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Conserved domains on  [gi|111120329|ref|NP_031769|]
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collagen alpha-2(I) chain preproprotein [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1137-1371 5.76e-150

Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


:

Pssm-ID: 460199  Cd Length: 233  Bit Score: 452.95  E-value: 5.76e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  1137 KDYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWNSDYYWIDPNQGCTMDAIKVYCDFSTGETCIQAQPVN 1216
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKAS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  1217 TPAKNSYSRAqaNKHVWLGETINGGSQFEYNVEGVSSKEMATQLAFMRLLANRASQNITYHCKNSIAYLDEETGSLNKAV 1296
Cdd:pfam01410   81 IPRKNWWTKE--SKHVWFGEFMNGGSQFSYGVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 111120329  1297 LLQGSNDVELVAEGNSRFTYSVLVDGCSKKTNEWGKTIIEYKTNKPSRLPFLDIAPLDIGGADQEFRVEVGPVCF 1371
Cdd:pfam01410  159 LLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 352-576 2.96e-39

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: 152.37  E-value: 2.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  352 GEPGPAGSKGESGNKGEPGSVGAQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGS 431
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  432 TGPAGIRGPNGDAGRPGEPGLMGPRGLPGSPGNvgpsGKEGPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPG 511
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 111120329  512 KPGERGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTTGEVGKP 576
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 469-728 2.23e-31

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 129.25  E-value: 2.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  469 GKEGPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPGKPGERGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGG 548
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  549 KGEQGPAGPPGFQGLPGPSGTTGEVGKPGERGLPGEfGLPGPAGPRGERGTPGESGAAGPSGPIGSRGPSGAPGPDGNKG 628
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  629 EAgavgapgsagasgpgglpGERGAAGIPggkgekgetglrGDTGNTGRDGARGIPGAVGAPGPAGASGDRGEAGAAGPS 708
Cdd:NF038329  276 KD------------------GERGPVGPA------------GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD 325

                         250       260
                  ....*....|....*....|
gi 111120329  709 GPAGPRGSPGERGEVGPAGP 728
Cdd:NF038329  326 GLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 822-1067 2.66e-31

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 128.87  E-value: 2.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  822 EGIRGPRGDQGPVGRTGETGASGPPGFVGEKGPSGEPGTAGAPGTAGPQGLLGAPGILGLPGSRGERGLPGIAGALGEPG 901
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  902 PLGisgppgargppgAVGSPGVNGAPGEAGRDGNPGSDGPPGRDGQPGhKGERGYPGSIGPTGAAGAPGPHGSVGPAGKH 981
Cdd:NF038329  196 PRG------------ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  982 GNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGDKGHRG---LPGLKGYSGLQGLPGLAGLHGDQGAPGPVGPAGP 1058
Cdd:NF038329  263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGqngKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342


                  ....*....
gi 111120329 1059 RGPAGPSGP 1067
Cdd:NF038329  343 KTPEVPQKP 351
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 83-333 6.91e-30

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 124.63  E-value: 6.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329   83 FAAQYSDKGVSSGPGPMGLMGPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRPGER 162
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  163 GVVGPQGARGFPGTPGLPGFKGVKGHSGMDGLKGQPGaQGVKGEPGAPGENGTPGQAGARGLPGE---RGRVGAPGPAGA 239
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKdgpRGDRGEAGPDGP 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  240 RGSDGSVGPVGPAGPIGsagppgfpgapgpkgELGPVGNPGPAGPAGPRGEVGLPGlsgpvgppgNPGTNGLTGAKGATG 319
Cdd:NF038329  274 DGKDGERGPVGPAGKDG---------------QNGKDGLPGKDGKDGQNGKDGLPG---------KDGKDGQPGKDGLPG 329

                         250
                  ....*....|....
gi 111120329  320 LPGVAGAPGLPGPR 333
Cdd:NF038329  330 KDGKDGQPGKPAPK 343
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1137-1371 5.76e-150

Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 460199  Cd Length: 233  Bit Score: 452.95  E-value: 5.76e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  1137 KDYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWNSDYYWIDPNQGCTMDAIKVYCDFSTGETCIQAQPVN 1216
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKAS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  1217 TPAKNSYSRAqaNKHVWLGETINGGSQFEYNVEGVSSKEMATQLAFMRLLANRASQNITYHCKNSIAYLDEETGSLNKAV 1296
Cdd:pfam01410   81 IPRKNWWTKE--SKHVWFGEFMNGGSQFSYGVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 111120329  1297 LLQGSNDVELVAEGNSRFTYSVLVDGCSKKTNEWGKTIIEYKTNKPSRLPFLDIAPLDIGGADQEFRVEVGPVCF 1371
Cdd:pfam01410  159 LLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1138-1372 2.11e-129

Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 197483  Cd Length: 232  Bit Score: 398.38  E-value: 2.11e-129
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329   1138 DYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWNSDYYWIDPNQGCTMDAIKVYCDFSTGETCIQAQPVNT 1217
Cdd:smart00038    1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETGETCVSPSPSSI 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329   1218 PAKNSYSraQANKHVWLGETINGGSQFEYnVEGVSSKEMATQLAFMRLLANRASQNITYHCKNSIAYLDEETGSLNKAVL 1297
Cdd:smart00038   81 PRKTWYS--GKSKHVWFGETMNGGFKFSY-GDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALR 157

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 111120329   1298 LQGSNDVELVAEGNSRFTYSVLVDGCSKKTNEWGKTIIEYKTNKPSRLPFLDIAPLDIGGADQEFRVEVGPVCFK 1372
Cdd:smart00038  158 LRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 352-576 2.96e-39

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: 152.37  E-value: 2.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  352 GEPGPAGSKGESGNKGEPGSVGAQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGS 431
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  432 TGPAGIRGPNGDAGRPGEPGLMGPRGLPGSPGNvgpsGKEGPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPG 511
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 111120329  512 KPGERGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTTGEVGKP 576
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 313-557 1.07e-32

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 133.11  E-value: 1.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  313 GAKGATGLPGVAGAPGLPGPRGIPGPAgaagatgarglvGEPGPAGSKGESGNKGEPGSVGAQGPPGPSGEEGKRGSPGE 392
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGET------------GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  393 AGSAGPAGPPGLRGSPGSRGLPGADGragvmgPPGNRGSTGPAGIRGPNGDAGRP--GEPGLMGPRGLPGSPGNVGPSGK 470
Cdd:NF038329  185 KGPAGEKGPQGPRGETGPAGEQGPAG------PAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGK 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  471 EGPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPGKPGERGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGGKG 550
Cdd:NF038329  259 DGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338


                  ....*..
gi 111120329  551 EQGPAGP 557
Cdd:NF038329  339 KPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 272-543 1.88e-31

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 129.25  E-value: 1.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  272 ELGPVGNPGPAGPAGPRGEvglpglsgpvgppgnpgtNGLTGAKGATGLPGVAGAPGLPGPRgipgpagaagatgarglv 351
Cdd:NF038329  121 EPGPAGPAGPAGEQGPRGD------------------RGETGPAGPAGPPGPQGERGEKGPA------------------ 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  352 GEPGPAGSKGESGNKGEPgsvGAQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGvMGPPGNRGS 431
Cdd:NF038329  165 GPQGEAGPQGPAGKDGEA---GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGD 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  432 TGPAGIRGPNGDAGRPGEPGLMGPRGLPGSPGNVGPSGKEGPVGLPGIDGRPGPIGPAGPrgeagnigfPGPKGPSGDPG 511
Cdd:NF038329  241 PGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGK---------DGKDGQNGKDG 311

                         250       260       270
                  ....*....|....*....|....*....|..
gi 111120329  512 KPGERGHPGLAGARGAPGPDGNNGAQGPPGPQ 543
Cdd:NF038329  312 LPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 469-728 2.23e-31

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 129.25  E-value: 2.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  469 GKEGPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPGKPGERGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGG 548
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  549 KGEQGPAGPPGFQGLPGPSGTTGEVGKPGERGLPGEfGLPGPAGPRGERGTPGESGAAGPSGPIGSRGPSGAPGPDGNKG 628
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  629 EAgavgapgsagasgpgglpGERGAAGIPggkgekgetglrGDTGNTGRDGARGIPGAVGAPGPAGASGDRGEAGAAGPS 708
Cdd:NF038329  276 KD------------------GERGPVGPA------------GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD 325

                         250       260
                  ....*....|....*....|
gi 111120329  709 GPAGPRGSPGERGEVGPAGP 728
Cdd:NF038329  326 GLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 822-1067 2.66e-31

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 128.87  E-value: 2.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  822 EGIRGPRGDQGPVGRTGETGASGPPGFVGEKGPSGEPGTAGAPGTAGPQGLLGAPGILGLPGSRGERGLPGIAGALGEPG 901
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  902 PLGisgppgargppgAVGSPGVNGAPGEAGRDGNPGSDGPPGRDGQPGhKGERGYPGSIGPTGAAGAPGPHGSVGPAGKH 981
Cdd:NF038329  196 PRG------------ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  982 GNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGDKGHRG---LPGLKGYSGLQGLPGLAGLHGDQGAPGPVGPAGP 1058
Cdd:NF038329  263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGqngKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342


                  ....*....
gi 111120329 1059 RGPAGPSGP 1067
Cdd:NF038329  343 KTPEVPQKP 351
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 83-333 6.91e-30

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 124.63  E-value: 6.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329   83 FAAQYSDKGVSSGPGPMGLMGPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRPGER 162
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  163 GVVGPQGARGFPGTPGLPGFKGVKGHSGMDGLKGQPGaQGVKGEPGAPGENGTPGQAGARGLPGE---RGRVGAPGPAGA 239
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKdgpRGDRGEAGPDGP 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  240 RGSDGSVGPVGPAGPIGsagppgfpgapgpkgELGPVGNPGPAGPAGPRGEVGLPGlsgpvgppgNPGTNGLTGAKGATG 319
Cdd:NF038329  274 DGKDGERGPVGPAGKDG---------------QNGKDGLPGKDGKDGQNGKDGLPG---------KDGKDGQPGKDGLPG 329

