|
Name |
Accession |
Description |
Interval |
E-value |
| COLFI |
pfam01410 |
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1659-1857 |
1.96e-56 |
|
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.
Pssm-ID: 460199 Cd Length: 233 Bit Score: 196.02 E-value: 1.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1659 EIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQKMVDGTYWVDPNLGCSSDTIEVSCNFThGGQTCLKPITAS-- 1736
Cdd:pfam01410 4 EVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFE-TGETCIYPTKASip 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1737 --------------------KVEF---------AISRVQMNFLHLLSSEVTQHITIHCLNMTVWQ-EGTGQTpaKQAVRF 1786
Cdd:pfam01410 83 rknwwtkeskhvwfgefmngGSQFsygvdgvgpSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMdQATGNL--KKALLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462626959 1787 RAWNGQIFEAGG--QFRPEVSMDGCKVQDGRWHQTLFTFRTQDPQQLPIISVDNLPPASSGKQYRLEVGPACF 1857
Cdd:pfam01410 161 QGSNDEEIRAEGnsRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
|
|
| COLFI |
smart00038 |
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1658-1858 |
3.76e-52 |
|
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.
Pssm-ID: 197483 Cd Length: 232 Bit Score: 183.82 E-value: 3.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1658 GEIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQKMVDGTYWVDPNLGCSSDTIEVSCNFThGGQTCLKPITAS- 1736
Cdd:smart00038 2 EEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFE-TGETCVSPSPSSi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1737 -----------------------KVEFAISR------VQMNFLHLLSSEVTQHITIHCLNMTVWQ-EGTGQTpaKQAVRF 1786
Cdd:smart00038 81 prktwysgkskhvwfgetmnggfKFSYGDSEgppvgvVQLTFLRLLSTEAHQNITYHCKNSVAYMdEATGNL--KKALRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462626959 1787 RAWNGQIFEAGGQFRP--EVSMDGCKVQDGRWHQTLFTFRTQDPQQLPIISVDNLPPASSGKQYRLEVGPACFL 1858
Cdd:smart00038 159 RGSNDVELSAEGNSKFtyEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1367-1596 |
3.56e-33 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 135.03 E-value: 3.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1367 EGVQGLRGKpGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEGIAGPDGlpg 1446
Cdd:NF038329 108 EGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG--- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1447 rdgqagqqgeqgDDGDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGtegrTGLPGNQGEPGSKGQP 1526
Cdd:NF038329 184 ------------AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGED 247
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1527 GDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLPGPKGDKGSRGDWG 1596
Cdd:NF038329 248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1353-1596 |
6.11e-33 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 134.26 E-value: 6.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1353 GDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGR 1432
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1433 QGLEGIAGPDGlpgrdgqagqqgeqgddgdpgPMGPAGKRGNPGVAGLPGAQGPPGfkgesglPGQLGPPGKRGTEGRTG 1512
Cdd:NF038329 197 RGETGPAGEQG---------------------PAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1513 LPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLPGPKGDKGSR 1592
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328
|
....
gi 2462626959 1593 GDWG 1596
Cdd:NF038329 329 GKDG 332
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1326-1561 |
1.92e-32 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 132.72 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1326 EKGEQGEDGKAegppGPPGDRGPVGDRGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGK 1405
Cdd:NF038329 118 EKGEPGPAGPA----GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1406 QGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEGIAGPDGlPGRDGQAGQQGEQGDDGDPGPMGPAGKRGNPGVAGLPGAQG 1485
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462626959 1486 PPGFKGESGLPgqlGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGP 1561
Cdd:NF038329 273 PDGKDGERGPV---GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
707-987 |
3.02e-30 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 126.17 E-value: 3.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 707 GHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGKMGM 786
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 787 PGFPGVFGERGPPGLDGnpgelglpgppgvpgligdlgvlgPIGYPGPKGMKGLMGSVGepglKGDKGEQGVPGVSGDPG 866
Cdd:NF038329 197 RGETGPAGEQGPAGPAG------------------------PDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 867 FQGDKGSQGLPGFPGARGKPGPLGKVGDKGsigfpgppgpegfpgDIGPPGDNGPEGMKGKPGARGLPGPRGQLGPEGde 946
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDG---------------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG-- 311
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2462626959 947 gpmgppgapgLEGQPGRKGFPGRPGLDGVKGEPGDPGRPGP 987
Cdd:NF038329 312 ----------LPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1181-1447 |
6.34e-30 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 125.40 E-value: 6.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1181 GQRGEPGLegdSGPMGPDGLKGDRGDPGPDGEHGEKGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQGEKGRTGAKGAKGY 1260
Cdd:NF038329 117 GEKGEPGP---AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1261 QGQLGEmgvpgdpgppgtPGPKGSRGSLGPTGAPGRMGAQGEPGLAGYDGhkgivgplgppgpkgeKGEQGEDGkaegpp 1340
Cdd:NF038329 194 QGPRGE------------TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------DGQQGPDG------ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1341 gppgdrgPVGDRGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGL 1420
Cdd:NF038329 240 -------DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL 312
|
250 260
....*....|....*....|....*..
gi 2462626959 1421 QGLPGPRGVVGRQGLEGIAGPDGLPGR 1447
Cdd:NF038329 313 PGKDGKDGQPGKDGLPGKDGKDGQPGK 339
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
689-887 |
5.52e-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: 5.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 689 GDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGS 768
Cdd:NF038329 141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 769 DGERGLPGVPGkRGKMGMPGFPGVFGERGPPGLDGNPGELGLPGPPGVPGLIGDLGVLGPIGYPGPKGMKGLMGSVGEPG 848
Cdd:NF038329 221 AGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462626959 849 LKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPG 887
Cdd:NF038329 300 KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1145-1403 |
2.71e-27 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 117.31 E-value: 2.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1145 GPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRGDPGPDGEHGEKGQEGLMGE 1224
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1225 dgppgppgvtgvRGPEGKSGKQGEKGRTGAKGAKGYQGQLGEMGVPGDPGppgtpgpkgsRGSLGPTGAPGRMGAQGEPG 1304
Cdd:NF038329 197 ------------RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ----------QGPDGDPGPTGEDGPQGPDG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1305 LAGYDGHKGIVGPLGPPGPKGEKGEQGEDGKAegppgppgdrGPVGDRGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGH 1384
Cdd:NF038329 255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPA----------GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324
|
250
....*....|....*....
gi 2462626959 1385 PGPRGWPGPKGSKGAEGPK 1403
Cdd:NF038329 325 DGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1120-1414 |
8.34e-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: 106.91 E-value: 8.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1120 PgtkglpgepgpqgpqgpigppgemGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDG 1199
Cdd:NF038329 128 A------------------------GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1200 LKGDRGDPGPDGEHGEKGQEGLMGEDgppgppgvtgvrGPEGKSGKQGEKGRTGAKGAKGyQGQLGEmgvpgdpgppgtp 1279
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPA------------GPAGPDGEAGPAGEDGPAGPAG-DGQQGP------------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1280 gpkgsRGSLGPTGAPGRMGAQGEPGLAGYDGHKGivgplgppgpkgEKGEQGEDGKAegppgppgdrgpvgdrGDRGEPG 1359
Cdd:NF038329 238 -----DGDPGPTGEDGPQGPDGPAGKDGPRGDRG------------EAGPDGPDGKD----------------GERGPVG 284
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 1360 DPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGR 1414
Cdd:NF038329 285 PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1058-1388 |
1.63e-22 |
|
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: 102.68 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1058 GAKGRRGPRGPDGPAGEQGSRGLKGPPGPQGRPGRPGQQGVAGERGHLGSRGFPGIPGPsgppgtkglpgepgpqgpqgp 1137
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP--------------------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1138 igppgeMGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGL--KGDRGDPGPDGEHGE 1215
Cdd:NF038329 176 ------AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGP 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1216 KGQEGLMGEDgppgppgvtgvrgpeGKSGKQGEKGRTGAKGakgyqgqlgemgvpgdpgppgtpgpkgSRGSLGPTGAPG 1295
Cdd:NF038329 250 QGPDGPAGKD---------------GPRGDRGEAGPDGPDG---------------------------KDGERGPVGPAG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1296 RMGAQGEPGLAGYDghkgivgplgppgpkgekGEQGEDGKAegppgppgdrgpvgdrgdrGEPGDPGYPGQEGVQGLRGK 1375
Cdd:NF038329 288 KDGQNGKDGLPGKD------------------GKDGQNGKD-------------------GLPGKDGKDGQPGKDGLPGK 330
|
330
....*....|...
gi 2462626959 1376 PGQQGQPGHPGPR 1388
Cdd:NF038329 331 DGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
623-835 |
4.47e-20 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 95.36 E-value: 4.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 623 GPPGPKGDCGLPGPPGLPGLPGIPGARGPRGPPGPYGNPGLPGPPGAKGQKGDPGLSPGKAHDGAKGDMGLPGLSGNPGP 702
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 703 PGRKGHKGYPGPAGHPGEQGQpGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRG 782
Cdd:NF038329 212 AGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462626959 783 KMGMPGFPGVFGERGPPGLDGNPGELGLPGPPGVPGLIGDLGVLGPIGYPGPK 835
Cdd:NF038329 291 QNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
972-1247 |
1.79e-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: 93.43 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 972 LDGVKGEPGDPGRPGPVGEQGFMGFIGLVGEPGIVGEKGDRGMMGPPGVPGPKGsmghpgmpggmgtpgEPGPQGPpgsr 1051
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------------EAGPQGP---- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1052 gppgmRGAKGRRGPRGPDGPAGEQGSRGLKGPpgpqgrpgrpgqqgvAGERGHLGsrgfpgipgpsgpPGTKGLPGEPGP 1131
Cdd:NF038329 176 -----AGKDGEAGAKGPAGEKGPQGPRGETGP---------------AGEQGPAG-------------PAGPDGEAGPAG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1132 QGPQGPIGPPGEMGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRGDPGPDG 1211
Cdd:NF038329 223 EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462626959 1212 EHGEKGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQG 1247
Cdd:NF038329 303 KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
842-1079 |
5.21e-19 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 92.28 E-value: 5.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 842 GSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLGKVGDKGSIgfpgppgpegfpgdiGPPGDNGP 921
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKDGE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 922 EGMKGKPGARGLPGPRGQLGPEGDEGPMGPPGAPGLEGQPGRKGFPGRPGlDGVKGEPGDPGRPGPVGEQgfmgfiGLVG 1001
Cdd:NF038329 182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ------GPDG 254
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462626959 1002 EPGIVGEKGDRGMMGPPGVPGPKGSMGHPGMPGGMGTPGEPGPQGPPGSRGPPGMRGAKGRRGPRGPDGPAGEQGSRG 1079
Cdd:NF038329 255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1461-1603 |
2.53e-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: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1461 GDPGPMGPAGKRGnpgvaglpgAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGL 1540
Cdd:NF038329 120 GEPGPAGPAGPAG---------EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 1541 FGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLP--GPKGDKGSRGDWGLQGPRGP 1603
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGP 255
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
867-1214 |
6.77e-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: 88.81 E-value: 6.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 867 FQGDKGSQGLPGFPGARGKPGPLGKVGDKGsigfpgppgpegFPGDIGPPGDNGPEGMKGKPGARGLPGPRGQLGPEGde 946
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETG------------PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG-- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 947 gpmgppgapglegQPGRKGFPGRPGLDGVKGEPGDPGRPGPVGEQGFMGFIGLVGEPGIVGEKGDrgmmgppgvpgpkgs 1026
Cdd:NF038329 181 -------------EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD--------------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1027 mghpgmpggmgtpgepgpqgppgsrgppgmrGAKGRRGPRGPDGPAGEQGSRGlkgppgpqgrpgrpgqqgvagERGHLG 1106
Cdd:NF038329 233 -------------------------------GQQGPDGDPGPTGEDGPQGPDG---------------------PAGKDG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1107 SRGFPGIPGPSgppgtkglpgepgpqgpqgpigppgemgpkGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEP 1186
Cdd:NF038329 261 PRGDRGEAGPD------------------------------GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD 310
|
330 340
....*....|....*....|....*...
