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Conserved domains on  [gi|1907153774|ref|XP_036019458|]
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collagen alpha-1(XVI) chain isoform X5 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 50-231 6.86e-57

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 194.50  E-value: 6.86e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774    50 GFNLIRRLNLM-KTSAIKKIRNPKGP-LILRLG-AAPVTQPTRRVFPRGLPEEFALVLTVLLKKhtfRNTWYLFQVTDAN 126
Cdd:smart00210    1 GQDLLQVFDLPsLSFAIRQVVGPEPGsPAYRLGdPALVPQPTRDLFPSGLPEDFSLLTTFRQTP---KSRGVLFAIYDAQ 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774   127 GYPQISLEVNSQERSLELRAQGQDGDFVSCIFPVPQLFDLRWHKLMLSVAGRVASVHVDCVSASSQPLGPR--QSIRPGG 204
Cdd:smart00210   78 NVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPgqPPIDTDG 157

                           170       180
                    ....*....|....*....|....*..
gi 1907153774   205 HVFLGLDAEQGKPVSFDLQQAHIYCDP 231
Cdd:smart00210  158 IEVRGAQAADRKPFQGDLQQLKIVCDP 184
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 665-868 2.64e-28

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 119.62  E-value: 2.64e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  665 GEKGEPGSPG-FGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGDgctacpslqgal 743
Cdd:NF038329   117 GEKGEPGPAGpAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA------------ 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  744 tdvsglPGKPGPKGEPGPEG-VGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGP 822
Cdd:NF038329   185 ------KGPAGEKGPQGPRGeTGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGK 258

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907153774  823 PGSAGEKGAQGSPGPKGAIGPMGPPGA-------GVSGPPGQKGSRGEKGEPG 868
Cdd:NF038329   259 DGPRGDRGEAGPDGPDGKDGERGPVGPagkdgqnGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 503-725 8.02e-24

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 105.76  E-value: 8.02e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  503 KGEKGDPCEVCPTLPEGSQNFVGLPGKPGPKGEPGDPAPAWEGlGTVGLKGDRGDPGIQGMKGEKGEPCSSCSSGVGaqh 582
Cdd:NF038329   134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA-GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA--- 209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  583 lGPSPGHGLPGLPGTSGIPGPRGlKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGEPCEPCTALSELQDGDMrvvHLPG 662
Cdd:NF038329   210 -GPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER---GPVG 284

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907153774  663 PAGEKGEPGSPGfgLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGP 725
Cdd:NF038329   285 PAGKDGQNGKDG--LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 331-541 3.81e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 57.22  E-value: 3.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  331 GPSGLKGGKGERGLTGPSGPKGEKGARGNDCVRVSPDAplqcvEGPKGEKGESGDLGPPGLPGPTGQKGQKGEKGDGGLK 410
Cdd:NF038329   147 GPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA-----KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  411 GLPGKPGRDGRP--GEICVIGPKGQKGDPGFVGPEGLAGEPGPPGLPGPPGIGLPGTPGDPGGPPGPKGEKGSSGIPGKE 488
Cdd:NF038329   222 GEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD 301

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907153774  489 GPGGKPGKPGVPGTKGEKGDPCEvcptlpegsqnfVGLPGKPGPKGEPGDPAP 541
Cdd:NF038329   302 GKDGQNGKDGLPGKDGKDGQPGK------------DGLPGKDGKDGQPGKPAP 342
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 799-982 7.84e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 56.07  E-value: 7.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  799 EGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGAIGPMGPPG----AGVSGPPGQKGSRGEKGEPGECSCP- 873
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGpqgeAGPQGPAGKDGEAGAKGPAGEKGPQg 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  874 SRGEPIFSGMPGAPGLwmGSSSQPGPQGPPGVPGPPGPPGMPGLQGVPGHNGLPGQPGLTAELGSlpiekhllksicgDC 953
Cdd:NF038329   196 PRGETGPAGEQGPAGP--AGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGK-------------DG 260

                          170       180
                   ....*....|....*....|....*....
gi 1907153774  954 AQGQTAHPAFLLEKGEKGDQGIPGVPGFD 982
Cdd:NF038329   261 PRGDRGEAGPDGPDGKDGERGPVGPAGKD 289
 
