|
Name |
Accession |
Description |
Interval |
E-value |
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
50-231 |
6.34e-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: 6.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 50 GFNLIRRLNLM-KTSAIKKIRNPKGP-LILRLG-AAPVTQPTRRVFPRGLPEEFALVLTVLLKKhtfRNTWYLFQVTDAN 126
Cdd:smart00210 1 GQDLLQVFDLPsLSFAIRQVVGPEPGsPAYRLGdPALVPQPTRDLFPSGLPEDFSLLTTFRQTP---KSRGVLFAIYDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 127 GYPQISLEVNSQERSLELRAQGQDGDFVSCIFPVPQLFDLRWHKLMLSVAGRVASVHVDCVSASSQPLGPR--QSIRPGG 204
Cdd:smart00210 78 NVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPgqPPIDTDG 157
|
170 180
....*....|....*....|....*..
gi 568928183 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 |
3.84e-28 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 118.85 E-value: 3.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 665 GEKGEPGSPG-FGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGDgctacpslqgal 743
Cdd:NF038329 117 GEKGEPGPAGpAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA------------ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 744 tdvsglPGKPGPKGEPGPEG-VGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGP 822
Cdd:NF038329 185 ------KGPAGEKGPQGPRGeTGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGK 258
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568928183 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 ... |
544-794 |
3.52e-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: 116.16 E-value: 3.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 544 EGLGTVGLKGDRGDPGIQGMKGEKGEPcsscssgvgaqhlgpspghGLPGLPGTSGIPGPRGLKGEKGSFGDTGPAGVPG 623
Cdd:NF038329 108 EGLQQLKGDGEKGEPGPAGPAGPAGEQ-------------------GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 624 SPGPVGPA------------GIKGAKGEPCEPCTALSELQDGDMRVVHLPGPAGEKGEPGSPGFGLPGKQGKAGERGLKG 691
Cdd:NF038329 169 EAGPQGPAgkdgeagakgpaGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 692 QKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGdgctacpslQGALTDVSGLPGKPGPKGEPGPEGVghPGKPG 771
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG---------KDGQNGKDGLPGKDGKDGQNGKDGL--PGKDG 317
|
250 260
....*....|....*....|...
gi 568928183 772 QPGLPGVQGPPGPKGTQGEPGPP 794
Cdd:NF038329 318 KDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
503-725 |
1.03e-23 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 105.37 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 503 KGEKGDPCEVCPTLPEGSQNFVGLPGKPGPKGEPGDPAPAWEGlGTVGLKGDRGDPGIQGMKGEKGEPCSSCSSGvgaqH 582
Cdd:NF038329 134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA-GKDGEAGAKGPAGEKGPQGPRGETGPAGEQG----P 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 583 LGPSPGHGLPGLPGTSGIPGPRGlKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGEPCEPCTALSELQDGDMrvvHLPG 662
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER---GPVG 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568928183 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 |
1.31e-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: 89.96 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 335 LKGGKGERGLTGPSGPKGEKgargndcvrvspdaplqcveGPKGEKGEsgdlgppglpgpTGQKGQKGEKGDGGLKGLPG 414
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQ--------------------GPRGDRGE------------TGPAGPAGPPGPQGERGEKG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 415 KPGRDGRPGEICVIGPKGQKGDPGFVGPeglagepgppglpgppgiglpgtpgdpggppgpkgekgssgipgkegpggkp 494
Cdd:NF038329 163 PAGPQGEAGPQGPAGKDGEAGAKGPAGE---------------------------------------------------- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 495 gkpgvpgtKGEKGDPCEVCPTLPEGSQNFVGLPGKPGPKGEPGDPAPAweGLGTVGLKGDRGDPGIQGMKGEKGEpcssc 574
Cdd:NF038329 191 --------KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPA--GDGQQGPDGDPGPTGEDGPQGPDGP----- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 575 ssgvgaqhlgpspghglpglpgtsgiPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGepcepctalselQDGd 654
Cdd:NF038329 256 --------------------------AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG------------KDG- 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 568928183 655 mrvvhLPGPAGEKGEPGSPgfGLPGKQGKAGERGLKGQKGDAGNPGDPGTP 705
Cdd:NF038329 297 -----LPGKDGKDGQNGKD--GLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
595-855 |
2.47e-10 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 64.28 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 595 PGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAkgepcepctalselqdgdmrvvhlPGPAGEKGEPGSPG 674
Cdd:COG5164 6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRP------------------------AQNQGSTTPAGNTG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 675 FGLP-GKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGdgctacpslqGALTDVSGLPGKP 753
Cdd:COG5164 62 GTRPaGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATG----------PPDDGGSTTPPSG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 754 GPKGEPGPEGVGHPGkPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQG 833
Cdd:COG5164 132 GSTTPPGDGGSTPPG-PGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVK 210
|
250 260
....*....|....*....|..