gi 2462626959 1187 GLEGDSGPMGPDGLKGDRGDPGPDGEHG 1214
Cdd:NF038329 311 GLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
272-603 |
4.51e-14 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 78.44 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 272 TATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAklsasnaldpmLPASVGGSTRTPRPAAA 351
Cdd:PHA03247 2636 NEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRA-----------ARPTVGSLTSLADPPPP 2704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 352 QPSQKITATKIPKSLPTKP-------SAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPtekPI 424
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPgpaaarqASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP---PR 2781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 425 QRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTeakitshASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPAT 504
Cdd:PHA03247 2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPA-------AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGG 2854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 505 MVPPTSGTS---TPRTAPAVPTPGSAPTGSKKPiGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPR-QPQP 580
Cdd:PHA03247 2855 SVAPGGDVRrrpPSRSPAAKPAAPARPPVRRLA-RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpQPPP 2933
|
330 340
....*....|....*....|...
gi 2462626959 581 SQQTTPALVLAPAQFLSSSPRPT 603
Cdd:PHA03247 2934 PPPPRPQPPLAPTTDPAGAGEPS 2956
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
43-218 |
7.05e-13 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 68.92 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 43 DVDILQRLGLSWTKAGSPAPPGVIPFQSGFIFTQRARLQAPTGTVIPAALGTELALVLSLCSHRVNHAFLFAVRSQKRKL 122
Cdd:smart00210 1 GQDLLQVFDLPSLSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDAQNVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 123 QLGLQFLPGKTVVHL------GSRRSVAF-DLDMHDGRWHHLALELRGRTVTLVTACGQR-RVPVLLPFHrdPALDPGGS 194
Cdd:smart00210 81 QFGLEVDGRANTLLLryqgvdGKQHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIdSRPLDRPGQ--PPIDTDGI 158
|
170 180
....*....|....*....|....
gi 2462626959 195 FLFGKMNPHAVQFEGALCQFSIYP 218
Cdd:smart00210 159 EVRGAQAADRKPFQGDLQQLKIVC 182
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
279-606 |
1.17e-12 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 72.69 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 279 SLPAGR-GPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLlpaKLSASNALDPMLPASVggSTRTPRPAAAQPSqki 357
Cdd:pfam17823 98 SEPATReGAADGAASRALAAAASSSPSSAAQSLPAAIAALPSE---AFSAPRAAACRANASA--APRAAIAAASAPH--- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 358 TATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKS-------------ALPTQKQVPPTSRPVPARVSrptekpi 424
Cdd:pfam17823 170 AASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPArgistaatatghpAAGTALAAVGNSSPAAGTVT------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 425 qrnpgmprppppstrplPPTTSSSKKPIPTLARTEAKITSHA-----SKPASARTSTHKPPPFTALSSSPAPTPGS-TRS 498
Cdd:pfam17823 243 -----------------AAVGTVTPAALATLAAAAGTVASAAgtinmGDPHARRLSPAKHMPSDTMARNPAAPMGAqAQG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 499 TRPPATMVPP---TSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSP 575
Cdd:pfam17823 306 PIIQVSTDQPvhnTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPSP 385
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2462626959 576 RqpQPSQQTT-PALVLAPAQF--------LSSSPRPTSSG 606
Cdd:pfam17823 386 L--LPTQGAAgPGILLAPEQVateatagtASAGPTPRSSG 423
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1498-1628 |
1.03e-10 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 66.08 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1498 QLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGIL 1577
Cdd:NF038329 112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2462626959 1578 GPSGLPGPKGDKGSRGDWGLQGPRGPPGPRGRPGPPGPPGGPIQLQQDDLG 1628
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG 242
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
689-745 |
5.93e-06 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 45.18 E-value: 5.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462626959 689 GDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPV 745
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1461-1515 |
7.40e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 42.10 E-value: 7.40e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 1461 GDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPG 1515
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| rad23 |
TIGR00601 |
UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
458-529 |
3.22e-04 |
|
UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273167 [Multi-domain] Cd Length: 378 Bit Score: 45.27 E-value: 3.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462626959 458 TEAKITSHASKPASARTSTHKPPPFTALSSSPAPTpgstrSTRPPATMVPPTSGTSTPRT-APAVPTPGSAPT 529
Cdd:TIGR00601 80 GTGKVAPPAATPTSAPTPTPSPPASPASGMSAAPA-----SAVEEKSPSEESATATAPESpSTSVPSSGSDAA 147
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
1422-1596 |
5.05e-04 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 44.64 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1422 GLPGPRGVVGRQGLEGIAGPDGLPGRDGQAGQQGEQGDDGDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGP 1501
Cdd:COG5164 10 GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1502 PGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLF--GPKGPPGDIGfkgiQGPRGpPGLMGKEGIVGPLGILGP 1579
Cdd:COG5164 90 TRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGG----STPPG-PGSTGPGGSTTPPGDGGS 164
|
170
....*....|....*..
gi 2462626959 1580 SGLPGPKGDKGSRGDWG 1596
Cdd:COG5164 165 TTPPGPGGSTTPPDDGG 181
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
134-202 |
1.19e-03 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 40.87 E-value: 1.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462626959 134 VVHLGSRRSVAFDLD--MHDGRWHHLALELRGRTVTLVTaCGQRRVPVLLPfHRDPALDPGGSFLFGKMNP 202
Cdd:pfam02210 33 RYDLGSGPESLLSSGknLNDGQWHSVRVERNGNTLTLSV-DGQTVVSSLPP-GESLLLNLNGPLYLGGLPP 101
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
1190-1446 |
1.89e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 43.09 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1190 GDSGPMGPDGLKGDRGDPGPDGEHGEKGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQGEKGRTGAKGAKGYQGQLGEMGV 1269
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1270 PGDPGPPGTPGPKGSRGSLGPTGAPGRMGAQGEPGLAGYDGHKGiVGPLGPPgpkgekGEQGEDGKAEGPPGPPGDRGPV 1349
Cdd:COG5164 87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPS-GGSTTPP------GDGGSTPPGPGSTGPGGSTTPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1350 GDRGDRGEPGDPGYPGQEGVQGlRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGvqGLQGLPGPRGV 1429
Cdd:COG5164 160 GDGGSTTPPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGPKDQRPK 236
|
250
....*....|....*..
gi 2462626959 1430 VGRQGLEGIAGPDGLPG 1446
Cdd:COG5164 237 TNPIERRGPERPEAAAL 253
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1144-1197 |
2.60e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.86 E-value: 2.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462626959 1144 MGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGP 1197
Cdd:pfam01391 3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| KLF8_N |
cd21440 |
N-terminal domain of Kruppel-like factor 8; Kruppel-like factor 8 (also known as Krueppel-like ... |
475-526 |
9.32e-03 |
|
N-terminal domain of Kruppel-like factor 8; Kruppel-like factor 8 (also known as Krueppel-like transcription factor 8, KLF8) is a CACCC-box binding protein that associates with C-terminal Binding Protein (CtBP) and represses transcription. It plays an essential role in the regulation of the cell cycle, apoptosis, and differentiation. It has been identified as a key component of the transcription factor network that controls terminal differentiation during adipogenesis. It also plays an important role in the formation of several human tumors, including the promotion of tumorigenesis, invasion, and metastasis of colorectal cancer cells, and the progression of pancreatic cancer. KLF8 belongs to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Although these factors bind to similar elements in vitro, they have distinct activities in vivo depending on their expression profile and the sequence of the N-terminal activation/repression domain, which differ between members. KLF8 contains an N-terminal repression domain that is related to that of KLF12.
Pssm-ID: 410607 [Multi-domain] Cd Length: 169 Bit Score: 39.05 E-value: 9.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462626959 475 STHKP--PPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGS 526
Cdd:cd21440 43 SLHKPkaPLQPPSVLSPSPMILSVSPSAPQSLVSSTGTGMGTTSAIPAVLSPGS 96
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COLFI |
pfam01410 |
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1659-1857 |
1.96e-56 |
|
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.
Pssm-ID: 460199 Cd Length: 233 Bit Score: 196.02 E-value: 1.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1659 EIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQKMVDGTYWVDPNLGCSSDTIEVSCNFThGGQTCLKPITAS-- 1736
Cdd:pfam01410 4 EVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFE-TGETCIYPTKASip 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1737 --------------------KVEF---------AISRVQMNFLHLLSSEVTQHITIHCLNMTVWQ-EGTGQTpaKQAVRF 1786
Cdd:pfam01410 83 rknwwtkeskhvwfgefmngGSQFsygvdgvgpSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMdQATGNL--KKALLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462626959 1787 RAWNGQIFEAGG--QFRPEVSMDGCKVQDGRWHQTLFTFRTQDPQQLPIISVDNLPPASSGKQYRLEVGPACF 1857
Cdd:pfam01410 161 QGSNDEEIRAEGnsRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
|
|
| COLFI |
smart00038 |
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1658-1858 |
3.76e-52 |
|
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.
Pssm-ID: 197483 Cd Length: 232 Bit Score: 183.82 E-value: 3.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1658 GEIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQKMVDGTYWVDPNLGCSSDTIEVSCNFThGGQTCLKPITAS- 1736
Cdd:smart00038 2 EEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFE-TGETCVSPSPSSi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1737 -----------------------KVEFAISR------VQMNFLHLLSSEVTQHITIHCLNMTVWQ-EGTGQTpaKQAVRF 1786
Cdd:smart00038 81 prktwysgkskhvwfgetmnggfKFSYGDSEgppvgvVQLTFLRLLSTEAHQNITYHCKNSVAYMdEATGNL--KKALRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462626959 1787 RAWNGQIFEAGGQFRP--EVSMDGCKVQDGRWHQTLFTFRTQDPQQLPIISVDNLPPASSGKQYRLEVGPACFL 1858
Cdd:smart00038 159 RGSNDVELSAEGNSKFtyEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1367-1596 |
3.56e-33 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 135.03 E-value: 3.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1367 EGVQGLRGKpGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEGIAGPDGlpg 1446
Cdd:NF038329 108 EGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG--- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1447 rdgqagqqgeqgDDGDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGtegrTGLPGNQGEPGSKGQP 1526
Cdd:NF038329 184 ------------AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGED 247
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1527 GDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLPGPKGDKGSRGDWG 1596
Cdd:NF038329 248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1353-1596 |
6.11e-33 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 134.26 E-value: 6.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1353 GDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGR 1432
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1433 QGLEGIAGPDGlpgrdgqagqqgeqgddgdpgPMGPAGKRGNPGVAGLPGAQGPPGfkgesglPGQLGPPGKRGTEGRTG 1512
Cdd:NF038329 197 RGETGPAGEQG---------------------PAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1513 LPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLPGPKGDKGSR 1592
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328
|
....