Name Accession Description Interval E-value
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 50-231 6.86e-57

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 194.50  E-value: 6.86e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774    50 GFNLIRRLNLM-KTSAIKKIRNPKGP-LILRLG-AAPVTQPTRRVFPRGLPEEFALVLTVLLKKhtfRNTWYLFQVTDAN 126
Cdd:smart00210    1 GQDLLQVFDLPsLSFAIRQVVGPEPGsPAYRLGdPALVPQPTRDLFPSGLPEDFSLLTTFRQTP---KSRGVLFAIYDAQ 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774   127 GYPQISLEVNSQERSLELRAQGQDGDFVSCIFPVPQLFDLRWHKLMLSVAGRVASVHVDCVSASSQPLGPR--QSIRPGG 204
Cdd:smart00210   78 NVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPgqPPIDTDG 157

                           170       180
                    ....*....|....*....|....*..
gi 1907153774   205 HVFLGLDAEQGKPVSFDLQQAHIYCDP 231
Cdd:smart00210  158 IEVRGAQAADRKPFQGDLQQLKIVCDP 184
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 665-868 2.64e-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: 2.64e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  665 GEKGEPGSPG-FGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGDgctacpslqgal 743
Cdd:NF038329   117 GEKGEPGPAGpAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA------------ 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  744 tdvsglPGKPGPKGEPGPEG-VGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGP 822
Cdd:NF038329   185 ------KGPAGEKGPQGPRGeTGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGK 258

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907153774  823 PGSAGEKGAQGSPGPKGAIGPMGPPGA-------GVSGPPGQKGSRGEKGEPG 868
Cdd:NF038329   259 DGPRGDRGEAGPDGPDGKDGERGPVGPagkdgqnGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 544-838 2.45e-27

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 116.54  E-value: 2.45e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  544 EGLGTVGLKGDRGDPGIQGMKGEKGEPcsscssgvgaqhlgpspghGLPGLPGTSGIPGPRGLKGEKGSFGDTGPAGVPG 623
Cdd:NF038329   108 EGLQQLKGDGEKGEPGPAGPAGPAGEQ-------------------GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  624 SPGPVGPAGIKGAKGEpcepctalselqdgdmrvvhlPGPAGEKGEPGSPG-FGLPGKQGKAGERGLKGQKGDAGNPGDP 702
Cdd:NF038329   169 EAGPQGPAGKDGEAGA---------------------KGPAGEKGPQGPRGeTGPAGEQGPAGPAGPDGEAGPAGEDGPA 227

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  703 GTPGiTGQPGISGEPGIRGPAGPKGEKGDgctacPSLQGALTDVsGLPGKPGPKGEPGPEG-VGHPGKPGQPGLPGVQGP 781
Cdd:NF038329   228 GPAG-DGQQGPDGDPGPTGEDGPQGPDGP-----AGKDGPRGDR-GEAGPDGPDGKDGERGpVGPAGKDGQNGKDGLPGK 300

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907153774  782 PGPKGTQGEPGPPGTgaEGPQGEPGTQGLPGtqglpgprgppgSAGEKGAQGSPGPK 838
Cdd:NF038329   301 DGKDGQNGKDGLPGK--DGKDGQPGKDGLPG------------KDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 503-725 8.02e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 105.76  E-value: 8.02e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  503 KGEKGDPCEVCPTLPEGSQNFVGLPGKPGPKGEPGDPAPAWEGlGTVGLKGDRGDPGIQGMKGEKGEPCSSCSSGVGaqh 582
Cdd:NF038329   134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA-GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA--- 209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  583 lGPSPGHGLPGLPGTSGIPGPRGlKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGEPCEPCTALSELQDGDMrvvHLPG 662
Cdd:NF038329   210 -GPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER---GPVG 284

