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Conserved domains on  [gi|86613790|ref|NP_031763|]
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collagen alpha-2(V) 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 ...
 1263-1496 1.67e-141

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: 432.92  E-value: 1.67e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   1263 DPGIHVTLKSLSSQIETMRSPDGSKKHPARTCDDLKLCHPTKQSGEYWIDPNQGSAEDAIKVYCNMETGETCISANPASV 1342
Cdd:pfam01410    2 DEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKASI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   1343 PRKTWWASKSpdnKPVWYGLDMNRGSQFTYG-DYQSPNTAITQMTFLRLLSKEASQNLTYICRNTVGYMDDQAKNLKKAV 1421
Cdd:pfam01410   82 PRKNWWTKES---KHVWFGEFMNGGSQFSYGvDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86613790   1422 VLKGSNDLEIKGEGNIRFRYTVLQDTCSKRNGNVGKTIFEYRTQNVARLPIIDVGPVDIGNADQEFGLDIGPVCF 1496
Cdd:pfam01410  159 LLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 316-601 2.79e-37

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: 146.97  E-value: 2.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   316 GAKGEAGPTGPMGAMGPLGPRGMPGERGRLGPQGAPGKRGAHGMPGKPGPMGPlgipgsSGFPGNPGMKGEAGPTGARGP 395
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE------AGPQGPAGKDGEAGAKGPAGE 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   396 EGPQGQRGETGPPGPAGSQGLPGAVGTDGTPGAKGPTGSAGtsgppglagppgspgpqgstgpQGIRGQSGDPGVPGFKG 475
Cdd:NF038329  191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------------DGQQGPDGDPGPTGEDG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   476 EAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERgapgnrgfpGSDGLPGPKGAQGERGPVGSSGPKGGQ 555
Cdd:NF038329  249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN---------GKDGLPGKDGKDGQNGKDGLPGKDGKD 319

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 86613790   556 GDPGRPGEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPG 601
Cdd:NF038329  320 GQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTAPHTPKTPQIPG 365
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 478-746 1.69e-33

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: 135.42  E-value: 1.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   478 GPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERGapgnrgfpgsdgLPGPKGAQGERGPVGSSGPKGGQGD 557
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERG------------EKGPAGPQGEAGPQGPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   558 PGRPGEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPGSIGiRGQPGSMGLPGPKGSSGDLGKPGEAGNAGVPG 637
Cdd:NF038329  185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   638 QRGAPGKDGEvgpsgpvgppglAGERGEQGPPGPtgfqglpgppgppgeggkAGDQGVPGEPGAVGPLGPRGERGNPGER 717
Cdd:NF038329  264 DRGEAGPDGP------------DGKDGERGPVGP------------------AGKDGQNGKDGLPGKDGKDGQNGKDGLP 313

                         250       260
                  ....*....|....*....|....*....
gi 86613790   718 GEPGITGLPGEKGMAGGHGPDGPKGNPGP 746
Cdd:NF038329  314 GKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 659-914 1.65e-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: 126.56  E-value: 1.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   659 LAGERGEQGPPGPtgfqglpgppgppgeggkagdqgvPGEPGAVGPLGPRGERGNPGERGEPGITGLPGEKGMAGGHGPD 738
Cdd:NF038329  115 GDGEKGEPGPAGP------------------------AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   739 GPKGNPGPTGTIGDTGPPGLQGMPGERGIAGTPGPKGDRGGIGEKGAEGTAGNDGArglpgplGPPGPAGPTGEKGEPGP 818
Cdd:NF038329  171 GPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP-------AGPAGDGQQGPDGDPGP 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   819 RGLVGPPGSRGNPGSRGENGPTGAVGFAGPQGPDGQPGVKGEPGEPGQKGDAGSPGPQglagspGPHGPHGVPGLKGGRG 898
Cdd:NF038329  244 TGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD------GKDGQNGKDGLPGKDG 317

                         250
                  ....*....|....*.
gi 86613790   899 TQGPPGATGFPGSAGR 914
Cdd:NF038329  318 KDGQPGKDGLPGKDGK 333
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 832-1109 2.17e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 117.31  E-value: 2.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   832 GSRGENGPTGAVGFAGPQGPDGQPGVKGEPGEPGQKGDAGSPGPQGLAGSPGPHGPHGVPGLKGGRGTQGPPGATGFPGS 911
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   912 AGRVGPPGPAGAPGPAGPAGEPGKEGPPGLRGDPGSHGRvgdrgpagppgspGDKGDPGEDGQPgpdgppgpagttGQRG 991
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQ-------------GPDGDPGPTGED------------GPQG 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   992 IVGMPGQRGERGMPGLPGPAGTPGKVGPTgatgdkgppgpvgppgsngpvgepGPEGPAGNDGTPGRDGAVGERGDRGDP 1071
Cdd:NF038329  252 PDGPAGKDGPRGDRGEAGPDGPDGKDGER------------------------GPVGPAGKDGQNGKDGLPGKDGKDGQN 307

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 86613790  1072 GPAGLPGSQGAPGTPGPVGAPGDAGQRGEPGSRGPVGP 1109
Cdd:NF038329  308 GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
VWC smart00214
von Willebrand factor (vWF) type C domain;
40-95 1.72e-22

von Willebrand factor (vWF) type C domain;


:

Pssm-ID: 214564  Cd Length: 59  Bit Score: 91.81  E-value: 1.72e-22
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 86613790      40 CTQHGQMYLNRDIWKPSPCQICVCDNGA-ILCDKIECPEVLNCANPIT--PTGECCPVC 95
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGTtVLCDPVECPPPPDCPNPERvkPPGECCPRC 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 280-336 7.99e-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: 7.99e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    280 GSPGARGFPGAPGLPGLKGHRGHKGLEGPKGEIGAPGAKGEAGPTGPMGAMGPLGPR 336
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 107-326 1.17e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 46.44  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   107 RGRKGQKGEPGLvpvvTGIRGRPGPAGPPGSQGPRGDRGPKGRPGPRGPQGIDGEPGVPGQPGAPGPPGHPSHPGPDGMS 186
Cdd:NF038329  131 AGEQGPRGDRGE----TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQ 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   187 RPfsAQMAGLDEKSGLGSQVGLMP-------GSVGPVGPRGPQGLQGQQGGVGPAGPPGEPGEPGPMGPIGSRGPEGPPG 259
Cdd:NF038329  207 GP--AGPAGPDGEAGPAGEDGPAGpagdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG 284

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790   260 KPGEDGEPGRNGNTGEVGFSGSPGARGFPGAPGLPGLKGHRGHKGLEGPKGEIGAPGAKGEAGPTGP 326
Cdd:NF038329  285 PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKP 351
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1093-1144 4.94e-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: 4.94e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 86613790   1093 GDAGQRGEPGSRGPVGPPGRAGKRGLPGPQGPRGDKGDNGDRGDRGQKGHRG 1144
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1263-1496 1.67e-141

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: 432.92  E-value: 1.67e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   1263 DPGIHVTLKSLSSQIETMRSPDGSKKHPARTCDDLKLCHPTKQSGEYWIDPNQGSAEDAIKVYCNMETGETCISANPASV 1342
Cdd:pfam01410    2 DEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKASI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   1343 PRKTWWASKSpdnKPVWYGLDMNRGSQFTYG-DYQSPNTAITQMTFLRLLSKEASQNLTYICRNTVGYMDDQAKNLKKAV 1421
Cdd:pfam01410   82 PRKNWWTKES---KHVWFGEFMNGGSQFSYGvDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86613790   1422 VLKGSNDLEIKGEGNIRFRYTVLQDTCSKRNGNVGKTIFEYRTQNVARLPIIDVGPVDIGNADQEFGLDIGPVCF 1496
Cdd:pfam01410  159 LLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1263-1497 1.07e-134

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: 414.56  E-value: 1.07e-134
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    1263 DPGIHVTLKSLSSQIETMRSPDGSKKHPARTCDDLKLCHPTKQSGEYWIDPNQGSAEDAIKVYCNMETGETCISANPASV 1342
Cdd:smart00038    1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETGETCVSPSPSSI 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    1343 PRKTWWASKSpdnKPVWYGLDMNRGSQFTYGDYQSPNTAITQMTFLRLLSKEASQNLTYICRNTVGYMDDQAKNLKKAVV 1422
Cdd:smart00038   81 PRKTWYSGKS---KHVWFGETMNGGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALR 157

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86613790    1423 LKGSNDLEIKGEGNIRFRYTVLQDTCSKRNGNVGKTIFEYRTQNVARLPIIDVGPVDIGNADQEFGLDIGPVCFM 1497
Cdd:smart00038  158 LRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 316-601 2.79e-37

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: 146.97  E-value: 2.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   316 GAKGEAGPTGPMGAMGPLGPRGMPGERGRLGPQGAPGKRGAHGMPGKPGPMGPlgipgsSGFPGNPGMKGEAGPTGARGP 395
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE------AGPQGPAGKDGEAGAKGPAGE 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   396 EGPQGQRGETGPPGPAGSQGLPGAVGTDGTPGAKGPTGSAGtsgppglagppgspgpqgstgpQGIRGQSGDPGVPGFKG 475
Cdd:NF038329  191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------------DGQQGPDGDPGPTGEDG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   476 EAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERgapgnrgfpGSDGLPGPKGAQGERGPVGSSGPKGGQ 555
Cdd:NF038329  249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN---------GKDGLPGKDGKDGQNGKDGLPGKDGKD 319

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 86613790   556 GDPGRPGEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPG 601
Cdd:NF038329  320 GQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTAPHTPKTPQIPG 365
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 382-616 1.17e-36

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 145.05  E-value: 1.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   382 GMKGEAGPTGARGPEGPQGQRGETGPPGPAGSQGLPGAVGTDGTPGAKGPTGSAGtsgppglagppgspgpqgSTGPQGI 461
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG------------------PQGPAGK 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   462 RGQSGDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPP-----GPMGERGAPGNRGFPGSDGLPGP 536
Cdd:NF038329  179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGK 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   537 KGAQGERGPVGSSGPKGGQGDPGRPGEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPGSIGIRGQPGSMGLPG 616
Cdd:NF038329  259 DGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 400-642 3.25e-35

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: 140.81  E-value: 3.25e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   400 GQRGETGPPGPAGSQGLPGAVGTDGTPGAKGPTGsagtsgppglagppgspgpqgstgPQGIRGQSGDPGVPGFKGEAGP 479
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAG------------------------PPGPQGERGEKGPAGPQGEAGP 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   480 KGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERGAPGNRGFPGSDGLPGP-----KGAQGERGPVGSSGPKGG 554
Cdd:NF038329  173 QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGP 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   555 QGDPGRPGEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPGSIGIRGQPGSMGLPGPKGSSGDLGKPGEAGNAG 634
Cdd:NF038329  253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332