gi 2462626959 1593 GDWG 1596
Cdd:NF038329 329 GKDG 332
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1326-1561 |
1.92e-32 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 132.72 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1326 EKGEQGEDGKAegppGPPGDRGPVGDRGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGK 1405
Cdd:NF038329 118 EKGEPGPAGPA----GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1406 QGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEGIAGPDGlPGRDGQAGQQGEQGDDGDPGPMGPAGKRGNPGVAGLPGAQG 1485
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462626959 1486 PPGFKGESGLPgqlGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGP 1561
Cdd:NF038329 273 PDGKDGERGPV---GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
707-987 |
3.02e-30 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 126.17 E-value: 3.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 707 GHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGKMGM 786
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 787 PGFPGVFGERGPPGLDGnpgelglpgppgvpgligdlgvlgPIGYPGPKGMKGLMGSVGepglKGDKGEQGVPGVSGDPG 866
Cdd:NF038329 197 RGETGPAGEQGPAGPAG------------------------PDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 867 FQGDKGSQGLPGFPGARGKPGPLGKVGDKGsigfpgppgpegfpgDIGPPGDNGPEGMKGKPGARGLPGPRGQLGPEGde 946
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDG---------------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG-- 311
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2462626959 947 gpmgppgapgLEGQPGRKGFPGRPGLDGVKGEPGDPGRPGP 987
Cdd:NF038329 312 ----------LPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1181-1447 |
6.34e-30 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 125.40 E-value: 6.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1181 GQRGEPGLegdSGPMGPDGLKGDRGDPGPDGEHGEKGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQGEKGRTGAKGAKGY 1260
Cdd:NF038329 117 GEKGEPGP---AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1261 QGQLGEmgvpgdpgppgtPGPKGSRGSLGPTGAPGRMGAQGEPGLAGYDGhkgivgplgppgpkgeKGEQGEDGkaegpp 1340
Cdd:NF038329 194 QGPRGE------------TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------DGQQGPDG------ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1341 gppgdrgPVGDRGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGL 1420
Cdd:NF038329 240 -------DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL 312
|
250 260
....*....|....*....|....*..
gi 2462626959 1421 QGLPGPRGVVGRQGLEGIAGPDGLPGR 1447
Cdd:NF038329 313 PGKDGKDGQPGKDGLPGKDGKDGQPGK 339
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
689-887 |
5.52e-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: 5.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 689 GDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGS 768
Cdd:NF038329 141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 769 DGERGLPGVPGkRGKMGMPGFPGVFGERGPPGLDGNPGELGLPGPPGVPGLIGDLGVLGPIGYPGPKGMKGLMGSVGEPG 848
Cdd:NF038329 221 AGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462626959 849 LKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPG 887
Cdd:NF038329 300 KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1145-1403 |
2.71e-27 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 117.31 E-value: 2.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1145 GPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRGDPGPDGEHGEKGQEGLMGE 1224
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1225 dgppgppgvtgvRGPEGKSGKQGEKGRTGAKGAKGYQGQLGEMGVPGDPGppgtpgpkgsRGSLGPTGAPGRMGAQGEPG 1304
Cdd:NF038329 197 ------------RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ----------QGPDGDPGPTGEDGPQGPDG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1305 LAGYDGHKGIVGPLGPPGPKGEKGEQGEDGKAegppgppgdrGPVGDRGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGH 1384
Cdd:NF038329 255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPA----------GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324
|
250
....*....|....*....
gi 2462626959 1385 PGPRGWPGPKGSKGAEGPK 1403
Cdd:NF038329 325 DGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1120-1414 |
8.34e-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: 106.91 E-value: 8.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1120 PgtkglpgepgpqgpqgpigppgemGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDG 1199
Cdd:NF038329 128 A------------------------GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1200 LKGDRGDPGPDGEHGEKGQEGLMGEDgppgppgvtgvrGPEGKSGKQGEKGRTGAKGAKGyQGQLGEmgvpgdpgppgtp 1279
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPA------------GPAGPDGEAGPAGEDGPAGPAG-DGQQGP------------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1280 gpkgsRGSLGPTGAPGRMGAQGEPGLAGYDGHKGivgplgppgpkgEKGEQGEDGKAegppgppgdrgpvgdrGDRGEPG 1359
Cdd:NF038329 238 -----DGDPGPTGEDGPQGPDGPAGKDGPRGDRG------------EAGPDGPDGKD----------------GERGPVG 284
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 1360 DPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGR 1414
Cdd:NF038329 285 PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1058-1388 |
1.63e-22 |
|
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: 102.68 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1058 GAKGRRGPRGPDGPAGEQGSRGLKGPPGPQGRPGRPGQQGVAGERGHLGSRGFPGIPGPsgppgtkglpgepgpqgpqgp 1137
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP--------------------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1138 igppgeMGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGL--KGDRGDPGPDGEHGE 1215
Cdd:NF038329 176 ------AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGP 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1216 KGQEGLMGEDgppgppgvtgvrgpeGKSGKQGEKGRTGAKGakgyqgqlgemgvpgdpgppgtpgpkgSRGSLGPTGAPG 1295
Cdd:NF038329 250 QGPDGPAGKD---------------GPRGDRGEAGPDGPDG---------------------------KDGERGPVGPAG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1296 RMGAQGEPGLAGYDghkgivgplgppgpkgekGEQGEDGKAegppgppgdrgpvgdrgdrGEPGDPGYPGQEGVQGLRGK 1375
Cdd:NF038329 288 KDGQNGKDGLPGKD------------------GKDGQNGKD-------------------GLPGKDGKDGQPGKDGLPGK 330
|
330
....*....|...
gi 2462626959 1376 PGQQGQPGHPGPR 1388
Cdd:NF038329 331 DGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
623-835 |
4.47e-20 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 95.36 E-value: 4.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 623 GPPGPKGDCGLPGPPGLPGLPGIPGARGPRGPPGPYGNPGLPGPPGAKGQKGDPGLSPGKAHDGAKGDMGLPGLSGNPGP 702
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 703 PGRKGHKGYPGPAGHPGEQGQpGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRG 782
Cdd:NF038329 212 AGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462626959 783 KMGMPGFPGVFGERGPPGLDGNPGELGLPGPPGVPGLIGDLGVLGPIGYPGPK 835
Cdd:NF038329 291 QNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
972-1247 |
1.79e-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: 93.43 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 972 LDGVKGEPGDPGRPGPVGEQGFMGFIGLVGEPGIVGEKGDRGMMGPPGVPGPKGsmghpgmpggmgtpgEPGPQGPpgsr 1051
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------------EAGPQGP---- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1052 gppgmRGAKGRRGPRGPDGPAGEQGSRGLKGPpgpqgrpgrpgqqgvAGERGHLGsrgfpgipgpsgpPGTKGLPGEPGP 1131
Cdd:NF038329 176 -----AGKDGEAGAKGPAGEKGPQGPRGETGP---------------AGEQGPAG-------------PAGPDGEAGPAG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1132 QGPQGPIGPPGEMGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRGDPGPDG 1211
Cdd:NF038329 223 EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462626959 1212 EHGEKGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQG 1247
Cdd:NF038329 303 KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
842-1079 |
5.21e-19 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 92.28 E-value: 5.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 842 GSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLGKVGDKGSIgfpgppgpegfpgdiGPPGDNGP 921
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKDGE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 922 EGMKGKPGARGLPGPRGQLGPEGDEGPMGPPGAPGLEGQPGRKGFPGRPGlDGVKGEPGDPGRPGPVGEQgfmgfiGLVG 1001
Cdd:NF038329 182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ------GPDG 254
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462626959 1002 EPGIVGEKGDRGMMGPPGVPGPKGSMGHPGMPGGMGTPGEPGPQGPPGSRGPPGMRGAKGRRGPRGPDGPAGEQGSRG 1079
Cdd:NF038329 255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1461-1603 |
2.53e-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: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1461 GDPGPMGPAGKRGnpgvaglpgAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGL 1540
Cdd:NF038329 120 GEPGPAGPAGPAG---------EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 1541 FGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLP--GPKGDKGSRGDWGLQGPRGP 1603
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGP 255
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
867-1214 |
6.77e-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: 88.81 E-value: 6.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 867 FQGDKGSQGLPGFPGARGKPGPLGKVGDKGsigfpgppgpegFPGDIGPPGDNGPEGMKGKPGARGLPGPRGQLGPEGde 946
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETG------------PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG-- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 947 gpmgppgapglegQPGRKGFPGRPGLDGVKGEPGDPGRPGPVGEQGFMGFIGLVGEPGIVGEKGDrgmmgppgvpgpkgs 1026
Cdd:NF038329 181 -------------EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD--------------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1027 mghpgmpggmgtpgepgpqgppgsrgppgmrGAKGRRGPRGPDGPAGEQGSRGlkgppgpqgrpgrpgqqgvagERGHLG 1106
Cdd:NF038329 233 -------------------------------GQQGPDGDPGPTGEDGPQGPDG---------------------PAGKDG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1107 SRGFPGIPGPSgppgtkglpgepgpqgpqgpigppgemgpkGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEP 1186
Cdd:NF038329 261 PRGDRGEAGPD------------------------------GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD 310
|
330 340
....*....|....*....|....*...
gi 2462626959 1187 GLEGDSGPMGPDGLKGDRGDPGPDGEHG 1214
Cdd:NF038329 311 GLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
272-603 |
4.51e-14 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 78.44 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 272 TATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAklsasnaldpmLPASVGGSTRTPRPAAA 351
Cdd:PHA03247 2636 NEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRA-----------ARPTVGSLTSLADPPPP 2704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 352 QPSQKITATKIPKSLPTKP-------SAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPtekPI 424
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPgpaaarqASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP---PR 2781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 425 QRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTeakitshASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPAT 504
Cdd:PHA03247 2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPA-------AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGG 2854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 505 MVPPTSGTS---TPRTAPAVPTPGSAPTGSKKPiGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPR-QPQP 580
Cdd:PHA03247 2855 SVAPGGDVRrrpPSRSPAAKPAAPARPPVRRLA-RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpQPPP 2933
|
330 340
....*....|....*....|...
gi 2462626959 581 SQQTTPALVLAPAQFLSSSPRPT 603
Cdd:PHA03247 2934 PPPPRPQPPLAPTTDPAGAGEPS 2956
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
43-218 |
7.05e-13 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 68.92 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 43 DVDILQRLGLSWTKAGSPAPPGVIPFQSGFIFTQRARLQAPTGTVIPAALGTELALVLSLCSHRVNHAFLFAVRSQKRKL 122
Cdd:smart00210 1 GQDLLQVFDLPSLSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDAQNVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 123 QLGLQFLPGKTVVHL------GSRRSVAF-DLDMHDGRWHHLALELRGRTVTLVTACGQR-RVPVLLPFHrdPALDPGGS 194
Cdd:smart00210 81 QFGLEVDGRANTLLLryqgvdGKQHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIdSRPLDRPGQ--PPIDTDGI 158
|
170 180
....*....|....*....|....