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907153774  663 PAGEKGEPGSPGfgLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGP 725
Cdd:NF038329   285 PAGKDGQNGKDG--LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 335-705 9.27e-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: 90.35  E-value: 9.27e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  335 LKGGKGERGLTGPSGPKGEKgargndcvrvspdaplqcveGPKGEKGEsgdlgppglpgpTGQKGQKGEKGDGGLKGLPG 414
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQ--------------------GPRGDRGE------------TGPAGPAGPPGPQGERGEKG 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  415 KPGRDGRPGEICVIGPKGQKGDPGFVGPeglagepgppglpgppgiglpgtpgdpggppgpkgekgssgipgkegpggkp 494
Cdd:NF038329   163 PAGPQGEAGPQGPAGKDGEAGAKGPAGE---------------------------------------------------- 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  495 gkpgvpgtKGEKGDPCEVCPTLPEGSQNFVGLPGKPGPKGEPGDPAPAweGLGTVGLKGDRGDPGIQGMKGEKGEpcssc 574
Cdd:NF038329   191 --------KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPA--GDGQQGPDGDPGPTGEDGPQGPDGP----- 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  575 ssgvgaqhlgpspghglpglpgtsgiPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGepcepctalselQDGd 654
Cdd:NF038329   256 --------------------------AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG------------KDG- 296

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907153774  655 mrvvhLPGPAGEKGEPGSPgfGLPGKQGKAGERGLKGQKGDAGNPGDPGTP 705
Cdd:NF038329   297 -----LPGKDGKDGQNGKD--GLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
595-855 2.22e-10

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 64.28  E-value: 2.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  595 PGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAkgepcepctalselqdgdmrvvhlPGPAGEKGEPGSPG 674
Cdd:COG5164      6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRP------------------------AQNQGSTTPAGNTG 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  675 FGLP-GKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGdgctacpslqGALTDVSGLPGKP 753
Cdd:COG5164     62 GTRPaGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATG----------PPDDGGSTTPPSG 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  754 GPKGEPGPEGVGHPGkPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQG 833
Cdd:COG5164    132 GSTTPPGDGGSTPPG-PGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVK 210

                          250       260
                   ....*....|....*....|..
gi 1907153774  834 SPGPKGAIGPmgPPGAGVSGPP 855
Cdd:COG5164    211 KDDKNGKGNP--PDDRGGKTGP 230
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 331-541 3.81e-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: 57.22  E-value: 3.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  331 GPSGLKGGKGERGLTGPSGPKGEKGARGNDCVRVSPDAplqcvEGPKGEKGESGDLGPPGLPGPTGQKGQKGEKGDGGLK 410
Cdd:NF038329   147 GPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA-----KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  411 GLPGKPGRDGRP--GEICVIGPKGQKGDPGFVGPEGLAGEPGPPGLPGPPGIGLPGTPGDPGGPPGPKGEKGSSGIPGKE 488
Cdd:NF038329   222 GEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD 301

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907153774  489 GPGGKPGKPGVPGTKGEKGDPCEvcptlpegsqnfVGLPGKPGPKGEPGDPAP 541
Cdd:NF038329   302 GKDGQNGKDGLPGKDGKDGQPGK------------DGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 799-982 7.84e-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: 56.07  E-value: 7.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  799 EGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGAIGPMGPPG----AGVSGPPGQKGSRGEKGEPGECSCP- 873
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGpqgeAGPQGPAGKDGEAGAKGPAGEKGPQg 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  874 SRGEPIFSGMPGAPGLwmGSSSQPGPQGPPGVPGPPGPPGMPGLQGVPGHNGLPGQPGLTAELGSlpiekhllksicgDC 953
Cdd:NF038329   196 PRGETGPAGEQGPAGP--AGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGK-------------DG 260

                          170       180
                   ....*....|....*....|....*....
gi 1907153774  954 AQGQTAHPAFLLEKGEKGDQGIPGVPGFD 982
Cdd:NF038329   261 PRGDRGEAGPDGPDGKDGERGPVGPAGKD 289
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 644-867 1.38e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.21  E-value: 1.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  644 CTALSELQDGDMRVVHLPGPAgekgePGSPGFGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPA 723
Cdd:PRK07764   571 VTALAEELGGDWQVEAVVGPA-----PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAP 645

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  724 GPKGEKGDGctACPSLQGALTDVSGLPGKPGPKGEPGPEGVGHPGKPGQPGlPGVQGPPGPKGTQGEPGPPGTGAEGPQG 803
Cdd:PRK07764   646 GVAAPEHHP--KHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA-GAAPAQPAPAPAATPPAGQADDPAAQPP 722