                  ....*...
gi 86613790   635 VPGQRGAP 642
Cdd:NF038329  333 KDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 478-746 1.69e-33

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: 135.42  E-value: 1.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   478 GPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERGapgnrgfpgsdgLPGPKGAQGERGPVGSSGPKGGQGD 557
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERG------------EKGPAGPQGEAGPQGPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   558 PGRPGEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPGSIGiRGQPGSMGLPGPKGSSGDLGKPGEAGNAGVPG 637
Cdd:NF038329  185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   638 QRGAPGKDGEvgpsgpvgppglAGERGEQGPPGPtgfqglpgppgppgeggkAGDQGVPGEPGAVGPLGPRGERGNPGER 717
Cdd:NF038329  264 DRGEAGPDGP------------DGKDGERGPVGP------------------AGKDGQNGKDGLPGKDGKDGQNGKDGLP 313

                         250       260
                  ....*....|....*....|....*....
gi 86613790   718 GEPGITGLPGEKGMAGGHGPDGPKGNPGP 746
Cdd:NF038329  314 GKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 463-671 2.80e-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: 131.95  E-value: 2.80e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   463 GQSGDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERGAPGNRGFPGSDGLPGPKGAQGE 542
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   543 RGPVGSSGPKGGQGDPGRPGEPGLPGARGLTGNPGV--QGPEGKLGPLGAPGEDGRPGPPGSIGIRGQPGSMGLPGPKGS 620
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 86613790   621 SGDLGKPGEAGNAGVPGQRGAPGKDGEvgpSGPVGPPGLAGERGEQGPPGP 671
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKDGK---DGQNGKDGLPGKDGKDGQPGK 324
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 659-914 1.65e-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: 126.56  E-value: 1.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   659 LAGERGEQGPPGPtgfqglpgppgppgeggkagdqgvPGEPGAVGPLGPRGERGNPGERGEPGITGLPGEKGMAGGHGPD 738
Cdd:NF038329  115 GDGEKGEPGPAGP------------------------AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   739 GPKGNPGPTGTIGDTGPPGLQGMPGERGIAGTPGPKGDRGGIGEKGAEGTAGNDGArglpgplGPPGPAGPTGEKGEPGP 818
Cdd:NF038329  171 GPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP-------AGPAGDGQQGPDGDPGP 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   819 RGLVGPPGSRGNPGSRGENGPTGAVGFAGPQGPDGQPGVKGEPGEPGQKGDAGSPGPQglagspGPHGPHGVPGLKGGRG 898
Cdd:NF038329  244 TGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD------GKDGQNGKDGLPGKDG 317

                         250
                  ....*....|....*.
gi 86613790   899 TQGPPGATGFPGSAGR 914
Cdd:NF038329  318 KDGQPGKDGLPGKDGK 333
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 265-503 4.21e-28

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 119.62  E-value: 4.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   265 GEPGRNGNTGEVGFSGSPGARGFPGAPGLPGLKGHRGHKGLEGPKGEigaPGAKGEAGPTGPMGAMGPLGPRGMPGERGR 344
Cdd:NF038329  129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP---AGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   345 LGPQGAPGKRGAHGMPGKPGPMGPLGIP--GSSGFPGNPGMKGEAGPTGARGPEGPQGQRGETGPPGPAGSQGLPGAVGT 422
Cdd:NF038329  206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   423 DGTPGAKGPTGSAgtsgppglagppgspgpqgstGPQGIRGQSGDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRG 502
Cdd:NF038329  286 AGKDGQNGKDGLP---------------------GKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKT 344


                  .
gi 86613790   503 P 503
Cdd:NF038329  345 P 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 645-887 7.19e-28

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 118.85  E-value: 7.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   645 DGEVGPSGPVGPPGLAGERGEQGPPGPTgfqGLPGPPGPPGEGGKAGDQGVPGEPGAVGPLGPRGERGNPGERGEPGITG 724
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGET---GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   725 LPGEKGMAGGHGPDGPKGNPGPTGTIGDTGPPGLQGMPGeRGIAGTPGPKGDRGGIGEKGAEGTAGNDGARglpgplgpp 804
Cdd:NF038329  193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR--------- 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   805 gpaGPTGEKGEPGPRGLVGPPGSRGNPGSRGENGPTGAVGFAGPQGPDGQPGVKGEPGEPGQKGDAGSPGPQGLAGSPGP 884
Cdd:NF038329  263 ---GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339


                  ...
gi 86613790   885 HGP 887
Cdd:NF038329  340 PAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 598-856 8.96e-28

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 118.47  E-value: 8.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   598 GPPGSIGIRGQPGSMGLPGPKGSSGDLGKPGEAGNAGVPGQRGAPGKDGEVGPSGPVGPPGLAGERGEQGPPGPTgfqgl 677
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK----- 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   678 pgppgppgeggkagdqGVPGEPGAVGPLGPRGERGNPGERGEPGITGLPGEKGMAgGHGPDGPKGNPGPTGTIGDTGPPG 757
Cdd:NF038329  192 ----------------GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPA-GDGQQGPDGDPGPTGEDGPQGPDG 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   758 LQGMPGERGIAGTPGPKGDRGGIGEKGAEGTAGNDGARglpgplgppgpagptGEKGEPGPRGLVGPPGSRGNPGSRGEN 837
Cdd:NF038329  255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN---------------GKDGLPGKDGKDGQNGKDGLPGKDGKD 319

                         250
                  ....*....|....*....
gi 86613790   838 GPTGAVGFAGPQGPDGQPG 856
Cdd:NF038329  320 GQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 832-1109 2.17e-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: 2.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   832 GSRGENGPTGAVGFAGPQGPDGQPGVKGEPGEPGQKGDAGSPGPQGLAGSPGPHGPHGVPGLKGGRGTQGPPGATGFPGS 911
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   912 AGRVGPPGPAGAPGPAGPAGEPGKEGPPGLRGDPGSHGRvgdrgpagppgspGDKGDPGEDGQPgpdgppgpagttGQRG 991
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQ-------------GPDGDPGPTGED------------GPQG 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   992 IVGMPGQRGERGMPGLPGPAGTPGKVGPTgatgdkgppgpvgppgsngpvgepGPEGPAGNDGTPGRDGAVGERGDRGDP 1071
Cdd:NF038329  252 PDGPAGKDGPRGDRGEAGPDGPDGKDGER------------------------GPVGPAGKDGQNGKDGLPGKDGKDGQN 307

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 86613790  1072 GPAGLPGSQGAPGTPGPVGAPGDAGQRGEPGSRGPVGP 1109
Cdd:NF038329  308 GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 735-970 5.23e-23

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 103.83  E-value: 5.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   735 HGPDGPKGNPGPTGTIGDTGPPGLQGMPGERGIAGTPGPKGDRGGIGEKGAEGtagndgarglpgplgPPGPAGPTGEKG 814
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG---------------PQGEAGPQGPAG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   815 EPGPRGLVGPPGSRGNPGSRGENGPTGAVGFAGPQGPDGQPGVKGEPGEPG-----QKGDAGSPGPQGLAGSPGPHGPHG 889
Cdd:NF038329  178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGPQGPDGPAG 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   890 VPGLKGGRGTQGPPGATGFPGSAGRVGPPGPAGAPGPAGPAGEPGKEGPPGLRGDPGSHGRVGDRGPAGPPGSPGDKGDP 969
Cdd:NF038329  258 KDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337


                  .
gi 86613790   970 G 970
Cdd:NF038329  338 G 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 865-1144 9.53e-23

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 103.06  E-value: 9.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   865 GQKGDAGSPGPQGLAGSPGPHGPHGVPGLKGGRGTQGPPGATGFPGSAGrvgppgpagapgpagpagepgKEGPPGLRGD 944
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG---------------------PQGEAGPQGP 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   945 PGSHGRVGDrgpagppgspgdKGDPGEDgqpgpdgppgpagttGQRGIVGMPGQRGERGMPGLPGPAGTPGKVGPTGAtg 1024
Cdd:NF038329  176 AGKDGEAGA------------KGPAGEK---------------GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP-- 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  1025 dkgppgpvGPPGSNGPVGEPGPEGPAGNDGTPGRDGAVGERGDRGDPGPAGLPGSQGAPGTPGPVGAPGDAGQRGEPGSR 1104
Cdd:NF038329  227 --------AGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLP 298

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 86613790  1105 GPVGPPGRAGKRGLPGPQGPRGDKGDNGDRGDRGQKGHRG 1144
Cdd:NF038329  299 GKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
VWC smart00214
von Willebrand factor (vWF) type C domain;
40-95 1.72e-22

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 91.81  E-value: 1.72e-22
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 86613790      40 CTQHGQMYLNRDIWKPSPCQICVCDNGA-ILCDKIECPEVLNCANPIT--PTGECCPVC 95
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGTtVLCDPVECPPPPDCPNPERvkPPGECCPRC 59
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 40-95 9.74e-22

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


Pssm-ID: 278520  Cd Length: 57  Bit Score: 89.79  E-value: 9.74e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 86613790     40 CTQHGQMYLNRDIWKPSPCQICVCDNGAILCDKIECPEvLNCANP--ITPTGECCPVC 95
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIICPP-LDCPNPrlEIPPGECCPVC 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 111-433 8.18e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 81.88  E-value: 8.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   111 GQKGEPGLVpvvtgirgrpGPAGPPGSQGPRGDRGPKGRPGPRGPQGIDGEpgvpgqpgapgppghpshpgpdgmsrpfs 190
Cdd:NF038329  117 GEKGEPGPA----------GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE----------------------------- 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   191 aqmagldeksglgsqvglmPGSVGPVGPRGPQglqgqqggvgpagppgepgepgpmgpigsrgpegppgkpgedGEPGRN 270
Cdd:NF038329  158 -------------------RGEKGPAGPQGEA------------------------------------------GPQGPA 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   271 GNTGEVGFSGSPGARGFPGAPGLPGLKGHRGHKGLEGPKGEIGAPGAKGEAGPTGPmGAMGPLGPRGMPGERGRLGPQGA 350
Cdd:NF038329  177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGP 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   351 PGKRGAHGMPGKPGPMGPLGIPGSSGFPGNPGMKGEAGPTGARGPEGPQGQRGETGPPGPAGSQGLPGAVGTDGTPGAKG 430
Cdd:NF038329  256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335