gi 2462626959 195 FLFGKMNPHAVQFEGALCQFSIYP 218
Cdd:smart00210 159 EVRGAQAADRKPFQGDLQQLKIVC 182
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
279-606 |
1.17e-12 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 72.69 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 279 SLPAGR-GPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLlpaKLSASNALDPMLPASVggSTRTPRPAAAQPSqki 357
Cdd:pfam17823 98 SEPATReGAADGAASRALAAAASSSPSSAAQSLPAAIAALPSE---AFSAPRAAACRANASA--APRAAIAAASAPH--- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 358 TATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKS-------------ALPTQKQVPPTSRPVPARVSrptekpi 424
Cdd:pfam17823 170 AASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPArgistaatatghpAAGTALAAVGNSSPAAGTVT------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 425 qrnpgmprppppstrplPPTTSSSKKPIPTLARTEAKITSHA-----SKPASARTSTHKPPPFTALSSSPAPTPGS-TRS 498
Cdd:pfam17823 243 -----------------AAVGTVTPAALATLAAAAGTVASAAgtinmGDPHARRLSPAKHMPSDTMARNPAAPMGAqAQG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 499 TRPPATMVPP---TSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSP 575
Cdd:pfam17823 306 PIIQVSTDQPvhnTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPSP 385
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2462626959 576 RqpQPSQQTT-PALVLAPAQF--------LSSSPRPTSSG 606
Cdd:pfam17823 386 L--LPTQGAAgPGILLAPEQVateatagtASAGPTPRSSG 423
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
273-629 |
2.11e-12 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 73.05 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 273 ATPALGSLPAG-RGPRGTVAPATPTKPQRTSPTNPhqhmaVGGPAQTPLLPAKLSASNALDPMLP--ASVGGSTRTPRPA 349
Cdd:PHA03247 2593 PQSARPRAPVDdRGDPRGPAPPSPLPPDTHAPDPP-----PPSPSPAANEPDPHPPPTVPPPERPrdDPAPGRVSRPRRA 2667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 350 AAQpsQKITATKIPKSLPTKPSAPST--SIVPIKSPHPTQKT--APSSFTKSALPTqkqvPPTSRPVPARVSRPTEKPIQ 425
Cdd:PHA03247 2668 RRL--GRAAQASSPPQRPRRRAARPTvgSLTSLADPPPPPPTpePAPHALVSATPL----PPGPAAARQASPALPAAPAP 2741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 426 RNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEA-----KITSHASKPASARTSTHKPP--PFTALSSSPAPTPGSTRS 498
Cdd:PHA03247 2742 PAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAagpprRLTRPAVASLSESRESLPSPwdPADPPAAVLAPAAALPPA 2821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 499 TRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKP-VPLRPGKAARDVPLSDLTTRPSP-- 575
Cdd:PHA03247 2822 ASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPaAPARPPVRRLARPAVSRSTESFAlp 2901
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462626959 576 -----RQPQPSQQTTPALVLAPAQFLSSSPRPTSSGYSIFHLAgstPFPLLMGPPGPKG 629
Cdd:PHA03247 2902 pdqpeRPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLA---PTTDPAGAGEPSG 2957
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
281-778 |
3.74e-12 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 72.28 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 281 PAGRGPRGTVAPATPTKPQRTSPTNPhqhmAVGGPAQTPLLP-----AKLSASNALDP-------MLPASVGGSTRTPRP 348
Cdd:PHA03247 2498 PGGGGPPDPDAPPAPSRLAPAILPDE----PVGEPVHPRMLTwirglEELASDDAGDPppplppaAPPAAPDRSVPPPRP 2573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 349 AAAQPSQKITATKIPKSLPTKPSAPSTsivPIKSPHPTQKTAPSSftksalPTQKQVPPTSRPVPARVSRPTEKPiqrnp 428
Cdd:PHA03247 2574 APRPSEPAVTSRARRPDAPPQSARPRA---PVDDRGDPRGPAPPS------PLPPDTHAPDPPPPSPSPAANEPD----- 2639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 429 GMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKPP--PFTALSSSPAPTPGSTRSTRPPATMV 506
Cdd:PHA03247 2640 PHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTvgSLTSLADPPPPPPTPEPAPHALVSAT 2719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 507 PPTSGTSTPRTA----PAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLR-----PGKAARDVPLSDLT----TRP 573
Cdd:PHA03247 2720 PLPPGPAAARQAspalPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAapaagPPRRLTRPAVASLSesreSLP 2799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 574 SPRQPQPSqqttPALVLAPAQFLSSSPRPTSsgysifhLAGSTPFPLLMGPPGPKGdcGLPGPPGLPGLPGIPGARGPRG 653
Cdd:PHA03247 2800 SPWDPADP----PAAVLAPAAALPPAASPAG-------PLPPPTSAQPTAPPPPPG--PPPPSLPLGGSVAPGGDVRRRP 2866
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 654 PPGPYGNPGLPGPPGAKGQKGDPGLSPgkahdgAKGDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAK 733
Cdd:PHA03247 2867 PSRSPAAKPAAPARPPVRRLARPAVSR------STESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ 2940
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2462626959 734 GYPGRQGLPGPVGDPGPKGSRGYIG--LPGLFGLPGSDGERGLPGVP 778
Cdd:PHA03247 2941 PPLAPTTDPAGAGEPSGAVPQPWLGalVPGRVAVPRFRVPQPAPSRE 2987
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
270-574 |
1.42e-11 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 70.35 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 270 LTTATPalgsLPAGRGPRGTVAPATPTKPqrTSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASvGGSTRTPRPA 349
Cdd:PHA03247 2715 LVSATP----LPPGPAAARQASPALPAAP--APPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA-GPPRRLTRPA 2787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 350 AAQ-------------PSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPP--------T 408
Cdd:PHA03247 2788 VASlsesreslpspwdPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPggdvrrrpP 2867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 409 SRPVPARVSRPTEKPIQRnpgmprpppPSTRPLPPTTSSSKKPIPTLARTEakitshaSKPASARTSTHKPPPFTALSSS 488
Cdd:PHA03247 2868 SRSPAAKPAAPARPPVRR---------LARPAVSRSTESFALPPDQPERPP-------QPQAPPPPQPQPQPPPPPQPQP 2931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 489 PAPTPGstrstRPPATMVPPTSGTSTPRTAPAVPTPgsaPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSD 568
Cdd:PHA03247 2932 PPPPPP-----RPQPPLAPTTDPAGAGEPSGAVPQP---WLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSR 3003
|
....*.
gi 2462626959 569 LTTRPS 574
Cdd:PHA03247 3004 VSSWAS 3009
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1498-1628 |
1.03e-10 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 66.08 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1498 QLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGIL 1577
Cdd:NF038329 112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2462626959 1578 GPSGLPGPKGDKGSRGDWGLQGPRGPPGPRGRPGPPGPPGGPIQLQQDDLG 1628
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG 242
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
269-624 |
2.23e-09 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 62.63 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 269 NLTTATPA---LGSLPAGRGPRGTVAPATPTKPQRTSPTNphqhmAVGGP---AQTPLLPAKLSASNALDPML-PASVGG 341
Cdd:pfam05109 472 DVTSPTPAgttSGASPVTPSPSPRDNGTESKAPDMTSPTS-----AVTTPtpnATSPTPAVTTPTPNATSPTLgKTSPTS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 342 STRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSsftksalpTQKQVPPTSRPVPARVSRPTE 421
Cdd:pfam05109 547 AVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGE--------TSPQANTTNHTLGGTSSTPVV 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 422 KPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIP---TLA-RTEAKITSH-----ASKPASARTSTHKPPPFTAL----SSS 488
Cdd:pfam05109 619 TSPPKNATSAVTTGQHNITSSSTSSMSLRPSSiseTLSpSTSDNSTSHmplltSAHPTGGENITQVTPASTSThhvsTSS 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 489 PAPTPGSTRSTRPP---ATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASkkAGPKSSPRKPVPLRPGKAARDVp 565
Cdd:pfam05109 699 PAPRPGTTSQASGPgnsSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTS--TGGKANSTTGGKHTTGHGARTS- 775
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462626959 566 lSDLTTRPSPRQPQPSQQTTPALVLAPAQFLSSSPRPTSSGYSIFHLAGSTPFPLLMGP 624
Cdd:pfam05109 776 -TEPTTDYGGDSTTPRTRYNATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPTSQP 833
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
270-605 |
2.68e-08 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 59.41 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 270 LTTATPALGSLPAGRGPRGTVAPATPTkpqrtSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPA 349
Cdd:PHA03307 50 LAAVTVVAGAAACDRFEPPTGPPPGPG-----TEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 350 AAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPTEKPiqrnpg 429
Cdd:PHA03307 125 SPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTP------ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 430 MPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHK------------PPPFTALSSSPAPTPGSTR 497
Cdd:PHA03307 199 PAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCgwgpenecplprPAPITLPTRIWEASGWNGP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 498 STRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKK-----PIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSdltTR 572
Cdd:PHA03307 279 SSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRAsssssSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSP---SR 355
|
330 340 350
....*....|....*....|....*....|...
gi 2462626959 573 PSPRQPQPSQQTTPALVLAPAQFLSSSPRPTSS 605
Cdd:PHA03307 356 PPPPADPSSPRKRPRPSRAPSSPAASAGRPTRR 388
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
235-587 |
5.90e-08 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 57.85 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 235 GQADTYQSPLGPLFSQDSGRPFTFQSDLAllglenltTATPALGSLPAGRGPrgtvaPATPTKPQRTSPTNPHQHMAVGG 314
Cdd:pfam03154 169 TQPPVLQAQSGAASPPSPPPPGTTQAATA--------GPTPSAPSVPPQGSP-----ATSQPPNQTQSTAAPHTLIQQTP 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 315 PAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPAAAQPSQ------KITATKIPKSLPTKP----SAPSTSIVP----I 380
Cdd:pfam03154 236 TLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPpmphslQTGPSHMQHPVPPQPfpltPQSSQSQVPpgpsP 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 381 KSPHPTQKTAPSSFTKSALPTQKqvPPTSRPV-PARVSRPTEKPiqrnpgmprppppstrplppttsSSKKPIPTLARTE 459
Cdd:pfam03154 316 AAPGQSQQRIHTPPSQSQLQSQQ--PPREQPLpPAPLSMPHIKP-----------------------PPTTPIPQLPNPQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 460 A-KITSHASKPASARTSTHKPPP--FTALSSSPAPTPGSTRStrPPATMVPPTSGTSTPRTAPAVPT--PGSAPTGSKKP 534
Cdd:pfam03154 371 ShKHPPHLSGPSPFQMNSNLPPPpaLKPLSSLSTHHPPSAHP--PPLQLMPQSQQLPPPPAQPPVLTqsQSLPPPAASHP 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 535 igSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQP--QPSQQTTPA 587
Cdd:pfam03154 449 --PTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPgiQPPSSASVS 501
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
235-546 |
1.63e-07 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 56.12 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 235 GQADTYQS--PLGPLFSQDSGRPFTFQSDLALLGLENLTTATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMAV 312
Cdd:pfam17823 105 GAADGAASraLAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 313 GGPAQTPLLPAKLSASNALDPMLPAS--VGGSTRTPRPAAAqpsqkiTATKipkSLPTKPSAPSTSIVPIKSPHP----T 386
Cdd:pfam17823 185 ASSTTAASSAPTTAASSAPATLTPARgiSTAATATGHPAAG------TALA---AVGNSSPAAGTVTAAVGTVTPaalaT 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 387 QKTAPSSFTKSALPTQKQVPPTSRPVPARvSRPTE----KPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKI 462
Cdd:pfam17823 256 LAAAAGTVASAAGTINMGDPHARRLSPAK-HMPSDtmarNPAAPMGAQAQGPIIQVSTDQPVHNTAGEPTPSPSNTTLEP 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 463 T---SHASKPASARTSTH---KPPpftalSSSPAPTPGSTRSTRPPATM-------VPPTSGTSTPRTAPAVPTPGSAPT 529
Cdd:pfam17823 335 NtpkSVASTNLAVVTTTKaqaKEP-----SASPVPVLHTSMIPEVEATSpttqpspLLPTQGAAGPGILLAPEQVATEAT 409
|
330
....*....|....*..
