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Conserved domains on  [gi|1907153777|ref|XP_036019459|]
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collagen alpha-1(XVI) chain isoform X6 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 103-306 2.74e-21

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 98.05  E-value: 2.74e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  103 GEKGEPGSPG-FGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGDgctacpslqgal 181
Cdd:NF038329   117 GEKGEPGPAGpAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA------------ 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  182 tdvsglPGKPGPKGEPGPEG-VGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGP 260
Cdd:NF038329   185 ------KGPAGEKGPQGPRGeTGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGK 258

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907153777  261 PGSAGEKGAQGSPGPKGAIGPMGPPGA-------GVSGPPGQKGSRGEKGEPG 306
Cdd:NF038329   259 DGPRGDRGEAGPDGPDGKDGERGPVGPagkdgqnGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 492-711 1.58e-18

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 89.58  E-value: 1.58e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  492 GSPGLPGLQGERGLTGLTGDKGEPGPPGQPGYPGAMGPPGLPGIKGERGYTGPSGEKGESGPPGSEGLPGPQGPAGPRGE 571
Cdd:NF038329   120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  572 RGPQGSSGEKGDQGFQGQPGFPGPPGPPGFPGKaGAPGPPGPQAEKGSEGIRGPSGLPGSPGPPGPPGIQGPAGLDGLDG 651
Cdd:NF038329   200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  652 KDGKPGLRGDPGPAGPPGLMGPPGFKGKTGHPGLPGPKGDCGKPGPPGSSGRPGAEGEPG 711
Cdd:NF038329   279 ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 22-163 3.44e-10

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: 63.39  E-value: 3.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777   22 GPSPGHGLPGLPGTSGIPGPRGlKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGEPCEPCTALSELQDGDMrvvHLPGP 101
Cdd:NF038329   210 GPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER---GPVGP 285

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907153777  102 AGEKGEPGSPGfgLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGP 163
Cdd:NF038329   286 AGKDGQNGKDG--LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 648-863 6.96e-09

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: 59.53  E-value: 6.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  648 GLDGKDGKPGLRGDPGPAGPPGLMGPPGFKGKTGHPGLPGPKGDCGKPGPPGSSGRPGAEGEPGAMGPQGRPGPPGHLGP 727
Cdd:NF038329   126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  728 QGPPGQpgppglstVGLKGDRGVPGERGLAGlPGQPGTPGHPGPPGEPGSDGAAGKEGPPGKQGLYGPPGPKGDPGPAGQ 807
Cdd:NF038329   206 QGPAGP--------AGPDGEAGPAGEDGPAG-PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907153777  808 KGQAGEKGRSGMPGGPGKSGSMGPIGPPGPAGERGHPGSPGPAGNPGLPGLPGSMG 863
Cdd:NF038329   277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 904-956 2.06e-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: 2.06e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907153777  904 PGRPGPPGKDGAPGRPGAPGSPGLPGQIGREGRQGLPGMRGLPGTKGEKGDIG 956
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 103-306 2.74e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 98.05  E-value: 2.74e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  103 GEKGEPGSPG-FGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGDgctacpslqgal 181
Cdd:NF038329   117 GEKGEPGPAGpAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA------------ 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  182 tdvsglPGKPGPKGEPGPEG-VGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGP 260
Cdd:NF038329   185 ------KGPAGEKGPQGPRGeTGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGK 258

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907153777  261 PGSAGEKGAQGSPGPKGAIGPMGPPGA-------GVSGPPGQKGSRGEKGEPG 306
Cdd:NF038329   259 DGPRGDRGEAGPDGPDGKDGERGPVGPagkdgqnGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 26-286 4.39e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 94.59  E-value: 4.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777   26 GHGLPGLPGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGEpcepctalselqdgdmrvvhlPGPAGEK 105
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGP---------------------QGEAGPQ 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  106 GEPGSpgfglPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGDGCTacpslqgaltdvs 185
Cdd:NF038329   174 GPAGK-----DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQ------------- 235