                         250
                  ....*....|....
gi 111120329  320 LPGVAGAPGLPGPR 333
Cdd:NF038329  330 KDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 192-473 2.87e-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: 122.71  E-value: 2.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  192 DGLKGQPGAQGVKGEPGAPGENGTPGQAGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGsagppgfpgapgpkg 271
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG--------------- 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  272 ELGPVGNPGPAGPAGPRGEVGLPGlsgpvgppgnpgTNGLTGAKGATGLPGVAGAPGLPGPRGipgpagaagatgarglv 351
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRGETGPAG------------EQGPAGPAGPDGEAGPAGEDGPAGPAG----------------- 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  352 gepgpAGSKGESGNKGEPGSVGAQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGS 431
Cdd:NF038329  232 -----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQ 306

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 111120329  432 TGPAGIRGPNGDAGRPGEPGLMGPRGLPGSPGNVGPSGKEGP 473
Cdd:NF038329  307 NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVP 348
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 521-752 2.03e-27

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 117.31  E-value: 2.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  521 LAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTTGEVGKPGERGLPGEFGLPGPAGPRGERGTP 600
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  601 GESGAAGPSGPIGSRGPSGAPGPDGNKGEAGAVgAPGSAGASGPGGLPGERGAAGIPGGKGEKGETGLRGDTGNTGRDGA 680
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPA-GPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 111120329  681 RGIPGAVGAPGPAGASGDRGEAGAAGPSGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGEKGTKGP 752
Cdd:NF038329  274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 535-766 2.72e-27

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: 116.93  E-value: 2.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  535 GAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTTGEVGKPGERGLPGEFGLPGPAGPRGERGTPGESGAAGPSGPIGS 614
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  615 RGPSGAPGPDGNKGEAGAvgapgsagasgpgglPGERGAAGiPGGKGEKGETGLRGDTGNTGRDGARGIPGAVGAPGPAG 694
Cdd:NF038329  197 RGETGPAGEQGPAGPAGP---------------DGEAGPAG-EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 111120329  695 ASGDRGEAGAAGPSGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGEKGTKGPKGENGIVGPTGSVG 766
Cdd:NF038329  261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 879-1090 1.11e-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: 115.00  E-value: 1.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  879 LGLPGSRGERGLPGIAGALGEPGPlgisgppgargppgavgspgvNGAPGEAGRDGNPGSDGPPGRDGQPGHKGERGYPG 958
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQGP---------------------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  959 SIGPTGAAGAPGPHGSVGPAGKHGNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGD--KGHRGLPGLKGYSGLQG 1036
Cdd:NF038329  172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQG 251

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 111120329 1037 LPGLAGLHGDQGAPGPVGPAGPRGPAGPSGPVGKDGRSGQPGPVGPAGVRGSQG 1090
Cdd:NF038329  252 PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG 305
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 678-949 2.27e-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: 2.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  678 DGARGIPGAVGAPGPAGASGDRGEAGAAGPSGPAGPRGSPGERGEVGPAGPngfagpagaagqpgaKGEKGTKGPKGENG 757
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGP---------------QGEAGPQGPAGKDG 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  758 IVGPTGSVGAAGPSGPNGPPGPVGSRGDGGPPGMTGFPGAAGRTGPPGPSGiagppgppgaagkEGIRGPRGDQGPVGRT 837
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------------DGQQGPDGDPGPTGED 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  838 GETGASGPPGFVGEKGPSGEPGTAGAPGTAGPQGLLGAPgilGLPGSRGERGLPGIAGALGEPgplgisgppgargppga 917
Cdd:NF038329  248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPA---GKDGQNGKDGLPGKDGKDGQN----------------- 307

                         250       260       270
                  ....*....|....*....|....*....|..
gi 111120329  918 vGSPGVNGAPGEAGRDGNPGSDGPPGRDGQPG 949
Cdd:NF038329  308 -GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 28-288 1.28e-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: 1.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329   28 GSVRKGPTGDRGPRGQRGPAGPRGRDGVDGPMGPPGPPGSPGppgspappgltgnfaaqysDKGVSSGPGPMGLMGPRGP 107
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG-------------------ERGEKGPAGPQGEAGPQGP 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  108 PGAVGAPGPQGFQGPAGEPGEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRPGERGvvgpqgaRGFPGTPGLPGFKGVKG 187
Cdd:NF038329  176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  188 HSGMDGLKGQPGAQGVKGEPGAPGENGTPGQAGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAP 267
Cdd:NF038329  249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328

                         250       260
                  ....*....|....*....|.
gi 111120329  268 GPKGELGPVGNPGPAGPAGPR 288
Cdd:NF038329  329 GKDGKDGQPGKPAPKTPEVPQ 349
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 744-1008 2.60e-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: 110.77  E-value: 2.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  744 KGEKGTKGPKGENGIVGPTGSVGAAGPSGPNGPPGPVGSRGDGGPPGMTGFPGAAGrtgppgpsgiagppgppgaagKEG 823
Cdd:NF038329  119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG---------------------PAG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  824 IRGPRGDQGPVGRTGETGASGPPGFVGEKGPSGEPGTAGAPGTAGPQGLLGAPGilglPGSRGERGLPGIAGALGEPGPL 903
Cdd:NF038329  178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPD 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  904 GisgppgargPPGAVGSPGVNGAPGEAGRDGNPGSDGPPGRDGQPGHKGERGYPGSIGPTGAAGAPGPHGSVGPAGKHGN 983
Cdd:NF038329  254 G---------PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324

                         250       260
                  ....*....|....*....|....*
gi 111120329  984 RGEPGPAGSVGPVGAVGPRGPSGPQ 1008
Cdd:NF038329  325 DGLPGKDGKDGQPGKPAPKTPEVPQ 349
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 982-1092 8.15e-14

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 75.33  E-value: 8.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  982 GNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGDKGHRGLPGLKGysglqglpglaglhgDQGAPGPVGPAGPRGP 1061
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG---------------PQGEAGPQGPAGKDGE 181

                          90       100       110
                  ....*....|....*....|....*....|.
gi 111120329 1062 AGPSGPVGKDGRSGQPGPVGPAGVRGSQGSQ 1092
Cdd:NF038329  182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPA 212
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
374-623 7.59e-13

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 72.76  E-value: 7.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  374 AQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGSTGPAGIRGPNGDagrPGEPGLM 453
Cdd:COG5164     5 GPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGP---AQNQGGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  454 GPRGLPGSPGNVGPSGKEGPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPGKPGERGHPGLAGARGAPGPDGN 533
Cdd:COG5164    82 TPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  534 NGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTTGEVGKPGERGLPGEFGLPGPAGPRGERGTPGESGAAGPSGPIG 613
Cdd:COG5164   162 GGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIE 241

                         250
                  ....*....|
gi 111120329  614 SRGPSGAPGP 623
Cdd:COG5164   242 RRGPERPEAA 251
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
472-728 2.76e-10

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 64.67  E-value: 2.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  472 GPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPGKPGERGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGE 551
Cdd:COG5164     7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  552 QGPAGPPGFQGLPGPSGTTGEVGKPGERGLPGEFGLPGP-AGPRGERGTPGESGAAGPSGPiGSRGPSGAPGPDGNKGEA 630
Cdd:COG5164    87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGStTPPSGGSTTPPGDGGSTPPGP-GSTGPGGSTTPPGDGGST 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  631 GavgapgsAGASGPGGLPGERGAAGIPGGKGEKGETGLRGDTGNTGRDGARGIPGAVGA-PGPAGASGDRGEAGAAGPSG 709
Cdd:COG5164   166 T-------PPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKgNPPDDRGGKTGPKDQRPKTN 238

                         250
                  ....*....|....*....
gi 111120329  710 PAGPRGSPGERGEVGPAGP 728
Cdd:COG5164   239 PIERRGPERPEAAALPAEL 257
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
198-484 2.98e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 58.12  E-value: 2.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  198 PGAQGVKGEPGAPGENGTPGQAGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPgpkgelGPVG 277
Cdd:COG5164     3 LYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGAT------GPAQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  278 NPGPAGPAGPRGEVGLPGLSGPVGPPGNPGTNGLTGAKGATGLPGVAGAPGLPGPRGIPGPAGAAGATGARGLVGEPGPA 357
Cdd:COG5164    77 NQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGST 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  358 GSKGESGNKGEPGSVGAQGPPGPSGEegkrGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGSTG---- 433
Cdd:COG5164   157 TPPGDGGSTTPPGPGGSTTPPDDGGS----TTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTgpkd 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 111120329  434 PAGIRGPNGDAGRPGEPGLMGPRGLPG--------SPGNVGPSGKEGPVGLPGIDGRPG 484
Cdd:COG5164   233 QRPKTNPIERRGPERPEAAALPAELTAleaenraaNPEPATKTIPETTTVKDLATVLGK 291
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 103-159 1.91e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.03  E-value: 1.91e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   103 GPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRP 159
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 373-429 4.07e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.26  E-value: 4.07e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   373 GAQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNR 429
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 362-557 8.06e-07

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 53.05  E-value: 8.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  362 ESGNKGEPGSVGAQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGSTGPAGIRGPN 441
Cdd:PHA03169   53 TSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPA 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  442 GDAGRPGEPGLMGPrGLPGSPGNVGPSGKEGPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPGKPGERGHPgl 521
Cdd:PHA03169  133 SHSPPPSPPSHPGP-HEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPD-- 209

