498 4.36e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 4.36e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 527504093  1445 PPGQPGENGYPGEKGYPGLPGDNGLSGPPGKAGYPGAPGTDGYPGPPGLSGMPG 1498
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1355-1411 4.49e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 4.49e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093  1355 GLEGDCGEDGYPGAPGAPGSNGYPGERGLPGVPGQQGRSGDNGYPGAPGQPGIKGPR 1411
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 367-417 4.81e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 4.81e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 527504093   367 GEAGPHGAQGFDGVQGGKGLPGHDGLPGPVGPRGPVGAPGAPGQPGIDGMP 417
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 734-789 5.26e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 5.26e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 527504093   734 GVDGMPGLPGDRGADGLPGLPGPVGPDGYPGTPGERGMDGLPGFPGLHGEPGMRGQ 789
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1146-1202 5.63e-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: 5.63e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093  1146 GSPGQPGYPGQQGREGEKGYPGIPGENGLPGLRGQDGQPGLKGENGLDGQPGYPGSA 1202
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 1424-1571 6.88e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 44.29  E-value: 6.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1424 GLPGRPGREGLPGPMA--MAVRNPPGQPGENGYPGEKGYP---GLPGdnglSGPPGKAGYPGAPGTDGYPGPPGLSGMPg 1498
Cdd:PRK14959  376 GGASAPSGSAAEGPASggAATIPTPGTQGPQGTAPAAGMTpssAAPA----TPAPSAAPSPRVPWDDAPPAPPRSGIPP- 450

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527504093 1499 hggdqgfqgaagrTGNPGLPGTPGYPGSPGGWAPSRGfTFAKHSQTTAVPQCPPGASQLWEGYSLLYVQGNGR 1571
Cdd:PRK14959  451 -------------RPAPRMPEASPVPGAPDSVASASD-APPTLGDPSDTAEHTPSGPRTWDGFLEFCQGRNGQ 509
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1447-1498 6.92e-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: 6.92e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 527504093  1447 GQPGENGYPGEKGYPGLPGDNGLSGPPGKAGYPGAPGTDGYPGPPGLSGMPG 1498
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1131-1185 7.49e-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: 7.49e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 527504093  1131 GQPGLEGECGEDGFPGSPGQPGYPGQQGREGEKGYPGIPGENGLPGLRGQDGQPG 1185
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 731-785 7.71e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 7.71e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 527504093   731 GQPGVDGMPGLPGDRGADGLPGLPGPVGPDGYPGTPGERGMDGLPGFPGLHGEPG 785
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 829-884 8.27e-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: 8.27e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 527504093   829 GQVGYPGPNGDAGAAGLPGPDGYPGRDGLPGTPGYPGEAGMNGQDGAPGQPGSRGE 884
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 88-143 9.49e-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: 9.49e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 527504093    88 GSKGARGDRGLPGSPGHPGLQGLDGLPGLKGEEGIPGCNGTDGFPGMPGLAGPPGQ 143
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 904-958 9.77e-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: 39.01  E-value: 9.77e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 527504093   904 GQDGGPGYSGEAGAPGQNGMDGYPGAPGDQGYPGSPGQDGYPGPSGIPGEDGLVG 958
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1322-1378 1.01e-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: 39.01  E-value: 1.01e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093  1322 GYPGERGLPGLDGKRGHDGLPGAPGVPGVEGVPGLEGDCGEDGYPGAPGAPGSNGYP 1378
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 85-141 1.08e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 1.08e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093    85 GDMGSKGARGDRGLPGSPGHPGLQGLDGLPGLKGEEGIPGCNGTDGFPGMPGLAGPP 141
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1122-1176 1.12e-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: 38.63  E-value: 1.12e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 527504093  1122 GRQGNDGIPGQPGLEGECGEDGFPGSPGQPGYPGQQGREGEKGYPGIPGENGLPG 1176
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 901-955 1.24e-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: 38.63  E-value: 1.24e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 527504093   901 GTRGQDGGPGYSGEAGAPGQNGMDGYPGAPGDQGYPGSPGQDGYPGPSGIPGEDG 955
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1334-1389 1.27e-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: 38.63  E-value: 1.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 527504093  1334 GKRGHDGLPGAPGVPGVEGVPGLEGDCGEDGYPGAPGAPGSNGYPGERGLPGVPGQ 1389
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 826-879 1.27e-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: 38.63  E-value: 1.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 527504093   826 GFPGQVGYPGPNGDAGAAGLPGPDGYPGRDGLPGTPGYPGEAGMNGQDGAPGQP 879
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 835-889 1.29e-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: 38.63  E-value: 1.29e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 527504093   835 GPNGDAGAAGLPGPDGYPGRDGLPGTPGYPGEAGMNGQDGAPGQPGSRGESGLVG 889
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 737-793 1.35e-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: 38.63  E-value: 1.35e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093   737 GMPGLPGDRGADGLPGLPGPVGPDGYPGTPGERGMDGLPGFPGLHGEPGMRGQQGEV 793
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1197-1248 1.35e-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: 38.63  E-value: 1.35e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 527504093  1197 GYPGSAGQLGTPGDVGYPGAPGENGDNGNQGRDGQPGLRGESGQPGQPGLPG 1248
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1427-1491 1.49e-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: 38.24  E-value: 1.49e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527504093  1427 GRPGREGLPGPmamavrnpPGQPGENGYPGEKGYPGLPGDNGLSGPPGKAGYPGAPGTDGYPGPP 1491
Cdd:pfam01391    1 GPPGPPGPPGP--------PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 844-900 1.58e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 1.58e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093   844 GLPGPDGYPGRDGLPGTPGYPGEAGMNGQDGAPGQPGSRGESGLVGIDGKKGRDGTP 900
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1164-1220 1.65e-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: 38.24  E-value: 1.65e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093  1164 GYPGIPGENGLPGLRGQDGQPGLKGENGLDGQPGYPGSAGQLGTPGDVGYPGAPGEN 1220
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1134-1190 1.65e-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: 38.24  E-value: 1.65e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093  1134 GLEGECGEDGFPGSPGQPGYPGQQGREGEKGYPGIPGENGLPGLRGQDGQPGLKGEN 1190
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 838-893 1.66e-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: 38.24  E-value: 1.66e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 527504093   838 GDAGAAGLPGPDGYPGRDGLPGTPGYPGEAGMNGQDGAPGQPGSRGESGLVGIDGK 893
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 385-443 1.70e-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: 38.24  E-value: 1.70e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 527504093   385 GLPGHDGLPGPVGPRGPVGAPGAPGQPGIDGMPGytEKGDRGEDGYPGFAGEPGLPGEP 443
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPG--PPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 781-943 2.00e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.65  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  781 HGEPGMRGQQGEVGFNGIDGDCGEPGLDGYPGAPGAPGAPGETGFGfpgqvgypGPNGDAGAAGLPGPDGYPGrdglpgt 860
Cdd:PHA03169   81 HGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGS--------SPESPASHSPPPSPPSHPG------- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  861 PGYPGEAGMNGQDGAPGQPGSRGESGLVGIDGKKGRDGTPGTRGQDGGPGYSGEAGAPGQNGMD--GYPGAPGDQGYPGS 938
Cdd:PHA03169  146 PHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDepGEPQSPTPQQAPSP 225


                  ....*
gi 527504093  939 PGQDG 943
Cdd:PHA03169  226 NTQQA 230
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 64-119 2.00e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 2.00e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 527504093    64 GQDGPEGAPGAPGMFGAEGDFGDMGSKGARGDRGLPGSPGHPGLQGLDGLPGLKGE 119
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1107-1162 2.08e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 2.08e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 527504093  1107 GMPGLKGESGLPGLPGRQGNDGIPGQPGLEGECGEDGFPGSPGQPGYPGQQGREGE 1162
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1143-1199 2.64e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.47  E-value: 2.64e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093  1143 GFPGSPGQPGYPGQQGREGEKGYPGIPGENGLPGLRGQDGQPGLKGENGLDGQPGYP 1199
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 1356-1533 2.70e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1356 LEGDCGEDGYPGAPGAPGSNGYPGERGLPGVPGQQGRSGDngyPGAPGQPGIKGPRGDDGFPGRDGLDGLPGRPGREGLP 1435
Cdd:PRK07764  578 LGGDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAA---PAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHP 654

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093 1436 GPMAM--AVRNPPGQPGENGYPGEKGYPGLPGDNGLSGPPGKAGYPGAPGTDGYPGPPGLSGMPGHGGDQGFQGAAGRTG 1513
Cdd:PRK07764  655 KHVAVpdASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPA 734

                         170       180
                  ....*....|....*....|...
gi 527504093 1514 NPG---LPGTPGYPGSPGGWAPS 1533
Cdd:PRK07764  735 ADDpvpLPPEPDDPPDPAGAPAQ 757
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 907-961 2.77e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.47  E-value: 2.77e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 527504093   907 GGPGYSGEAGAPGQNGMDGYPGAPGDQGYPGSPGQDGYPGPSGIPGEDGLVGFPG 961
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 892-947 2.97e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.47  E-value: 2.97e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 527504093   892 GKKGRDGTPGTRGQDGGPGYSGEAGAPGQNGMDGYPGAPGDQGYPGSPGQDGYPGP 947
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1453-1509 3.03e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.47  E-value: 3.03e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093  1453 GYPGEKGYPGLPGDNGLSGPPGKAGYPGAPGTDGYPGPPGLSGMPGHGGDQGFQGAA 1509
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 985-1041 3.95e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 3.95e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093   985 GLDGVPGYPGEHGTDGLPGLPGADGQPGFVGEAGEPGTPGYRGQPGEPGNLAYPGQP 1041
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 834-1032 4.15e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  834 PGPNGDAGAAGLPGPDGYPGRDGLPGTPGYPGEAGMNGQDGAPGQPGSRGESGLVGIDGkkGRDGTPGTRGQDGGPGYSG 913
Cdd:PRK07764  603 PASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPD--ASDGGDGWPAKAGGAAPAA 680