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  186 GLPGKPGPKGEPGPEG-VGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPgtGAEGPQGEPGTQGLPGTQGLPGPRGPPGSA 264
Cdd:NF038329   236 GPDGDPGPTGEDGPQGpDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV--GPAGKDGQNGKDGLPGKDGKDGQNGKDGLP 313

                          250       260
                   ....*....|....*....|..
gi 1907153777  265 GEKGAQGSPGPKGAIGPMGPPG 286
Cdd:NF038329   314 GKDGKDGQPGKDGLPGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 22-232 1.82e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 92.66  E-value: 1.82e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777   22 GPSPGHGLPGLPGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIK---GAKGEPCEPCTALSELQDGDMRVVHL 98
Cdd:NF038329   129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDgeaGAKGPAGEKGPQGPRGETGPAGEQGP 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777   99 PGPAGEKGEPGSPGFGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGDGCTACPSLQ 178
Cdd:NF038329   209 AGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK 288

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907153777  179 GALTDVSGLPGKPGPKGEPGPEGVghPGKPGQPGLPGVQGPPGPKGTQGEPGPP 232
Cdd:NF038329   289 DGQNGKDGLPGKDGKDGQNGKDGL--PGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 492-711 1.58e-18

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 89.58  E-value: 1.58e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  492 GSPGLPGLQGERGLTGLTGDKGEPGPPGQPGYPGAMGPPGLPGIKGERGYTGPSGEKGESGPPGSEGLPGPQGPAGPRGE 571
Cdd:NF038329   120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  572 RGPQGSSGEKGDQGFQGQPGFPGPPGPPGFPGKaGAPGPPGPQAEKGSEGIRGPSGLPGSPGPPGPPGIQGPAGLDGLDG 651
Cdd:NF038329   200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  652 KDGKPGLRGDPGPAGPPGLMGPPGFKGKTGHPGLPGPKGDCGKPGPPGSSGRPGAEGEPG 711
Cdd:NF038329   279 ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 498-711 4.90e-17

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: 84.96  E-value: 4.90e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  498 GLQGERGLTGLTGDKGEPGPPGQPGYPGAMGPPGLPGIKGERGYTGPSGEKGESGPPGSEGLPGPQGPAGPRGERGPQGS 577
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  578 SGEKGDQGFQGQPGFPGPPGPPGFPGKAGAPGPP-----GPQAEKGSEGIRGPSGLPGSPGPPGPPGIQGPAGLDGLDGK 652
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907153777  653 DGKPGLRGDPGPAGPPGLMGPPGFKGKTGHPGLPGPKGDCGKPGPPGSSGRPGAEGEPG 711
Cdd:NF038329   277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 528-712 4.31e-15

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 78.79  E-value: 4.31e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  528 GPPGLPGIKGERGYTGPSGEKGESGPPGSEGLPGPQGPAGPRGERGPQGSSGEKGDQGFQGQPGFPGPPGPPGFPGKAGA 607
Cdd:NF038329   126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  608 PGPPGPQAEKGSEGIRGPSGLPGSPGPP--GPPGIQGPAGLDGLDGKDGKPGLRGDPGPAGPPGLMGPPGFKGKTGHPGL 685
Cdd:NF038329   206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285

                          170       180
                   ....*....|....*....|....*..
gi 1907153777  686 PGPKGDCGKPGPPGSSGRPGAEGEPGA 712
Cdd:NF038329   286 AGKDGQNGKDGLPGKDGKDGQNGKDGL 312
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 546-849 2.37e-11

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: 67.24  E-value: 2.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  546 GEKGESGPPGSEGLPGPQGPAGPRGERGPQGSSGEKGDQGfqgqpgfpgppgppgfpgKAGAPGPPGPQAEKGSEGirgp 625
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG------------------ERGEKGPAGPQGEAGPQG---- 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  626 sglpgspgppgppgiqgpagldgLDGKDGKPGLRGDPGPagppglmgppgfKGKTGHPGLPGPKGDCGKPGPPGSSGRPG 705
Cdd:NF038329   175 -----------------------PAGKDGEAGAKGPAGE------------KGPQGPRGETGPAGEQGPAGPAGPDGEAG 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  706 AEGEPGAMGPQGRPGPPGHlgpqgppgqpgppglstvGLKGDRGVPGERGLAGLPGQPGTPGHPGPPGEPGSDGAAGKEG 785
Cdd:NF038329   220 PAGEDGPAGPAGDGQQGPD------------------GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907153777  786 PPGKQGLYGPPGPKGDPGPAGQKGQAgekGRSGMPGGPGKSGSMGPIGPPGPAGERGHPGSPGP 849
Cdd:NF038329   282 PVGPAGKDGQNGKDGLPGKDGKDGQN---GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 22-163 3.44e-10