gi 2462626959 530 GSKKPIGSEASKKAGPK 546
Cdd:pfam17823 410 AGTASAGPTPRSSGDPK 426
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
246-554 |
2.59e-07 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 55.93 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 246 PLFSQDSGRPFTFQSDLALLGLENLTTATPALGSLPAGRGPRGTVAPATPTKPQRTS-PTNPH------QHMAVGGPAQT 318
Cdd:pfam03154 218 PNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQmPPMPHslqtgpSHMQHPVPPQP 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 319 PLLPAKLSASNALDPMLPASVGGSTRT-------PRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSP----HPTQ 387
Cdd:pfam03154 298 FPLTPQSSQSQVPPGPSPAAPGQSQQRihtppsqSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPqshkHPPH 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 388 KTAPSSFT-KSALPTQKQVPPTSRPVPARVSRPTEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHA 466
Cdd:pfam03154 378 LSGPSPFQmNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVP 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 467 SKPASARTS--THKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTstprtAPAVPTPGSAPTGSKKPIGSEASKKAG 544
Cdd:pfam03154 458 SQSPFPQHPfvPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGP-----VPAAVSCPLPPVQIKEEALDEAEEPES 532
|
330
....*....|
gi 2462626959 545 PKSSPRKPVP 554
Cdd:pfam03154 533 PPPPPRSPSP 542
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
275-586 |
3.92e-07 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 55.24 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 275 PALGslpAGRGPRGTVAPATPTkpqrtsptnphqhmAVGGPAQTPLLPAKLSASnaldPMLPASVGGSTRTPRPAAAQPS 354
Cdd:PRK07003 360 PAVT---GGGAPGGGVPARVAG--------------AVPAPGARAAAAVGASAV----PAVTAVTGAAGAALAPKAAAAA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 355 QKiTATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPTEKPIQRNpgmprpp 434
Cdd:PRK07003 419 AA-TRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAF------- 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 435 ppstrplppttsSSKKPIPTLARTEAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTR-----PPATMVPPT 509
Cdd:PRK07003 491 ------------EPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAAraggaAAALDVLRN 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 510 SG----TSTPRTAPAVPTPGSAPTGSKKPigseaskkagpkSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTT 585
Cdd:PRK07003 559 AGmrvsSDRGARAAAAAKPAAAPAAAPKP------------AAPRVAVQVPTPRARAATGDAPPNGAARAEQAAESRGAP 626
|
.
gi 2462626959 586 P 586
Cdd:PRK07003 627 P 627
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
273-592 |
4.68e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 55.33 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 273 ATPALGSLPAGRG-PRGTVAPATPTKPQR-------TSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTR 344
Cdd:PHA03247 2731 ASPALPAAPAPPAvPAGPATPGGPARPARppttagpPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 345 TPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQ---------KTAPSSFTKSALPTQKQVPPTSRPVPAR 415
Cdd:PHA03247 2811 VLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGgsvapggdvRRRPPSRSPAAKPAAPARPPVRRLARPA 2890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 416 VSRPTE-------------KPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLA-RTEAKITSHASKPASARTSTHKPPP 481
Cdd:PHA03247 2891 VSRSTEsfalppdqperppQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLApTTDPAGAGEPSGAVPQPWLGALVPG 2970
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 482 FTALSSSPAPTPGSTRSTrpPATMVPPTSGTSTPRTAP----------AVPTPGSAPTGSKKPIGSEASKKAGPKSSPRK 551
Cdd:PHA03247 2971 RVAVPRFRVPQPAPSREA--PASSTPPLTGHSLSRVSSwasslalheeTDPPPVSLKQTLWPPDDTEDSDADSLFDSDSE 3048
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2462626959 552 PVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTTPALVLAP 592
Cdd:PHA03247 3049 RSDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSSQFGP 3089
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
266-612 |
6.28e-07 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 54.54 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 266 GLENLTTATPALGSLPAGRGPRGTvAPAT--PTKPQRTSPTNPHQHMAVGGPAQTPLLPAkLSASNALDPMLPASVGGST 343
Cdd:pfam05109 375 GCENISGAFASNRTFDITVSGLGT-APKTliITRTATNATTTTHKVIFSKAPESTTTSPT-LNTTGFAAPNTTTGLPSST 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 344 RTPRPAAAQPSQKITATKIPKSLPTkPSAPSTSIVPIK-SPHPTQKTAPSSFTKSALPTQKQVPPT---SRPVPArVSRP 419
Cdd:pfam05109 453 HVPTNLTAPASTGPTVSTADVTSPT-PAGTTSGASPVTpSPSPRDNGTESKAPDMTSPTSAVTTPTpnaTSPTPA-VTTP 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 420 TEKPIQrnpgmprppppstrplppttssskkpiPTLARTEakitshaskPASARTSthkPPPftalsSSPAPTPGSTRST 499
Cdd:pfam05109 531 TPNATS---------------------------PTLGKTS---------PTSAVTT---PTP-----NATSPTPAVTTPT 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 500 rPPATMvpPTSGTSTPRTAPAVPTP-GSAPT-GSKKPIGSEASKKAGPKSSprKPVPLRPGKAArdvplsdlTTRPSPRQ 577
Cdd:pfam05109 567 -PNATI--PTLGKTSPTSAVTTPTPnATSPTvGETSPQANTTNHTLGGTSS--TPVVTSPPKNA--------TSAVTTGQ 633
|
330 340 350
....*....|....*....|....*....|....*
gi 2462626959 578 PQPSQQTTPALVLAPAQfLSSSPRPTSSGYSIFHL 612
Cdd:pfam05109 634 HNITSSSTSSMSLRPSS-ISETLSPSTSDNSTSHM 667
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
689-745 |
5.93e-06 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 45.18 E-value: 5.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462626959 689 GDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPV 745
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
326-547 |
6.57e-06 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 50.32 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 326 SASNALDPMLPASVGGSTRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIkSPHPTQKTAPSSFTKSALpTQKQV 405
Cdd:PRK10905 33 SGEKSIDLAGNATDQANGVQPAPGTTSAEQTAGNTQQDVSLPPISSTPTQGQTPV-ATDGQQRVEVQGDLNNAL-TQPQN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 406 PPTSRPVPARVSRPTE----KPIQRNPGMPRPPPPStrplppttSSSKKPIPTLARTEAKItsHASKPASARTSTHKPPP 481
Cdd:PRK10905 111 QQQLNNVAVNSTLPTEpatvAPVRNGNASRQTAKTQ--------TAERPATTRPARKQAVI--EPKKPQATAKTEPKPVA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462626959 482 FTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKS 547
Cdd:PRK10905 181 QTPKRTEPAAPVASTKAPAATSTPAPKETATTAPVQTASPAQTTATPAAGGKTAGNVGSLKSAPSS 246
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
457-616 |
6.86e-06 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 50.73 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 457 RTEAKITSHA---SKPASaRTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTApAVPTPGSAptGSKK 533
Cdd:pfam17823 85 EVTAEHTPHGtdlSEPAT-REGAADGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAA-ACRANASA--APRA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 534 PIGSEASKKAG---PKSSPRKPVPLRPGKAARDVPLSDLTTRPS---PRQPQPSQQT---TPALVLAPAQFLSSSPRPTS 604
Cdd:pfam17823 161 AIAAASAPHAAspaPRTAASSTTAASSTTAASSAPTTAASSAPAtltPARGISTAATatgHPAAGTALAAVGNSSPAAGT 240
|
170
....*....|..
gi 2462626959 605 SGYSIFHLAGST 616
Cdd:pfam17823 241 VTAAVGTVTPAA 252
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
695-750 |
9.41e-06 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 44.79 E-value: 9.41e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462626959 695 GLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGP 750
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
348-584 |
9.48e-06 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 50.70 E-value: 9.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 348 PAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSrPVParvSRPTEKPIQRN 427
Cdd:PLN03209 324 PSQRVPPKESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYTAYEDLKPPTS-PIP---TPPSSSPASSK 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 428 PGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHAS--------KPAS---------ARTSTHKPPPFTALSSSPA 490
Cdd:PLN03209 400 SVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSpyaryedlKPPTspsptaptgVSPSVSSTSSVPAVPDTAP 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 491 PTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLT 570
Cdd:PLN03209 480 ATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQPKPRPLSPYT 559
|
250
....*....|....*...
gi 2462626959 571 T----RPsPRQPQPSQQT 584
Cdd:PLN03209 560 MyedlKP-PTSPTPSPVL 576
|
|
| PHA03269 |
PHA03269 |
envelope glycoprotein C; Provisional |
446-554 |
1.58e-05 |
|
envelope glycoprotein C; Provisional
Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 49.73 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 446 SSSKKPIPTLARTEAkiTSHASKPASARTS--THKPPPFTALSSS------PAPTPGSTRSTRPPATMVPPTSGTSTPRt 517
Cdd:PHA03269 35 AATQKPDPAPAPHQA--ASRAPDPAVAPTSaaSRKPDLAQAPTPAasekfdPAPAPHQAASRAPDPAVAPQLAAAPKPD- 111
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462626959 518 aPAVPtPGSAPTgskkpiGSEASKKAGPKSSPRKPVP 554
Cdd:PHA03269 112 -AAEA-FTSAAQ------AHEAPADAGTSAASKKPDP 140
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
340-586 |
2.17e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 49.69 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 340 GGSTRTPRPAAA-QPSQKITATKIPkSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSR 418
Cdd:PTZ00449 555 GEVGKKPGPAKEhKPSKIPTLSKKP-EFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSP 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 419 PTEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPI-PTLA-RTEAKITSHASKPASARTSTHKPPPFTALSSSPAP-TPGS 495
Cdd:PTZ00449 634 KRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFdPKFKeKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPeTPGT 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 496 TRSTRPPATMVPPT--SGTSTPRTAPAVPTPgSAPTGSKKPIGSEASKKAGPKSSPrkpvplRPGKAARDVPLSDLTTRP 573
Cdd:PTZ00449 714 PFTTPRPLPPKLPRdeEFPFEPIGDPDAEQP-DDIEFFTPPEEERTFFHETPADTP------LPDILAEEFKEEDIHAET 786
|
250 260
....*....|....*....|.
gi 2462626959 574 S--------PRQPQPSQQTTP 586
Cdd:PTZ00449 787 GepdeamkrPDSPSEHEDKPP 807
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
701-755 |
2.51e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 43.25 E-value: 2.51e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 701 GPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRG 755
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
370-552 |
2.97e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 49.30 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 370 PSAPSTSIVPIKSP---------HPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPTEKPIQrnpgmprppppstrp 440
Cdd:PTZ00449 511 PEGPEASGLPPKAPgdkegeegeHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTL--------------- 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 441 lppttssSKKPiptlarTEAKITSHASKPASARTSTHkppPFTALSSSPAPTPgstrsTRPPATMVPPTSGTSTPRTAPA 520
Cdd:PTZ00449 576 -------SKKP------EFPKDPKHPKDPEEPKKPKR---PRSAQRPTRPKSP-----KLPELLDIPKSPKRPESPKSPK 634
|
170 180 190
....*....|....*....|....*....|..
gi 2462626959 521 VPTPGSAPTGSKKPIGSEASKKAGPKSSPRKP 552
Cdd:PTZ00449 635 RPPPPQRPSSPERPEGPKIIKSPKPPKSPKPP 666
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
336-593 |
3.86e-05 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 48.91 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 336 PASVGGSTRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSfTKSALPTQ---KQVPPTSRPV 412
Cdd:PHA03378 553 PASTEPVHDQLLPAPGLGPLQIQPLTSPTTSQLASSAPSYAQTPWPVPHPSQTPEPPT-TQSHIPETsapRQWPMPLRPI 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 413 PARVSR-----------------PTEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKP--IPTLARTEAKITSHASKPASAR 473
Cdd:PHA03378 632 PMRPLRmqpitfnvlvfptphqpPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIqwAPGTMQPPPRAPTPMRPPAAPP 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 474 TSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTpRTAPAVPTPGSAPTgskkpigseaskkagPKSSPRKPV 553
Cdd:PHA03378 712 GRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPG-RARPPAAAPGRARP---------------PAAAPGAPT 775
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2462626959 554 PLRPGKAArDVPLSDLTTRPSPrQPQPSQQTTPALVLAPA 593
Cdd:PHA03378 776 PQPPPQAP-PAPQQRPRGAPTP-QPPPQAGPTSMQLMPRA 813
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
698-754 |
4.53e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 42.87 E-value: 4.53e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462626959 698 GNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSR 754
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| DUF4045 |
pfam13254 |
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ... |
278-553 |
5.91e-05 |
|
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.