                  ...
gi 86613790   431 PTG 433
Cdd:NF038329  336 QPG 338
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
301-545 3.08e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 61.20  E-value: 3.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  301 GHKGLEGPKGEIGAPGAKGEAGPTGPMGAMGPLGPRGMPGERGRLGPQGAPGKRGAHGMPGKPGPMGPLGIPGSSGFPGN 380
Cdd:COG5164    7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  381 PGMKGEAGPTGARGPEGPQGQRGETGPPGPAGSQGLPGAVG------------TDGTPGAKGPTGSAGTSGPPGLAGPPG 448
Cdd:COG5164   87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTppsggsttppgdGGSTPPGPGSTGPGGSTTPPGDGGSTT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  449 SPGPQGSTGPQGIRGqSGDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPP-GPMGERGAPGNRGF 527
Cdd:COG5164  167 PPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPkDQRPKTNPIERRGP 245

                        250
                 ....*....|....*...
gi 86613790  528 PGSDGLPGPKGAQGERGP 545
Cdd:COG5164  246 ERPEAAALPAELTALEAE 263
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1042-1098 2.13e-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: 2.13e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790   1042 GEPGPEGPAGNDGTPGRDGAVGERGDRGDPGPAGLPGSQGAPGTPGPVGAPGDAGQR 1098
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 511-567 3.28e-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: 48.64  E-value: 3.28e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    511 GPPGPMGERGAPGNRGFPGSDGLPGPKGAQGERGPVGSSGPKGGQGDPGRPGEPGLP 567
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 814-870 5.79e-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: 5.79e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    814 GEPGPRGLVGPPGSRGNPGSRGENGPTGAVGFAGPQGPDGQPGVKGEPGEPGQKGDA 870
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
609-873 2.94e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 51.57  E-value: 2.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  609 PGSMGLPGPKGSSGDLGKPGEAGNAGVPGQRGAPGKDGEVGPSGPVGPPGLAGERGEQGPPGPTGFQGLPGPPGPPGEGG 688
Cdd:COG5164    6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  689 KAGDQGVPGEPGAVGPLGPRGERGNPGERGEPGITGLPGEKGMAGGHGPDGPKGNPGPTGTIGDTGPPGLQGMPGERGIA 768
Cdd:COG5164   86 NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGST 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  769 GTPGPKGDRGGIGEKGAeGTAGNDGARGLPGPLGPPGPAGPTGEKGEPGPRGLVGPPGSRGnpgsrGENGPTGAVGFAGP 848
Cdd:COG5164  166 TPPGPGGSTTPPDDGGS-TTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG-----GKTGPKDQRPKTNP 239

                        250       260
                 ....*....|....*....|....*
gi 86613790  849 QGPDGQPGVKGEPGEPGQKGDAGSP 873
Cdd:COG5164  240 IERRGPERPEAAALPAELTALEAEN 264
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 1293-1330 5.01e-06

fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 44.86  E-value: 5.01e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 86613790  1293 TCDDLKLCHPTKQSGEYWIDPNQGSAEDAIKVYCNMET 1330
Cdd:NF040941    1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTT 38
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 499-888 9.57e-06

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 50.39  E-value: 9.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    499 GKRGPRGDPGTVGPPGPMG-ERGAPGNrgfpGSDGLPGPKGAQGERGPVGSSGPKGGQGDPGRPGEPGlPGARGLTGNPG 577
Cdd:pfam09606   93 GTRPQMMGPMGPGPGGPMGqQMGGPGT----ASNLLASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAG-GMMQPSSGQPG 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    578 VQGPEgKLGPLGAPGEDGRPGPPGSIG---IRGQPGSMGLPGPKGSSgdlgKPGEAGNAGVPGQRGAPGKDGEVGPSGPV 654
Cdd:pfam09606  168 SGTPN-QMGPNGGPGQGQAGGMNGGQQgpmGGQMPPQMGVPGMPGPA----DAGAQMGQQAQANGGMNPQQMGGAPNQVA 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    655 GppglagergEQGPPGPTGFQGLPGPPGPPGEGGKAGDQGVPGEPGAVGPLGPRGERgnPGERGEPGITGLPGEKGMAGG 734
Cdd:pfam09606  243 M---------QQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQ--PGAMPNVMSIGDQNNYQQQQT 311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    735 HGPDGPKGNPGPTGTIGDTGPPGLQG---MPGERGIAGTPGPKGDRGGIGEKGAEGtaGNDGARGLPGPLGPPGPAGPTG 811
Cdd:pfam09606  312 RQQQQQQGGNHPAAHQQQMNQSVGQGgqvVALGGLNHLETWNPGNFGGLGANPMQR--GQPGMMSSPSPVPGQQVRQVTP 389

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    812 EKG-EPGPRGLV---GPPGSRGNPGSRGENGPTGAVGFAGPQGPDGQPgvkGEPGEPGQKGDAGSPGPQGLAGSPGPHGP 887
Cdd:pfam09606  390 NQFmRQSPQPSVpspQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQP---AQQRTIGQDSPGGSLNTPGQSAVNSPLNP 466


                   .
gi 86613790    888 H 888
Cdd:pfam09606  467 Q 467
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 387-570 9.74e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 50.37  E-value: 9.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   387 AGPTGARGPEG---PQGQRGETGPPGPAGSQGLPGAVGTDGTPGAKGPTGSAGTSGPPGLAGPPGSPGPQGSTGPQGIRG 463
Cdd:PRK07764  589 GPAPGAAGGEGppaPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDG 668

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   464 QSGDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERGAPGNRGFPGSDG----LPGPKGA 539
Cdd:PRK07764  669 WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDpvplPPEPDDP 748

                         170       180       190
                  ....*....|....*....|....*....|.
gi 86613790   540 QGERGPVGSSGPKGGQGDPGRPGEPGLPGAR 570
Cdd:PRK07764  749 PDPAGAPAQPPPPPAPAPAAAPAAAPPPSPP 779
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 1001-1144 2.11e-05

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 49.13  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  1001 ERGMPGLPGPAGTPGKVGPTGATGDKGPPGPVGPPGSNGPVGEPGPEGPAGndGTPGRDGAVGERGDRGDPGPAGLPGSQ 1080
Cdd:PRK12678   83 AAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRER--GEAARRGAARKAGEGGEQPATEARADA 160

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  1081 G------APGTPGPVGAPGDAGQRGEPGSRGPVGPPGRAGKRGLPGPQGPRGDKGDNGDRGDRGQKGHRG 1144
Cdd:PRK12678  161 AerteeeERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRR 230
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 280-336 7.99e-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: 7.99e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    280 GSPGARGFPGAPGLPGLKGHRGHKGLEGPKGEIGAPGAKGEAGPTGPMGAMGPLGPR 336
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 107-326 1.17e-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: 46.44  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   107 RGRKGQKGEPGLvpvvTGIRGRPGPAGPPGSQGPRGDRGPKGRPGPRGPQGIDGEPGVPGQPGAPGPPGHPSHPGPDGMS 186
Cdd:NF038329  131 AGEQGPRGDRGE----TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQ 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   187 RPfsAQMAGLDEKSGLGSQVGLMP-------GSVGPVGPRGPQGLQGQQGGVGPAGPPGEPGEPGPMGPIGSRGPEGPPG 259
Cdd:NF038329  207 GP--AGPAGPDGEAGPAGEDGPAGpagdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG 284

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790   260 KPGEDGEPGRNGNTGEVGFSGSPGARGFPGAPGLPGLKGHRGHKGLEGPKGEIGAPGAKGEAGPTGP 326
Cdd:NF038329  285 PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKP 351
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 695-887 4.70e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   695 VPGEPGAVGPLGPRGE--RGNPGERGEPGITGLPGEKGMAGGHGPDGPKGNPGPTGTIGDTGPPGLQGMPGERGIAGTPG 772
Cdd:PRK07764  588 VGPAPGAAGGEGPPAPasSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   773 PKGDRGGIGEKGAEGTAGNDGARGLPGPLGPPGPAGPTGeKGEPGPRGLVGPPGSRGNPGSRGENGPTGAVGFAGPQGPD 852
Cdd:PRK07764  668 GWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPA-ATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD 746

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 86613790   853 GQPGVKGEPGEPGQKGDAGSPGPQGLAGSPGPHGP 887
Cdd:PRK07764  747 DPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSE 781
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
883-1135 2.71e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 41.94  E-value: 2.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  883 GPHGPhGVPGLKGGRGTQGPPGATGFPGSAGRVGPPGPAGAPGPAGPAGEPGKEGPPGLRGDPGSHGRVGDRGPAGPPGS 962
Cdd:COG5164    2 GLYGP-GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  963 PGDKGDPGEDGQPGPDGPPGPAGTTGQRGIVGMPGQRGERGMPGLPGPA--GTPGKVGPTGATGDKGPPGPVGPPGSNGP 1040
Cdd:COG5164   81 TTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGGSTPPGPGSTGPGGSTTPPG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790 1041 VGEPGPEGPAGNDGTPGRDGAVGERGDRGDPGPAGLPGSQGAPGTPGPVGAPGDAGQRGEPGSRGPVGPPgrAGKRGLPG 1120
Cdd:COG5164  161 DGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGP--KDQRPKTN 238

                        250
                 ....*....|....*
gi 86613790 1121 PQGPRGDKGDNGDRG 1135
Cdd:COG5164  239 PIERRGPERPEAAAL 253
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1093-1144 4.94e-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: 4.94e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 86613790   1093 GDAGQRGEPGSRGPVGPPGRAGKRGLPGPQGPRGDKGDNGDRGDRGQKGHRG 1144
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 495-712 7.38e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 7.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   495 PGEEGKRGPRGDPGTVGPPGPMGERGAPGNRGFPGSDGLPGPKGAQGERGPVGSSGPKGGQGDPGRPGEPGLPGARGltg 574
Cdd:PRK07764  588 VGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASD--- 664

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   575 npGVQGPEGKLGPLGAPGEDGRPGPPGSIGIRGQPGSMGLPGPKGSSGDLGKPGEAGNAGVPGQRGAPGKDGEVGPSGPV 654
Cdd:PRK07764  665 --GGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLP 742

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 86613790   655 GPPGLAGERGEQGPPGPTGFQGLPGPPGPPGEGGKAGDQGVPGEPGAVGPLGPRGERG 712
Cdd:PRK07764  743 PEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRD 800
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 494-585 9.49e-03

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 40.12  E-value: 9.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  494 PPGEEGKRgprgdPGTVGPPGPMGERGAPGNrgfpgsDGLPGPKGAQGERGPVGSSGPKGGQGDPGRPGEPGLPGARGLT 573
Cdd:cd05922  277 PPERILEK-----PGSIGLAIPGGEFEILDD------DGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHT 345