gi 568928183 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 ... |
754-1034 |
2.44e-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: 60.69 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 754 GPKGEPGPEG-VGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPG-TGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGA 831
Cdd:NF038329 117 GEKGEPGPAGpAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGeKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 832 QGSPGPKGAIGPMGPPGAgvSGPPGQKGSRGEKGEPGECSCPSRGEPIFSGMPGAPGlwmgsssqpgpqgppgvpgppgp 911
Cdd:NF038329 197 RGETGPAGEQGPAGPAGP--DGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG----------------------- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 912 pgmpgLQGVPGHNGLPGQPGLTAELGslpiekhllksicgdcaqgqtahpafllEKGEKGDQGIPGVPGfdncarcfier 991
Cdd:NF038329 252 -----PDGPAGKDGPRGDRGEAGPDG----------------------------PDGKDGERGPVGPAG----------- 287
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568928183 992 erpraeeargdnsegepgcsgspglpgppgMPGQRGEEGPPVP 1034
Cdd:NF038329 288 ------------------------------KDGQNGKDGLPGK 300
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
331-541 |
4.16e-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: 56.84 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 331 GPSGLKGGKGERGLTGPSGPKGEKGARGNDCVRVSPDAplqcvEGPKGEKGESGDLGPPGLPGPTGQKGQKGEKGDGGLK 410
Cdd:NF038329 147 GPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA-----KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 411 GLPGKPGRDGRP--GEICVIGPKGQKGDPGFVGPEGLAGEPGPPGLPGPPGIGLPGTPGDPGGPPGPKGEKGSSGIPGKE 488
Cdd:NF038329 222 GEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD 301
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568928183 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 |
9.10e-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: 55.68 E-value: 9.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 799 EGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGAIGPMGPPG----AGVSGPPGQKGSRGEKGEPGECSCP- 873
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGpqgeAGPQGPAGKDGEAGAKGPAGEKGPQg 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 874 SRGEPIFSGMPGAPGLwmGSSSQPGPQGPPGVPGPPGPPGMPGLQGVPGHNGLPGQPGLTAELGSlpiekhllksicgDC 953
Cdd:NF038329 196 PRGETGPAGEQGPAGP--AGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGK-------------DG 260
|
170 180
....*....|....*....|....*....
gi 568928183 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 568928183 644 CTALSELQDGDMRVVHLPGPAgekgePGSPGFGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPA 723
Cdd:PRK07764 571 VTALAEELGGDWQVEAVVGPA-----PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAP 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 724 GPKGEKGDGctACPSLQGALTDVSGLPGKPGPKGEPGPEGVGHPGKPGQPGlPGVQGPPGPKGTQGEPGPPGTGAEGPQG 803
Cdd:PRK07764 646 GVAAPEHHP--KHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA-GAAPAQPAPAPAATPPAGQADDPAAQPP 722
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568928183 804 EPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGAiGPMGPPGAGVSGPPGQKGSRGEKGEP 867
Cdd:PRK07764 723 QAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPP-PPPAPAPAAAPAAAPPPSPPSEEEEM 785
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
619-869 |
6.21e-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: 46.93 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 619 AGVPGSP-GPVGPAGIKGAKGEPCEPCTALSELQDGDMRVvhlPGPAGEKGEPGSPgfglpgkqgKAGERGLKGQKGDAG 697
Cdd:pfam09606 57 AAQQQQPqGGQGNGGMGGGQQGMPDPINALQNLAGQGTRP---QMMGPMGPGPGGP---------MGQQMGGPGTASNLL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 698 NPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGdgctacPSLQGALTDVSGLPGKPGPKGEPGPEGVghPGKPGQPGLPG 777
Cdd:pfam09606 125 ASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGG------MMQPSSGQPGSGTPNQMGPNGGPGQGQA--GGMNGGQQGPM 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 778 VQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGA-IGPMGPPGAGVSGPPG 856
Cdd:pfam09606 197 GGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMgINQMQQMPQGVGGGAG 276
|
250
....*....|...