Pssm-ID: 433066 [Multi-domain] Cd Length: 415 Bit Score: 47.47 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 278 GSLPAGRGprGTVAPATPTKPQRTS-------PTNPHQHMAVGGPAQTPLLPAKLSASNAlDPMLPASvggsTRTPRPAA 350
Cdd:pfam13254 47 GSVAGPSG--SLSPGLSPTKLSREGspestsrPSSSHSEATIVRHSKDDERPSTPDEGFV-KPALPRH----SRSSSALS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 351 AQPSQKITAtkipkSLPTKPSAPSTSIVPiKSPHPTqktaPSSFTKSAL-----PTQKQVPPT----------------- 408
Cdd:pfam13254 120 NTGSEEDSP-----SLPTSPPSPSKTMDP-KRWSPT----KSSWLESALnrpesPKPKAQPSQpaqpawmkelnkirqsr 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 409 -----SRPVPARVSRPTEkpIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTlARTEAKITSHASKPASARTSTHKPPPFT 483
Cdd:pfam13254 190 asvdlGRPNSFKEVTPVG--LMRSPAPGGHSKSPSVSGISADSSPTKEEPS-EEADTLSTDKEQSPAPTSASEPPPKTKE 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462626959 484 ALSSS---PAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSkKPIGSEASKKAGPKSSPRKPV 553
Cdd:pfam13254 267 LPKDSeepAAPSKSAEASTEKKEPDTESSPETSSEKSAPSLLSPVSKASID-KPLSSPDRDPLSPKPKPQSPP 338
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
451-627 |
6.18e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 47.95 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 451 PIPTLARTEAKITSHASKPASA---RTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSA 527
Cdd:PRK12323 374 PATAAAAPVAQPAPAAAAPAAAapaPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 528 PTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAArdvplsdlttrpsprQPQPSQQTTPALVLAPAQFLSSSPRPTSSGY 607
Cdd:PRK12323 454 PAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAA---------------APAPADDDPPPWEELPPEFASPAPAQPDAAP 518
|
170 180
....*....|....*....|
gi 2462626959 608 SIFHLAgSTPFPLLMGPPGP 627
Cdd:PRK12323 519 AGWVAE-SIPDPATADPDDA 537
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1461-1515 |
7.40e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 42.10 E-value: 7.40e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 1461 GDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPG 1515
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
725-781 |
1.09e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 41.71 E-value: 1.09e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462626959 725 GPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKR 781
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PHA03269 |
PHA03269 |
envelope glycoprotein C; Provisional |
397-529 |
1.36e-04 |
|
envelope glycoprotein C; Provisional
Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 46.65 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 397 SALPTQKQVPPTSRPVPARVSRPTEKPIQRnpgmprPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTST 476
Cdd:PHA03269 20 ANLNTNIPIPELHTSAATQKPDPAPAPHQA------ASRAPDPAVAPTSAASRKPDLAQAPTPAASEKFDPAPAPHQAAS 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462626959 477 HKPPPFTALSSSPAPTPG-----STRSTRPPATMVPPTSgTSTPRTAPAVPTPGSAPT 529
Cdd:PHA03269 94 RAPDPAVAPQLAAAPKPDaaeafTSAAQAHEAPADAGTS-AASKKPDPAAHTQHSPPP 150
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
281-527 |
1.49e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 46.79 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 281 PAGRGprGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPAAaqpsqkitat 360
Cdd:PRK12323 365 PGQSG--GGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEA---------- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 361 kipksLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPTEKPIQRNPGMPRPPPPSTRP 440
Cdd:PRK12323 433 -----LAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 441 LPPTTSSSKKPIPTLArteAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPP---ATMVPPTSGTSTPRT 517
Cdd:PRK12323 508 SPAPAQPDAAPAGWVA---ESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPrasASGLPDMFDGDWPAL 584
|
250
....*....|
gi 2462626959 518 APAVPTPGSA 527
Cdd:PRK12323 585 AARLPVRGLA 594
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1479-1533 |
1.90e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 40.94 E-value: 1.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 1479 GLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMG 1533
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
466-606 |
2.28e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 46.25 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 466 ASKPASARTSTHKPPPFTALSSSPAPTP--GSTRSTRPPATMVPPtsgtsTPRTAPAVPTPGSAPtgskkpigSEASKKA 543
Cdd:PRK14951 370 AEAAAPAEKKTPARPEAAAPAAAPVAQAaaAPAPAAAPAAAASAP-----AAPPAAAPPAPVAAP--------AAAAPAA 436
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462626959 544 GPKSSPRkPVPLRPGKAARDVP-LSDLTTRPSPRQPQPSQQTTPALVLAPAqflssSPRPTSSG 606
Cdd:PRK14951 437 APAAAPA-AVALAPAPPAQAAPeTVAIPVRVAPEPAVASAAPAPAAAPAAA-----RLTPTEEG 494
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
358-604 |
2.87e-04 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 45.72 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 358 TATKIPKSLPTKPSAP---STSIVPIKSPHPTQKTAPS-------SFTKSALPTqkqvPPTSRPVPARVSRPTekpiqrn 427
Cdd:pfam17823 64 TAAPAPVTLTKGTSAAhlnSTEVTAEHTPHGTDLSEPAtregaadGAASRALAA----AASSSPSSAAQSLPA------- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 428 pgmprppppstrpLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHkpppftalSSSPAPTPGSTRSTRPPATMVP 507
Cdd:pfam17823 133 -------------AIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPH--------AASPAPRTAASSTTAASSTTAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 508 PTSGTSTPRTAPAVPTPGS----APTGSKKPIGSEASKKAGPKSsprkPVPLRPGKAARDVPLSDLTT------------ 571
Cdd:pfam17823 192 SSAPTTAASSAPATLTPARgistAATATGHPAAGTALAAVGNSS----PAAGTVTAAVGTVTPAALATlaaaagtvasaa 267
|
250 260 270
....*....|....*....|....*....|....*....
gi 2462626959 572 ------RPSPRQPQPSQQTtpalvlaPAQFLSSSPRPTS 604
Cdd:pfam17823 268 gtinmgDPHARRLSPAKHM-------PSDTMARNPAAPM 299
|
|
| rad23 |
TIGR00601 |
UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
458-529 |
3.22e-04 |
|
UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273167 [Multi-domain] Cd Length: 378 Bit Score: 45.27 E-value: 3.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462626959 458 TEAKITSHASKPASARTSTHKPPPFTALSSSPAPTpgstrSTRPPATMVPPTSGTSTPRT-APAVPTPGSAPT 529
Cdd:TIGR00601 80 GTGKVAPPAATPTSAPTPTPSPPASPASGMSAAPA-----SAVEEKSPSEESATATAPESpSTSVPSSGSDAA 147
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1473-1527 |
4.26e-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: 39.78 E-value: 4.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 1473 GNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPG 1527
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1377-1431 |
4.89e-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: 4.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 1377 GQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVG 1431
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
451-630 |
4.99e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.31 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 451 PIPTLARTE-AKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAP---------- 519
Cdd:PHA03247 255 PAPPPVVGEgADRAPETARGATGPPPPPEAAAPNGAAAPPDGVWGAALAGAPLALPAPPDPPPPAPAGDAeeeddedgam 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 520 --AVPTP---GSAPTGSKK-------PIGSEASKKAGPKSSPRKPVPLRPGKAARDV-------PLSDLTTRPSPRQPQP 580
Cdd:PHA03247 335 evVSPLPrprQHYPLGFPKrrrptwtPPSSLEDLSAGRHHPKRASLPTRKRRSARHAatpfargPGGDDQTRPAAPVPAS 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462626959 581 SQQTTPALVLAPAQFLSSSPRPTSSGYSifhlAGSTPFPLLMGPPGPKGD 630
Cdd:PHA03247 415 VPTPAPTPVPASAPPPPATPLPSAEPGS----DDGPAPPPERQPPAPATE 460
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
1422-1596 |
5.05e-04 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 44.64 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1422 GLPGPRGVVGRQGLEGIAGPDGLPGRDGQAGQQGEQGDDGDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGP 1501
Cdd:COG5164 10 GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1502 PGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLF--GPKGPPGDIGfkgiQGPRGpPGLMGKEGIVGPLGILGP 1579
Cdd:COG5164 90 TRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGG----STPPG-PGSTGPGGSTTPPGDGGS 164
|
170
....*....|....*..
gi 2462626959 1580 SGLPGPKGDKGSRGDWG 1596
Cdd:COG5164 165 TTPPGPGGSTTPPDDGG 181
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1380-1434 |
5.24e-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: 5.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 1380 GQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQG 1434
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Metaviral_G |
pfam09595 |
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. ... |
359-511 |
5.25e-04 |
|
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. It is high in serine and threonine suggesting it is highly glycosylated.