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907153774  804 EPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGAiGPMGPPGAGVSGPPGQKGSRGEKGEP 867
Cdd:PRK07764   723 QAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPP-PPPAPAPAAAPAAAPPPSPPSEEEEM 785
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 754-812 4.97e-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: 4.97e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  754 GPKGEPGPegvghPGKPGQPGLPGVQGPPGPKGTQGEPGPPG-TGAEGPQGEPGTQGLPG 812
Cdd:pfam01391    1 GPPGPPGP-----PGPPGPPGPPGPPGPPGPPGPPGEPGPPGpPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 590-643 1.48e-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: 1.48e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907153774  590 GLPGLPGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGEPCEP 643
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 671-888 3.13e-03

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 41.52  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  671 GSPGFGLPGKQGKAGERGlkgqkgdAGNPGDPGTPGITGQP-GISGEPGIRGPAGPKGEKGDGCTAcpslQGAltdvSGL 749
Cdd:cd21118    123 GSGGHGAYGSQGGPGVQG-------HGIPGGTGGPWASGGNyGTNSLGGSVGQGGNGGPLNYGTNS----QGA----VAQ 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  750 PGKPGPKGEPGPEGVGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEK 829
Cdd:cd21118    188 PGYGTVRGNNQNSGCTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNG 267

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  830 GAQG-SPGPKGAIGPMGPPGAGVSGPPGQKGSRGEKGEPgECSCPSRGepifSGMPGAPG 888
Cdd:cd21118    268 GSSGnSGSGSGGSSSGGSNGWGGSSSSGGSGGSGGGNKP-ECNNPGND----VRMAGGGG 322
 
Name Accession Description Interval E-value
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 50-231 6.86e-57

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 194.50  E-value: 6.86e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774    50 GFNLIRRLNLM-KTSAIKKIRNPKGP-LILRLG-AAPVTQPTRRVFPRGLPEEFALVLTVLLKKhtfRNTWYLFQVTDAN 126
Cdd:smart00210    1 GQDLLQVFDLPsLSFAIRQVVGPEPGsPAYRLGdPALVPQPTRDLFPSGLPEDFSLLTTFRQTP---KSRGVLFAIYDAQ 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774   127 GYPQISLEVNSQERSLELRAQGQDGDFVSCIFPVPQLFDLRWHKLMLSVAGRVASVHVDCVSASSQPLGPR--QSIRPGG 204
Cdd:smart00210   78 NVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPgqPPIDTDG 157

                           170       180
                    ....*....|....*....|....*..
gi 1907153774   205 HVFLGLDAEQGKPVSFDLQQAHIYCDP 231
Cdd:smart00210  158 IEVRGAQAADRKPFQGDLQQLKIVCDP 184
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 665-868 2.64e-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: 2.64e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  665 GEKGEPGSPG-FGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGDgctacpslqgal 743
Cdd:NF038329   117 GEKGEPGPAGpAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA------------ 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  744 tdvsglPGKPGPKGEPGPEG-VGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGP 822
Cdd:NF038329   185 ------KGPAGEKGPQGPRGeTGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGK 258

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907153774  823 PGSAGEKGAQGSPGPKGAIGPMGPPGA-------GVSGPPGQKGSRGEKGEPG 868
Cdd:NF038329   259 DGPRGDRGEAGPDGPDGKDGERGPVGPagkdgqnGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 544-838 2.45e-27

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 116.54  E-value: 2.45e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  544 EGLGTVGLKGDRGDPGIQGMKGEKGEPcsscssgvgaqhlgpspghGLPGLPGTSGIPGPRGLKGEKGSFGDTGPAGVPG 623
Cdd:NF038329   108 EGLQQLKGDGEKGEPGPAGPAGPAGEQ-------------------GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  624 SPGPVGPAGIKGAKGEpcepctalselqdgdmrvvhlPGPAGEKGEPGSPG-FGLPGKQGKAGERGLKGQKGDAGNPGDP 702
Cdd:NF038329   169 EAGPQGPAGKDGEAGA---------------------KGPAGEKGPQGPRGeTGPAGEQGPAGPAGPDGEAGPAGEDGPA 227