gi 568928183 857 QKGSRGEKGEPGE 869
Cdd:pfam09606 277 QGGPGQPMGPPGQ 289
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
590-643 |
1.81e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 40.17 E-value: 1.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568928183 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 |
3.17e-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: 41.14 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 671 GSPGFGLPGKQGKAGERGlkgqkgdAGNPGDPGTPGITGQP-GISGEPGIRGPAGPKGEKGDGCTAcpslQGAltdvSGL 749
Cdd:cd21118 123 GSGGHGAYGSQGGPGVQG-------HGIPGGTGGPWASGGNyGTNSLGGSVGQGGNGGPLNYGTNS----QGA----VAQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 750 PGKPGPKGEPGPEGVGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEK 829
Cdd:cd21118 188 PGYGTVRGNNQNSGCTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNG 267
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 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 |
6.34e-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: 6.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 50 GFNLIRRLNLM-KTSAIKKIRNPKGP-LILRLG-AAPVTQPTRRVFPRGLPEEFALVLTVLLKKhtfRNTWYLFQVTDAN 126
Cdd:smart00210 1 GQDLLQVFDLPsLSFAIRQVVGPEPGsPAYRLGdPALVPQPTRDLFPSGLPEDFSLLTTFRQTP---KSRGVLFAIYDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 127 GYPQISLEVNSQERSLELRAQGQDGDFVSCIFPVPQLFDLRWHKLMLSVAGRVASVHVDCVSASSQPLGPR--QSIRPGG 204
Cdd:smart00210 78 NVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPgqPPIDTDG 157
|
170 180
....*....|....*....|....*..
gi 568928183 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 |
3.84e-28 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 118.85 E-value: 3.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 665 GEKGEPGSPG-FGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGDgctacpslqgal 743
Cdd:NF038329 117 GEKGEPGPAGpAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA------------ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 744 tdvsglPGKPGPKGEPGPEG-VGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGP 822
Cdd:NF038329 185 ------KGPAGEKGPQGPRGeTGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGK 258
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568928183 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 ... |
544-794 |
3.52e-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: 116.16 E-value: 3.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 544 EGLGTVGLKGDRGDPGIQGMKGEKGEPcsscssgvgaqhlgpspghGLPGLPGTSGIPGPRGLKGEKGSFGDTGPAGVPG 623
Cdd:NF038329 108 EGLQQLKGDGEKGEPGPAGPAGPAGEQ-------------------GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 624 SPGPVGPA------------GIKGAKGEPCEPCTALSELQDGDMRVVHLPGPAGEKGEPGSPGFGLPGKQGKAGERGLKG 691
Cdd:NF038329 169 EAGPQGPAgkdgeagakgpaGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 692 QKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGdgctacpslQGALTDVSGLPGKPGPKGEPGPEGVghPGKPG 771
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG---------KDGQNGKDGLPGKDGKDGQNGKDGL--PGKDG 317
|
250 260
....*....|....*....|...
gi 568928183 772 QPGLPGVQGPPGPKGTQGEPGPP 794
Cdd:NF038329 318 KDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
503-725 |
1.03e-23 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 105.37 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 503 KGEKGDPCEVCPTLPEGSQNFVGLPGKPGPKGEPGDPAPAWEGlGTVGLKGDRGDPGIQGMKGEKGEPCSSCSSGvgaqH 582
Cdd:NF038329 134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA-GKDGEAGAKGPAGEKGPQGPRGETGPAGEQG----P 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 583 LGPSPGHGLPGLPGTSGIPGPRGlKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGEPCEPCTALSELQDGDMrvvHLPG 662
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER---GPVG 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568928183 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 |
1.31e-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: 89.96 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 335 LKGGKGERGLTGPSGPKGEKgargndcvrvspdaplqcveGPKGEKGEsgdlgppglpgpTGQKGQKGEKGDGGLKGLPG 414
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQ--------------------GPRGDRGE------------TGPAGPAGPPGPQGERGEKG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 415 KPGRDGRPGEICVIGPKGQKGDPGFVGPeglagepgppglpgppgiglpgtpgdpggppgpkgekgssgipgkegpggkp 494
Cdd:NF038329 163 PAGPQGEAGPQGPAGKDGEAGAKGPAGE---------------------------------------------------- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 495 gkpgvpgtKGEKGDPCEVCPTLPEGSQNFVGLPGKPGPKGEPGDPAPAweGLGTVGLKGDRGDPGIQGMKGEKGEpcssc 574
Cdd:NF038329 191 --------KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPA--GDGQQGPDGDPGPTGEDGPQGPDGP----- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 575 ssgvgaqhlgpspghglpglpgtsgiPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAKGepcepctalselQDGd 654
Cdd:NF038329 256 --------------------------AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG------------KDG- 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 568928183 655 mrvvhLPGPAGEKGEPGSPgfGLPGKQGKAGERGLKGQKGDAGNPGDPGTP 705
Cdd:NF038329 297 -----LPGKDGKDGQNGKD--GLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
595-855 |
2.47e-10 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 64.28 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 595 PGTSGIPGPRGLKGEKGSFGDTGPAGVPGSPGPVGPAGIKGAkgepcepctalselqdgdmrvvhlPGPAGEKGEPGSPG 674
Cdd:COG5164 6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRP------------------------AQNQGSTTPAGNTG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 675 FGLP-GKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGdgctacpslqGALTDVSGLPGKP 753
Cdd:COG5164 62 GTRPaGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATG----------PPDDGGSTTPPSG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 754 GPKGEPGPEGVGHPGkPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQG 833
Cdd:COG5164 132 GSTTPPGDGGSTPPG-PGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVK 210
|
250 260
....*....|....*....|..