                         90
                 ....*....|..
gi 86613790  574 GNPGVQGPEGKL 585
Cdd:cd05922  346 GDLARRDEDGFL 357
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1263-1496 1.67e-141

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: 432.92  E-value: 1.67e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   1263 DPGIHVTLKSLSSQIETMRSPDGSKKHPARTCDDLKLCHPTKQSGEYWIDPNQGSAEDAIKVYCNMETGETCISANPASV 1342
Cdd:pfam01410    2 DEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKASI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   1343 PRKTWWASKSpdnKPVWYGLDMNRGSQFTYG-DYQSPNTAITQMTFLRLLSKEASQNLTYICRNTVGYMDDQAKNLKKAV 1421
Cdd:pfam01410   82 PRKNWWTKES---KHVWFGEFMNGGSQFSYGvDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86613790   1422 VLKGSNDLEIKGEGNIRFRYTVLQDTCSKRNGNVGKTIFEYRTQNVARLPIIDVGPVDIGNADQEFGLDIGPVCF 1496
Cdd:pfam01410  159 LLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1263-1497 1.07e-134

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: 414.56  E-value: 1.07e-134
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    1263 DPGIHVTLKSLSSQIETMRSPDGSKKHPARTCDDLKLCHPTKQSGEYWIDPNQGSAEDAIKVYCNMETGETCISANPASV 1342
Cdd:smart00038    1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETGETCVSPSPSSI 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    1343 PRKTWWASKSpdnKPVWYGLDMNRGSQFTYGDYQSPNTAITQMTFLRLLSKEASQNLTYICRNTVGYMDDQAKNLKKAVV 1422
Cdd:smart00038   81 PRKTWYSGKS---KHVWFGETMNGGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALR 157

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86613790    1423 LKGSNDLEIKGEGNIRFRYTVLQDTCSKRNGNVGKTIFEYRTQNVARLPIIDVGPVDIGNADQEFGLDIGPVCFM 1497
Cdd:smart00038  158 LRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 316-601 2.79e-37

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: 146.97  E-value: 2.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   316 GAKGEAGPTGPMGAMGPLGPRGMPGERGRLGPQGAPGKRGAHGMPGKPGPMGPlgipgsSGFPGNPGMKGEAGPTGARGP 395
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE------AGPQGPAGKDGEAGAKGPAGE 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   396 EGPQGQRGETGPPGPAGSQGLPGAVGTDGTPGAKGPTGSAGtsgppglagppgspgpqgstgpQGIRGQSGDPGVPGFKG 475
Cdd:NF038329  191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------------DGQQGPDGDPGPTGEDG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   476 EAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERgapgnrgfpGSDGLPGPKGAQGERGPVGSSGPKGGQ 555
Cdd:NF038329  249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN---------GKDGLPGKDGKDGQNGKDGLPGKDGKD 319

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 86613790   556 GDPGRPGEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPG 601
Cdd:NF038329  320 GQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTAPHTPKTPQIPG 365
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 382-616 1.17e-36

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 145.05  E-value: 1.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   382 GMKGEAGPTGARGPEGPQGQRGETGPPGPAGSQGLPGAVGTDGTPGAKGPTGSAGtsgppglagppgspgpqgSTGPQGI 461
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG------------------PQGPAGK 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   462 RGQSGDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPP-----GPMGERGAPGNRGFPGSDGLPGP 536
Cdd:NF038329  179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGK 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   537 KGAQGERGPVGSSGPKGGQGDPGRPGEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPGSIGIRGQPGSMGLPG 616
Cdd:NF038329  259 DGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 400-642 3.25e-35

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: 140.81  E-value: 3.25e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   400 GQRGETGPPGPAGSQGLPGAVGTDGTPGAKGPTGsagtsgppglagppgspgpqgstgPQGIRGQSGDPGVPGFKGEAGP 479
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAG------------------------PPGPQGERGEKGPAGPQGEAGP 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   480 KGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERGAPGNRGFPGSDGLPGP-----KGAQGERGPVGSSGPKGG 554
Cdd:NF038329  173 QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGP 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   555 QGDPGRPGEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPGSIGIRGQPGSMGLPGPKGSSGDLGKPGEAGNAG 634
Cdd:NF038329  253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332


                  ....*...
gi 86613790   635 VPGQRGAP 642
Cdd:NF038329  333 KDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 478-746 1.69e-33

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: 135.42  E-value: 1.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   478 GPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERGapgnrgfpgsdgLPGPKGAQGERGPVGSSGPKGGQGD 557
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERG------------EKGPAGPQGEAGPQGPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   558 PGRPGEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPGSIGiRGQPGSMGLPGPKGSSGDLGKPGEAGNAGVPG 637
Cdd:NF038329  185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   638 QRGAPGKDGEvgpsgpvgppglAGERGEQGPPGPtgfqglpgppgppgeggkAGDQGVPGEPGAVGPLGPRGERGNPGER 717
Cdd:NF038329  264 DRGEAGPDGP------------DGKDGERGPVGP------------------AGKDGQNGKDGLPGKDGKDGQNGKDGLP 313

                         250       260
                  ....*....|....*....|....*....
gi 86613790   718 GEPGITGLPGEKGMAGGHGPDGPKGNPGP 746
Cdd:NF038329  314 GKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 463-671 2.80e-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: 131.95  E-value: 2.80e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   463 GQSGDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERGAPGNRGFPGSDGLPGPKGAQGE 542
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   543 RGPVGSSGPKGGQGDPGRPGEPGLPGARGLTGNPGV--QGPEGKLGPLGAPGEDGRPGPPGSIGIRGQPGSMGLPGPKGS 620
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 86613790   621 SGDLGKPGEAGNAGVPGQRGAPGKDGEvgpSGPVGPPGLAGERGEQGPPGP 671
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKDGK---DGQNGKDGLPGKDGKDGQPGK 324
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 659-914 1.65e-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: 126.56  E-value: 1.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   659 LAGERGEQGPPGPtgfqglpgppgppgeggkagdqgvPGEPGAVGPLGPRGERGNPGERGEPGITGLPGEKGMAGGHGPD 738
Cdd:NF038329  115 GDGEKGEPGPAGP------------------------AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   739 GPKGNPGPTGTIGDTGPPGLQGMPGERGIAGTPGPKGDRGGIGEKGAEGTAGNDGArglpgplGPPGPAGPTGEKGEPGP 818
Cdd:NF038329  171 GPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP-------AGPAGDGQQGPDGDPGP 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   819 RGLVGPPGSRGNPGSRGENGPTGAVGFAGPQGPDGQPGVKGEPGEPGQKGDAGSPGPQglagspGPHGPHGVPGLKGGRG 898
Cdd:NF038329  244 TGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD------GKDGQNGKDGLPGKDG 317

                         250
                  ....*....|....*.
gi 86613790   899 TQGPPGATGFPGSAGR 914
Cdd:NF038329  318 KDGQPGKDGLPGKDGK 333
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 265-503 4.21e-28

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 119.62  E-value: 4.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   265 GEPGRNGNTGEVGFSGSPGARGFPGAPGLPGLKGHRGHKGLEGPKGEigaPGAKGEAGPTGPMGAMGPLGPRGMPGERGR 344
Cdd:NF038329  129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP---AGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   345 LGPQGAPGKRGAHGMPGKPGPMGPLGIP--GSSGFPGNPGMKGEAGPTGARGPEGPQGQRGETGPPGPAGSQGLPGAVGT 422
Cdd:NF038329  206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   423 DGTPGAKGPTGSAgtsgppglagppgspgpqgstGPQGIRGQSGDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRG 502
Cdd:NF038329  286 AGKDGQNGKDGLP---------------------GKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKT 344


                  .
gi 86613790   503 P 503
Cdd:NF038329  345 P 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 645-887 7.19e-28

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 118.85  E-value: 7.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   645 DGEVGPSGPVGPPGLAGERGEQGPPGPTgfqGLPGPPGPPGEGGKAGDQGVPGEPGAVGPLGPRGERGNPGERGEPGITG 724
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGET---GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   725 LPGEKGMAGGHGPDGPKGNPGPTGTIGDTGPPGLQGMPGeRGIAGTPGPKGDRGGIGEKGAEGTAGNDGARglpgplgpp 804
Cdd:NF038329  193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR--------- 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   805 gpaGPTGEKGEPGPRGLVGPPGSRGNPGSRGENGPTGAVGFAGPQGPDGQPGVKGEPGEPGQKGDAGSPGPQGLAGSPGP 884
Cdd:NF038329  263 ---GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339


                  ...
gi 86613790   885 HGP 887
Cdd:NF038329  340 PAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 598-856 8.96e-28

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 118.47  E-value: 8.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   598 GPPGSIGIRGQPGSMGLPGPKGSSGDLGKPGEAGNAGVPGQRGAPGKDGEVGPSGPVGPPGLAGERGEQGPPGPTgfqgl 677
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK----- 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   678 pgppgppgeggkagdqGVPGEPGAVGPLGPRGERGNPGERGEPGITGLPGEKGMAgGHGPDGPKGNPGPTGTIGDTGPPG 757
Cdd:NF038329  192 ----------------GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPA-GDGQQGPDGDPGPTGEDGPQGPDG 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   758 LQGMPGERGIAGTPGPKGDRGGIGEKGAEGTAGNDGARglpgplgppgpagptGEKGEPGPRGLVGPPGSRGNPGSRGEN 837
Cdd:NF038329  255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN---------------GKDGLPGKDGKDGQNGKDGLPGKDGKD 319

                         250
                  ....*....|....*....
gi 86613790   838 GPTGAVGFAGPQGPDGQPG 856
Cdd:NF038329  320 GQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 832-1109 2.17e-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: 2.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   832 GSRGENGPTGAVGFAGPQGPDGQPGVKGEPGEPGQKGDAGSPGPQGLAGSPGPHGPHGVPGLKGGRGTQGPPGATGFPGS 911
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   912 AGRVGPPGPAGAPGPAGPAGEPGKEGPPGLRGDPGSHGRvgdrgpagppgspGDKGDPGEDGQPgpdgppgpagttGQRG 991
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQ-------------GPDGDPGPTGED------------GPQG 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   992 IVGMPGQRGERGMPGLPGPAGTPGKVGPTgatgdkgppgpvgppgsngpvgepGPEGPAGNDGTPGRDGAVGERGDRGDP 1071
Cdd:NF038329  252 PDGPAGKDGPRGDRGEAGPDGPDGKDGER------------------------GPVGPAGKDGQNGKDGLPGKDGKDGQN 307

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 86613790  1072 GPAGLPGSQGAPGTPGPVGAPGDAGQRGEPGSRGPVGP 1109
Cdd:NF038329  308 GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 735-970 5.23e-23