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: 63.39  E-value: 3.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777   22 GPSPGHGLPGLPGTSGIPGPRGlKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGEPCEPCTALSELQDGDMrvvHLPGP 101
Cdd:NF038329   210 GPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER---GPVGP 285

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907153777  102 AGEKGEPGSPGfgLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGP 163
Cdd:NF038329   286 AGKDGQNGKDG--LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 648-863 6.96e-09

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: 59.53  E-value: 6.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  648 GLDGKDGKPGLRGDPGPAGPPGLMGPPGFKGKTGHPGLPGPKGDCGKPGPPGSSGRPGAEGEPGAMGPQGRPGPPGHLGP 727
Cdd:NF038329   126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  728 QGPPGQpgppglstVGLKGDRGVPGERGLAGlPGQPGTPGHPGPPGEPGSDGAAGKEGPPGKQGLYGPPGPKGDPGPAGQ 807
Cdd:NF038329   206 QGPAGP--------AGPDGEAGPAGEDGPAG-PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907153777  808 KGQAGEKGRSGMPGGPGKSGSMGPIGPPGPAGERGHPGSPGPAGNPGLPGLPGSMG 863
Cdd:NF038329   277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 742-956 1.81e-08

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: 57.99  E-value: 1.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  742 VGLKGDRGVPGERGLAGLPGQPGTPGHPGPPGEPGSDGAAGKEGPPGKQGLYGPPGPKGDPGPAGQKGQAGEKGRSGMPG 821
Cdd:NF038329   125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  822 GPGKSGSMGPIGPPGPAGERGHPGSP-----GPAGNPGLPGLPGSMG-DMVNYDDIKRFIRQEIIKlfdermayytsrmQ 895
Cdd:NF038329   205 EQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGpDGPAGKDGPRGDRGEAGP-------------D 271

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907153777  896 FPMEVAAAPGRPGPPGKDGAPGRPGAPGSPGLPGQIGREGRQGLPGMRGLPGTKGEKGDIG 956
Cdd:NF038329   272 GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 752-956 5.19e-08

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: 56.45  E-value: 5.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  752 GERGLAGLPGQPGTPGHPGPPGEPGSDGAAGKEGPPGKQGLYGPPGPKGDPGPAGQKGQAGEKGRSGMPGGPGKSGSMGP 831
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  832 IGPPGPAGERGHPGSPGPAGNPGLPGLPGSMGDMVNYDDIKRfirqeiiklfdermayytsRMQFPMEVAAAPGRPGPPG 911
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD-------------------GDPGPTGEDGPQGPDGPAG 257

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907153777  912 KDGAPGRPGAPGSPGLPGQIGREGRQGLPGMRGLPGTKGEKGDIG 956
Cdd:NF038329   258 KDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 527-580 2.73e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.56  E-value: 2.73e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907153777  527 MGPPGLPGIKGERGYTGPSGEKGESGPPGSEGLPGPQGPAGPRGERGPQGSSGE 580
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 904-956 2.06e-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: 2.06e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907153777  904 PGRPGPPGKDGAPGRPGAPGSPGLPGQIGREGRQGLPGMRGLPGTKGEKGDIG 956
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 82-305 3.06e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 3.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777   82 CTALSELQDGDMRVVHLPGPAgekgePGSPGFGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPA 161
Cdd:PRK07764   571 VTALAEELGGDWQVEAVVGPA-----PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAP 645

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  162 GPKGEKGDGctACPSLQGALTDVSGLPGKPGPKGEPGPEGVGHPGKPGQPGlPGVQGPPGPKGTQGEPGPPGTGAEGPQG 241
Cdd:PRK07764   646 GVAAPEHHP--KHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA-GAAPAQPAPAPAATPPAGQADDPAAQPP 722