Pssm-ID: 462833 [Multi-domain] Cd Length: 183 Bit Score: 43.02 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 359 ATKIPKSLPTKPSAPSTSIVP---IKSPHPTQKTAPSSftkSALPTQKQVPPTSRPvparvsRPTEKPIQRNPGMPRPPP 435
Cdd:pfam09595 31 ASLILIGESNKEAALIITDIIdinINKQHPEQEHHENP---PLNEAAKEAPSESED------APDIDPNNQHPSQDRSEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 436 PSTRPLPPTTSSSKKP--IPTLARTEAKITSHASKPASART----STHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPT 509
Cdd:pfam09595 102 PPLEPAAKTKPSEHEPanPPDASNRLSPPDASTAAIREARTfrkpSTGKRNNPSSAQSDQSPPRANHEAIGRANPFAMSS 181
|
..
gi 2462626959 510 SG 511
Cdd:pfam09595 182 TG 183
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1371-1427 |
5.34e-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: 5.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462626959 1371 GLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPR 1427
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
686-734 |
5.72e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.40 E-value: 5.72e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2462626959 686 GAKGDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKG 734
Cdd:pfam01391 7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
466-580 |
6.67e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 44.47 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 466 ASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVP--TPGSAPTGSKKPIGSEASKKA 543
Cdd:PRK07994 358 AFHPAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPlpETTSQLLAARQQLQRAQGATK 437
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462626959 544 GPKSSPRKPVPLRPGKAARDvPLSDLTTRPSPRQPQP 580
Cdd:PRK07994 438 AKKSEPAAASRARPVNSALE-RLASVRPAPSALEKAP 473
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1374-1428 |
7.54e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.40 E-value: 7.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 1374 GKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRG 1428
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1500-1554 |
7.92e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.01 E-value: 7.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 1500 GPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKG 1554
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| motB |
PRK12799 |
flagellar motor protein MotB; Reviewed |
461-604 |
9.15e-04 |
|
flagellar motor protein MotB; Reviewed
Pssm-ID: 183756 [Multi-domain] Cd Length: 421 Bit Score: 43.94 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 461 KITSHASKPASArtsthkPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGsapTGSKKPIGSEAS 540
Cdd:PRK12799 292 QIDTHGTVPVAA------VTPSSAVTQSSAITPSSAAIPSPAVIPSSVTTQSATTTQASAVALSS---AGVLPSDVTLPG 362
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462626959 541 KKAGPKSSPRKPVPlRPGKAARDVPLSDLTTRPSPRQPqpsqqtTPALVLAPAQflSSSPRPTS 604
Cdd:PRK12799 363 TVALPAAEPVNMQP-QPMSTTETQQSSTGNITSTANGP------TTSLPAAPAS--NIPVSPTS 417
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1362-1416 |
9.83e-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: 9.83e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 1362 GYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRG 1416
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
336-529 |
1.11e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 43.71 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 336 PASVGGSTRTPRPAAAQPSQKITATKIPKSL---PTKPSAPSTSIVPIKSPHPTQKTAPS--SFTKSALPTQKQV----- 405
Cdd:PRK12323 365 PGQSGGGAGPATAAAAPVAQPAPAAAAPAAAapaPAAPPAAPAAAPAAAAAARAVAAAPArrSPAPEALAAARQAsargp 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 406 ------PPTSRPVPARVSRPTEKPIQRNPGMpRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKP 479
Cdd:PRK12323 445 ggapapAPAPAAAPAAAARPAAAGPRPVAAA-AAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVA 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462626959 480 PPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPT 529
Cdd:PRK12323 524 ESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGL 573
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1491-1547 |
1.16e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 38.63 E-value: 1.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462626959 1491 GESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPP 1547
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1383-1437 |
1.18e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 38.63 E-value: 1.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 1383 GHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEG 1437
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
134-202 |
1.19e-03 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 40.87 E-value: 1.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462626959 134 VVHLGSRRSVAFDLD--MHDGRWHHLALELRGRTVTLVTaCGQRRVPVLLPfHRDPALDPGGSFLFGKMNP 202
Cdd:pfam02210 33 RYDLGSGPESLLSSGknLNDGQWHSVRVERNGNTLTLSV-DGQTVVSSLPP-GESLLLNLNGPLYLGGLPP 101
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1476-1531 |
1.47e-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: 38.24 E-value: 1.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462626959 1476 GVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGE 1531
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
282-586 |
1.57e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 43.45 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 282 AGRG--PRGTVAPATPTKPQRT------SPTNPHQHMAVGGPAQTPLLPAklSASNALDPMLPAS----VGGSTRTPRPA 349
Cdd:TIGR00927 97 VGRDeaTPSIAMENTPSPPRRTakitptTPKNNYSPTAAGTERVKEDTPA--TPSRALNHYISTSgrqrVKSYTPKPRGE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 350 AAQPSQKITATKIPKSLPT------KPSAPSTSIVPIKS----PHPTQKTAPSSFTKSALPTQ--KQVPPTSRPVPAR-- 415
Cdd:TIGR00927 175 VKSSSPTQTREKVRKYTPSplgrmvNSYAPSTFMTMPRShgitPRTTVKDSEITATYKMLETNpsKRTAGKTTPTPLKgm 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 416 -------VSRPTEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKPPPFTALSSS 488
Cdd:TIGR00927 255 tdntptfLTREVETDLLTSPRSVVEKNTLTTPRRVESNSSTNHWGLVGKNNLTTPQGTVLEHTPATSEGQVTISIMTGSS 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 489 PAPTPGSTRSTRppatMVPPTSGTSTP--RTAPA-----VPTPGSAPTGSKKPigseaSKKAGPKSSPRKPVPLRPGKAA 561
Cdd:TIGR00927 335 PAETKASTAAWK----IRNPLSRTSAPavRIASAtfrglEKNPSTAPSTPATP-----RVRAVLTTQVHHCVVVKPAPAV 405
|
330 340
....*....|....*....|....*
gi 2462626959 562 RDVPLSDLTTRPSPRQPQPSQQTTP 586
Cdd:TIGR00927 406 PTTPSPSLTTALFPEAPSPSPSALP 430
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
833-888 |
1.76e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 38.24 E-value: 1.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462626959 833 GPKGMKGLMGSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGP 888
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
419-627 |
1.87e-03 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 42.99 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 419 PTEK-----PIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTH--KPPpftalsSSPAP 491
Cdd:PLN03209 315 PMEEllakiPSQRVPPKESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYTAYEdlKPP------TSPIP 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 492 TPGSTRSTRPPatmvpPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKS---------SPRKPVPlrpgKAAR 562
Cdd:PLN03209 389 TPPSSSPASSK-----SVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSpyaryedlkPPTSPSP----TAPT 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462626959 563 DVPLSDLTTRPSPRQPQPSQQTTPALVLAPAqflSSSPRPTSSGYSIFHLAGST-PFPLLMGPPGP 627
Cdd:PLN03209 460 GVSPSVSSTSSVPAVPDTAPATAATDAAAPP---PANMRPLSPYAVYDDLKPPTsPSPAAPVGKVA 522
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
1190-1446 |
1.89e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 43.09 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1190 GDSGPMGPDGLKGDRGDPGPDGEHGEKGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQGEKGRTGAKGAKGYQGQLGEMGV 1269
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1270 PGDPGPPGTPGPKGSRGSLGPTGAPGRMGAQGEPGLAGYDGHKGiVGPLGPPgpkgekGEQGEDGKAEGPPGPPGDRGPV 1349
Cdd:COG5164 87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPS-GGSTTPP------GDGGSTPPGPGSTGPGGSTTPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 1350 GDRGDRGEPGDPGYPGQEGVQGlRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGvqGLQGLPGPRGV 1429
Cdd:COG5164 160 GDGGSTTPPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGPKDQRPK 236
|
250
....*....|....*..
gi 2462626959 1430 VGRQGLEGIAGPDGLPG 1446
Cdd:COG5164 237 TNPIERRGPERPEAAAL 253
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1518-1573 |
2.06e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.86 E-value: 2.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462626959 1518 GEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGP 1573
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
454-595 |
2.17e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 42.84 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 454 TLARTEAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATmvpPTSGTSTPRTAPAVPTPGSAPTGSKK 533
Cdd:PRK14971 363 TQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSA---PQSATQPAGTPPTVSVDPPAAVPVNP 439
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462626959 534 PIGSEASKKAGPKSSPRKPVPLRPGKAARdvplsdLTTRPSPRQPQPSQQTTPALVLAPAQF 595
Cdd:PRK14971 440 PSTAPQAVRPAQFKEEKKIPVSKVSSLGP------STLRPIQEKAEQATGNIKEAPTGTQKE 495
|
|
| PRK14954 |
PRK14954 |
DNA polymerase III subunits gamma and tau; Provisional |
479-544 |
2.20e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184918 [Multi-domain] Cd Length: 620 Bit Score: 43.01 E-value: 2.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462626959 479 PPPFTALSSSPAPTpGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAG 544
Cdd:PRK14954 396 EPDLPQPDRHPGPA-KPEAPGARPAELPSPASAPTPEQQPPVARSAPLPPSPQASAPRNVASGKPG 460
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1144-1197 |
2.60e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.86 E-value: 2.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462626959 1144 MGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGP 1197
Cdd:pfam01391 3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1509-1563 |
2.66e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.86 E-value: 2.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 1509 GRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPG 1563
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
336-558 |
2.68e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 336 PASVGGSTRTPRPAAAQPSQKITATKIPKSLPTKPS----------APSTSIVPIKSPHPTQKTAPSSfTKSALPTQKQV 405
Cdd:PHA03247 259 PVVGEGADRAPETARGATGPPPPPEAAAPNGAAAPPdgvwgaalagAPLALPAPPDPPPPAPAGDAEE-EDDEDGAMEVV 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 406 PPTSRP-------VPARvSRPTEKPiqrnpgmprppppstRPLPPTTSSSKKPIP--TLARTEAKITSHASKPASARTST 476
Cdd:PHA03247 338 SPLPRPrqhyplgFPKR-RRPTWTP---------------PSSLEDLSAGRHHPKraSLPTRKRRSARHAATPFARGPGG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 477 HKPPPFTAL--SSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSK---KPIGSEASKKAGPKSSPRK 551
Cdd:PHA03247 402 DDQTRPAAPvpASVPTPAPTPVPASAPPPPATPLPSAEPGSDDGPAPPPERQPPAPATepaPDDPDDATRKALDALRERR 481
|
....*..
gi 2462626959 552 PvPLRPG 558
Cdd:PHA03247 482 P-PEPPG 487
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
370-631 |
3.03e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.85 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 370 PSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPTEKPIQRNPGMPRPPPPSTRPLPPTTSSSK 449
Cdd:PHA03307 63 DRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 450 KPIPTLARTEAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGStrstrPPATMVPPTSGTSTPRTAPAVPTPGSAPT 529
Cdd:PHA03307 143 SPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSS-----PPAEPPPSTPPAAASPRPPRRSSPISASA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 530 GSKKPigseaskkAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTTPALVLAPAQFLSSSPRPTSSgysi 609
Cdd:PHA03307 218 SSPAP--------APGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPA---- 285
|
250 260
....*....|....*....|..
gi 2462626959 610 fhlAGSTPFPLLMGPPGPKGDC 631
Cdd:PHA03307 286 ---SSSSSPRERSPSPSPSSPG 304
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
498-608 |
3.34e-03 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 41.85 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 498 STRP--PATmVPPTSGTSTPRTAPAVPTPGSAPTG----------SKKPigsEASKKAGPKSSPRKPVPLRPGKAARDVP 565
Cdd:PRK10905 121 STLPtePAT-VAPVRNGNASRQTAKTQTAERPATTrparkqaviePKKP---QATAKTEPKPVAQTPKRTEPAAPVASTK 196
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2462626959 566 LSDLTTRPsprQPQPSQQTTPALVLAPAQflsSSPRPTSSGYS 608
Cdd:PRK10905 197 APAATSTP---APKETATTAPVQTASPAQ---TTATPAAGGKT 233
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
734-788 |
3.50e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.47 E-value: 3.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 734 GYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGKMGMPG 788
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1352-1395 |
3.57e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.47 E-value: 3.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2462626959 1352 RGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKG 1395
Cdd:pfam01391 12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| KAR9 |
pfam08580 |
Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal ... |
374-628 |
3.57e-03 |
|
Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal protein required for karyogamy, correct positioning of the mitotic spindle and for orientation of cytoplasmic microtubules. KAR9 localizes at the shmoo tip in mating cells and at the tip of the growing bud in anaphase.