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  703 GTPGiTGQPGISGEPGIRGPAGPKGEKGDgctacPSLQGALTDVsGLPGKPGPKGEPGPEG-VGHPGKPGQPGLPGVQGP 781
Cdd:NF038329   228 GPAG-DGQQGPDGDPGPTGEDGPQGPDGP-----AGKDGPRGDR-GEAGPDGPDGKDGERGpVGPAGKDGQNGKDGLPGK 300

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907153774  782 PGPKGTQGEPGPPGTgaEGPQGEPGTQGLPGtqglpgprgppgSAGEKGAQGSPGPK 838
Cdd:NF038329   301 DGKDGQNGKDGLPGK--DGKDGQPGKDGLPG------------KDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 503-725 8.02e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 105.76  E-value: 8.02e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  503 KGEKGDPCEVCPTLPEGSQNFVGLPGKPGPKGEPGDPAPAWEGlGTVGLKGDRGDPGIQGMKGEKGEPCSSCSSGVGaqh 582
Cdd:NF038329   134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA-GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA--- 209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  583 lGPSPGHGLPGLPGTSGIPGPRGlKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGEPCEPCTALSELQDGDMrvvHLPG 662
Cdd:NF038329   210 -GPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER---GPVG 284

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907153774  663 PAGEKGEPGSPGfgLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGP 725
Cdd:NF038329   285 PAGKDGQNGKDG--LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 335-705 9.27e-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: 90.35  E-value: 9.27e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  335 LKGGKGERGLTGPSGPKGEKgargndcvrvspdaplqcveGPKGEKGEsgdlgppglpgpTGQKGQKGEKGDGGLKGLPG 414
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQ--------------------GPRGDRGE------------TGPAGPAGPPGPQGERGEKG 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  415 KPGRDGRPGEICVIGPKGQKGDPGFVGPeglagepgppglpgppgiglpgtpgdpggppgpkgekgssgipgkegpggkp 494
Cdd:NF038329   163 PAGPQGEAGPQGPAGKDGEAGAKGPAGE---------------------------------------------------- 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  495 gkpgvpgtKGEKGDPCEVCPTLPEGSQNFVGLPGKPGPKGEPGDPAPAweGLGTVGLKGDRGDPGIQGMKGEKGEpcssc 574
Cdd:NF038329   191 --------KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPA--GDGQQGPDGDPGPTGEDGPQGPDGP----- 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  575 ssgvgaqhlgpspghglpglpgtsgiPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGepcepctalselQDGd 654
Cdd:NF038329   256 --------------------------AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG------------KDG- 296

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907153774  655 mrvvhLPGPAGEKGEPGSPgfGLPGKQGKAGERGLKGQKGDAGNPGDPGTP 705
Cdd:NF038329   297 -----LPGKDGKDGQNGKD--GLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
595-855 2.22e-10

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 64.28  E-value: 2.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  595 PGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAkgepcepctalselqdgdmrvvhlPGPAGEKGEPGSPG 674
Cdd:COG5164      6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRP------------------------AQNQGSTTPAGNTG 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  675 FGLP-GKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGdgctacpslqGALTDVSGLPGKP 753
Cdd:COG5164     62 GTRPaGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATG----------PPDDGGSTTPPSG 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  754 GPKGEPGPEGVGHPGkPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQG 833
Cdd:COG5164    132 GSTTPPGDGGSTPPG-PGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVK 210

                          250       260
                   ....*....|....*....|..
gi 1907153774  834 SPGPKGAIGPmgPPGAGVSGPP 855
Cdd:COG5164    211 KDDKNGKGNP--PDDRGGKTGP 230
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 331-541 3.81e-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: 57.22  E-value: 3.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  331 GPSGLKGGKGERGLTGPSGPKGEKGARGNDCVRVSPDAplqcvEGPKGEKGESGDLGPPGLPGPTGQKGQKGEKGDGGLK 410
Cdd:NF038329   147 GPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA-----KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  411 GLPGKPGRDGRP--GEICVIGPKGQKGDPGFVGPEGLAGEPGPPGLPGPPGIGLPGTPGDPGGPPGPKGEKGSSGIPGKE 488
Cdd:NF038329   222 GEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD 301