gi 568928183 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 ... |
754-1034 |
2.44e-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: 60.69 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 754 GPKGEPGPEG-VGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPG-TGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGA 831
Cdd:NF038329 117 GEKGEPGPAGpAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGeKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 832 QGSPGPKGAIGPMGPPGAgvSGPPGQKGSRGEKGEPGECSCPSRGEPIFSGMPGAPGlwmgsssqpgpqgppgvpgppgp 911
Cdd:NF038329 197 RGETGPAGEQGPAGPAGP--DGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG----------------------- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 912 pgmpgLQGVPGHNGLPGQPGLTAELGslpiekhllksicgdcaqgqtahpafllEKGEKGDQGIPGVPGfdncarcfier 991
Cdd:NF038329 252 -----PDGPAGKDGPRGDRGEAGPDG----------------------------PDGKDGERGPVGPAG----------- 287
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568928183 992 erpraeeargdnsegepgcsgspglpgppgMPGQRGEEGPPVP 1034
Cdd:NF038329 288 ------------------------------KDGQNGKDGLPGK 300
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
331-541 |
4.16e-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: 56.84 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 331 GPSGLKGGKGERGLTGPSGPKGEKGARGNDCVRVSPDAplqcvEGPKGEKGESGDLGPPGLPGPTGQKGQKGEKGDGGLK 410
Cdd:NF038329 147 GPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA-----KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 411 GLPGKPGRDGRP--GEICVIGPKGQKGDPGFVGPEGLAGEPGPPGLPGPPGIGLPGTPGDPGGPPGPKGEKGSSGIPGKE 488
Cdd:NF038329 222 GEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD 301
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568928183 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 |
9.10e-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: 55.68 E-value: 9.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 799 EGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGAIGPMGPPG----AGVSGPPGQKGSRGEKGEPGECSCP- 873
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGpqgeAGPQGPAGKDGEAGAKGPAGEKGPQg 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 874 SRGEPIFSGMPGAPGLwmGSSSQPGPQGPPGVPGPPGPPGMPGLQGVPGHNGLPGQPGLTAELGSlpiekhllksicgDC 953
Cdd:NF038329 196 PRGETGPAGEQGPAGP--AGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGK-------------DG 260
|
170 180
....*....|....*....|....*....
gi 568928183 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 568928183 644 CTALSELQDGDMRVVHLPGPAgekgePGSPGFGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPA 723
Cdd:PRK07764 571 VTALAEELGGDWQVEAVVGPA-----PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAP 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 724 GPKGEKGDGctACPSLQGALTDVSGLPGKPGPKGEPGPEGVGHPGKPGQPGlPGVQGPPGPKGTQGEPGPPGTGAEGPQG 803
Cdd:PRK07764 646 GVAAPEHHP--KHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA-GAAPAQPAPAPAATPPAGQADDPAAQPP 722
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568928183 804 EPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGAiGPMGPPGAGVSGPPGQKGSRGEKGEP 867
Cdd:PRK07764 723 QAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPP-PPPAPAPAAAPAAAPPPSPPSEEEEM 785
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
619-869 |
6.21e-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: 46.93 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 619 AGVPGSP-GPVGPAGIKGAKGEPCEPCTALSELQDGDMRVvhlPGPAGEKGEPGSPgfglpgkqgKAGERGLKGQKGDAG 697
Cdd:pfam09606 57 AAQQQQPqGGQGNGGMGGGQQGMPDPINALQNLAGQGTRP---QMMGPMGPGPGGP---------MGQQMGGPGTASNLL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 698 NPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGdgctacPSLQGALTDVSGLPGKPGPKGEPGPEGVghPGKPGQPGLPG 777
Cdd:pfam09606 125 ASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGG------MMQPSSGQPGSGTPNQMGPNGGPGQGQA--GGMNGGQQGPM 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 778 VQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGA-IGPMGPPGAGVSGPPG 856
Cdd:pfam09606 197 GGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMgINQMQQMPQGVGGGAG 276
|
250
....*....|...