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 111120329  522 agargAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGP 557
Cdd:PHA03169  210 -----EPGEPQSPTPQQAPSPNTQQAVEHEDEPTEP 240
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 553-608 1.33e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.72  E-value: 1.33e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 111120329   553 GPAGPPGFQGLPGPSGTTGEVGKPGERGLPGEFGLPGPAGPRGERGTPGESGAAGP 608
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
103-408 8.19e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 50.03  E-value: 8.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  103 GPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGF 182
Cdd:COG5164     7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  183 KGVKGHSGMDGLKGQPGAQGVKGEPGAPGENGTPGQAGARGlPGERGRVGAPGPAGARGSDGsvGPVGPAGPIGSAGPPG 262
Cdd:COG5164    87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-PPSGGSTTPPGDGGSTPPGP--GSTGPGGSTTPPGDGG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  263 FPGAPGPKGELGPVGNPGPAGPAGPrGEVGLPGLSGPVGPPGNPGTNGLTGAKGATGLPGVAGAPGLPGPRGIPGPAGAA 342
Cdd:COG5164   164 STTPPGPGGSTTPPDDGGSTTPPNK-GETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIER 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 111120329  343 GATGARGLVGEPGPAGSKGESGNKGEPGSVGAQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSP 408
Cdd:COG5164   243 RGPERPEAAALPAELTALEAENRAANPEPATKTIPETTTVKDLATVLGKKGSDLVTNLMKKGKGTN 308
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 95-290 1.19e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.98  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329   95 GPGPMGLMGPRGPPGAVGAPGPQGFQgPAGEPGEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRPGERGVVGPQGARGFP 174
Cdd:PRK07764  589 GPAPGAAGGEGPPAPASSGPPEEAAR-PAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  175 GTPGLPGFKGVKGHSGMDGLKGQPGAQGVKGEPGAPGENGTPGQAGARGLPGERGRVGAPGPAGARGSDGSVGPvgPAGP 254
Cdd:PRK07764  668 GWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPL--PPEP 745

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 111120329  255 IGSAGPPGFPGAPGPKGELGPVGNPGPAGPAGPRGE 290
Cdd:PRK07764  746 DDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSE 781
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 960-1133 1.60e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.60  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  960 IGPTGAAGAPGPHGSVGPAGKHGNRGEP----GPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGDKGHRGLPGLKGYSGLQ 1035
Cdd:PRK07764  588 VGPAPGAAGGEGPPAPASSGPPEEAARPaapaAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329 1036 GLPGLAGLHGDQGAPGPVGPAGPRGPAGPSGPVGKDGRSGQPGPVGPAGVRGSQGSQGPAGPPGPPGPPGPPGVSGGGYD 1115
Cdd:PRK07764  668 GWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD 747

                         170
                  ....*....|....*...
gi 111120329 1116 FGFEGDFYRADQPRSQPS 1133
Cdd:PRK07764  748 PPDPAGAPAQPPPPPAPA 765
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 940-996 1.80e-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: 43.64  E-value: 1.80e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   940 GPPGRDGQPGHKGERGYPGSIGPTGAAGAPGPHGSVGPAGKHGNRGEPGPAGSVGPV 996
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 493-719 3.57e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.44  E-value: 3.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  493 GEAGNIGFPGPKGPSGdPGKPGERGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPS-GTTG 571
Cdd:PRK07764  590 PAPGAAGGEGPPAPAS-SGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASdGGDG 668

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  572 EVGKPGERGLPGEFGLPGPAGPRGERGTPGESGAAGPSGPIGSRGPSGAPGPDGNKGEAGAVGAPGSAGASGPGGLPGER 651
Cdd:PRK07764  669 WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDP 748

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 111120329  652 GAAGIPGGKGekgetglrgdtgnTGRDGARGIPGAVGAPGPAGASGDRGEAGAAGPSGPAGPRGSPGE 719
Cdd:PRK07764  749 PDPAGAPAQP-------------PPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEE 803
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1034-1092 1.53e-04

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: 46.05  E-value: 1.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 111120329 1034 LQGLPGLAGLHGDQGAPGPVGPAGPRGPAGPSGPVGKDGRSGQPGPVGPAGVRGSQGSQ 1092
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ 173
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
919-1084 1.98e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.79  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  919 GSPGVNGAPGEAGRDGNPGSDGPPGRDGQPGHKGERGYPGSIGPTGAAGAPGPHGSVGPAGKHGNRGEPGPAGSVGPVGA 998
Cdd:COG5164    16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  999 VGPRGPSGPQGIRGDKGEPGDKGHRGLPGLKG--YSGLQGLPGLAG-LHGDQGAPGPVGPAGPRGPAGPSGPVGKDGRSG 1075
Cdd:COG5164    96 TGGTTPAGDGGATGPPDDGGATGPPDDGGSTTppSGGSTTPPGDGGsTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTT 175


                  ....*....
gi 111120329 1076 QPGPVGPAG 1084
Cdd:COG5164   176 PPDDGGSTT 184
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1137-1371 5.76e-150

Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 460199  Cd Length: 233  Bit Score: 452.95  E-value: 5.76e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  1137 KDYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWNSDYYWIDPNQGCTMDAIKVYCDFSTGETCIQAQPVN 1216
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKAS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  1217 TPAKNSYSRAqaNKHVWLGETINGGSQFEYNVEGVSSKEMATQLAFMRLLANRASQNITYHCKNSIAYLDEETGSLNKAV 1296
Cdd:pfam01410   81 IPRKNWWTKE--SKHVWFGEFMNGGSQFSYGVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 111120329  1297 LLQGSNDVELVAEGNSRFTYSVLVDGCSKKTNEWGKTIIEYKTNKPSRLPFLDIAPLDIGGADQEFRVEVGPVCF 1371
Cdd:pfam01410  159 LLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1138-1372 2.11e-129

Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 197483  Cd Length: 232  Bit Score: 398.38  E-value: 2.11e-129
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329   1138 DYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWNSDYYWIDPNQGCTMDAIKVYCDFSTGETCIQAQPVNT 1217
Cdd:smart00038    1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETGETCVSPSPSSI 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329   1218 PAKNSYSraQANKHVWLGETINGGSQFEYnVEGVSSKEMATQLAFMRLLANRASQNITYHCKNSIAYLDEETGSLNKAVL 1297
Cdd:smart00038   81 PRKTWYS--GKSKHVWFGETMNGGFKFSY-GDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALR 157

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 111120329   1298 LQGSNDVELVAEGNSRFTYSVLVDGCSKKTNEWGKTIIEYKTNKPSRLPFLDIAPLDIGGADQEFRVEVGPVCFK 1372
Cdd:smart00038  158 LRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 352-576 2.96e-39

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: 152.37  E-value: 2.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  352 GEPGPAGSKGESGNKGEPGSVGAQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGS 431
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  432 TGPAGIRGPNGDAGRPGEPGLMGPRGLPGSPGNvgpsGKEGPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPG 511
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 111120329  512 KPGERGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTTGEVGKP 576
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 313-557 1.07e-32

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 133.11  E-value: 1.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  313 GAKGATGLPGVAGAPGLPGPRGIPGPAgaagatgarglvGEPGPAGSKGESGNKGEPGSVGAQGPPGPSGEEGKRGSPGE 392
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGET------------GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  393 AGSAGPAGPPGLRGSPGSRGLPGADGragvmgPPGNRGSTGPAGIRGPNGDAGRP--GEPGLMGPRGLPGSPGNVGPSGK 470
Cdd:NF038329  185 KGPAGEKGPQGPRGETGPAGEQGPAG------PAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGK 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  471 EGPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPGKPGERGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGGKG 550
Cdd:NF038329  259 DGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338


                  ....*..
gi 111120329  551 EQGPAGP 557
Cdd:NF038329  339 KPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 272-543 1.88e-31

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 129.25  E-value: 1.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  272 ELGPVGNPGPAGPAGPRGEvglpglsgpvgppgnpgtNGLTGAKGATGLPGVAGAPGLPGPRgipgpagaagatgarglv 351
Cdd:NF038329  121 EPGPAGPAGPAGEQGPRGD------------------RGETGPAGPAGPPGPQGERGEKGPA------------------ 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  352 GEPGPAGSKGESGNKGEPgsvGAQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGvMGPPGNRGS 431
Cdd:NF038329  165 GPQGEAGPQGPAGKDGEA---GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGD 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  432 TGPAGIRGPNGDAGRPGEPGLMGPRGLPGSPGNVGPSGKEGPVGLPGIDGRPGPIGPAGPrgeagnigfPGPKGPSGDPG 511
Cdd:NF038329  241 PGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGK---------DGKDGQNGKDG 311

                         250       260       270
                  ....*....|....*....|....*....|..
gi 111120329  512 KPGERGHPGLAGARGAPGPDGNNGAQGPPGPQ 543
Cdd:NF038329  312 LPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 469-728 2.23e-31

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 129.25  E-value: 2.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  469 GKEGPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPGKPGERGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGG 548
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  549 KGEQGPAGPPGFQGLPGPSGTTGEVGKPGERGLPGEfGLPGPAGPRGERGTPGESGAAGPSGPIGSRGPSGAPGPDGNKG 628
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  629 EAgavgapgsagasgpgglpGERGAAGIPggkgekgetglrGDTGNTGRDGARGIPGAVGAPGPAGASGDRGEAGAAGPS 708
Cdd:NF038329  276 KD------------------GERGPVGPA------------GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD 325

                         250       260
                  ....*....|....*....|
gi 111120329  709 GPAGPRGSPGERGEVGPAGP 728
Cdd:NF038329  326 GLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 822-1067 2.66e-31

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 128.87  E-value: 2.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  822 EGIRGPRGDQGPVGRTGETGASGPPGFVGEKGPSGEPGTAGAPGTAGPQGLLGAPGILGLPGSRGERGLPGIAGALGEPG 901
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  902 PLGisgppgargppgAVGSPGVNGAPGEAGRDGNPGSDGPPGRDGQPGhKGERGYPGSIGPTGAAGAPGPHGSVGPAGKH 981
Cdd:NF038329  196 PRG------------ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  982 GNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGDKGHRG---LPGLKGYSGLQGLPGLAGLHGDQGAPGPVGPAGP 1058
Cdd:NF038329  263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGqngKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342


                  ....*....
gi 111120329 1059 RGPAGPSGP 1067
Cdd:NF038329  343 KTPEVPQKP 351
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 83-333 6.91e-30

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 124.63  E-value: 6.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329   83 FAAQYSDKGVSSGPGPMGLMGPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRPGER 162
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  163 GVVGPQGARGFPGTPGLPGFKGVKGHSGMDGLKGQPGaQGVKGEPGAPGENGTPGQAGARGLPGE---RGRVGAPGPAGA 239
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKdgpRGDRGEAGPDGP 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  240 RGSDGSVGPVGPAGPIGsagppgfpgapgpkgELGPVGNPGPAGPAGPRGEVGLPGlsgpvgppgNPGTNGLTGAKGATG 319
Cdd:NF038329  274 DGKDGERGPVGPAGKDG---------------QNGKDGLPGKDGKDGQNGKDGLPG---------KDGKDGQPGKDGLPG 329