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907153777  242 EPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGAiGPMGPPGAGVSGPPGQKGSRGEKGEP 305
Cdd:PRK07764   723 QAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPP-PPPAPAPAAAPAAAPPPSPPSEEEEM 785
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 192-250 3.14e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 3.14e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  192 GPKGEPGPegvghPGKPGQPGLPGVQGPPGPKGTQGEPGPPG-TGAEGPQGEPGTQGLPG 250
Cdd:pfam01391    1 GPPGPPGP-----PGPPGPPGPPGPPGPPGPPGPPGEPGPPGpPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
33-293 3.46e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 44.25  E-value: 3.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777   33 PGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAkgepcepctalselqdgdmrvvhlPGPAGEKGEPGSPG 112
Cdd:COG5164      6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRP------------------------AQNQGSTTPAGNTG 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  113 FGLP-GKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGdgctacpslqGALTDVSGLPGKP 191
Cdd:COG5164     62 GTRPaGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATG----------PPDDGGSTTPPSG 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  192 GPKGEPGPEGVGHPGkPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQG 271
Cdd:COG5164    132 GSTTPPGDGGSTPPG-PGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVK 210

                          250       260
                   ....*....|....*....|..
gi 1907153777  272 SPGPKGAIGPmgPPGAGVSGPP 293
Cdd:COG5164    211 KDDKNGKGNP--PDDRGGKTGP 230
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 28-81 5.61e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 5.61e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907153777   28 GLPGLPGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGEPCEP 81
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 224-575 1.27e-03

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: 42.58  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  224 GTQGEPGPpgTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGAIGPMGPPGAgvSGPPGQKGSRGEKG 303
Cdd:NF038329   117 GEKGEPGP--AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK--DGEAGAKGPAGEKG 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  304 EPGEcscpsRGEPIFSGMPGAPGLwmgsssqpgpqgppgvpgppgppgmpglqgvPGHNGLPGQPGLTAELGSlpiekhl 383
Cdd:NF038329   193 PQGP-----RGETGPAGEQGPAGP-------------------------------AGPDGEAGPAGEDGPAGP------- 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  384 lksiCGDCAQGQTAHPAfllEKGEKGDQGIPGVPGFDncarcfiererpraeeargdnsegepgcsgspglpgppgmpgq 463
Cdd:NF038329   230 ----AGDGQQGPDGDPG---PTGEDGPQGPDGPAGKD------------------------------------------- 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  464 rgeegppgmrgspgppgpigppgfpgavGSPGLPGLQGERGLTGLTGDKGEPGPPGQPGYPGAMGPPGLPGIKGERGYTG 543
Cdd:NF038329   260 ----------------------------GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1907153777  544 PSGEKGESGPPGSEGLPGPQGPAGPRGERGPQ 575
Cdd:NF038329   312 LPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 807-1008 3.04e-03

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: 41.43  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  807 QKGQAGEKGRSGMPGGPGKSGSMGPIGPPGPAGERGHPGSPGPAGNPGLPGLPGSMGDmvnyddikrfirqeiiklfder 886
Cdd:NF038329   112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE---------------------- 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  887 mayytsrmqfpmevaaaPGRPGPPGKDGAPGRPGAPGSPGLPGQIGREGRQGLPGMRGLPGTKGEKGDIG-VGIAGENGL 965
Cdd:NF038329   170 -----------------AGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGeDGPAGPAGD 232

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1907153777  966 PGPPGPQGPPGYGKMGATGPMGQQGIPGIPGPPGPMGQPGKAG 1008
Cdd:NF038329   233 GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 103-306 2.74e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 98.05  E-value: 2.74e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  103 GEKGEPGSPG-FGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGDgctacpslqgal 181
Cdd:NF038329   117 GEKGEPGPAGpAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA------------ 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  182 tdvsglPGKPGPKGEPGPEG-VGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGP 260
Cdd:NF038329   185 ------KGPAGEKGPQGPRGeTGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGK 258