Pssm-ID: 430088 [Multi-domain] Cd Length: 684 Bit Score: 42.12 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 374 STSIVPIKSPhptQKTAPSSFTKSALPTQKQVPPTSRP----VPARVSRPTEKPIQRNpgmprppppstrplppttssSK 449
Cdd:pfam08580 421 PATLVANKTP---GSSPPSSVIMTPVNKGSKTPSSRRGssfdFGSSSERVINSKLRRE--------------------SK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 450 KPIPTLARTEAKITSHASKPASARTSTHKPPPFTalSSSPAPTPGSTRSTRPPatmvPPTSGTStPRTAPAVPTPGSAPT 529
Cdd:pfam08580 478 LPQIASTLKQTKRPSKIPRASPNHSGFLSTPSNT--ATSETPTPALRPPSRPQ----PPPPGNR-PRWNASTNTNDLDVG 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 530 GSKKPIgseaskkagpKSSPRKPVPLRpgkaardvplsdlTTRPSPRQPQPSQQTTPAlvlapaqflSSSPRPTSSGYSI 609
Cdd:pfam08580 551 HNFKPL----------TLTTPSPTPSR-------------SSRSSSTLPPVSPLSRDK---------SRSPAPTCRSVSR 598
|
250
....*....|....*....
gi 2462626959 610 FHLAGSTPFPLLMGPPGPK 628
Cdd:pfam08580 599 ASRRRASRKPTRIGSPNSR 617
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
474-562 |
3.66e-03 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 42.18 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 474 TSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPV 553
Cdd:PRK12270 39 GSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVT 118
|
....*....
gi 2462626959 554 PLRpGKAAR 562
Cdd:PRK12270 119 PLR-GAAAA 126
|
|
| TALPID3 |
pfam15324 |
Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for ... |
499-630 |
3.73e-03 |
|
Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for Hedgehog signalling. Mutations in this gene noticed first in chickens lead to multiple abnormalities of development.
Pssm-ID: 434634 [Multi-domain] Cd Length: 1288 Bit Score: 42.18 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 499 TRPPATMVP-PTSGTSTPRTAPaVPTPGSAPTGSKKPIGSEASKKAGPKSSPRkpvplrpgkaardvpLSDLTTRPSP-R 576
Cdd:pfam15324 966 EPPVAASVPgDLPTKETLLPTP-VPTPQPTPPCSPPSPLKEPSPVKTPDSSPC---------------VSEHDFFPVKeI 1029
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462626959 577 QPQPSQQTTPA--LVLAPAQFLSSSPR------PTSSGYSIFHLAGSTPfpllmGPPGPKGD 630
Cdd:pfam15324 1030 PPEKGADTGPAvsLVITPTVTPIATPPpaatptPPLSENSIDKLKSPSP-----ELPKPWED 1086
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1353-1409 |
3.94e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.09 E-value: 3.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462626959 1353 GDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKA 1409
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
845-897 |
4.22e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.09 E-value: 4.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2462626959 845 GEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLGKVGDKGS 897
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1530-1585 |
4.35e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.09 E-value: 4.35e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462626959 1530 GEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLPGP 1585
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
281-627 |
4.83e-03 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 41.97 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 281 PAGRGPRGTVAPATPTKPQRTSPTNPHqhmavgGPAQTPLLP----AKLSASNALDPMLPASVGGSTRTPRPAAAQPSQK 356
Cdd:PHA03379 411 PTYGTPRPPVEKPRPEVPQSLETATSH------GSAQVPEPPpvhdLEPGPLHDQHSMAPCPVAQLPPGPLQDLEPGDQL 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 357 ITATKIPKSLPTKPSAPSTSIVPIKSPHPTQktAPSSFTKSALPTQKQVPPTSRPVPARVSRPTEKPIQRNPGMPRPPPP 436
Cdd:PHA03379 485 PGVVQDGRPACAPVPAPAGPIVRPWEASLSQ--VPGVAFAPVMPQPMPVEPVPVPTVALERPVCPAPPLIAMQGPGETSG 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 437 STRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKP----PPFTALSSSPAPTpgsTRSTRPPATMVPPTSGT 512
Cdd:PHA03379 563 IVRVRERWRPAPWTPNPPRSPSQMSVRDRLARLRAEAQPYQASvevqPPQLTQVSPQQPM---EYPLEPEQQMFPGSPFS 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 513 STPRTAPAVPTPGSAPTGSKKPIGSEASKKA--GPKSSPRKPVPLRPGKAAR--DVPLSD-LTTRPSPRQPQPSQQTTPA 587
Cdd:PHA03379 640 QVADVMRAGGVPAMQPQYFDLPLQQPISQGAplAPLRASMGPVPPVPATQPQyfDIPLTEpINQGASAAHFLPQQPMEGP 719
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2462626959 588 LV----LAPAQFLSSSPRPTSSGYSIFHLAGSTPF----PLLMGPPGP 627
Cdd:PHA03379 720 LVperwMFQGATLSQSVRPGVAQSQYFDLPLTQPInhgaPAAHFLHQP 767
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
455-569 |
4.83e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 41.72 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 455 LARTEAKITS----HASKPASARTSTHKPPPftALSSSPAPTPGSTRSTRPP-ATMVPPTSGTSTPRTAPAVPTPGSAPT 529
Cdd:PRK14950 353 LAVIEALLVPvpapQPAKPTAAAPSPVRPTP--APSTRPKAAAAANIPPKEPvRETATPPPVPPRPVAPPVPHTPESAPK 430
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462626959 530 GSKKPIGSEASKKAGPkssprkPVPLRPGKAARDVPLSDL 569
Cdd:PRK14950 431 LTRAAIPVDEKPKYTP------PAPPKEEEKALIADGDVL 464
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
914-988 |
5.24e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.70 E-value: 5.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 914 GPPGDNGPEGMKGKPGARGLPGPRGQLGPegdegpmgppgapglegqPGRKGFPGRPGLDGVKGEPGDPGRPGPV 988
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGP------------------PGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PHA03132 |
PHA03132 |
thymidine kinase; Provisional |
385-610 |
5.33e-03 |
|
thymidine kinase; Provisional
Pssm-ID: 222997 [Multi-domain] Cd Length: 580 Bit Score: 41.67 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 385 PTQKTAPSSFTKSAL-PTQKQVPPTSRPVPARVSRPTEKPIQRNPGMPRPPPPSTrplpPTTSSSKKPIPTLARtEAKIT 463
Cdd:PHA03132 40 LGSTSEATSEDDDDLyPPRETGSGGGVATSTIYTVPRPPRGPEQTLDKPDSLPAS----RELPPGPTPVPPGGF-RGASS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 464 SHASKPASARTSTHKPPPFTALSSSPAPTPGSTR-STRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKK 542
Cdd:PHA03132 115 PRLGADSTSPRFLYQVNFPVILAPIGESNSSSEElSEEEEHSRPPPSESLKVKNGGKVYPKGFSKHKTHKRSEFSGLTKK 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462626959 543 AGPKSSPRKPVPLRPGKAARDVPLSDLTTR-PSPRQPQPSQQTTPALVLAPaqFLSSSPRPTSSGYSIF 610
Cdd:PHA03132 195 AARKRKGSFVFKPSQLKELSGSLKNLLHLDdSAETDPATRQVPVPVHVLYP--PLLTEYVPYKPACFLF 261
|
|
| rad23 |
TIGR00601 |
UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
467-543 |
5.75e-03 |
|
UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273167 [Multi-domain] Cd Length: 378 Bit Score: 41.03 E-value: 5.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462626959 467 SKPASARTSTHKPPPftalSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKA 543
Cdd:TIGR00601 75 SKPKTGTGKVAPPAA----TPTSAPTPTPSPPASPASGMSAAPASAVEEKSPSEESATATAPESPSTSVPSSGSDAA 147
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
332-588 |
7.00e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 41.61 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 332 DPML-------PASVGGSTRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPH---PTQKTAPSSFTKSALPT 401
Cdd:PRK10263 308 DPLLngapitePVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQtgePVIAPAPEGYPQQSQYA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 402 QKQVP---PTSRPVPArvsrptEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPAS------- 471
Cdd:PRK10263 388 QPAVQynePLQQPVQP------QQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQStfapqst 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 472 -----------ARTSTHKPPPFTALSSSPAPTPG--STRSTRPP------------------ATMVPPtsgTSTPRTAPA 520
Cdd:PRK10263 462 yqteqtyqqpaAQEPLYQQPQPVEQQPVVEPEPVveETKPARPPlyyfeeveekrarereqlAAWYQP---IPEPVKEPE 538
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462626959 521 VPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARD-VPLSDLTTRPSPRqPQPSQQTTPAL 588
Cdd:PRK10263 539 PIKSSLKAPSVAAVPPVEAAAAVSPLASGVKKATLATGAAATVaAPVFSLANSGGPR-PQVKEGIGPQL 606
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
281-421 |
7.59e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 41.24 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 281 PAGRGPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAKLSASNALdpmlPASVGGSTRTPRPAAAQPSqkiTAT 360
Cdd:PRK14951 367 AAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAP----PAAAPPAPVAAPAAAAPAA---APA 439
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462626959 361 KIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSsftksalPTQKQVPPTSRPVPARVsRPTE 421
Cdd:PRK14951 440 AAPAAVALAPAPPAQAAPETVAIPVRVAPEPA-------VASAAPAPAAAPAAARL-TPTE 492
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
470-591 |
8.55e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 40.95 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626959 470 ASARTSTHKPPPF------TALSSSPAPTPGSTRSTRPPAtmVPPTSGTST-PRTAPAVPTPGSAPTGSKKPIGSEASKK 542
Cdd:PRK14950 339 FQLRTTSYGQLPLelavieALLVPVPAPQPAKPTAAAPSP--VRPTPAPSTrPKAAAAANIPPKEPVRETATPPPVPPRP 416
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2462626959 543 AGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTTPALVLA 591
Cdd:PRK14950 417 VAPPVPHTPESAPKLTRAAIPVDEKPKYTPPAPPKEEEKALIADGDVLE 465
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1392-1446 |
8.75e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.32 E-value: 8.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462626959 1392 GPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEGIAGPDGLPG 1446
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
758-807 |
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: 36.32 E-value: 8.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2462626959 758 GLPGLFGLPGSDGERGLPGVPGKRGKMGMPGFPGVFGERGPPGLDGNPGE 807
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
839-890 |
9.19e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.32 E-value: 9.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2462626959 839 GLMGSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLG 890
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
|
|
| KLF8_N |
cd21440 |
N-terminal domain of Kruppel-like factor 8; Kruppel-like factor 8 (also known as Krueppel-like ... |
475-526 |
9.32e-03 |
|
N-terminal domain of Kruppel-like factor 8; Kruppel-like factor 8 (also known as Krueppel-like transcription factor 8, KLF8) is a CACCC-box binding protein that associates with C-terminal Binding Protein (CtBP) and represses transcription. It plays an essential role in the regulation of the cell cycle, apoptosis, and differentiation. It has been identified as a key component of the transcription factor network that controls terminal differentiation during adipogenesis. It also plays an important role in the formation of several human tumors, including the promotion of tumorigenesis, invasion, and metastasis of colorectal cancer cells, and the progression of pancreatic cancer. KLF8 belongs to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Although these factors bind to similar elements in vitro, they have distinct activities in vivo depending on their expression profile and the sequence of the N-terminal activation/repression domain, which differ between members. KLF8 contains an N-terminal repression domain that is related to that of KLF12.
Pssm-ID: 410607 [Multi-domain] Cd Length: 169 Bit Score: 39.05 E-value: 9.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462626959 475 STHKP--PPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGS 526
Cdd:cd21440 43 SLHKPkaPLQPPSVLSPSPMILSVSPSAPQSLVSSTGTGMGTTSAIPAVLSPGS 96
|
|
| |