                         250
                  ....*....|....
gi 111120329  320 LPGVAGAPGLPGPR 333
Cdd:NF038329  330 KDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 192-473 2.87e-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: 122.71  E-value: 2.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  192 DGLKGQPGAQGVKGEPGAPGENGTPGQAGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGsagppgfpgapgpkg 271
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG--------------- 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  272 ELGPVGNPGPAGPAGPRGEVGLPGlsgpvgppgnpgTNGLTGAKGATGLPGVAGAPGLPGPRGipgpagaagatgarglv 351
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRGETGPAG------------EQGPAGPAGPDGEAGPAGEDGPAGPAG----------------- 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  352 gepgpAGSKGESGNKGEPGSVGAQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGS 431
Cdd:NF038329  232 -----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQ 306

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 111120329  432 TGPAGIRGPNGDAGRPGEPGLMGPRGLPGSPGNVGPSGKEGP 473
Cdd:NF038329  307 NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVP 348
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 521-752 2.03e-27

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 117.31  E-value: 2.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  521 LAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTTGEVGKPGERGLPGEFGLPGPAGPRGERGTP 600
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  601 GESGAAGPSGPIGSRGPSGAPGPDGNKGEAGAVgAPGSAGASGPGGLPGERGAAGIPGGKGEKGETGLRGDTGNTGRDGA 680
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPA-GPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 111120329  681 RGIPGAVGAPGPAGASGDRGEAGAAGPSGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGEKGTKGP 752
Cdd:NF038329  274 DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 535-766 2.72e-27

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: 116.93  E-value: 2.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  535 GAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTTGEVGKPGERGLPGEFGLPGPAGPRGERGTPGESGAAGPSGPIGS 614
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  615 RGPSGAPGPDGNKGEAGAvgapgsagasgpgglPGERGAAGiPGGKGEKGETGLRGDTGNTGRDGARGIPGAVGAPGPAG 694
Cdd:NF038329  197 RGETGPAGEQGPAGPAGP---------------DGEAGPAG-EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 111120329  695 ASGDRGEAGAAGPSGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGEKGTKGPKGENGIVGPTGSVG 766
Cdd:NF038329  261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 879-1090 1.11e-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: 115.00  E-value: 1.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  879 LGLPGSRGERGLPGIAGALGEPGPlgisgppgargppgavgspgvNGAPGEAGRDGNPGSDGPPGRDGQPGHKGERGYPG 958
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQGP---------------------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  959 SIGPTGAAGAPGPHGSVGPAGKHGNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGD--KGHRGLPGLKGYSGLQG 1036
Cdd:NF038329  172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQG 251

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 111120329 1037 LPGLAGLHGDQGAPGPVGPAGPRGPAGPSGPVGKDGRSGQPGPVGPAGVRGSQG 1090
Cdd:NF038329  252 PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG 305
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 678-949 2.27e-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: 2.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  678 DGARGIPGAVGAPGPAGASGDRGEAGAAGPSGPAGPRGSPGERGEVGPAGPngfagpagaagqpgaKGEKGTKGPKGENG 757
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGP---------------QGEAGPQGPAGKDG 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  758 IVGPTGSVGAAGPSGPNGPPGPVGSRGDGGPPGMTGFPGAAGRTGPPGPSGiagppgppgaagkEGIRGPRGDQGPVGRT 837
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------------DGQQGPDGDPGPTGED 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  838 GETGASGPPGFVGEKGPSGEPGTAGAPGTAGPQGLLGAPgilGLPGSRGERGLPGIAGALGEPgplgisgppgargppga 917
Cdd:NF038329  248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPA---GKDGQNGKDGLPGKDGKDGQN----------------- 307

                         250       260       270
                  ....*....|....*....|....*....|..
gi 111120329  918 vGSPGVNGAPGEAGRDGNPGSDGPPGRDGQPG 949
Cdd:NF038329  308 -GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 28-288 1.28e-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: 1.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329   28 GSVRKGPTGDRGPRGQRGPAGPRGRDGVDGPMGPPGPPGSPGppgspappgltgnfaaqysDKGVSSGPGPMGLMGPRGP 107
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG-------------------ERGEKGPAGPQGEAGPQGP 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  108 PGAVGAPGPQGFQGPAGEPGEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRPGERGvvgpqgaRGFPGTPGLPGFKGVKG 187
Cdd:NF038329  176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  188 HSGMDGLKGQPGAQGVKGEPGAPGENGTPGQAGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAP 267
Cdd:NF038329  249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328

                         250       260
                  ....*....|....*....|.
gi 111120329  268 GPKGELGPVGNPGPAGPAGPR 288
Cdd:NF038329  329 GKDGKDGQPGKPAPKTPEVPQ 349
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 744-1008 2.60e-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: 110.77  E-value: 2.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  744 KGEKGTKGPKGENGIVGPTGSVGAAGPSGPNGPPGPVGSRGDGGPPGMTGFPGAAGrtgppgpsgiagppgppgaagKEG 823
Cdd:NF038329  119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG---------------------PAG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  824 IRGPRGDQGPVGRTGETGASGPPGFVGEKGPSGEPGTAGAPGTAGPQGLLGAPGilglPGSRGERGLPGIAGALGEPGPL 903
Cdd:NF038329  178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPD 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  904 GisgppgargPPGAVGSPGVNGAPGEAGRDGNPGSDGPPGRDGQPGHKGERGYPGSIGPTGAAGAPGPHGSVGPAGKHGN 983
Cdd:NF038329  254 G---------PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324

                         250       260
                  ....*....|....*....|....*
gi 111120329  984 RGEPGPAGSVGPVGAVGPRGPSGPQ 1008
Cdd:NF038329  325 DGLPGKDGKDGQPGKPAPKTPEVPQ 349
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 982-1092 8.15e-14

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 75.33  E-value: 8.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  982 GNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGDKGHRGLPGLKGysglqglpglaglhgDQGAPGPVGPAGPRGP 1061
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG---------------PQGEAGPQGPAGKDGE 181

                          90       100       110
                  ....*....|....*....|....*....|.
gi 111120329 1062 AGPSGPVGKDGRSGQPGPVGPAGVRGSQGSQ 1092
Cdd:NF038329  182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPA 212
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
374-623 7.59e-13

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 72.76  E-value: 7.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  374 AQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGSTGPAGIRGPNGDagrPGEPGLM 453
Cdd:COG5164     5 GPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGP---AQNQGGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  454 GPRGLPGSPGNVGPSGKEGPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPGKPGERGHPGLAGARGAPGPDGN 533
Cdd:COG5164    82 TPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  534 NGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTTGEVGKPGERGLPGEFGLPGPAGPRGERGTPGESGAAGPSGPIG 613
Cdd:COG5164   162 GGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIE 241

                         250
                  ....*....|
gi 111120329  614 SRGPSGAPGP 623
Cdd:COG5164   242 RRGPERPEAA 251
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
472-728 2.76e-10

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 64.67  E-value: 2.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  472 GPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPGKPGERGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGE 551
Cdd:COG5164     7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  552 QGPAGPPGFQGLPGPSGTTGEVGKPGERGLPGEFGLPGP-AGPRGERGTPGESGAAGPSGPiGSRGPSGAPGPDGNKGEA 630
Cdd:COG5164    87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGStTPPSGGSTTPPGDGGSTPPGP-GSTGPGGSTTPPGDGGST 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  631 GavgapgsAGASGPGGLPGERGAAGIPGGKGEKGETGLRGDTGNTGRDGARGIPGAVGA-PGPAGASGDRGEAGAAGPSG 709
Cdd:COG5164   166 T-------PPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKgNPPDDRGGKTGPKDQRPKTN 238

                         250
                  ....*....|....*....
gi 111120329  710 PAGPRGSPGERGEVGPAGP 728
Cdd:COG5164   239 PIERRGPERPEAAALPAEL 257
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
198-484 2.98e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 58.12  E-value: 2.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  198 PGAQGVKGEPGAPGENGTPGQAGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPgpkgelGPVG 277
Cdd:COG5164     3 LYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGAT------GPAQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  278 NPGPAGPAGPRGEVGLPGLSGPVGPPGNPGTNGLTGAKGATGLPGVAGAPGLPGPRGIPGPAGAAGATGARGLVGEPGPA 357
Cdd:COG5164    77 NQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGST 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  358 GSKGESGNKGEPGSVGAQGPPGPSGEegkrGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGSTG---- 433
Cdd:COG5164   157 TPPGDGGSTTPPGPGGSTTPPDDGGS----TTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTgpkd 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 111120329  434 PAGIRGPNGDAGRPGEPGLMGPRGLPG--------SPGNVGPSGKEGPVGLPGIDGRPG 484
Cdd:COG5164   233 QRPKTNPIERRGPERPEAAALPAELTAleaenraaNPEPATKTIPETTTVKDLATVLGK 291
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
233-496 1.10e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 56.19  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  233 APGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGELGPVGNPGPAGPAGPRGEVGLPGLSGPVGPPGNPGTNGLT 312
Cdd:COG5164     5 GPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  313 GAKGATGLPGVAGAPGLPGPRGIPGPAGAAGATGARGLVGEPGPAgskgeSGNKGEPGSVGAQGPPGP--SGEEGKRGSP 390
Cdd:COG5164    85 QNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPP-----SGGSTTPPGDGGSTPPGPgsTGPGGSTTPP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  391 GEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVmGPPGNRGSTGPAGIRGPNGDAGRPGEPGLMGPRGlpGSPGNVGPSGK 470
Cdd:COG5164   160 GDGGSTTPPGPGGSTTPPDDGGSTTPPNKGET-GTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGPKDQRPK 236