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 103.83  E-value: 5.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   735 HGPDGPKGNPGPTGTIGDTGPPGLQGMPGERGIAGTPGPKGDRGGIGEKGAEGtagndgarglpgplgPPGPAGPTGEKG 814
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG---------------PQGEAGPQGPAG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   815 EPGPRGLVGPPGSRGNPGSRGENGPTGAVGFAGPQGPDGQPGVKGEPGEPG-----QKGDAGSPGPQGLAGSPGPHGPHG 889
Cdd:NF038329  178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGPQGPDGPAG 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   890 VPGLKGGRGTQGPPGATGFPGSAGRVGPPGPAGAPGPAGPAGEPGKEGPPGLRGDPGSHGRVGDRGPAGPPGSPGDKGDP 969
Cdd:NF038329  258 KDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337


                  .
gi 86613790   970 G 970
Cdd:NF038329  338 G 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 865-1144 9.53e-23

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 103.06  E-value: 9.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   865 GQKGDAGSPGPQGLAGSPGPHGPHGVPGLKGGRGTQGPPGATGFPGSAGrvgppgpagapgpagpagepgKEGPPGLRGD 944
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG---------------------PQGEAGPQGP 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   945 PGSHGRVGDrgpagppgspgdKGDPGEDgqpgpdgppgpagttGQRGIVGMPGQRGERGMPGLPGPAGTPGKVGPTGAtg 1024
Cdd:NF038329  176 AGKDGEAGA------------KGPAGEK---------------GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP-- 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  1025 dkgppgpvGPPGSNGPVGEPGPEGPAGNDGTPGRDGAVGERGDRGDPGPAGLPGSQGAPGTPGPVGAPGDAGQRGEPGSR 1104
Cdd:NF038329  227 --------AGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLP 298

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 86613790  1105 GPVGPPGRAGKRGLPGPQGPRGDKGDNGDRGDRGQKGHRG 1144
Cdd:NF038329  299 GKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
VWC smart00214
von Willebrand factor (vWF) type C domain;
40-95 1.72e-22

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 91.81  E-value: 1.72e-22
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 86613790      40 CTQHGQMYLNRDIWKPSPCQICVCDNGA-ILCDKIECPEVLNCANPIT--PTGECCPVC 95
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGTtVLCDPVECPPPPDCPNPERvkPPGECCPRC 59
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 40-95 9.74e-22

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


Pssm-ID: 278520  Cd Length: 57  Bit Score: 89.79  E-value: 9.74e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 86613790     40 CTQHGQMYLNRDIWKPSPCQICVCDNGAILCDKIECPEvLNCANP--ITPTGECCPVC 95
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIICPP-LDCPNPrlEIPPGECCPVC 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 111-433 8.18e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 81.88  E-value: 8.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   111 GQKGEPGLVpvvtgirgrpGPAGPPGSQGPRGDRGPKGRPGPRGPQGIDGEpgvpgqpgapgppghpshpgpdgmsrpfs 190
Cdd:NF038329  117 GEKGEPGPA----------GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE----------------------------- 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   191 aqmagldeksglgsqvglmPGSVGPVGPRGPQglqgqqggvgpagppgepgepgpmgpigsrgpegppgkpgedGEPGRN 270
Cdd:NF038329  158 -------------------RGEKGPAGPQGEA------------------------------------------GPQGPA 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   271 GNTGEVGFSGSPGARGFPGAPGLPGLKGHRGHKGLEGPKGEIGAPGAKGEAGPTGPmGAMGPLGPRGMPGERGRLGPQGA 350
Cdd:NF038329  177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGP 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   351 PGKRGAHGMPGKPGPMGPLGIPGSSGFPGNPGMKGEAGPTGARGPEGPQGQRGETGPPGPAGSQGLPGAVGTDGTPGAKG 430
Cdd:NF038329  256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335


                  ...
gi 86613790   431 PTG 433
Cdd:NF038329  336 QPG 338
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
301-545 3.08e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 61.20  E-value: 3.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  301 GHKGLEGPKGEIGAPGAKGEAGPTGPMGAMGPLGPRGMPGERGRLGPQGAPGKRGAHGMPGKPGPMGPLGIPGSSGFPGN 380
Cdd:COG5164    7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  381 PGMKGEAGPTGARGPEGPQGQRGETGPPGPAGSQGLPGAVG------------TDGTPGAKGPTGSAGTSGPPGLAGPPG 448
Cdd:COG5164   87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTppsggsttppgdGGSTPPGPGSTGPGGSTTPPGDGGSTT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  449 SPGPQGSTGPQGIRGqSGDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPP-GPMGERGAPGNRGF 527
Cdd:COG5164  167 PPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPkDQRPKTNPIERRGP 245

                        250
                 ....*....|....*...
gi 86613790  528 PGSDGLPGPKGAQGERGP 545
Cdd:COG5164  246 ERPEAAALPAELTALEAE 263
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
426-672 3.50e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 57.73  E-value: 3.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  426 PGAKGPTGSAGTSGPPGLAGPPGSPGPQGSTGPQGIRGQSGDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRGPRG 505
Cdd:COG5164    6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  506 DPGTVGPPG------PMGERGAPGNRGFPGSDGLPGPKGAQGERGPVGSSGPKGGQGDPGRPGEPGLPGARGLTGNPGVQ 579
Cdd:COG5164   86 NQGGTRPAGntggttPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGST 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  580 GPEGKLGPLGAPGEDGRPGPPGSIGIrGQPGSMGLPGPKGSSGDLGKPGEAGNAGVPGQRGapGKDGEVGPSGPVGPPGL 659
Cdd:COG5164  166 TPPGPGGSTTPPDDGGSTTPPNKGET-GTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGPKDQRPKTNPIER 242

                        250
                 ....*....|...
gi 86613790  660 AGERGEQGPPGPT 672
Cdd:COG5164  243 RGPERPEAAALPA 255
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1042-1098 2.13e-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: 2.13e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790   1042 GEPGPEGPAGNDGTPGRDGAVGERGDRGDPGPAGLPGSQGAPGTPGPVGAPGDAGQR 1098
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 511-567 3.28e-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: 48.64  E-value: 3.28e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    511 GPPGPMGERGAPGNRGFPGSDGLPGPKGAQGERGPVGSSGPKGGQGDPGRPGEPGLP 567
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 814-870 5.79e-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: 5.79e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    814 GEPGPRGLVGPPGSRGNPGSRGENGPTGAVGFAGPQGPDGQPGVKGEPGEPGQKGDA 870
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1069-1125 1.51e-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: 1.51e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790   1069 GDPGPAGLPGSQGAPGTPGPVGAPGDAGQRGEPGSRGPVGPPGRAGKRGLPGPQGPR 1125
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 847-903 2.01e-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: 2.01e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    847 GPQGPDGQPGVKGEPGEPGQKGDAGSPGPQGLAGSPGPHGPHGVPGLKGGRGTQGPP 903
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1060-1116 2.84e-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: 45.95  E-value: 2.84e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790   1060 GAVGERGDRGDPGPAGLPGSQGAPGTPGPVGAPGDAGQRGEPGSRGPVGPPGRAGKR 1116
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
609-873 2.94e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 51.57  E-value: 2.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  609 PGSMGLPGPKGSSGDLGKPGEAGNAGVPGQRGAPGKDGEVGPSGPVGPPGLAGERGEQGPPGPTGFQGLPGPPGPPGEGG 688
Cdd:COG5164    6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  689 KAGDQGVPGEPGAVGPLGPRGERGNPGERGEPGITGLPGEKGMAGGHGPDGPKGNPGPTGTIGDTGPPGLQGMPGERGIA 768
Cdd:COG5164   86 NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGST 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  769 GTPGPKGDRGGIGEKGAeGTAGNDGARGLPGPLGPPGPAGPTGEKGEPGPRGLVGPPGSRGnpgsrGENGPTGAVGFAGP 848
Cdd:COG5164  166 TPPGPGGSTTPPDDGGS-TTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG-----GKTGPKDQRPKTNP 239

                        250       260
                 ....*....|....*....|....*
gi 86613790  849 QGPDGQPGVKGEPGEPGQKGDAGSP 873
Cdd:COG5164  240 IERRGPERPEAAALPAELTALEAEN 264
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1075-1131 3.63e-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: 3.63e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790   1075 GLPGSQGAPGTPGPVGAPGDAGQRGEPGSRGPVGPPGRAGKRGLPGPQGPRGDKGDN 1131
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 496-551 4.00e-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: 4.00e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 86613790    496 GEEGKRGPRGDPGTVGPPGPMGERGAPGNRGFPGSDGLPGPKGAQGERGPVGSSGP 551
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1054-1110 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 86613790   1054 GTPGRDGAVGERGDRGDPGPAGLPGSQGAPGTPGPVGAPGDAGQRGEPGSRGPVGPP 1110
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 829-884 4.77e-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: 4.77e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 86613790    829 GNPGSRGENGPTGAVGFAGPQGPDGQPGVKGEPGEPGQKGDAGSPGPQGLAGSPGP 884
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 1293-1330 5.01e-06

fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 44.86  E-value: 5.01e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 86613790  1293 TCDDLKLCHPTKQSGEYWIDPNQGSAEDAIKVYCNMET 1330
Cdd:NF040941    1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTT 38
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1066-1121 5.21e-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: 5.21e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 86613790   1066 GDRGDPGPAGLPGSQGAPGTPGPVGAPGDAGQRGEPGSRGPVGPPGRAGKRGLPGP 1121
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 475-529 5.42e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.18  E-value: 5.42e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 86613790    475 GEAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERGAPGNRGFPG 529
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 481-536 6.41e-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: 6.41e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 86613790    481 GEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERGAPGNRGFPGSDGLPGP 536
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 379-435 7.80e-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: 7.80e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    379 GNPGMKGEAGPTGARGPEGPQGQRGETGPPGPAGSQGLPGAVGTDGTPGAKGPTGSA 435
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 490-546 8.60e-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: 8.60e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    490 GPIGPPGEEGKRGPRGDPGTVGPPGPMGERGAPGNRGFPGSDGLPGPKGAQGERGPV 546
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 499-888 9.57e-06