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907153777  261 PGSAGEKGAQGSPGPKGAIGPMGPPGA-------GVSGPPGQKGSRGEKGEPG 306
Cdd:NF038329   259 DGPRGDRGEAGPDGPDGKDGERGPVGPagkdgqnGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 26-286 4.39e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 94.59  E-value: 4.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777   26 GHGLPGLPGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGEpcepctalselqdgdmrvvhlPGPAGEK 105
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGP---------------------QGEAGPQ 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  106 GEPGSpgfglPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGDGCTacpslqgaltdvs 185
Cdd:NF038329   174 GPAGK-----DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQ------------- 235

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  186 GLPGKPGPKGEPGPEG-VGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPgtGAEGPQGEPGTQGLPGTQGLPGPRGPPGSA 264
Cdd:NF038329   236 GPDGDPGPTGEDGPQGpDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV--GPAGKDGQNGKDGLPGKDGKDGQNGKDGLP 313

                          250       260
                   ....*....|....*....|..
gi 1907153777  265 GEKGAQGSPGPKGAIGPMGPPG 286
Cdd:NF038329   314 GKDGKDGQPGKDGLPGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 22-232 1.82e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 92.66  E-value: 1.82e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777   22 GPSPGHGLPGLPGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIK---GAKGEPCEPCTALSELQDGDMRVVHL 98
Cdd:NF038329   129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDgeaGAKGPAGEKGPQGPRGETGPAGEQGP 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777   99 PGPAGEKGEPGSPGFGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGDGCTACPSLQ 178
Cdd:NF038329   209 AGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK 288

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907153777  179 GALTDVSGLPGKPGPKGEPGPEGVghPGKPGQPGLPGVQGPPGPKGTQGEPGPP 232
Cdd:NF038329   289 DGQNGKDGLPGKDGKDGQNGKDGL--PGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 492-711 1.58e-18

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 89.58  E-value: 1.58e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  492 GSPGLPGLQGERGLTGLTGDKGEPGPPGQPGYPGAMGPPGLPGIKGERGYTGPSGEKGESGPPGSEGLPGPQGPAGPRGE 571
Cdd:NF038329   120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  572 RGPQGSSGEKGDQGFQGQPGFPGPPGPPGFPGKaGAPGPPGPQAEKGSEGIRGPSGLPGSPGPPGPPGIQGPAGLDGLDG 651
Cdd:NF038329   200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  652 KDGKPGLRGDPGPAGPPGLMGPPGFKGKTGHPGLPGPKGDCGKPGPPGSSGRPGAEGEPG 711
Cdd:NF038329   279 ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 498-711 4.90e-17

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: 84.96  E-value: 4.90e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  498 GLQGERGLTGLTGDKGEPGPPGQPGYPGAMGPPGLPGIKGERGYTGPSGEKGESGPPGSEGLPGPQGPAGPRGERGPQGS 577
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  578 SGEKGDQGFQGQPGFPGPPGPPGFPGKAGAPGPP-----GPQAEKGSEGIRGPSGLPGSPGPPGPPGIQGPAGLDGLDGK 652
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907153777  653 DGKPGLRGDPGPAGPPGLMGPPGFKGKTGHPGLPGPKGDCGKPGPPGSSGRPGAEGEPG 711
Cdd:NF038329   277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 528-712 4.31e-15

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 78.79  E-value: 4.31e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  528 GPPGLPGIKGERGYTGPSGEKGESGPPGSEGLPGPQGPAGPRGERGPQGSSGEKGDQGFQGQPGFPGPPGPPGFPGKAGA 607
Cdd:NF038329   126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  608 PGPPGPQAEKGSEGIRGPSGLPGSPGPP--GPPGIQGPAGLDGLDGKDGKPGLRGDPGPAGPPGLMGPPGFKGKTGHPGL 685
Cdd:NF038329   206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285

                          170       180
                   ....*....|....*....|....*..
gi 1907153777  686 PGPKGDCGKPGPPGSSGRPGAEGEPGA 712
Cdd:NF038329   286 AGKDGQNGKDGLPGKDGKDGQNGKDGL 312
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 546-849 2.37e-11

