|
Name |
Accession |
Description |
Interval |
E-value |
| COLFI |
pfam01410 |
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1661-1859 |
2.00e-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: 2.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1661 EIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQKMVDGTYWVDPNLGCSSDTIEVSCNFThGGQTCLKPITAS-- 1738
Cdd:pfam01410 4 EVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFE-TGETCIYPTKASip 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1739 --------------------KVEF---------AISRVQMNFLHLLSSEVTQHITIHCLNMTVWQ-EGTGQTpaKQAVRF 1788
Cdd:pfam01410 83 rknwwtkeskhvwfgefmngGSQFsygvdgvgpSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMdQATGNL--KKALLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24251209 1789 RAWNGQIFEAGG--QFRPEVSMDGCKVQDGRWHQTLFTFRTQDPQQLPIISVDNLPPASSGKQYRLEVGPACF 1859
Cdd:pfam01410 161 QGSNDEEIRAEGnsRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
|
|
| COLFI |
smart00038 |
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1660-1860 |
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 24251209 1660 GEIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQKMVDGTYWVDPNLGCSSDTIEVSCNFThGGQTCLKPITAS- 1738
Cdd:smart00038 2 EEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFE-TGETCVSPSPSSi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1739 -----------------------KVEFAISR------VQMNFLHLLSSEVTQHITIHCLNMTVWQ-EGTGQTpaKQAVRF 1788
Cdd:smart00038 81 prktwysgkskhvwfgetmnggfKFSYGDSEgppvgvVQLTFLRLLSTEAHQNITYHCKNSVAYMdEATGNL--KKALRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24251209 1789 RAWNGQIFEAGGQFRP--EVSMDGCKVQDGRWHQTLFTFRTQDPQQLPIISVDNLPPASSGKQYRLEVGPACFL 1860
Cdd:smart00038 159 RGSNDVELSAEGNSKFtyEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1369-1598 |
3.44e-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: 3.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1369 EGVQGLRGKpGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEGIAGPDGlpg 1448
Cdd:NF038329 108 EGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG--- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1449 rdgqagqqgeqgDDGDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGtegrTGLPGNQGEPGSKGQP 1528
Cdd:NF038329 184 ------------AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGED 247
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1529 GDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLPGPKGDKGSRGDWG 1598
Cdd:NF038329 248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1355-1598 |
5.68e-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: 5.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1355 GDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGR 1434
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1435 QGLEGIAGPDGlpgrdgqagqqgeqgddgdpgPMGPAGKRGNPGVAGLPGAQGPPGfkgesglPGQLGPPGKRGTEGRTG 1514
Cdd:NF038329 197 RGETGPAGEQG---------------------PAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1515 LPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLPGPKGDKGSR 1594
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328
|
....
gi 24251209 1595 GDWG 1598
Cdd:NF038329 329 GKDG 332
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1328-1563 |
1.90e-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: 1.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1328 EKGEQGEDGKAegppGPPGDRGPVGDRGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGK 1407
Cdd:NF038329 118 EKGEPGPAGPA----GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1408 QGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEGIAGPDGlPGRDGQAGQQGEQGDDGDPGPMGPAGKRGNPGVAGLPGAQG 1487
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24251209 1488 PPGFKGESGLPgqlGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGP 1563
Cdd:NF038329 273 PDGKDGERGPV---GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
709-989 |
2.87e-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: 2.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 709 GHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGKMGM 788
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 789 PGFPGVFGERGPPGLDGnpgelglpgppgvpgligdlgvlgPIGYPGPKGMKGLMGSVGepglKGDKGEQGVPGVSGDPG 868
Cdd:NF038329 197 RGETGPAGEQGPAGPAG------------------------PDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 869 FQGDKGSQGLPGFPGARGKPGPLGKVGDKGsigfpgppgpegfpgDIGPPGDNGPEGMKGKPGARGLPGPRGQLGPEGde 948
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDG---------------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG-- 311
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 24251209 949 gpmgppgapgLEGQPGRKGFPGRPGLDGVKGEPGDPGRPGP 989
Cdd:NF038329 312 ----------LPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1183-1449 |
5.84e-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: 5.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1183 GQRGEPGLegdSGPMGPDGLKGDRGDPGPDGEHGEKGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQGEKGRTGAKGAKGY 1262
Cdd:NF038329 117 GEKGEPGP---AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1263 QGQLGEmgvpgdpgppgtPGPKGSRGSLGPTGAPGRMGAQGEPGLAGYDGhkgivgplgppgpkgeKGEQGEDGkaegpp 1342
Cdd:NF038329 194 QGPRGE------------TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------DGQQGPDG------ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1343 gppgdrgPVGDRGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGL 1422
Cdd:NF038329 240 -------DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL 312
|
250 260
....*....|....*....|....*..