                         250       260
                  ....*....|....*....|....*.
gi 111120329  471 EGPVGLPGIDGRPGPIGPAGPRGEAG 496
Cdd:COG5164   237 TNPIERRGPERPEAAALPAELTALEA 262
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 103-159 1.91e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.03  E-value: 1.91e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   103 GPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRP 159
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 97-153 3.35e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.26  E-value: 3.35e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329    97 GPMGLMGPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPAGPRGPAGSPGKAGEDGHP 153
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 373-429 4.07e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.26  E-value: 4.07e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   373 GAQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNR 429
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 478-534 4.90e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.87  E-value: 4.90e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   478 GIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPGKPGERGHPGLAGARGAPGPDGNN 534
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 502-558 6.45e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.49  E-value: 6.45e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   502 GPKGPSGDPGKPGERGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPP 558
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 109-163 7.40e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.49  E-value: 7.40e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 111120329   109 GAVGAPGPQGFQGPAGEPGEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRPGERG 163
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 362-557 8.06e-07

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 53.05  E-value: 8.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  362 ESGNKGEPGSVGAQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGSTGPAGIRGPN 441
Cdd:PHA03169   53 TSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPA 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  442 GDAGRPGEPGLMGPrGLPGSPGNVGPSGKEGPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPGKPGERGHPgl 521
Cdd:PHA03169  133 SHSPPPSPPSHPGP-HEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPD-- 209

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 111120329  522 agargAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGP 557
Cdd:PHA03169  210 -----EPGEPQSPTPQQAPSPNTQQAVEHEDEPTEP 240
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 352-408 8.25e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.10  E-value: 8.25e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   352 GEPGPAGSKGESGNKGEPGSVGAQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSP 408
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 124-180 9.94e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.10  E-value: 9.94e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   124 GEPGEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLP 180
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 367-421 9.94e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.10  E-value: 9.94e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 111120329   367 GEPGSVGAQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAG 421
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 487-542 1.03e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.10  E-value: 1.03e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 111120329   487 GPAGPRGEAGNIGFPGPKGPSGDPGKPGERGHPGLAGARGAPGPDGNNGAQGPPGP 542
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 484-540 1.06e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.10  E-value: 1.06e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   484 GPIGPAGPRGEAGNIGFPGPKGPSGDPGKPGERGHPGLAGARGAPGPDGNNGAQGPP 540
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 553-608 1.33e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.72  E-value: 1.33e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 111120329   553 GPAGPPGFQGLPGPSGTTGEVGKPGERGLPGEFGLPGPAGPRGERGTPGESGAAGP 608
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 91-147 1.50e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.33  E-value: 1.50e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329    91 GVSSGPGPMGLMGPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPAGPRGPAGSPGKA 147
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 96-149 1.58e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.33  E-value: 1.58e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 111120329    96 PGPMGLMGPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPAGPRGPAGSPGKAGE 149
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 351-543 2.38e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 52.30  E-value: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  351 VGEPGPAGSKGESGNKGEPGSVGAQG-PPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNR 429
Cdd:PRK07764  588 VGPAPGAAGGEGPPAPASSGPPEEAArPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  430 GSTGPAGIRGPNGDAGRPGEPGLMGPRGLPGSPGNVGPSGKEGPVglPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGD 509
Cdd:PRK07764  668 GWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAG--QADDPAAQPPQAAQGASAPSPAADDPVPLPPEP 745

                         170       180       190
                  ....*....|....*....|....*....|....
gi 111120329  510 PGKPGERGHPGLAGARGAPGPDGNNGAQGPPGPQ 543
Cdd:PRK07764  746 DDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPP 779
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 367-558 2.59e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 51.91  E-value: 2.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  367 GEPGSVGAQGPPGPSGEEGKRGSP---GEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGSTGPAGIRGPNGD 443
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAArpaAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  444 AGRPGEPGLMGPRGLPGSPGNVGPSGKEGPVGLPGIDGRPGPIGPAGPRGEagnigfpgPKGPSGDPGKPGERGHPGLAG 523
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQ--------PPQAAQGASAPSPAADDPVPL 741

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 111120329  524 ARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPP 558
Cdd:PRK07764  742 PPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPP 776
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 673-729 3.13e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.56  E-value: 3.13e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   673 GNTGRDGARGIPGAVGAPGPAGASGDRGEAGAAGPSGPAGPRGSPGERGEVGPAGPN 729
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 523-579 4.33e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.18  E-value: 4.33e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   523 GARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTTGEVGKPGER 579
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 133-187 4.68e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.18  E-value: 4.68e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 111120329   133 GPAGPRGPAGSPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGVKG 187
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 112-167 5.22e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.79  E-value: 5.22e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 111120329   112 GAPGPQGFQGPAGEPGEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRPGERGVVGP 167
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 385-441 6.16e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.79  E-value: 6.16e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   385 GKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGSTGPAGIRGPN 441
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 115-171 6.22e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.79  E-value: 6.22e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   115 GPQGFQGPAGEPGEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRPGERGVVGPQGAR 171
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
103-408 8.19e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 50.03  E-value: 8.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  103 GPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGF 182
Cdd:COG5164     7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  183 KGVKGHSGMDGLKGQPGAQGVKGEPGAPGENGTPGQAGARGlPGERGRVGAPGPAGARGSDGsvGPVGPAGPIGSAGPPG 262
Cdd:COG5164    87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-PPSGGSTTPPGDGGSTPPGP--GSTGPGGSTTPPGDGG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  263 FPGAPGPKGELGPVGNPGPAGPAGPrGEVGLPGLSGPVGPPGNPGTNGLTGAKGATGLPGVAGAPGLPGPRGIPGPAGAA 342
Cdd:COG5164   164 STTPPGPGGSTTPPDDGGSTTPPNK-GETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIER 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 111120329  343 GATGARGLVGEPGPAGSKGESGNKGEPGSVGAQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSP 408
Cdd:COG5164   243 RGPERPEAAALPAELTALEAENRAANPEPATKTIPETTTVKDLATVLGKKGSDLVTNLMKKGKGTN 308
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 127-181 9.49e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.41  E-value: 9.49e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 111120329   127 GEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPG 181
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 130-184 1.06e-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: 44.02  E-value: 1.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 111120329   130 GQTGPAGPRGPAGSPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKG 184
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 400-456 1.12e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.02  E-value: 1.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   400 GPPGLRGSPGSRGLPGADGRAGVMGPPGNRGSTGPAGIRGPNGDAGRPGEPGLMGPR 456
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 95-290 1.19e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.98  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329   95 GPGPMGLMGPRGPPGAVGAPGPQGFQgPAGEPGEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRPGERGVVGPQGARGFP 174
Cdd:PRK07764  589 GPAPGAAGGEGPPAPASSGPPEEAAR-PAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  175 GTPGLPGFKGVKGHSGMDGLKGQPGAQGVKGEPGAPGENGTPGQAGARGLPGERGRVGAPGPAGARGSDGSVGPvgPAGP 254
Cdd:PRK07764  668 GWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPL--PPEP 745

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 111120329  255 IGSAGPPGFPGAPGPKGELGPVGNPGPAGPAGPRGE 290
Cdd:PRK07764  746 DDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSE 781
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 370-728 1.19e-05

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 50.01  E-value: 1.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329   370 GSVGAQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPgadgRAGVMGPPGNrGSTGPAGIRGPNGDAGRPGE 449
Cdd:pfam09606   65 GGQGNGGMGGGQQGMPDPINALQNLAGQGTRPQMMGPMGPGPGGP----MGQQMGGPGT-ASNLLASLGRPQMPMGGAGF 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329   450 PGLMGPRGLPGSPGNVGPsgkegpvGLPGIDGRPGPIGPAGPrGEAGNIGFPGPKGPSGDPGKPGERGHPGLAGARGAPG 529
Cdd:pfam09606  140 PSQMSRVGRMQPGGQAGG-------MMQPSSGQPGSGTPNQM-GPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPG 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329   530 P--DGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTTGEVGKPGERGLPGEFGLPGPAGprgeRGTPGESGAAG 607
Cdd:pfam09606  212 PadAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAG----QGGPGQPMGPP 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329   608 PSGPiGSRGPSGAPGPDGNKGEAGAVGAPGSAGASGPGGLPGERGAAGIPGGKGEKGETGLRGDTGNTGRDGARGIPGAV 687
Cdd:pfam09606  288 GQQP-GAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQ 366

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 111120329   688 GAPGPAGASGDRGEAGAAGPSGPAGPRGSPGERGEVGPAGP 728
Cdd:pfam09606  367 RGQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGP 407
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 517-573 1.20e-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: 44.02  E-value: 1.20e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   517 GHPGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTTGEV 573
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 577-633 1.34e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 1.34e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   577 GERGLPGEFGLPGPAGPRGERGTPGESGAAGPSGPIGSRGPSGAPGPDGNKGEAGAV 633
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 526-582 1.48e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 1.48e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   526 GAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTTGEVGKPGERGLP 582
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 457-513 1.54e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 1.54e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   457 GLPGSPGNVGPSGKEGPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPGKP 513
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 960-1133 1.60e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.60  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  960 IGPTGAAGAPGPHGSVGPAGKHGNRGEP----GPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGDKGHRGLPGLKGYSGLQ 1035
Cdd:PRK07764  588 VGPAPGAAGGEGPPAPASSGPPEEAARPaapaAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329 1036 GLPGLAGLHGDQGAPGPVGPAGPRGPAGPSGPVGKDGRSGQPGPVGPAGVRGSQGSQGPAGPPGPPGPPGPPGVSGGGYD 1115
Cdd:PRK07764  668 GWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD 747

                         170
                  ....*....|....*...
gi 111120329 1116 FGFEGDFYRADQPRSQPS 1133
Cdd:PRK07764  748 PPDPAGAPAQPPPPPAPA 765
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 940-996 1.80e-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: 43.64  E-value: 1.80e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   940 GPPGRDGQPGHKGERGYPGSIGPTGAAGAPGPHGSVGPAGKHGNRGEPGPAGSVGPV 996
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 199-254 1.80e-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: 43.64  E-value: 1.80e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 111120329   199 GAQGVKGEPGAPGENGTPGQAGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGP 254
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 396-597 1.83e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.21  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  396 AGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGSTGPAGIRGPNGDAGrPGEPGLMGPRGLPGSPGNVGPSGKEGPVG 475
Cdd:PRK07764  586 AVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAA-PAEASAAPAPGVAAPEHHPKHVAVPDASD 664