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907153774  489 GPGGKPGKPGVPGTKGEKGDPCEvcptlpegsqnfVGLPGKPGPKGEPGDPAP 541
Cdd:NF038329   302 GKDGQNGKDGLPGKDGKDGQPGK------------DGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 799-982 7.84e-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: 56.07  E-value: 7.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  799 EGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGAIGPMGPPG----AGVSGPPGQKGSRGEKGEPGECSCP- 873
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGpqgeAGPQGPAGKDGEAGAKGPAGEKGPQg 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  874 SRGEPIFSGMPGAPGLwmGSSSQPGPQGPPGVPGPPGPPGMPGLQGVPGHNGLPGQPGLTAELGSlpiekhllksicgDC 953
Cdd:NF038329   196 PRGETGPAGEQGPAGP--AGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGK-------------DG 260

                          170       180
                   ....*....|....*....|....*....
gi 1907153774  954 AQGQTAHPAFLLEKGEKGDQGIPGVPGFD 982
Cdd:NF038329   261 PRGDRGEAGPDGPDGKDGERGPVGPAGKD 289
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 644-867 1.38e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.21  E-value: 1.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  644 CTALSELQDGDMRVVHLPGPAgekgePGSPGFGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPA 723
Cdd:PRK07764   571 VTALAEELGGDWQVEAVVGPA-----PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAP 645

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  724 GPKGEKGDGctACPSLQGALTDVSGLPGKPGPKGEPGPEGVGHPGKPGQPGlPGVQGPPGPKGTQGEPGPPGTGAEGPQG 803
Cdd:PRK07764   646 GVAAPEHHP--KHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA-GAAPAQPAPAPAATPPAGQADDPAAQPP 722

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907153774  804 EPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGAiGPMGPPGAGVSGPPGQKGSRGEKGEP 867
Cdd:PRK07764   723 QAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPP-PPPAPAPAAAPAAAPPPSPPSEEEEM 785
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 754-812 4.97e-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: 4.97e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  754 GPKGEPGPegvghPGKPGQPGLPGVQGPPGPKGTQGEPGPPG-TGAEGPQGEPGTQGLPG 812
Cdd:pfam01391    1 GPPGPPGP-----PGPPGPPGPPGPPGPPGPPGPPGEPGPPGpPGPPGPPGPPGAPGAPG 55
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 619-869 5.74e-05

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 47.31  E-value: 5.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  619 AGVPGSP-GPVGPAGIKGAKGEPCEPCTALSELQDGDMRVvhlPGPAGEKGEPGSPgfglpgkqgKAGERGLKGQKGDAG 697
Cdd:pfam09606   57 AAQQQQPqGGQGNGGMGGGQQGMPDPINALQNLAGQGTRP---QMMGPMGPGPGGP---------MGQQMGGPGTASNLL 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  698 NPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGdgctacPSLQGALTDVSGLPGKPGPKGEPGPEGVghPGKPGQPGLPG 777
Cdd:pfam09606  125 ASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGG------MMQPSSGQPGSGTPNQMGPNGGPGQGQA--GGMNGGQQGPM 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  778 VQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGA-IGPMGPPGAGVSGPPG 856
Cdd:pfam09606  197 GGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMgINQMQQMPQGVGGGAG 276

                          250
                   ....*....|...
gi 1907153774  857 QKGSRGEKGEPGE 869
Cdd:pfam09606  277 QGGPGQPMGPPGQ 289
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 583-805 1.15e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  583 LGPSPGHGLPGLPGTSGIPGPRGLKGEkgsfgdtgPAGVPGSPGPVGPAGIKGAkGEPCEPCTALSELQdgdmrvvhlPG 662
Cdd:PRK07764   588 VGPAPGAAGGEGPPAPASSGPPEEAAR--------PAAPAAPAAPAAPAPAGAA-AAPAEASAAPAPGV---------AA 649

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  663 PAGEKGEPGSPGFGLPGkQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPgiRGPAGPKGEKGDGCTACP----- 737
Cdd:PRK07764   650 PEHHPKHVAVPDASDGG-DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAP--APAATPPAGQADDPAAQPpqaaq 726