gi 24251209 1423 QGLPGPRGVVGRQGLEGIAGPDGLPGR 1449
Cdd:NF038329 313 PGKDGKDGQPGKDGLPGKDGKDGQPGK 339
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
691-889 |
5.28e-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: 5.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 691 GDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGS 770
Cdd:NF038329 141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 771 DGERGLPGVPGkRGKMGMPGFPGVFGERGPPGLDGNPGELGLPGPPGVPGLIGDLGVLGPIGYPGPKGMKGLMGSVGEPG 850
Cdd:NF038329 221 AGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299
|
170 180 190
....*....|....*....|....*....|....*....
gi 24251209 851 LKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPG 889
Cdd:NF038329 300 KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1147-1405 |
2.57e-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: 2.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1147 GPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRGDPGPDGEHGEKGQEGLMGE 1226
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1227 dgppgppgvtgvRGPEGKSGKQGEKGRTGAKGAKGYQGQLGEMGVPGDPGppgtpgpkgsRGSLGPTGAPGRMGAQGEPG 1306
Cdd:NF038329 197 ------------RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ----------QGPDGDPGPTGEDGPQGPDG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1307 LAGYDGHKGIVGPLGPPGPKGEKGEQGEDGKAegppgppgdrGPVGDRGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGH 1386
Cdd:NF038329 255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPA----------GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324
|
250
....*....|....*....
gi 24251209 1387 PGPRGWPGPKGSKGAEGPK 1405
Cdd:NF038329 325 DGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1122-1416 |
8.05e-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: 8.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1122 PgtkglpgepgpqgpqgpigppgemGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDG 1201
Cdd:NF038329 128 A------------------------GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1202 LKGDRGDPGPDGEHGEKGQEGLMGEDgppgppgvtgvrGPEGKSGKQGEKGRTGAKGAKGyQGQLGEmgvpgdpgppgtp 1281
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPA------------GPAGPDGEAGPAGEDGPAGPAG-DGQQGP------------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1282 gpkgsRGSLGPTGAPGRMGAQGEPGLAGYDGHKGivgplgppgpkgEKGEQGEDGKAegppgppgdrgpvgdrGDRGEPG 1361
Cdd:NF038329 238 -----DGDPGPTGEDGPQGPDGPAGKDGPRGDRG------------EAGPDGPDGKD----------------GERGPVG 284
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 24251209 1362 DPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGR 1416
Cdd:NF038329 285 PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1060-1390 |
1.56e-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: 103.06 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1060 GAKGRRGPRGPDGPAGEQGSRGLKGPPGPQGRPGRPGQQGVAGERGHLGSRGFPGIPGPsgppgtkglpgepgpqgpqgp 1139
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP--------------------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1140 igppgeMGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGL--KGDRGDPGPDGEHGE 1217
Cdd:NF038329 176 ------AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGP 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1218 KGQEGLMGEDgppgppgvtgvrgpeGKSGKQGEKGRTGAKGakgyqgqlgemgvpgdpgppgtpgpkgSRGSLGPTGAPG 1297
Cdd:NF038329 250 QGPDGPAGKD---------------GPRGDRGEAGPDGPDG---------------------------KDGERGPVGPAG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1298 RMGAQGEPGLAGYDghkgivgplgppgpkgekGEQGEDGKAegppgppgdrgpvgdrgdrGEPGDPGYPGQEGVQGLRGK 1377
Cdd:NF038329 288 KDGQNGKDGLPGKD------------------GKDGQNGKD-------------------GLPGKDGKDGQPGKDGLPGK 330
|
330
....*....|...
gi 24251209 1378 PGQQGQPGHPGPR 1390
Cdd:NF038329 331 DGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
625-837 |
4.39e-20 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 95.36 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 625 GPPGPKGDCGLPGPPGLPGLPGIPGARGPRGPPGPYGNPGLPGPPGAKGQKGDPGLSPGKAHDGAKGDMGLPGLSGNPGP 704
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 705 PGRKGHKGYPGPAGHPGEQGQpGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRG 784
Cdd:NF038329 212 AGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24251209 785 KMGMPGFPGVFGERGPPGLDGNPGELGLPGPPGVPGLIGDLGVLGPIGYPGPK 837
Cdd:NF038329 291 QNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
974-1249 |
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 24251209 974 LDGVKGEPGDPGRPGPVGEQGFMGFIGLVGEPGIVGEKGDRGMMGPPGVPGPKGsmghpgmpggmgtpgEPGPQGPpgsr 1053
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------------EAGPQGP---- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1054 gppgmRGAKGRRGPRGPDGPAGEQGSRGLKGPpgpqgrpgrpgqqgvAGERGHLGsrgfpgipgpsgpPGTKGLPGEPGP 1133
Cdd:NF038329 176 -----AGKDGEAGAKGPAGEKGPQGPRGETGP---------------AGEQGPAG-------------PAGPDGEAGPAG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1134 QGPQGPIGPPGEMGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRGDPGPDG 1213
Cdd:NF038329 223 EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302
|
250 260 270
....*....|....*....|....*....|....*.