gi 568928183 857 QKGSRGEKGEPGE 869
Cdd:pfam09606 277 QGGPGQPMGPPGQ 289
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
754-812 |
6.44e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 41.71 E-value: 6.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 754 GPKGEPGPegvghPGKPGQPGLPGVQGPPGPKGTQGEPGPPG-TGAEGPQGEPGTQGLPG 812
Cdd:pfam01391 1 GPPGPPGP-----PGPPGPPGPPGPPGPPGPPGPPGEPGPPGpPGPPGPPGPPGAPGAPG 55
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
583-805 |
1.17e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 46.13 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 583 LGPSPGHGLPGLPGTSGIPGPRGLKGEkgsfgdtgPAGVPGSPGPVGPAGIKGAkGEPCEPCTALSELQdgdmrvvhlPG 662
Cdd:PRK07764 588 VGPAPGAAGGEGPPAPASSGPPEEAAR--------PAAPAAPAAPAAPAPAGAA-AAPAEASAAPAPGV---------AA 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 663 PAGEKGEPGSPGFGLPGkQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPgiRGPAGPKGEKGDGCTACP----- 737
Cdd:PRK07764 650 PEHHPKHVAVPDASDGG-DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAP--APAATPPAGQADDPAAQPpqaaq 726
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568928183 738 ---SLQGALTDVSGLPGKPGPKGEPGPEGVGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEP 805
Cdd:PRK07764 727 gasAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDED 797
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
751-869 |
1.27e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 46.13 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 751 GKPGPKGEPGPEGVGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKG 830
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
|
90 100 110
....*....|....*....|....*....|....*....
gi 568928183 831 AQGSPGPKGAIGPMGPPGAGVSGPPGQKGSRGEKGEPGE 869
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAAT 708
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
750-930 |
1.51e-04 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 45.41 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 750 PGKPGPKGEPGPEGVGHP-GKPGQPGLPGVQGPPGPKGTQGEPGPPGT-GAEGPQGEPGTQGLPGTQGLPGPRGPPGSAG 827
Cdd:COG5164 3 LYGPGKTGPSDPGGVTTPaGSQGSTKPAQNQGSTRPAGNTGGTRPAQNqGSTTPAGNTGGTRPAGNQGATGPAQNQGGTT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 828 EKGAQGSPGPKGAIGPMGPPGAGVS-GPPGQKGSRGEKGEPGECSCPSRGEPIFSGMPGAPGLWMGSSSQPGPQGPPGVP 906
Cdd:COG5164 83 PAQNQGGTRPAGNTGGTTPAGDGGAtGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDG 162
|
170 180
....*....|....*....|....
gi 568928183 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 |
1.81e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 40.17 E-value: 1.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568928183 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 |
2.29e-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: 2.29e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568928183 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 |
2.38e-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: 2.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568928183 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 |
2.60e-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: 2.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568928183 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 |
2.84e-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: 2.84e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568928183 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 |
3.26e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.40 E-value: 3.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568928183 676 GLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKG 730
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
713-888 |
4.01e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.59 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 713 ISGEPGIRGPAGPKGEKGDGCtacPSLQGALTDVSGLPGKPGPKGEPGPegvGHPGKPGQPGLPGVQGPPGPKGTQGEPG 792
Cdd:PRK07764 588 VGPAPGAAGGEGPPAPASSGP---PEEAARPAAPAAPAAPAAPAPAGAA---AAPAEASAAPAPGVAAPEHHPKHVAVPD 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 793 PPGTGAEGPqGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGAiGPMGPPGAGVSGPPGQKGSRGEKGEPGECSC 872
Cdd:PRK07764 662 ASDGGDGWP-AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAAT-PPAGQADDPAAQPPQAAQGASAPSPAADDPV 739
|
170
....*....|....*.