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907153774  738 ---SLQGALTDVSGLPGKPGPKGEPGPEGVGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEP 805
Cdd:PRK07764   727 gasAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDED 797
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 751-869 1.29e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  751 GKPGPKGEPGPEGVGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKG 830
Cdd:PRK07764   590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907153774  831 AQGSPGPKGAIGPMGPPGAGVSGPPGQKGSRGEKGEPGE 869
Cdd:PRK07764   670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAAT 708
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
750-930 1.47e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.79  E-value: 1.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  750 PGKPGPKGEPGPEGVGHP-GKPGQPGLPGVQGPPGPKGTQGEPGPPGT-GAEGPQGEPGTQGLPGTQGLPGPRGPPGSAG 827
Cdd:COG5164      3 LYGPGKTGPSDPGGVTTPaGSQGSTKPAQNQGSTRPAGNTGGTRPAQNqGSTTPAGNTGGTRPAGNQGATGPAQNQGGTT 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  828 EKGAQGSPGPKGAIGPMGPPGAGVS-GPPGQKGSRGEKGEPGECSCPSRGEPIFSGMPGAPGLWMGSSSQPGPQGPPGVP 906
Cdd:COG5164     83 PAQNQGGTRPAGNTGGTTPAGDGGAtGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDG 162

                          170       180
                   ....*....|....*....|....
gi 1907153774  907 GPPGPPGMPGLQGVPGHNGLPGQP 930
Cdd:COG5164    163 GSTTPPGPGGSTTPPDDGGSTTPP 186
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 590-643 1.48e-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: 1.48e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907153774  590 GLPGLPGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGEPCEP 643
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 584-640 1.88e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 1.88e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907153774  584 GPSPGHGLPGLPGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGEP 640
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 660-717 1.93e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 1.93e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907153774  660 LPGPAGEKGEPGSPGFglPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEP 717
Cdd:pfam01391    2 PPGPPGPPGPPGPPGP--PGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 590-643 2.19e-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: 2.19e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907153774  590 GLPGLPGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGEPCEP 643
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 682-730 2.37e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 2.37e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1907153774  682 GKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKG 730
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 676-730 2.67e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 2.67e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907153774  676 GLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKG 730
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 713-888 4.07e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 4.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  713 ISGEPGIRGPAGPKGEKGDGCtacPSLQGALTDVSGLPGKPGPKGEPGPegvGHPGKPGQPGLPGVQGPPGPKGTQGEPG 792
Cdd:PRK07764   588 VGPAPGAAGGEGPPAPASSGP---PEEAARPAAPAAPAAPAAPAPAGAA---AAPAEASAAPAPGVAAPEHHPKHVAVPD 661

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  793 PPGTGAEGPqGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGAiGPMGPPGAGVSGPPGQKGSRGEKGEPGECSC 872
Cdd:PRK07764   662 ASDGGDGWP-AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAAT-PPAGQADDPAAQPPQAAQGASAPSPAADDPV 739

                          170
                   ....*....|....*.
gi 1907153774  873 PSRGEPIFSGMPGAPG 888
Cdd:PRK07764   740 PLPPEPDDPPDPAGAP 755
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 584-878 4.52e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 4.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  584 GPSPGHGLPGLPGTSGIPGPrglkgekgsfgdtGPAGVPGSPGP-VGPAGIKGAKGEPCEPCTAlselqDGDMRVVHLPG 662
Cdd:PHA03307    98 ASPAREGSPTPPGPSSPDPP-------------PPTPPPASPPPsPAPDLSEMLRPVGSPGPPP-----AASPPAAGASP 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  663 PAGEKGEPGSPGFGLPGKQGKAGERGL-------KGQKGDAGNPGDPGTPGITGQPGiSGEPGIRGPAGPKGEKGDGCTA 735
Cdd:PHA03307   160 AAVASDAASSRQAALPLSSPEETARAPssppaepPPSTPPAAASPRPPRRSSPISAS-ASSPAPAPGRSAADDAGASSSD 238

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  736 CPSLQGALTDVSG-------------LPGKPGPKGEPGPEGVGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQ 802
Cdd:PHA03307   239 SSSSESSGCGWGPenecplprpapitLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSS 318