gi 24251209 1214 EHGEKGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQG 1249
Cdd:NF038329 303 KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
844-1081 |
5.08e-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: 5.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 844 GSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLGKVGDKGSIgfpgppgpegfpgdiGPPGDNGP 923
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKDGE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 924 EGMKGKPGARGLPGPRGQLGPEGDEGPMGPPGAPGLEGQPGRKGFPGRPGlDGVKGEPGDPGRPGPVGEQgfmgfiGLVG 1003
Cdd:NF038329 182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ------GPDG 254
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24251209 1004 EPGIVGEKGDRGMMGPPGVPGPKGSMGHPGMPGGMGTPGEPGPQGPPGSRGPPGMRGAKGRRGPRGPDGPAGEQGSRG 1081
Cdd:NF038329 255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1463-1605 |
2.40e-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: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1463 GDPGPMGPAGKRGnpgvaglpgAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGL 1542
Cdd:NF038329 120 GEPGPAGPAGPAG---------EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24251209 1543 FGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLP--GPKGDKGSRGDWGLQGPRGP 1605
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGP 255
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
869-1216 |
6.54e-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: 6.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 869 FQGDKGSQGLPGFPGARGKPGPLGKVGDKGsigfpgppgpegFPGDIGPPGDNGPEGMKGKPGARGLPGPRGQLGPEGde 948
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETG------------PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG-- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 949 gpmgppgapglegQPGRKGFPGRPGLDGVKGEPGDPGRPGPVGEQGFMGFIGLVGEPGIVGEKGDrgmmgppgvpgpkgs 1028
Cdd:NF038329 181 -------------EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD--------------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1029 mghpgmpggmgtpgepgpqgppgsrgppgmrGAKGRRGPRGPDGPAGEQGSRGlkgppgpqgrpgrpgqqgvagERGHLG 1108
Cdd:NF038329 233 -------------------------------GQQGPDGDPGPTGEDGPQGPDG---------------------PAGKDG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1109 SRGFPGIPGPSgppgtkglpgepgpqgpqgpigppgemgpkGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEP 1188
Cdd:NF038329 261 PRGDRGEAGPD------------------------------GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD 310
|
330 340
....*....|....*....|....*...
gi 24251209 1189 GLEGDSGPMGPDGLKGDRGDPGPDGEHG 1216
Cdd:NF038329 311 GLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
274-605 |
4.44e-14 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 78.44 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 274 TATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAklsasnaldpmLPASVGGSTRTPRPAAA 353
Cdd:PHA03247 2636 NEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRA-----------ARPTVGSLTSLADPPPP 2704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 354 QPSQKITATKIPKSLPTKP-------SAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPaekPI 426
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPgpaaarqASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP---PR 2781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 427 QRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTeakitshASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPAT 506
Cdd:PHA03247 2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPA-------AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGG 2854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 507 MVPPTSGTS---TPRTAPAVPTPGSAPTGSKKPiGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPR-QPQP 582
Cdd:PHA03247 2855 SVAPGGDVRrrpPSRSPAAKPAAPARPPVRRLA-RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpQPPP 2933
|
330 340
....*....|....*....|...
gi 24251209 583 SQQTTPALVLAPAQFLSSSPRPT 605
Cdd:PHA03247 2934 PPPPRPQPPLAPTTDPAGAGEPS 2956
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
45-220 |
6.61e-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: 6.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 45 DVDILQRLGLSWTKAGSPAPPGVIPFQSGFIFTQRARLQAPTGTVIPAALGTELALVLSLCSHRVNHAFLFAVRSQKRKL 124
Cdd:smart00210 1 GQDLLQVFDLPSLSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDAQNVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 125 QLGLQFLPGKTVVHL------GSRRSVAF-DLDMHDGRWHHLALELRGRTVTLVTACGQR-RVPVLLPFHrdPALDPGGS 196
Cdd:smart00210 81 QFGLEVDGRANTLLLryqgvdGKQHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIdSRPLDRPGQ--PPIDTDGI 158
|
170 180
....*....|....*....|....