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  914 EAGAPGQNGMDGYPGAPGDQGYPGSPGQDGYPGPSGIPGEDglvgfpglrgehgdnglPGLEGECGEEGSRGLDGVPGYP 993
Cdd:PRK07764  681 PPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQP-----------------PQAAQGASAPSPAADDPVPLPP 743

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 527504093  994 GEHGTDGLPGLPGADGQPGFVGEAGEPGTPGYRGQPGEP 1032
Cdd:PRK07764  744 EPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 856-910 4.41e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 4.41e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 527504093   856 GLPGTPGYPGEAGMNGQDGAPGQPGSRGESGLVGIDGKKGRDGTPGTRGQDGGPG 910
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1191-1247 5.06e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.70  E-value: 5.06e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093  1191 GLDGQPGYPGSAGQLGTPGDVGYPGAPGENGDNGNQGRDGQPGLRGESGQPGQPGLP 1247
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1158-1214 5.31e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.70  E-value: 5.31e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093  1158 GREGEKGYPGIPGENGLPGLRGQDGQPGLKGENGLDGQPGYPGSAGQLGTPGDVGYP 1214
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 913-969 5.53e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.70  E-value: 5.53e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093   913 GEAGAPGQNGMDGYPGAPGDQGYPGSPGQDGYPGPSGIPGEDGLVGFPGLRGEHGDN 969
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1188-1244 7.36e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 7.36e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 527504093  1188 GENGLDGQPGYPGSAGQLGTPGDVGYPGAPGENGDNGNQGRDGQPGLRGESGQPGQP 1244
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
71-344 7.61e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 40.78  E-value: 7.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093   71 APGAPGMFGAEGDFGDMGSKGARGDRGLPGSPGHPGLQGLDGLPGLKGEEGIPGCNGTDGFPGMPGLAGPPGQSGQNGNP 150
Cdd:COG5164     5 GPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  151 GRPGLSGPPGeggvnSQGRKGVKGESGRSGVPGLPGNSGYPGLKGAKGdpgpyglPGFPGVSGLKGRMGVRTSGVKGEKG 230
Cdd:COG5164    85 QNQGGTRPAG-----NTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-------PPSGGSTTPPGDGGSTPPGPGSTGP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  231 LPGPPGPPGQPGSYPWASKPIEMEVLQGPVGPAGVKGEKGRDGPVGPPGMLGLDGPPGYPGLKGQKGDLGDAGqrGKRGK 310
Cdd:COG5164   153 GGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGP 230

                         250       260       270
                  ....*....|....*....|....*....|....
gi 527504093  311 DGVPGNYGEKGSQGEQGLGGTPGYPGTKGGAGEP 344
Cdd:COG5164   231 KDQRPKTNPIERRGPERPEAAALPAELTALEAEN 264
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 983-1033 7.81e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 7.81e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 527504093   983 SRGLDGVPGYPGEHGTDGLPGLPGADGQPGFVGEAGEPGTPGYRGQPGEPG 1033
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 730-784 8.12e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 8.12e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 527504093   730 AGQPGVDGMPGLPGDRGADGLPGLPGPVGPDGYPGTPGERGMDGLPGFPGLHGEP 784
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 988-1042 9.32e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.93  E-value: 9.32e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 527504093   988 GVPGYPGEHGTDGLPGLPGADGQPGFVGEAGEPGTPGYRGQPGEPGNLAYPGQPG 1042
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 889-1030 9.36e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.34  E-value: 9.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527504093  889 GIDGKKGRDGTPGTRGQDGGPGYSGEAGAPGQNGMDGYPGAPGDQGYPGSPGQDGYPGPSGIPGEDGLVGFPGLRGEHGD 968
Cdd:PHA03169   90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQP 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 527504093  969 NGLPGLEGECGEEGSRGLDGVPGYPGEHGTDGLPGLPGADgqpgfvgEAGEPGTPGYRGQPG 1030
Cdd:PHA03169  170 SHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPD-------EPGEPQSPTPQQAPS 224
 
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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