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 50.39  E-value: 9.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    499 GKRGPRGDPGTVGPPGPMG-ERGAPGNrgfpGSDGLPGPKGAQGERGPVGSSGPKGGQGDPGRPGEPGlPGARGLTGNPG 577
Cdd:pfam09606   93 GTRPQMMGPMGPGPGGPMGqQMGGPGT----ASNLLASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAG-GMMQPSSGQPG 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    578 VQGPEgKLGPLGAPGEDGRPGPPGSIG---IRGQPGSMGLPGPKGSSgdlgKPGEAGNAGVPGQRGAPGKDGEVGPSGPV 654
Cdd:pfam09606  168 SGTPN-QMGPNGGPGQGQAGGMNGGQQgpmGGQMPPQMGVPGMPGPA----DAGAQMGQQAQANGGMNPQQMGGAPNQVA 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    655 GppglagergEQGPPGPTGFQGLPGPPGPPGEGGKAGDQGVPGEPGAVGPLGPRGERgnPGERGEPGITGLPGEKGMAGG 734
Cdd:pfam09606  243 M---------QQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQ--PGAMPNVMSIGDQNNYQQQQT 311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    735 HGPDGPKGNPGPTGTIGDTGPPGLQG---MPGERGIAGTPGPKGDRGGIGEKGAEGtaGNDGARGLPGPLGPPGPAGPTG 811
Cdd:pfam09606  312 RQQQQQQGGNHPAAHQQQMNQSVGQGgqvVALGGLNHLETWNPGNFGGLGANPMQR--GQPGMMSSPSPVPGQQVRQVTP 389

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    812 EKG-EPGPRGLV---GPPGSRGNPGSRGENGPTGAVGFAGPQGPDGQPgvkGEPGEPGQKGDAGSPGPQGLAGSPGPHGP 887
Cdd:pfam09606  390 NQFmRQSPQPSVpspQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQP---AQQRTIGQDSPGGSLNTPGQSAVNSPLNP 466


                   .
gi 86613790    888 H 888
Cdd:pfam09606  467 Q 467
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 387-570 9.74e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 50.37  E-value: 9.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   387 AGPTGARGPEG---PQGQRGETGPPGPAGSQGLPGAVGTDGTPGAKGPTGSAGTSGPPGLAGPPGSPGPQGSTGPQGIRG 463
Cdd:PRK07764  589 GPAPGAAGGEGppaPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDG 668

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   464 QSGDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERGAPGNRGFPGSDG----LPGPKGA 539
Cdd:PRK07764  669 WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDpvplPPEPDDP 748

                         170       180       190
                  ....*....|....*....|....*....|.
gi 86613790   540 QGERGPVGSSGPKGGQGDPGRPGEPGLPGAR 570
Cdd:PRK07764  749 PDPAGAPAQPPPPPAPAPAAAPAAAPPPSPP 779
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 505-561 1.01e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.41  E-value: 1.01e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    505 GDPGTVGPPGPMGERGAPGNRGFPGSDGLPGPKGAQGERGPVGSSGPKGGQGDPGRP 561
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 373-428 1.26e-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: 1.26e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 86613790    373 GSSGFPGNPGMKGEAGPTGARGPEGPQGQRGETGPPGPAGSQGLPGAVGTDGTPGA 428
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 361-417 1.35e-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: 44.02  E-value: 1.35e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    361 GKPGPMGPLGIPGSSGFPGNPGMKGEAGPTGARGPEGPQGQRGETGPPGPAGSQGLP 417
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 358-412 1.69e-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: 1.69e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 86613790    358 GMPGKPGPMGPLGIPGSSGFPGNPGMKGEAGPTGARGPEGPQGQRGETGPPGPAG 412
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 838-892 1.76e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 1.76e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 86613790    838 GPTGAVGFAGPQGPDGQPGVKGEPGEPGQKGDAGSPGPQGLAGSPGPHGPHGVPG 892
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 355-411 1.92e-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: 1.92e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    355 GAHGMPGKPGPMGPLGIPGSSGFPGNPGMKGEAGPTGARGPEGPQGQRGETGPPGPA 411
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 487-543 1.94e-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: 1.94e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    487 GIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERGAPGNRGFPGSDGLPGPKGAQGER 543
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 313-368 2.00e-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: 2.00e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 86613790    313 GAPGAKGEAGPTGPMGAMGPLGPRGMPGERGRLGPQGAPGKRGAHGMPGKPGPMGP 368
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 1001-1144 2.11e-05

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 49.13  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  1001 ERGMPGLPGPAGTPGKVGPTGATGDKGPPGPVGPPGSNGPVGEPGPEGPAGndGTPGRDGAVGERGDRGDPGPAGLPGSQ 1080
Cdd:PRK12678   83 AAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRER--GEAARRGAARKAGEGGEQPATEARADA 160

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  1081 G------APGTPGPVGAPGDAGQRGEPGSRGPVGPPGRAGKRGLPGPQGPRGDKGDNGDRGDRGQKGHRG 1144
Cdd:PRK12678  161 AerteeeERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRR 230
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1078-1134 2.19e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 2.19e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790   1078 GSQGAPGTPGPVGAPGDAGQRGEPGSRGPVGPPGRAGKRGLPGPQGPRGDKGDNGDR 1134
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 372-564 2.43e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.21  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   372 PGSSGFPGNPGMKG------EAGPTGARGPEGPQGQRGETGPPGPAGSQGLPGAVGTDGTPGAKGPTGSAGTSGPPGLAG 445
Cdd:PRK07764  592 PGAAGGEGPPAPASsgppeeAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA 671

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   446 PPGSPGPQGSTGPQGIRGQSGDPGVPGfkgeagpkGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERGAPgnr 525
Cdd:PRK07764  672 KAGGAAPAAPPPAPAPAAPAAPAGAAP--------AQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVP--- 740

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 86613790   526 GFPGSDGLPGPKGAQGERGPVGSSGPKGGQGDPGRPGEP 564
Cdd:PRK07764  741 LPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPP 779
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 703-757 2.71e-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: 2.71e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 86613790    703 GPLGPRGERGNPGERGEPGITGLPGEKGMAGGHGPDGPKGNPGPTGTIGDTGPPG 757
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 532-587 3.33e-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: 3.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 86613790    532 GLPGPKGAQGERGPVGSSGPKGGQGDPGRPGEPGLPGARGLTGNPGVQGPEGKLGP 587
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 313-522 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 86613790   313 GAPGAKGEAGPTGPmgamgplGPRGMPGERGRLGPQGAPGKRGAHGMPGKPGPMGPLGIPGSSGFPGNPGMKGEAGPTGA 392
Cdd:PRK07764  590 PAPGAAGGEGPPAP-------ASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDA 662

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   393 rgPEGPQGQRGETGPPGPAGSQGLPGAVGTDG-TPGAKGPTGSAGTSGPPGLAGPPGSPGPQGSTGPQGIRGQSGDPGVP 471
Cdd:PRK07764  663 --SDGGDGWPAKAGGAAPAAPPPAPAPAAPAApAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVP 740

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 86613790   472 GFkgeagpkgePGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERGAP 522
Cdd:PRK07764  741 LP---------PEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 370-426 3.86e-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: 3.86e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    370 GIPGSSGFPGNPGMKGEAGPTGARGPEGPQGQRGETGPPGPAGSQGLPGAVGTDGTP 426
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1081-1137 4.18e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 4.18e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790   1081 GAPGTPGPVGAPGDAGQRGEPGSRGPVGPPGRAGKRGLPGPQGPRGDKGDNGDRGDR 1137
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 499-553 4.48e-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: 42.48  E-value: 4.48e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 86613790    499 GKRGPRGDPGTVGPPGPMGERGAPGNRGFPGSDGLPGPKGAQGERGPVGSSGPKG 553
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 466-522 5.14e-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: 5.14e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    466 GDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERGAP 522
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 841-895 5.72e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 5.72e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 86613790    841 GAVGFAGPQGPDGQPGVKGEPGEPGQKGDAGSPGPQGLAGSPGPHGPHGVPGLKG 895
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 280-336 7.99e-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: 7.99e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    280 GSPGARGFPGAPGLPGLKGHRGHKGLEGPKGEIGAPGAKGEAGPTGPMGAMGPLGPR 336
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 694-748 8.48e-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: 41.71  E-value: 8.48e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 86613790    694 GVPGEPGAVGPLGPRGERGNPGERGEPGITGLPGEKGMAGGHGPDGPKGNPGPTG 748
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 592-647 8.91e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 8.91e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 86613790    592 GEDGRPGPPGSIGIRGQPGSMGLPGPKGSSGDLGKPGEAGNAGVPGQRGAPGKDGE 647
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 334-389 9.17e-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: 9.17e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 86613790    334 GPRGMPGERGRLGPQGAPGKRGAHGMPGKPGPMGPLGIPGSSGFPGNPGMKGEAGP 389
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 697-751 1.02e-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: 41.33  E-value: 1.02e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 86613790    697 GEPGAVGPLGPRGERGNPGERGEPGITGLPGEKGMAGGHGPDGPKGNPGPTGTIG 751
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 328-382 1.13e-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: 41.33  E-value: 1.13e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 86613790    328 GAMGPLGPRGMPGERGRLGPQGAPGKRGAHGMPGKPGPMGPLGIPGSSGFPGNPG 382
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 559-615 1.15e-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: 41.33  E-value: 1.15e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    559 GRPGEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPGSIGIRGQPGSMGLP 615
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 107-326 1.17e-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: 46.44  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   107 RGRKGQKGEPGLvpvvTGIRGRPGPAGPPGSQGPRGDRGPKGRPGPRGPQGIDGEPGVPGQPGAPGPPGHPSHPGPDGMS 186
Cdd:NF038329  131 AGEQGPRGDRGE----TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQ 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   187 RPfsAQMAGLDEKSGLGSQVGLMP-------GSVGPVGPRGPQGLQGQQGGVGPAGPPGEPGEPGPMGPIGSRGPEGPPG 259
Cdd:NF038329  207 GP--AGPAGPDGEAGPAGEDGPAGpagdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG 284

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790   260 KPGEDGEPGRNGNTGEVGFSGSPGARGFPGAPGLPGLKGHRGHKGLEGPKGEIGAPGAKGEAGPTGP 326
Cdd:NF038329  285 PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKP 351
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 325-381 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: 41.33  E-value: 1.26e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    325 GPMGAMGPLGPRGMPGERGRLGPQGAPGKRGAHGMPGKPGPMGPLGIPGSSGFPGNP 381
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 562-617 1.43e-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: 40.94  E-value: 1.43e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 86613790    562 GEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPGSIGIRGQPGSMGLPGP 617
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 311-602 1.51e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.70  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   311 EIGAPGAKGEAGPTGPmgamGPLGPRGMPGERGRLGPQGAPGKRGAHGMPGKPGPMGPlgipGSSGFPGNPGMKGEAGPT 390
Cdd:PHA03307   96 APASPAREGSPTPPGP----SSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPA----ASPPAAGASPAAVASDAA 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   391 GARGPEGPQGQRGETGPPGPAGSQGLPGAVGTDGTPGAKGPTGSAGTSGPPGLAGPPGSPGPQGSTGPQGIRGQSGDPGV 470
Cdd:PHA03307  168 SSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGC 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   471 PGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRGPRgdPGTVGPPGPMGERGAPGNRGFPGSDGLPGPKGAQGERGPVGSSG 550
Cdd:PHA03307  248 GWGPENECPLPRPAPITLPTRIWEASGWNGPSSR--PGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESS 325