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: 67.24  E-value: 2.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  546 GEKGESGPPGSEGLPGPQGPAGPRGERGPQGSSGEKGDQGfqgqpgfpgppgppgfpgKAGAPGPPGPQAEKGSEGirgp 625
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG------------------ERGEKGPAGPQGEAGPQG---- 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  626 sglpgspgppgppgiqgpagldgLDGKDGKPGLRGDPGPagppglmgppgfKGKTGHPGLPGPKGDCGKPGPPGSSGRPG 705
Cdd:NF038329   175 -----------------------PAGKDGEAGAKGPAGE------------KGPQGPRGETGPAGEQGPAGPAGPDGEAG 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  706 AEGEPGAMGPQGRPGPPGHlgpqgppgqpgppglstvGLKGDRGVPGERGLAGLPGQPGTPGHPGPPGEPGSDGAAGKEG 785
Cdd:NF038329   220 PAGEDGPAGPAGDGQQGPD------------------GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907153777  786 PPGKQGLYGPPGPKGDPGPAGQKGQAgekGRSGMPGGPGKSGSMGPIGPPGPAGERGHPGSPGP 849
Cdd:NF038329   282 PVGPAGKDGQNGKDGLPGKDGKDGQN---GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 22-163 3.44e-10

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: 63.39  E-value: 3.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777   22 GPSPGHGLPGLPGTSGIPGPRGlKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGEPCEPCTALSELQDGDMrvvHLPGP 101
Cdd:NF038329   210 GPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER---GPVGP 285

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907153777  102 AGEKGEPGSPGfgLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGP 163
Cdd:NF038329   286 AGKDGQNGKDG--LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 648-863 6.96e-09

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: 59.53  E-value: 6.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  648 GLDGKDGKPGLRGDPGPAGPPGLMGPPGFKGKTGHPGLPGPKGDCGKPGPPGSSGRPGAEGEPGAMGPQGRPGPPGHLGP 727
Cdd:NF038329   126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  728 QGPPGQpgppglstVGLKGDRGVPGERGLAGlPGQPGTPGHPGPPGEPGSDGAAGKEGPPGKQGLYGPPGPKGDPGPAGQ 807
Cdd:NF038329   206 QGPAGP--------AGPDGEAGPAGEDGPAG-PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907153777  808 KGQAGEKGRSGMPGGPGKSGSMGPIGPPGPAGERGHPGSPGPAGNPGLPGLPGSMG 863
Cdd:NF038329   277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 742-956 1.81e-08

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: 57.99  E-value: 1.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  742 VGLKGDRGVPGERGLAGLPGQPGTPGHPGPPGEPGSDGAAGKEGPPGKQGLYGPPGPKGDPGPAGQKGQAGEKGRSGMPG 821
Cdd:NF038329   125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  822 GPGKSGSMGPIGPPGPAGERGHPGSP-----GPAGNPGLPGLPGSMG-DMVNYDDIKRFIRQEIIKlfdermayytsrmQ 895
Cdd:NF038329   205 EQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGpDGPAGKDGPRGDRGEAGP-------------D 271

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907153777  896 FPMEVAAAPGRPGPPGKDGAPGRPGAPGSPGLPGQIGREGRQGLPGMRGLPGTKGEKGDIG 956
Cdd:NF038329   272 GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 752-956 5.19e-08

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: 56.45  E-value: 5.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  752 GERGLAGLPGQPGTPGHPGPPGEPGSDGAAGKEGPPGKQGLYGPPGPKGDPGPAGQKGQAGEKGRSGMPGGPGKSGSMGP 831
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  832 IGPPGPAGERGHPGSPGPAGNPGLPGLPGSMGDMVNYDDIKRfirqeiiklfdermayytsRMQFPMEVAAAPGRPGPPG 911
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD-------------------GDPGPTGEDGPQGPDGPAG 257