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  476 lpGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPGKPGERGHPglAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPA 555
Cdd:PRK07764  665 --GGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPA--ATPPAGQADDPAAQPPQAAQGASAPSPAADDPVP 740

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 111120329  556 GPPGFQGLPGPSGTTGEVGKPGERGLPGEFGLPGPAGPRGER 597
Cdd:PRK07764  741 LPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 466-520 2.02e-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: 2.02e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 111120329   466 GPSGKEGPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPGKPGERGHPG 520
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 571-625 2.44e-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: 2.44e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 111120329   571 GEVGKPGERGLPGEFGLPGPAGPRGERGTPGESGAAGPSGPIGSRGPSGAPGPDG 625
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 406-462 2.46e-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: 2.46e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   406 GSPGSRGLPGADGRAGVMGPPGNRGSTGPAGIRGPNGDAGRPGEPGLMGPRGLPGSP 462
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
85-336 2.54e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 48.49  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329   85 AQYSDKGVSSGPGPMGLMGPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRPGERGV 164
Cdd:COG5164    16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  165 VGPQGARGFPGTPGLPGFKGVKGHSGMDGLKGQP--GAQGVKGEPGA-PGENGTPGQAGARGLPGERGRVGAPGPAGARG 241
Cdd:COG5164    96 TGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGGStPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  242 SDGSVGPVGPAGPigsagppgfpgapgpkGELGPVGNPGPAGPAGPRGEVGLPGlsGPVGPPGNPGTNGLTGAKGATGLP 321
Cdd:COG5164   176 PPDDGGSTTPPNK----------------GETGTDIPTGGTPRQGPDGPVKKDD--KNGKGNPPDDRGGKTGPKDQRPKT 237

                         250
                  ....*....|....*
gi 111120329  322 GVAGAPGLPGPRGIP 336
Cdd:COG5164   238 NPIERRGPERPEAAA 252
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 379-435 2.58e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 2.58e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   379 GPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGSTGPA 435
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 538-594 2.74e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 2.74e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   538 GPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTTGEVGKPGERGLPGEFGLPGPAGPR 594
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 445-503 3.44e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 3.44e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 111120329   445 GRPGEPGLMGPRGLPGSPGNVGPSGKEGPvglPGIDGRPGPIGPAGPRGEAGNIGFPGP 503
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGP---PGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 493-719 3.57e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.44  E-value: 3.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  493 GEAGNIGFPGPKGPSGdPGKPGERGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPS-GTTG 571
Cdd:PRK07764  590 PAPGAAGGEGPPAPAS-SGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASdGGDG 668

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  572 EVGKPGERGLPGEFGLPGPAGPRGERGTPGESGAAGPSGPIGSRGPSGAPGPDGNKGEAGAVGAPGSAGASGPGGLPGER 651
Cdd:PRK07764  669 WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDP 748

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 111120329  652 GAAGIPGGKGekgetglrgdtgnTGRDGARGIPGAVGAPGPAGASGDRGEAGAAGPSGPAGPRGSPGE 719
Cdd:PRK07764  749 PDPAGAPAQP-------------PPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEE 803
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 424-478 4.35e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 4.35e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 111120329   424 GPPGNRGSTGPAGIRGPNGDAGRPGEPGLMGPRGLPGSPGNVGPSGKEGPVGLPG 478
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 439-623 5.55e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.67  E-value: 5.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  439 GPNGDAGRPGEPGLMGPRGLPGSPGNvgPSGKEGPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPGKPGERGH 518
Cdd:PRK07764  589 GPAPGAAGGEGPPAPASSGPPEEAAR--PAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGG 666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  519 PGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQG-PAGPPGFQGLPGPSGTTGEVGKPGERGLPGEFGLPGPAGPRGER 597
Cdd:PRK07764  667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPaPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD 746

                         170       180
                  ....*....|....*....|....*.
gi 111120329  598 GTPGESGAAGPSGPIGSRGPSGAPGP 623
Cdd:PRK07764  747 DPPDPAGAPAQPPPPPAPAPAAAPAA 772
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 196-252 5.73e-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: 5.73e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   196 GQPGAQGVKGEPGAPGENGTPGQAGARGLPGERGRVGAPGPAGARGSDGSVGPVGPA 252
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 181-237 6.07e-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: 6.07e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   181 GFKGVKGHSGMDGLKGQPGAQGVKGEPGAPGENGTPGQAGARGLPGERGRVGAPGPA 237
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 934-990 6.32e-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: 6.32e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   934 GNPGSDGPPGRDGQPGHKGERGYPGSIGPTGAAGAPGPHGSVGPAGKHGNRGEPGPA 990
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 196-606 6.92e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.29  E-value: 6.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  196 GQPGAQGVKGEPGAPGENGTPGQAGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGELGP 275
Cdd:PRK07764  397 AAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEP 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  276 VGNPGPAGPAGPRGEVGLPGLSGPVGPPGNPGTNGL-----------TGAKGATgLPGVAGAPGLPGPRGiPGPAGAAGA 344
Cdd:PRK07764  477 TAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLrerwpeilaavPKRSRKT-WAILLPEATVLGVRG-DTLVLGFST 554

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  345 TGARGLVGEPGPAGSKGESGNKGEPGSVGAQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMG 424
Cdd:PRK07764  555 GGLARRFASPGNAEVLVTALAEELGGDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAA 634

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  425 PPGNRGSTGPAGIRGPNGDAGRPGEPGlmGPRGLPGSPGNVGPSGKEGPVGLPGIDGRPGPIGPAGPRGEAGnigfpGPK 504
Cdd:PRK07764  635 APAEASAAPAPGVAAPEHHPKHVAVPD--ASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPA-----PAA 707

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  505 GPSGDPGKPGERGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTTGEVGKPGERglPGE 584
Cdd:PRK07764  708 TPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE--EEM 785

                         410       420
                  ....*....|....*....|..
gi 111120329  585 FGLPGPAGPRGERGTPGESGAA 606
Cdd:PRK07764  786 AEDDAPSMDDEDRRDAEEVAME 807
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 565-621 7.32e-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: 7.32e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   565 GPSGTTGEVGKPGERGLPGEFGLPGPAGPRGERGTPGESGAAGPSGPIGSRGPSGAP 621
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 233-622 7.76e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.47  E-value: 7.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  233 APGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGELGPVGNPGPAGPAGPRGEVGLPGLSGPVGPPGNPGTNGLT 312
Cdd:PHA03307   27 TPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  313 GAKGATGLPGVAGA--PGLPGPRGIPGpagaagatgarglVGEPGPAGSKGESGNKGEPGSVGAQGPPGPSGEEGKRGSP 390
Cdd:PHA03307  107 TPPGPSSPDPPPPTppPASPPPSPAPD-------------LSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  391 ---GEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGSTGPAGIRGPNGDAGRPGEPGLMGPRGLPGS---PGN 464
Cdd:PHA03307  174 lplSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCgwgPEN 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  465 VGPSGKEGPVGLPGIDGRPGPIGPAGPR-GEAGNIGFPGPKGPSGDPGKPGERGHPGLAGARGAPGPDGNNGAQGP---- 539
Cdd:PHA03307  254 ECPLPRPAPITLPTRIWEASGWNGPSSRpGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTssss 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  540 --PGPQGVQGGKGEQGPAGPPGfqglPGPSGTTGEVGKPGERGLPGEFGLPGPAGPRGERGTPGESGAAGPSGPIGSRGP 617
Cdd:PHA03307  334 esSRGAAVSPGPSPSRSPSPSR----PPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPA 409


                  ....*
gi 111120329  618 SGAPG 622
Cdd:PHA03307  410 GRPRP 414
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 841-896 9.93e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 9.93e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 111120329   841 GASGPPGFVGEKGPSGEPGTAGAPGTAGPQGLLGAPGILGLPGSRGERGLPGIAGA 896
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 955-1009 1.26e-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: 40.94  E-value: 1.26e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 111120329   955 GYPGSIGPTGAAGAPGPHGSVGPAGKHGNRGEPGPAGSVGPVGAVGPRGPSGPQG 1009
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 823-877 1.37e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 1.37e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 111120329   823 GIRGPRGDQGPVGRTGETGASGPPGFVGEKGPSGEPGTAGAPGTAGPQGLLGAPG 877
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 322-393 1.52e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 1.52e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 111120329   322 GVAGAPGLPGPRGIPgpagaagatgarglvGEPGPAGSKGESGNKGEPGSVGAQGPPGPSGEEGKRGSPGEA 393
Cdd:pfam01391    1 GPPGPPGPPGPPGPP---------------GPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1034-1092 1.53e-04

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: 46.05  E-value: 1.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 111120329 1034 LQGLPGLAGLHGDQGAPGPVGPAGPRGPAGPSGPVGKDGRSGQPGPVGPAGVRGSQGSQ 1092
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ 173
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 922-978 1.67e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 1.67e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   922 GVNGAPGEAGRDGNPGSDGPPGRDGQPGHKGERGYPGSIGPTGAAGAPGPHGSVGPA 978
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 118-475 1.93e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  118 GFQGPAGEPGEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGVKGHSGMDGLKGQ 197
Cdd:PRK07764  386 GVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQ 465

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  198 PGAQGVKGEPGAPGENGTPGQAGARGLPGERGRVGAPGPAG--------------------------ARGSDGSVGPV-G 250
Cdd:PRK07764  466 PAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGAddaatlrerwpeilaavpkrsrktwaILLPEATVLGVrG 545

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  251 PAGPIGSAGPPGFPGAPGPK--------------GELGPVGNPGPAGPAGPRGEVGLPGLSGPVGPPGNPGTNGLTGAKG 316
Cdd:PRK07764  546 DTLVLGFSTGGLARRFASPGnaevlvtalaeelgGDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPA 625

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  317 ATGLPGVAGAPGLPGPRGIPGPAGAAGAtgarglvgEPGPAGSKGESGNKGEPGSVGAQGPPGPSGeegkrgSPGEAGSA 396
Cdd:PRK07764  626 APAPAGAAAAPAEASAAPAPGVAAPEHH--------PKHVAVPDASDGGDGWPAKAGGAAPAAPPP------APAPAAPA 691