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 86613790   551 PKGGQGDPGRPGEPGLPGARGLTGNPGVQGPEGKLGPlGAPGEDGRPGPPGS 602
Cdd:PHA03307  326 SSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADP-SSPRKRPRPSRAPS 376
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 457-507 1.96e-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: 1.96e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 86613790    457 GPQGIRGQSGDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDP 507
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 286-342 2.05e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 2.05e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    286 GFPGAPGLPGLKGHRGHKGLEGPKGEIGAPGAKGEAGPTGPMGAMGPLGPRGMPGER 342
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 417-631 2.34e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   417 PGAVGTDGTPGAKGPTGSAGTSGPPGLAGPPGSPGPQGSTGPQGIRGQSGDPGVPGFKGEAGPKGEPGPHGIQGPIGPPG 496
Cdd:PRK07764  592 PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA 671

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   497 EEGKRGPRGDPGTVGPPGPMGERGAPGNRGFPGSDGLPGPKGAQGERGPVGSSGPKGGQGDPGRPGEPGLPGARGLTGNP 576
Cdd:PRK07764  672 KAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDP 751

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 86613790   577 GvQGPEGKLGPLGAPGEDGRPGPPGSIGIRGQPGSMGLPGPKGSSGDLGKPGEAG 631
Cdd:PRK07764  752 A-GAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVA 805
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 271-326 2.81e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 2.81e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 86613790    271 GNTGEVGFSGSPGARGFPGAPGLPGLKGHRGHKGLEGPKGEIGAPGAKGEAGPTGP 326
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Amnionless pfam14828
Amnionless; The amnionless protein forms a complex with cubilin. This complex is necessary for ...
 14-95 3.66e-04

Amnionless; The amnionless protein forms a complex with cubilin. This complex is necessary for vitamin B12 uptake.


Pssm-ID: 464340  Cd Length: 449  Bit Score: 44.69  E-value: 3.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790     14 LSVLLGYC-------VSIKAQEQENDEYDEEIACTQHGQMYLNRD---IWKPSPC---QICVCDNGAIL---CDKIE--C 75
Cdd:pfam14828  137 FRVDLESGrpirvksVSLLGQTFTSDEDFAEFLSSRLGQLQFHGAgalRVGPEACsdpSGCGCGNDENLeriCANVLqrC 216

                           90       100
                   ....*....|....*....|
gi 86613790     76 PeVLNCANPITPTGECCPVC 95
Cdd:pfam14828  217 P-PPHCLSPLRPEGHCCDVC 235
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 695-887 4.70e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   695 VPGEPGAVGPLGPRGE--RGNPGERGEPGITGLPGEKGMAGGHGPDGPKGNPGPTGTIGDTGPPGLQGMPGERGIAGTPG 772
Cdd:PRK07764  588 VGPAPGAAGGEGPPAPasSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   773 PKGDRGGIGEKGAEGTAGNDGARGLPGPLGPPGPAGPTGeKGEPGPRGLVGPPGSRGNPGSRGENGPTGAVGFAGPQGPD 852
Cdd:PRK07764  668 GWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPA-ATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD 746

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 86613790   853 GQPGVKGEPGEPGQKGDAGSPGPQGLAGSPGPHGP 887
Cdd:PRK07764  747 DPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSE 781
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 466-642 5.33e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   466 GDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGP----------PGPMGERGAPGNRGFPGSDGLPG 535
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPaeasaapapgVAAPEHHPKHVAVPDASDGGDGW 669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   536 PKGAQGERGPVGSSGPKGGQGDPGRPGEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPGSIGIRGQPGSMGLP 615
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749

                         170       180
                  ....*....|....*....|....*..
gi 86613790   616 GPKGSSGDLGKPGEAGNAGVPGQRGAP 642
Cdd:PRK07764  750 DPAGAPAQPPPPPAPAPAAAPAAAPPP 776
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 227-625 5.60e-04

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: 44.61  E-value: 5.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    227 QQGGVGPAGPPGEPGEPGPMGPIGSRGPEGPPGKPGEDGEPGRNgntgevgfsgSPGARGFPGAPGLPGLKGHRGHKGLE 306
Cdd:pfam09606   66 GQGNGGMGGGQQGMPDPINALQNLAGQGTRPQMMGPMGPGPGGP----------MGQQMGGPGTASNLLASLGRPQMPMG 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    307 GPKGEIGAPGAKGEAGPTGPMGAMGPLGPRGMPGERGRLGPQGAPGKRGAHGM-PGKPGPMGPlGIPGSSGFPGNPGM-- 383
Cdd:pfam09606  136 GAGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMnGGQQGPMGG-QMPPQMGVPGMPGPad 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    384 KGEAGPTGARGPEGPQGQRGETGPPGPAGSQGLPGAVGTDGTPGAK-GPTGSAGTSGPPGLAGPPGSPGPQGSTGPQGIR 462
Cdd:pfam09606  215 AGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGiNQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAM 294

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    463 GQSGDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERGAPGNRGFPGSDGL-PGPKGAQG 541
Cdd:pfam09606  295 PNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMqRGQPGMMS 374

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    542 ERGPVGSSGPKGGQGDPG--RPGEPGLPGARGLTGNPGVQGPEgklGPLGAPGEDGRPGPPGSIGIRgQPGSMGLPGPKG 619
Cdd:pfam09606  375 SPSPVPGQQVRQVTPNQFmrQSPQPSVPSPQGPGSQPPQSHPG---GMIPSPALIPSPSPQMSQQPA-QQRTIGQDSPGG 450


                   ....*.
gi 86613790    620 SSGDLG 625
Cdd:pfam09606  451 SLNTPG 456
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 344-551 6.65e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.21  E-value: 6.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   344 RLGPQGAPGKRGAHGMPGKPGPMGPLGIPGSSGFPGNPgmkgeAGPTGARGPEGPQGQRGETGPPGPAGSQGLPGAVGTD 423
Cdd:PRK07764  587 VVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAP-----AAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPD 661

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   424 GTPGAKGPTGSAGTSGPPGLAGPPGSpgpqgsTGPQGIRGQSGDPGVPgfKGEAGPKGEPGPHGIQGPIGPPGEEGKRGP 503
Cdd:PRK07764  662 ASDGGDGWPAKAGGAAPAAPPPAPAP------AAPAAPAGAAPAQPAP--APAATPPAGQADDPAAQPPQAAQGASAPSP 733

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 86613790   504 RGDPGTVGPPGPMGERGAPGNRGFPGSDGLPGPKGAQGERGPVGSSGP 551
Cdd:PRK07764  734 AADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSE 781
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 997-1144 9.47e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 43.74  E-value: 9.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   997 GQRGERGMPGLPGPAGTPGKVGPTGATGDKGPPGPVGPPGSNGPVGEPGPEGPAGNDGTPGRDGAVGERGDRGDPGPAGL 1076
Cdd:PRK12678  134 GEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGD 213

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86613790  1077 PGSQGAPGTPGPVGAPGDAGQRGEPGSRGPVGPPGRAGKRGLPGPQGPRGDKGDNGDRGDRGQKGHRG 1144
Cdd:PRK12678  214 RREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGDGGN 281
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 275-511 9.65e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 9.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   275 EVGFSGSPGARGFPGAPGLPGlkghrghkglEGPKGEIGAPGA-KGEAGPTGPMGAMGPLGPRGMPGERGRLGPQGAPGK 353
Cdd:PRK07764  585 EAVVGPAPGAAGGEGPPAPAS----------SGPPEEAARPAApAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHP 654

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   354 RGAhgmpgkPGPMGPLGIPGSSGFPGNPGMKGEAGPTGARGPEGPQGQRGetGPPGPAGSQGLPGAVGTDGTPGAKGPTG 433
Cdd:PRK07764  655 KHV------AVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAP--AQPAPAPAATPPAGQADDPAAQPPQAAQ 726

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86613790   434 SAGTSGPPGLAGPPGSPGPQGSTGPQGIRGQSGDPGVPGFKGEAGPKGEPGPHG-IQGPIGPPGEEGKRGPRGDPGTVG 511
Cdd:PRK07764  727 GASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSeEEEMAEDDAPSMDDEDRRDAEEVA 805
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 1011-1144 1.01e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 43.74  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  1011 AGTPGKVGPTGATGDKGPPGPVGPPGSNGPVGEPGPEGPAGNDGTPGRDGAVGERGDRGDPGPAGLPGSQGAP-GTPGPV 1089
Cdd:PRK12678   60 GGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRErGEAARR 139

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 86613790  1090 GAPGDAGQRGEPGSRGPVGPPGRAGKRGLPGPQGPRGDKGDNGDRGDRGQKGHRG 1144
Cdd:PRK12678  140 GAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRRE 194
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 574-630 1.08e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 1.08e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    574 GNPGVQGPEGKLGPLGAPGEDGRPGPPGSIGIRGQPGSMGLPGPKGSSGDLGKPGEA 630
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 391-437 1.21e-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: 1.21e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 86613790    391 GARGPEGPQGQRGETGPPGPAGSQGLPGAVGTDGTPGAKGPTGSAGT 437
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 550-604 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 86613790    550 GPKGGQGDPGRPGEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPGSIG 604
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 274-329 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 86613790    274 GEVGFSGSPGARGFPGAPGLPGLKGHRGHKGLEGPKGEIGAPGAKGEAGPTGPMGA 329
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 706-762 1.36e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 1.36e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 86613790    706 GPRGERGNPGERGEPGITGLPGEKGMAGGHGPDGPKGNPGPTGTIGDTGPPGLQGMP 762
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 694-744 2.14e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 2.14e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 86613790    694 GVPGEPGAVGPLGPRGERGNPGERGEPGITGLPGEKGMAGGHGPDGPKGNP 744
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 768-1144 2.53e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   768 AGTPGPKGDRGGIGEKGAEGTAGNDGARGLPGPLGPPGPAGPTGEKGEPGPRGLVGPPGSRGNP----------GSRGEN 837
Cdd:PHA03307   25 PATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPtwslstlapaSPAREG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   838 GPTgavgfAGPQGPDGQPGVKGEPGEPGQKGDAGSPGPQGLAGSPGPHGPH-----GVPGLKGGRGTQGPPGATGFPGSA 912
Cdd:PHA03307  105 SPT-----PPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAAsppaaGASPAAVASDAASSRQAALPLSSP 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   913 GRVGPPGPAGAPGPAGPAGEPGKEGPPGLRGDPGSHGR-----VGDRGPAGPPGSPGDKGDPGEDGQPGPdgppgpagtt 987
Cdd:PHA03307  180 EETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASAsspapAPGRSAADDAGASSSDSSSSESSGCGW---------- 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   988 gqrgivgmpgqrGERGMPGLPGPAGTPGKVGPTGATGDKGPPGPVGPPGSNGPVGEPGPEGPAGNDGTPGRDGAVGERGD 1067
Cdd:PHA03307  250 ------------GPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSS 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  1068 RGDPGPAGL-------PGSQGAPGTPGPVGAPGDAGQRGEPGSRGPvgPPGRAGkRGLPGPQGPRGDKGDNGDRGDRGQK 1140
Cdd:PHA03307  318 SSSSRESSSsstssssESSRGAAVSPGPSPSRSPSPSRPPPPADPS--SPRKRP-RPSRAPSSPAASAGRPTRRRARAAV 394