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907153777  912 KDGAPGRPGAPGSPGLPGQIGREGRQGLPGMRGLPGTKGEKGDIG 956
Cdd:NF038329   258 KDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 527-580 2.73e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.56  E-value: 2.73e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907153777  527 MGPPGLPGIKGERGYTGPSGEKGESGPPGSEGLPGPQGPAGPRGERGPQGSSGE 580
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 904-956 2.06e-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: 2.06e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907153777  904 PGRPGPPGKDGAPGRPGAPGSPGLPGQIGREGRQGLPGMRGLPGTKGEKGDIG 956
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 82-305 3.06e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 3.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777   82 CTALSELQDGDMRVVHLPGPAgekgePGSPGFGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPA 161
Cdd:PRK07764   571 VTALAEELGGDWQVEAVVGPA-----PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAP 645

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  162 GPKGEKGDGctACPSLQGALTDVSGLPGKPGPKGEPGPEGVGHPGKPGQPGlPGVQGPPGPKGTQGEPGPPGTGAEGPQG 241
Cdd:PRK07764   646 GVAAPEHHP--KHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA-GAAPAQPAPAPAATPPAGQADDPAAQPP 722

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907153777  242 EPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGAiGPMGPPGAGVSGPPGQKGSRGEKGEP 305
Cdd:PRK07764   723 QAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPP-PPPAPAPAAAPAAAPPPSPPSEEEEM 785
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 192-250 3.14e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 3.14e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  192 GPKGEPGPegvghPGKPGQPGLPGVQGPPGPKGTQGEPGPPG-TGAEGPQGEPGTQGLPG 250
Cdd:pfam01391    1 GPPGPPGP-----PGPPGPPGPPGPPGPPGPPGPPGEPGPPGpPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
33-293 3.46e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 44.25  E-value: 3.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777   33 PGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAkgepcepctalselqdgdmrvvhlPGPAGEKGEPGSPG 112
Cdd:COG5164      6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRP------------------------AQNQGSTTPAGNTG 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  113 FGLP-GKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGdgctacpslqGALTDVSGLPGKP 191
Cdd:COG5164     62 GTRPaGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATG----------PPDDGGSTTPPSG 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  192 GPKGEPGPEGVGHPGkPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQG 271
Cdd:COG5164    132 GSTTPPGDGGSTPPG-PGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVK 210

                          250       260
                   ....*....|....*....|..
gi 1907153777  272 SPGPKGAIGPmgPPGAGVSGPP 293
Cdd:COG5164    211 KDDKNGKGNP--PDDRGGKTGP 230
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 903-953 4.18e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 4.18e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907153777  903 APGRPGPPGKDGAPGRPGAPGSPGLPGQIGREGRQGLPGMRGLPGTKGEKG 953
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 28-81 5.61e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 5.61e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907153777   28 GLPGLPGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGEPCEP 81
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 22-78 7.54e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 7.54e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907153777   22 GPSPGHGLPGLPGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGEP 78
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 28-81 8.40e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 8.40e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907153777   28 GLPGLPGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGEPCEP 81
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 189-307 8.72e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 8.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  189 GKPGPKGEPGPEGVGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKG 268
Cdd:PRK07764   590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907153777  269 AQGSPGPKGAIGPMGPPGAGVSGPPGQKGSRGEKGEPGE 307
Cdd:PRK07764   670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAAT 708
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 98-155 9.00e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 9.00e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907153777   98 LPGPAGEKGEPGSPGFglPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEP 155
Cdd:pfam01391    2 PPGPPGPPGPPGPPGP--PGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 120-168 9.09e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 9.09e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1907153777  120 GKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKG 168
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 114-168 1.03e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 1.03e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907153777  114 GLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKG 168
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 224-575 1.27e-03