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  397 GPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGSTGPAGIRGPNGDAGRPGEPGL-MGPRGLPGSPGNVGPSGKEGPVG 475
Cdd:PRK07764  692 APAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDpPDPAGAPAQPPPPPAPAPAAAPA 771
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
919-1084 1.98e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.79  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  919 GSPGVNGAPGEAGRDGNPGSDGPPGRDGQPGHKGERGYPGSIGPTGAAGAPGPHGSVGPAGKHGNRGEPGPAGSVGPVGA 998
Cdd:COG5164    16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  999 VGPRGPSGPQGIRGDKGEPGDKGHRGLPGLKG--YSGLQGLPGLAG-LHGDQGAPGPVGPAGPRGPAGPSGPVGKDGRSG 1075
Cdd:COG5164    96 TGGTTPAGDGGATGPPDDGGATGPPDDGGSTTppSGGSTTPPGDGGsTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTT 175


                  ....*....
gi 111120329 1076 QPGPVGPAG 1084
Cdd:COG5164   176 PPDDGGSTT 184
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 961-1017 2.16e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 2.16e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   961 GPTGAAGAPGPHGSVGPAGKHGNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEP 1017
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 668-723 2.25e-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: 2.25e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 111120329   668 LRGDTGNTGRDGARGIPGAVGAPGPAGASGDRGEAGAAGPSGPAGPRGSPGERGEV 723
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
684-1004 2.31e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.41  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  684 PGAVGAPGPAGASGDRGEAGAAGPSGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGEKGTKGPKGENGIVGPTG 763
Cdd:COG5164     6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  764 SVGAAGPSGPNGPPGPVGSRGDGGPPGmtgfpgaagrtgppgpsgiagppgPPgaagkegirgprgdqGPVGRTGETGAS 843
Cdd:COG5164    86 NQGGTRPAGNTGGTTPAGDGGATGPPD------------------------DG---------------GATGPPDDGGST 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  844 GPPGFVGEKGPSGEPGTAGAPGTAGPQGLLGAPGILGLPGSRGERGLPGIAGALGEPGPlGISGPPGARGPPGAVGSPGV 923
Cdd:COG5164   127 TPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTP-PNKGETGTDIPTGGTPRQGP 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  924 NGAPGEAgrDGNPGSDGPPGRDGQPGHKGERGYPGSIGPTGAAGAPGPHGSVGPAGKHGnrgePGPAGSVGPVGAVGPRG 1003
Cdd:COG5164   206 DGPVKKD--DKNGKGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTALEA----ENRAANPEPATKTIPET 279


                  .
gi 111120329 1004 P 1004
Cdd:COG5164   280 T 280
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 110-290 3.00e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  110 AVGAPGPQGFQGPAGEPGEPGQTGPAGPRgPAGSPGkAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGVKGHS 189
Cdd:PRK07764  586 AVVGPAPGAAGGEGPPAPASSGPPEEAAR-PAAPAA-PAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAS 663

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  190 -GMDGLKGQPGAQGVKGEPGAPGENGTPGQAGARGLPGERGRVGAP--GPAGARGSDGSVGPVGPAGPIGSAGPPGFPGA 266
Cdd:PRK07764  664 dGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPpaGQADDPAAQPPQAAQGASAPSPAADDPVPLPP 743

                         170       180
                  ....*....|....*....|....
gi 111120329  267 PGPKGELGPVGNPGPAGPAGPRGE 290
Cdd:PRK07764  744 EPDDPPDPAGAPAQPPPPPAPAPA 767
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 847-902 3.33e-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: 3.33e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 111120329   847 GFVGEKGPSGEPGTAGAPGTAGPQGLLGAPGILGLPGSRGERGLPGIAGALGEPGP 902
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 985-1039 4.43e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 4.43e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 111120329   985 GEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGDKGHRGLPGLKGYSGLQGLPG 1039
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
882-1090 4.87e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 44.25  E-value: 4.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  882 PGSRGERGLPGIAGALGEPGPLGISGPPGARGPPGAVGSPGVNGAPGEAGRDGNPGSDGPPGRDGQPGHKGERGYPGSIG 961
Cdd:COG5164     6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  962 PTGAAGAPGPHGSVGPAGKHGNRGEPGPAGSVGPVGAVGPRGP-----SGPQGIRG----DKGEPGDKGHRGLPGLKGYS 1032
Cdd:COG5164    86 NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPpsggsTTPPGDGGstppGPGSTGPGGSTTPPGDGGST 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329 1033 GLQGLPGLAGLHGDQGAPGPVGPA--GPRGPAGPSGPVGKDGRSGQPGPVGPAGVRGSQG 1090
Cdd:COG5164   166 TPPGPGGSTTPPDDGGSTTPPNKGetGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG 225
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 431-728 5.14e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 5.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  431 STGPAGIRGPNGDAGRPGEPGLMGPRGLPGSPGNVGPSGKEGPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDP 510
Cdd:PHA03307   44 VSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPP 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  511 GKPGERGHPGLAGARGAPGPDGNNGAQGPPGPqGVQGGKGEQGPAGPPG---FQGLPGPSGTTGEVGKPGERGLPGEFGL 587
Cdd:PHA03307  124 ASPPPSPAPDLSEMLRPVGSPGPPPAASPPAA-GASPAAVASDAASSRQaalPLSSPEETARAPSSPPAEPPPSTPPAAA 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  588 PGPAGPRGE-----RGTPGESGAAGPSGPIGSRGPSGAPGPDGNKGEAGAVGAPGSAGASGPGGLPGERGAAGIPGGKGE 662
Cdd:PHA03307  203 SPRPPRRSSpisasASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRP 282

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 111120329  663 KGETGlRGDTGNTGRDGARGIPGAVGAPGPAGASGDRGEAGAAGPSGPAgpRGSPGERGEVGPAGP 728
Cdd:PHA03307  283 GPASS-SSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTS--SSSESSRGAAVSPGP 345
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 190-244 5.18e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 5.18e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 111120329   190 GMDGLKGQPGAQGVKGEPGAPGENGTPGQAGARGLPGERGRVGAPGPAGARGSDG 244
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 832-888 6.12e-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: 6.12e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   832 GPVGRTGETGASGPPGFVGEKGPSGEPGTAGAPGTAGPQGLLGAPGILGLPGSRGER 888
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 899-1083 7.14e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.21  E-value: 7.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  899 EPGPLGISGPPGARGPPGAVGSPGVNGAPGEAGRDGNPGSDGPPGRDGQPGHKGERGYPGSIGPTGAAGAPG-PHGSVGP 977
Cdd:PRK07764  587 VVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAvPDASDGG 666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  978 AGKHGNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGDKGHRGLPGLKGYSGLQGLPGLAGLH-GDQGAPGPVGPA 1056
Cdd:PRK07764  667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPaADDPVPLPPEPD 746

                         170       180
                  ....*....|....*....|....*..
gi 111120329 1057 GPRGPAGPSGPVGKDGRSGQPGPVGPA 1083
Cdd:PRK07764  747 DPPDPAGAPAQPPPPPAPAPAAAPAAA 773
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 208-258 7.46e-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: 7.46e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 111120329   208 GAPGENGTPGQAGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSA 258
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 919-969 9.82e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 9.82e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 111120329   919 GSPGVNGAPGEAGRDGNPGSDGPPGRDGQPGHKGERGYPGSIGPTGAAGAP 969
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 352-507 9.89e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.42  E-value: 9.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  352 GEPGPAGSKGESGNKGEPGSVGAQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGA--DGRAGVMGPPGNR 429
Cdd:PHA03169  103 PTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLqpSHEDSPEEPEPPT 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 111120329  430 GSTGPAGIRGPNGDAGRPGEPGLMGPRGlPGSPGNVGPSGKEGPVGLPGIDGRPGPIGPagprgEAGNIGFPGPKGPS 507
Cdd:PHA03169  183 SEPEPDSPGPPQSETPTSSPPPQSPPDE-PGEPQSPTPQQAPSPNTQQAVEHEDEPTEP-----EREGPPFPGHRSHS 254
PHA03169 PHA03169
hypothetical protein; Provisional
 424-622 1.14e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.04  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  424 GPPGNRGSTGPAGIRGPNGDAGRPGEPGLMGPRGLPGSPGNVGPSGKEGPVGLPGIDGRPGPIGPAGPrgeagnigfpgp 503
Cdd:PHA03169   82 GEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEP------------ 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  504 kGPSGDPGKPGERGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTTGEVGKPGERGLPG 583
Cdd:PHA03169  150 -APPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQ 228

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 111120329  584 EFGLPGPAGPRGERGTPGESGAAGPSGPIGSRGPSGAPG 622
Cdd:PHA03169  229 QAVEHEDEPTEPEREGPPFPGHRSHSYTVVGWKPSTRPG 267
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 136-190 1.23e-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: 1.23e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 111120329   136 GPRGPAGSPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGVKGHSG 190
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 967-1021 1.28e-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: 1.28e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 111120329   967 GAPGPHGSVGPAGKHGNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGDKG 1021
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 476-876 1.31e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  476 LPGIDGRPGPIGPAGPRGEAGnIGFPGPKGPSGDPGKPGERGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPA 555
Cdd:PRK07764  364 LPSASDDERGLLARLERLERR-LGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPP 442

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  556 GPPGFQGLPGPSGTTGEVGKPGERGLPGEFGLPGPAGPRGERGTPGESGA--AGPSGPIGSRGPSGAPGPDG-------- 625
Cdd:PRK07764  443 SPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAapAAPAAPAAPAGADDAATLRErwpeilaa 522

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  626 ----NKGEAGAVGAPGSAGASGPGGL------PGERGAAGIPGGKGEKGETgLRGDTGNTGRDGAR--GIPGAVGAPGPA 693
Cdd:PRK07764  523 vpkrSRKTWAILLPEATVLGVRGDTLvlgfstGGLARRFASPGNAEVLVTA-LAEELGGDWQVEAVvgPAPGAAGGEGPP 601

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  694 GASGDRGEAGAAGPSGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGEKGTKGPKGENGIVGPTGSVGAAGPSGP 773
Cdd:PRK07764  602 APASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAP 681