gi 568928183 873 PSRGEPIFSGMPGAPG 888
Cdd:PRK07764 740 PLPPEPDDPPDPAGAP 755
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
584-878 |
4.89e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.39 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 584 GPSPGHGLPGLPGTSGIPGPrglkgekgsfgdtGPAGVPGSPGP-VGPAGIKGAKGEPCEPCTAlselqDGDMRVVHLPG 662
Cdd:PHA03307 98 ASPAREGSPTPPGPSSPDPP-------------PPTPPPASPPPsPAPDLSEMLRPVGSPGPPP-----AASPPAAGASP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 663 PAGEKGEPGSPGFGLPGKQGKAGERGL-------KGQKGDAGNPGDPGTPGITGQPGiSGEPGIRGPAGPKGEKGDGCTA 735
Cdd:PHA03307 160 AAVASDAASSRQAALPLSSPEETARAPssppaepPPSTPPAAASPRPPRRSSPISAS-ASSPAPAPGRSAADDAGASSSD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 736 CPSLQGALTDVSG-------------LPGKPGPKGEPGPEGVGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQ 802
Cdd:PHA03307 239 SSSSESSGCGWGPenecplprpapitLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSS 318
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568928183 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 |
6.49e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 38.63 E-value: 6.49e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568928183 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 |
6.75e-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: 6.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 568928183 665 GEKGEPGSPGFglPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGQPGISGEPGIRGPA 723
Cdd:pfam01391 1 GPPGPPGPPGP--PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
618-867 |
2.28e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 618 PAGVPGSPGPVGPAGIKGAK----GEPCEPCTALSELQDG-DMRVVHLPGPAGEKGE--PGSPGFGLPGKQGKAGERGLK 690
Cdd:PHA03247 2713 HALVSATPLPPGPAAARQASpalpAAPAPPAVPAGPATPGgPARPARPPTTAGPPAPapPAAPAAGPPRRLTRPAVASLS 2792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 691 GQKGDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKgekgdgctacPSLQGALTDVSGLPGKPGPKGEPgPEGVGHPGKP 770
Cdd:PHA03247 2793 ESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL----------PPPTSAQPTAPPPPPGPPPPSLP-LGGSVAPGGD 2861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 771 GQPGLPGVQGPPGPKGTqgePGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEKGAQGSPGPKGAIGPMGPPGAG 850
Cdd:PHA03247 2862 VRRRPPSRSPAAKPAAP---ARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938
|
250
....*....|....*..
gi 568928183 851 VSGPPGQKGSRGEKGEP 867
Cdd:PHA03247 2939 PQPPLAPTTDPAGAGEP 2955
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
747-930 |
2.58e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.90 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 747 SGLPGKPGPKGEPGPEGVGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSA 826
Cdd:PRK07764 592 PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 827 GEKGAQGSPGPKGAIGPMGPPGAGVSGPPGQkgSRGEKGEPGECSCPSRGEPIFSGMPGAPGLWMGSSSQPGPQGPPGVP 906
Cdd:PRK07764 672 KAGGAAPAAPPPAPAPAAPAAPAGAAPAQPA--PAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749
|
170 180
....*....|....*....|....
gi 568928183 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 |
3.17e-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: 41.14 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 671 GSPGFGLPGKQGKAGERGlkgqkgdAGNPGDPGTPGITGQP-GISGEPGIRGPAGPKGEKGDGCTAcpslQGAltdvSGL 749
Cdd:cd21118 123 GSGGHGAYGSQGGPGVQG-------HGIPGGTGGPWASGGNyGTNSLGGSVGQGGNGGPLNYGTNS----QGA----VAQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 750 PGKPGPKGEPGPEGVGHPGKPGQPGLPGVQGPPGPKGTQGEPGPPGTGAEGPQGEPGTQGLPGTQGLPGPRGPPGSAGEK 829
Cdd:cd21118 188 PGYGTVRGNNQNSGCTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNG 267
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 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 |
8.92e-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: 8.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928183 694 GDAGNPGDPGTPGITGQPGISGEPGIRGPAGPKGEKGdgctacpslqgaltdVSGLPGKPGPKGEPGPEG 763
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPG---------------PPGPPGPPGPPGAPGAPG 55
|
|
| |