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907153774  803 GEPGTQGLPGTqglpgprgPPGSAGEKGAQGSPGPKGAIGPMGPPGAGVS-GPPGQKGSRGEKGEPGECSCPSRGEP 878
Cdd:PHA03307   319 SSSRESSSSST--------SSSSESSRGAAVSPGPSPSRSPSPSRPPPPAdPSSPRKRPRPSRAPSSPAASAGRPTR 387
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 676-728 5.32e-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: 5.32e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907153774  676 GLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGE 728
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 665-723 5.48e-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: 5.48e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907153774  665 GEKGEPGSPGFglPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPA 723
Cdd:pfam01391    1 GPPGPPGPPGP--PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03247 PHA03247
large tegument protein UL36; Provisional
 618-867 2.20e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  618 PAGVPGSPGPVGPAGIKGAK----GEPCEPCTALSELQDG-DMRVVHLPGPAGEKGE--PGSPGFGLPGKQGKAGERGLK 690
Cdd:PHA03247  2713 HALVSATPLPPGPAAARQASpalpAAPAPPAVPAGPATPGgPARPARPPTTAGPPAPapPAAPAAGPPRRLTRPAVASLS 2792

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  691 GQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKgekgdgctacPSLQGALTDVSGLPGKPGPKGEPgPEGVGHPGKP 770
Cdd:PHA03247  2793 ESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL----------PPPTSAQPTAPPPPPGPPPPSLP-LGGSVAPGGD 2861

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  771 GQPGLPGVQGPPGPKGTqgePGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGAIGPMGPPGAG 850
Cdd:PHA03247  2862 VRRRPPSRSPAAKPAAP---ARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938

                          250
                   ....*....|....*..
gi 1907153774  851 VSGPPGQKGSRGEKGEP 867
Cdd:PHA03247  2939 PQPPLAPTTDPAGAGEP 2955
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 747-930 2.80e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 2.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  747 SGLPGKPGPKGEPGPEGVGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSA 826
Cdd:PRK07764   592 PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA 671

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  827 GEKGAQGSPGPKGAIGPMGPPGAGVSGPPGQkgSRGEKGEPGECSCPSRGEPIFSGMPGAPGLWMGSSSQPGPQGPPGVP 906
Cdd:PRK07764   672 KAGGAAPAAPPPAPAPAAPAAPAGAAPAQPA--PAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749

                          170       180
                   ....*....|....*....|....
gi 1907153774  907 GPPGPPGMPGLQGVPGHNGLPGQP 930
Cdd:PRK07764   750 DPAGAPAQPPPPPAPAPAAAPAAA 773
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 671-888 3.13e-03

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 41.52  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  671 GSPGFGLPGKQGKAGERGlkgqkgdAGNPGDPGTPGITGQP-GISGEPGIRGPAGPKGEKGDGCTAcpslQGAltdvSGL 749
Cdd:cd21118    123 GSGGHGAYGSQGGPGVQG-------HGIPGGTGGPWASGGNyGTNSLGGSVGQGGNGGPLNYGTNS----QGA----VAQ 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  750 PGKPGPKGEPGPEGVGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEK 829
Cdd:cd21118    188 PGYGTVRGNNQNSGCTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNG 267

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  830 GAQG-SPGPKGAIGPMGPPGAGVSGPPGQKGSRGEKGEPgECSCPSRGepifSGMPGAPG 888
Cdd:cd21118    268 GSSGnSGSGSGGSSSGGSNGWGGSSSSGGSGGSGGGNKP-ECNNPGND----VRMAGGGG 322
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 694-763 7.23e-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: 35.93  E-value: 7.23e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153774  694 GDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGdgctacpslqgaltdVSGLPGKPGPKGEPGPEG 763
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPG---------------PPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 780-847 8.47e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.55  E-value: 8.47e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907153774  780 GPPGPKGTQGEPGPPGtgAEGPQGEPGTQGLPGtqglpgprgPPGSAGEKGAQGSPGPKGAIGPMGPP 847
Cdd:pfam01391    1 GPPGPPGPPGPPGPPG--PPGPPGPPGPPGPPG---------EPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
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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