                  ....
gi 86613790  1141 GHRG 1144
Cdd:PHA03307  395 AGRA 398
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
883-1135 2.71e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 41.94  E-value: 2.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  883 GPHGPhGVPGLKGGRGTQGPPGATGFPGSAGRVGPPGPAGAPGPAGPAGEPGKEGPPGLRGDPGSHGRVGDRGPAGPPGS 962
Cdd:COG5164    2 GLYGP-GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  963 PGDKGDPGEDGQPGPDGPPGPAGTTGQRGIVGMPGQRGERGMPGLPGPA--GTPGKVGPTGATGDKGPPGPVGPPGSNGP 1040
Cdd:COG5164   81 TTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGGSTPPGPGSTGPGGSTTPPG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790 1041 VGEPGPEGPAGNDGTPGRDGAVGERGDRGDPGPAGLPGSQGAPGTPGPVGAPGDAGQRGEPGSRGPVGPPgrAGKRGLPG 1120
Cdd:COG5164  161 DGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGP--KDQRPKTN 238

                        250
                 ....*....|....*
gi 86613790 1121 PQGPRGDKGDNGDRG 1135
Cdd:COG5164  239 PIERRGPERPEAAAL 253
dnaA PRK14086
chromosomal replication initiator protein DnaA;
457-624 3.53e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 41.73  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   457 GPQGIRGqsGDPGVPGFKG-EAGPKGEPGPHGIQGPIGPPGEEgKRGPRGDPGTV-GPPGPMGERGAPgnRGFPGSDGLP 534
Cdd:PRK14086  107 EPELPRP--GRRPYEGYGGpRADDRPPGLPRQDQLPTARPAYP-AYQQRPEPGAWpRAADDYGWQQQR--LGFPPRAPYA 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   535 GP----KGAQGERGPVGSSGPKGGQG-----------DPGRPGEPGLPGARGLTGNPGVQGPeGKLGPLGAPGEDGRPGP 599
Cdd:PRK14086  182 SPasyaPEQERDREPYDAGRPEYDQRrrdydhprpdwDRPRRDRTDRPEPPPGAGHVHRGGP-GPPERDDAPVVPIRPSA 260

                         170       180
                  ....*....|....*....|....*
gi 86613790   600 PGSIGIRGQPGsmglPGPKGSSGDL 624
Cdd:PRK14086  261 PGPLAAQPAPA----PGPGEPTARL 281
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1093-1144 4.94e-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: 4.94e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 86613790   1093 GDAGQRGEPGSRGPVGPPGRAGKRGLPGPQGPRGDKGDNGDRGDRGQKGHRG 1144
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 724-778 5.67e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.70  E-value: 5.67e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 86613790    724 GLPGEKGMAGGHGPDGPKGNPGPTGTIGDTGPPGLQGMPGERGIAGTPGPKGDRG 778
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 1010-1132 6.56e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 6.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  1010 PAGTPGKVGPTGATGDKGPPGPVGPPGSNGPVGEPGPEGPAGNDGTPGRDGAVGERGDRGDPGPAGLPGSQGAPGTPGPV 1089
Cdd:PRK07764  615 PAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA 694

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 86613790  1090 GAPGDAGQRGEPGSRGPVGPPGRAG-KRGLPGPQGPRGDKGDNG 1132
Cdd:PRK07764  695 GAAPAQPAPAPAATPPAGQADDPAAqPPQAAQGASAPSPAADDP 738
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 390-762 7.09e-03

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 40.76  E-value: 7.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    390 TGARGPEGPQGQRGETGPPGPAGSQGLPGAVGTDGTPGAKGPTGSAGtsgppglagPPGSPGPQGStGPQGIRGQSGDPG 469
Cdd:pfam09606   55 KKAAQQQQPQGGQGNGGMGGGQQGMPDPINALQNLAGQGTRPQMMGP---------MGPGPGGPMG-QQMGGPGTASNLL 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    470 VPGFKGEAGPKGEPGPHGIQGPIGppGEEGKRGPRGDPGTVGPPGPmGERGAPGNRGFPGSDGLPGPKGAQGErGPVGSS 549
Cdd:pfam09606  125 ASLGRPQMPMGGAGFPSQMSRVGR--MQPGGQAGGMMQPSSGQPGS-GTPNQMGPNGGPGQGQAGGMNGGQQG-PMGGQM 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    550 GPKGGQGDPGRPGEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGP-PGSIGIRGQPGSMGlPGPKGSSGDLGKPG 628
Cdd:pfam09606  201 PPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQqGQQSQLGMGINQMQ-QMPQGVGGGAGQGG 279

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    629 EAGNAGVPGQR----GAPGKDGEVGPSGPVGPPGLAGERGEQGPPGPTGFQGLPGPPGPPGEGGKAGDQGVPGEPGAVGP 704
Cdd:pfam09606  280 PGQPMGPPGQQpgamPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGG 359

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790    705 LG-PRGERGNPGERGEPGITGLPGEKGMAGGHG-----------PDGPKGNPGPTGTIGDTGPPGLQGMP 762
Cdd:pfam09606  360 LGaNPMQRGQPGMMSSPSPVPGQQVRQVTPNQFmrqspqpsvpsPQGPGSQPPQSHPGGMIPSPALIPSP 429
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 495-712 7.38e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 7.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   495 PGEEGKRGPRGDPGTVGPPGPMGERGAPGNRGFPGSDGLPGPKGAQGERGPVGSSGPKGGQGDPGRPGEPGLPGARGltg 574
Cdd:PRK07764  588 VGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASD--- 664

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   575 npGVQGPEGKLGPLGAPGEDGRPGPPGSIGIRGQPGSMGLPGPKGSSGDLGKPGEAGNAGVPGQRGAPGKDGEVGPSGPV 654
Cdd:PRK07764  665 --GGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLP 742

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 86613790   655 GPPGLAGERGEQGPPGPTGFQGLPGPPGPPGEGGKAGDQGVPGEPGAVGPLGPRGERG 712
Cdd:PRK07764  743 PEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRD 800
PHA03169 PHA03169
hypothetical protein; Provisional
 997-1139 7.45e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.72  E-value: 7.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   997 GQRGERGMPGLPGPAGTPGKVGPTGATGDKGPPGPVGPPGSNGPVGEPGPEGPAGNDGTPGRDGAVGERGDRGDPGPAGL 1076
Cdd:PHA03169   90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQP 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86613790  1077 PGSQGAPGTPGPVGAPGDAGQRGEPGSRGPVGPPGRAGKRGLPGPQGPRGDKGDNGDRGDRGQ 1139
Cdd:PHA03169  170 SHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVE 232
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 423-611 8.53e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 8.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   423 DGTPGAKGPTGSAGtSGPPGLAGPPGSPGPQGSTGPQGIRGQSGDPGVPGFKGEAGPKGEPGPHGIQGPigPPGEEGKRG 502
Cdd:PRK07764  589 GPAPGAAGGEGPPA-PASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKH--VAVPDASDG 665

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   503 PRGDPGTVGPPGPMGERGAPGNRGFPGSDGLPGPKGAQGERGPVGSSGPKGGQGDPGRPGEPGLPGARGltGNPGVQGPE 582
Cdd:PRK07764  666 GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPA--ADDPVPLPP 743

                         170       180
                  ....*....|....*....|....*....
gi 86613790   583 GKLGPLGAPGEDGRPGPPGSIGIRGQPGS 611
Cdd:PRK07764  744 EPDDPPDPAGAPAQPPPPPAPAPAAAPAA 772
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 490-601 8.92e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 40.43  E-value: 8.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   490 GPIGPPGEEGKRGP-RGDPGTVGPPGPMGERGAPGNRGFPGSDGLPG---PKGAQGERGPVGSSGPK-GGQGDPGRPgEP 564
Cdd:PRK14959  376 GGASAPSGSAAEGPaSGGAATIPTPGTQGPQGTAPAAGMTPSSAAPAtpaPSAAPSPRVPWDDAPPApPRSGIPPRP-AP 454

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 86613790   565 GLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPG 601
Cdd:PRK14959  455 RMPEASPVPGAPDSVASASDAPPTLGDPSDTAEHTPS 491
PHA03169 PHA03169
hypothetical protein; Provisional
 313-499 9.24e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.34  E-value: 9.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   313 GAPGAKGEAGPTGPmGAMGPLGPRGMPGERGRLGPQGAPGKRGAHGMPGKPGPMGPLGIPGSSGFPGNPGMKGEAGPTGA 392
Cdd:PHA03169   82 GEKEERGQGGPSGS-GSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPN 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790   393 RGPEGPQGQRGETGPPGPAGSQGLPGAVGTDGTPGAKGPTGSAGTSGPPGLAGPPGSPGPQGSTGPQGIRGQSGDPGVPG 472
Cdd:PHA03169  161 QQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEP 240

                         170       180
                  ....*....|....*....|....*..
gi 86613790   473 FKGEAGPKGEPGPHGIQGPIGPPGEEG 499
Cdd:PHA03169  241 EREGPPFPGHRSHSYTVVGWKPSTRPG 267
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 494-585 9.49e-03

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 40.12  E-value: 9.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86613790  494 PPGEEGKRgprgdPGTVGPPGPMGERGAPGNrgfpgsDGLPGPKGAQGERGPVGSSGPKGGQGDPGRPGEPGLPGARGLT 573
Cdd:cd05922  277 PPERILEK-----PGSIGLAIPGGEFEILDD------DGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHT 345

                         90
                 ....*....|..
gi 86613790  574 GNPGVQGPEGKL 585
Cdd:cd05922  346 GDLARRDEDGFL 357
 
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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