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: 42.58  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  224 GTQGEPGPpgTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGAIGPMGPPGAgvSGPPGQKGSRGEKG 303
Cdd:NF038329   117 GEKGEPGP--AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK--DGEAGAKGPAGEKG 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  304 EPGEcscpsRGEPIFSGMPGAPGLwmgsssqpgpqgppgvpgppgppgmpglqgvPGHNGLPGQPGLTAELGSlpiekhl 383
Cdd:NF038329   193 PQGP-----RGETGPAGEQGPAGP-------------------------------AGPDGEAGPAGEDGPAGP------- 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  384 lksiCGDCAQGQTAHPAfllEKGEKGDQGIPGVPGFDncarcfiererpraeeargdnsegepgcsgspglpgppgmpgq 463
Cdd:NF038329   230 ----AGDGQQGPDGDPG---PTGEDGPQGPDGPAGKD------------------------------------------- 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  464 rgeegppgmrgspgppgpigppgfpgavGSPGLPGLQGERGLTGLTGDKGEPGPPGQPGYPGAMGPPGLPGIKGERGYTG 543
Cdd:NF038329   260 ----------------------------GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1907153777  544 PSGEKGESGPPGSEGLPGPQGPAGPRGERGPQ 575
Cdd:NF038329   312 LPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 114-166 1.94e-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: 37.47  E-value: 1.94e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907153777  114 GLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGE 166
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 528-572 2.25e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 2.25e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1907153777  528 GPPGLPGIKGERGYTGPSGEKGESGPPGSEGLPGPQGPAGPRGER 572
Cdd:pfam01391   13 GPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 103-161 2.46e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 2.46e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907153777  103 GEKGEPGSPGFglPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPA 161
Cdd:pfam01391    1 GPPGPPGPPGP--PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 33-243 3.02e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 3.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777   33 PGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAkGEPCEPCTAlselQDGDMRVVHLPGPAGEKGEPGSPG 112
Cdd:PRK07764   592 PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAA-AAPAEASAA----PAPGVAAPEHHPKHVAVPDASDGG 666

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  113 FGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGDGCTACPSLQGALTDVSGLPGKPG 192
Cdd:PRK07764   667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD 746

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907153777  193 PKGEPGPEGVGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEP 243
Cdd:PRK07764   747 DPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDED 797
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 807-1008 3.04e-03

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: 41.43  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  807 QKGQAGEKGRSGMPGGPGKSGSMGPIGPPGPAGERGHPGSPGPAGNPGLPGLPGSMGDmvnyddikrfirqeiiklfder 886
Cdd:NF038329   112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE---------------------- 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  887 mayytsrmqfpmevaaaPGRPGPPGKDGAPGRPGAPGSPGLPGQIGREGRQGLPGMRGLPGTKGEKGDIG-VGIAGENGL 965
Cdd:NF038329   170 -----------------AGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGeDGPAGPAGD 232

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1907153777  966 PGPPGPQGPPGYGKMGATGPMGQQGIPGIPGPPGPMGQPGKAG 1008
Cdd:NF038329   233 GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 151-326 5.90e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 5.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  151 ISGEPGIRGPAGPKGEKGDGCtacPSLQGALTDVSGLPGKPGPKGEPGPegvGHPGKPGQPGLPGVQGPPGPKGTQGEPG 230
Cdd:PRK07764   588 VGPAPGAAGGEGPPAPASSGP---PEEAARPAAPAAPAAPAAPAPAGAA---AAPAEASAAPAPGVAAPEHHPKHVAVPD 661

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  231 PPGTGAEGPqGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGAiGPMGPPGAGVSGPPGQKGSRGEKGEPGECSC 310
Cdd:PRK07764   662 ASDGGDGWP-AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAAT-PPAGQADDPAAQPPQAAQGASAPSPAADDPV 739

                          170
                   ....*....|....*.
gi 1907153777  311 PSRGEPIFSGMPGAPG 326
Cdd:PRK07764   740 PLPPEPDDPPDPAGAP 755
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 185-368 9.82e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.97  E-value: 9.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  185 SGLPGKPGPKGEPGPEGVGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSA 264
Cdd:PRK07764   592 PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA 671

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153777  265 GEKGAQGSPGPKGAIGPMGPPGAGVSGPPGQkgSRGEKGEPGECSCPSRGEPIFSGMPGAPGLWMGSSSQPGPQGPPGVP 344
Cdd:PRK07764   672 KAGGAAPAAPPPAPAPAAPAAPAGAAPAQPA--PAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749

                          170       180
                   ....*....|....*....|....
gi 1907153777  345 GPPGPPGMPGLQGVPGHNGLPGQP 368
Cdd:PRK07764   750 DPAGAPAQPPPPPAPAPAAAPAAA 773
 
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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