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  774 NGPPGPVGSRGDGGPPGMTGFPGAAGRTGPPGPSGIAGPPgppgaagkegiRGPRGDQGPVGRTGETGASGPPGFVGEKG 853
Cdd:PRK07764  682 PPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQP-----------PQAAQGASAPSPAADDPVPLPPEPDDPPD 750

                         410       420
                  ....*....|....*....|...
gi 111120329  854 PSGEPGTAGAPGTAGPQGLLGAP 876
Cdd:PRK07764  751 PAGAPAQPPPPPAPAPAAAPAAA 773
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 970-1026 1.59e-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: 1.59e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   970 GPHGSVGPAGKHGNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGDKGHRGLP 1026
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 946-1002 2.18e-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: 2.18e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 111120329   946 GQPGHKGERGYPGSIGPTGAAGAPGPHGSVGPAGKHGNRGEPGPAGSVGPVGAVGPR 1002
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 973-1027 2.99e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 2.99e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 111120329   973 GSVGPAGKHGNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGDKGHRGLPG 1027
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 395-563 3.17e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 41.97  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  395 SAGPAGPPGLRGSPGsrglpGADGRAGVMGPPGNRGSTGPAGIRGPNGDAGRPGEPglmgprglpgspgnvGPSGKEGPv 474
Cdd:PRK14959  374 SGGGASAPSGSAAEG-----PASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATP---------------APSAAPSP- 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  475 GLPGIDGRPGPIGPAGPrgeagnigfpgpkgPSGDPGKPGERGHPGlagargapGPDGNNGAQGPPGPQGVQGGKGEQGP 554
Cdd:PRK14959  433 RVPWDDAPPAPPRSGIP--------------PRPAPRMPEASPVPG--------APDSVASASDAPPTLGDPSDTAEHTP 490


                  ....*....
gi 111120329  555 AGPPGFQGL 563
Cdd:PRK14959  491 SGPRTWDGF 499
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 99-481 3.26e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329   99 MGLMGPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPG 178
Cdd:PRK07764  385 LGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSA 464

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  179 LPG-FKGVKGHSGMDGLKGQPGAQGVKGEPGAPGENGTP-GQAGARGL-------------------------------- 224
Cdd:PRK07764  465 QPApAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPaGADDAATLrerwpeilaavpkrsrktwaillpeatvlgvr 544

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  225 ----------PGERGRVGAPGPAG------ARGSDGSVGP---VGPAGPIGSAGPPGFPGAPGPKGELG-PVGNPGPAGP 284
Cdd:PRK07764  545 gdtlvlgfstGGLARRFASPGNAEvlvtalAEELGGDWQVeavVGPAPGAAGGEGPPAPASSGPPEEAArPAAPAAPAAP 624

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  285 AGPRGEvglpglsgpvgppgnpgtnglTGAKGATGLPGVAGAPGLPGPRGIPGPAGAAGATGARGLVGEPGPAGSKGESG 364
Cdd:PRK07764  625 AAPAPA---------------------GAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPP 683

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  365 NKGEPGSVGAQGPPGPSGEEGKRGSPGEAGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGSTGPAGIRGPNGDA 444
Cdd:PRK07764  684 APAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPA 763

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 111120329  445 GRPGEPGLMGPRGLPGSPGNVGPSGKEGPVGLPGIDG 481
Cdd:PRK07764  764 PAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRD 800
PHA03247 PHA03247
large tegument protein UL36; Provisional
 320-623 4.17e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 4.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  320 LPGVAGAPGLPGPRGIPGPAGAAGATGARGLVGEPGPAGSKGESGNKGEPGSVGAQGPPGPSGEEGKRGSPGEAGSAGPA 399
Cdd:PHA03247 2559 APPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEP 2638

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  400 GPPGLRGSPGSRGLPGADGRAGVMGPPGNRGSTGPAGIRGPNGDAGRPGEPGLMGPRGLPGSPGNVGPSGKEGPVglPGI 479
Cdd:PHA03247 2639 DPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPH--ALV 2716

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  480 DGRPGPIGPAGPRGE-----AGNIGFPGPKGPSGdPGKPGERGHPGLAGARGAPGPDGNNGAQGPPG-PQGVQGGKGEQG 553
Cdd:PHA03247 2717 SATPLPPGPAAARQAspalpAAPAPPAVPAGPAT-PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRlTRPAVASLSESR 2795

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 111120329  554 PAGPPGFQGLPGPSGTTGEVGKPGERGLPGEFGLP----GPAGPRGERGTPGES----GAAGPSGPIGSRGPSGAPGP 623
Cdd:PHA03247 2796 ESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPptsaQPTAPPPPPGPPPPSlplgGSVAPGGDVRRRPPSRSPAA 2873
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 688-756 4.48e-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: 4.48e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 111120329   688 GAPGPAGASGDRGEAGAAGPSGPAGPRGSPGERGEVGPAGPNgfagpagaagqpGAKGEKGTKGPKGEN 756
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPP------------GPPGPPGAPGAPGPP 57
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 95-293 4.54e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 41.53  E-value: 4.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329    95 GPGPMGLMGPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPAGPRGPAGSPGKAGEDGHPGKPGRPGERGVVGPQGARGfp 174
Cdd:pfam09606  167 GSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQ-- 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329   175 GTPGLPGFKGVKGHSGMDGLKGQPGAQGVKGEPGAPGENGTPGQAGarglPGERGRVGAPGPAGARGSDGSVGPVGPAGP 254
Cdd:pfam09606  245 QQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQ----PGAMPNVMSIGDQNNYQQQQTRQQQQQQGG 320

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 111120329   255 IG-SAGPPGFPGAPGPKGELGPVGNPGPAGPAGPRGEVGL 293
Cdd:pfam09606  321 NHpAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGL 360
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 535-588 4.80e-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: 4.80e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 111120329   535 GAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTTGEVGKPGERGLPGEFGLP 588
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 480-628 5.18e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.11  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  480 DGRPGPIGPAGPRGEAGNiGFPGPKGPSGDPGKPGERGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPG 559
Cdd:PHA03169   78 ESRHGEKEERGQGGPSGS-GSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHN 156

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 111120329  560 FQGLPGPSGTTGEVGKPGERGLPGEFGLP---GPAGPRGERGTPGESGAAGPS--GPIGSRGPSGAPGPDGNKG 628
Cdd:PHA03169  157 PSPNQQPSSFLQPSHEDSPEEPEPPTSEPepdSPGPPQSETPTSSPPPQSPPDepGEPQSPTPQQAPSPNTQQA 230
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 463-632 5.28e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 5.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  463 GNVGPSGKEGPVGLPGIDGRPGPIGPAGPRGEAGNigfPGPKGPSGDPGKPGERGHPGLAGARGAPGPDGNNGAQGPPGP 542
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAP---AAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGG 666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  543 QGVQGGKGEQGPAGPPGFQGLPGPSGTTGEVGKPGERGLPGEFGLPGPAGPRGERGTPGESGAAGPSGPIGSRGPSGAPG 622
Cdd:PRK07764  667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD 746

                         170
                  ....*....|
gi 111120329  623 PDGNKGEAGA 632
Cdd:PRK07764  747 DPPDPAGAPA 756
PHA03169 PHA03169
hypothetical protein; Provisional
 880-1024 5.94e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.72  E-value: 5.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  880 GLPGSRGERGLPGIAGALGEPGPLGISGPPGARGPPGAVGSPGVNGAPGEAGRDGNPGSDGPPGRDGQPGHKGERGYpgs 959
Cdd:PHA03169   90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSF--- 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 111120329  960 IGPTGAAGAPGPHGSVGPAGKHGNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGDKGHRG 1024
Cdd:PHA03169  167 LQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAV 231
PHA03247 PHA03247
large tegument protein UL36; Provisional
 103-519 5.94e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 5.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  103 GPRGPPGAVGAPGPQGFQGPAGEPGEPGQTgPAGPRGPAGSPGKAGEDGHPGKPGRPGE----RGVVGPQGARGFPGTPG 178
Cdd:PHA03247 2603 DDRGDPRGPAPPSPLPPDTHAPDPPPPSPS-PAANEPDPHPPPTVPPPERPRDDPAPGRvsrpRRARRLGRAAQASSPPQ 2681

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  179 LPGFKGVKGHSGMDGLKGQPGAQGVKGEPG----APGENGTPGQAGARGLPGERGRVGAPGPAGArgsdgsvGPVGPAGP 254
Cdd:PHA03247 2682 RPRRRAARPTVGSLTSLADPPPPPPTPEPAphalVSATPLPPGPAAARQASPALPAAPAPPAVPA-------GPATPGGP 2754

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  255 IGSAGPPGFPGAPGPKGELGPVGNPGPAGPAgPRGEVGLPGLSGPVGPPGNPGTNGLTGAKGATGLPGVAGAPGLPGPRg 334
Cdd:PHA03247 2755 ARPARPPTTAGPPAPAPPAAPAAGPPRRLTR-PAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPT- 2832

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  335 ipgpagaagatgarglvgEPGPAGSKGESGNKGEPGSVGaqGPPGPSGEEGKRGSPGEAgSAGPAGPPGLRGSPGSRGLP 414
Cdd:PHA03247 2833 ------------------SAQPTAPPPPPGPPPPSLPLG--GSVAPGGDVRRRPPSRSP-AAKPAAPARPPVRRLARPAV 2891

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111120329  415 GADGRAGVMGPPGNRGSTGPAGIRGPNGDAGRPGEPGLMGPRGLPGSPG-----NVGPSGKEGPVGLPGiDGRPGPIGPA 489
Cdd:PHA03247 2892 SRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQpplapTTDPAGAGEPSGAVP-QPWLGALVPG 2970

                         410       420       430
                  ....*....|....*....|....*....|
gi 111120329  490 GPRGEAGNIGFPGPKGPSGDPGKPGERGHP 519
Cdd:PHA03247 2971 RVAVPRFRVPQPAPSREAPASSTPPLTGHS 3000
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 976-1030 9.85e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.55  E-value: 9.85e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 111120329   976 GPAGKHGNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGDKGHRGLPGLKG 1030
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
 
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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