gi 24251209 197 FLFGKMNPHAVQFEGALCQFSIYP 220
Cdd:smart00210 159 EVRGAQAADRKPFQGDLQQLKIVC 182
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
281-608 |
1.02e-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: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 281 SLPAGR-GPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLlpaKLSASNALDPMLPASVggSTRTPRPAAAQPSqki 359
Cdd:pfam17823 98 SEPATReGAADGAASRALAAAASSSPSSAAQSLPAAIAALPSE---AFSAPRAAACRANASA--APRAAIAAASAPH--- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 360 TATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKS-------------ALPTQKQVPPTSRPVPARVSrpaekpi 426
Cdd:pfam17823 170 AASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPArgistaatatghpAAGTALAAVGNSSPAAGTVT------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 427 qrnpgmprppppstrplPPTTSSSKKPIPTLARTEAKITSHA-----SKPASARTSTHKPPPFTALSSSPAPTPGS-TRS 500
Cdd:pfam17823 243 -----------------AAVGTVTPAALATLAAAAGTVASAAgtinmGDPHARRLSPAKHMPSDTMARNPAAPMGAqAQG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 501 TRPPATMVPP---TSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSP 577
Cdd:pfam17823 306 PIIQVSTDQPvhnTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPSP 385
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 24251209 578 RqpQPSQQTT-PALVLAPAQF--------LSSSPRPTSSG 608
Cdd:pfam17823 386 L--LPTQGAAgPGILLAPEQVateatagtASAGPTPRSSG 423
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1500-1630 |
9.89e-11 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 66.08 E-value: 9.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1500 QLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGIL 1579
Cdd:NF038329 112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 24251209 1580 GPSGLPGPKGDKGSRGDWGLQGPRGPPGPRGRPGPPGPPGGPIQLQQDDLG 1630
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG 242
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
691-747 |
6.00e-06 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 45.18 E-value: 6.00e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 24251209 691 GDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPV 747
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1463-1517 |
7.48e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 42.10 E-value: 7.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 24251209 1463 GDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPG 1517
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| rad23 |
TIGR00601 |
UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
460-531 |
3.23e-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: 3.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24251209 460 TEAKITSHASKPASARTSTHKPPPFTALSSSPAPTpgstrSTRPPATMVPPTSGTSTPRT-APAVPTPGSAPT 531
Cdd:TIGR00601 80 GTGKVAPPAATPTSAPTPTPSPPASPASGMSAAPA-----SAVEEKSPSEESATATAPESpSTSVPSSGSDAA 147
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
1424-1598 |
4.64e-04 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 45.02 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1424 GLPGPRGVVGRQGLEGIAGPDGLPGRDGQAGQQGEQGDDGDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGP 1503
Cdd:COG5164 10 GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1504 PGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLF--GPKGPPGDIGfkgiQGPRGpPGLMGKEGIVGPLGILGP 1581
Cdd:COG5164 90 TRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGG----STPPG-PGSTGPGGSTTPPGDGGS 164
|
170
....*....|....*..
gi 24251209 1582 SGLPGPKGDKGSRGDWG 1598
Cdd:COG5164 165 TTPPGPGGSTTPPDDGG 181
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
136-204 |
1.16e-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: 1.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24251209 136 VVHLGSRRSVAFDLD--MHDGRWHHLALELRGRTVTLVTaCGQRRVPVLLPfHRDPALDPGGSFLFGKMNP 204
Cdd:pfam02210 33 RYDLGSGPESLLSSGknLNDGQWHSVRVERNGNTLTLSV-DGQTVVSSLPP-GESLLLNLNGPLYLGGLPP 101
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
1192-1448 |
1.83e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 43.09 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1192 GDSGPMGPDGLKGDRGDPGPDGEHGEKGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQGEKGRTGAKGAKGYQGQLGEMGV 1271
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1272 PGDPGPPGTPGPKGSRGSLGPTGAPGRMGAQGEPGLAGYDGHKGiVGPLGPPgpkgekGEQGEDGKAEGPPGPPGDRGPV 1351
Cdd:COG5164 87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPS-GGSTTPP------GDGGSTPPGPGSTGPGGSTTPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1352 GDRGDRGEPGDPGYPGQEGVQGlRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGvqGLQGLPGPRGV 1431
Cdd:COG5164 160 GDGGSTTPPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGPKDQRPK 236
|
250
....*....|....*..
gi 24251209 1432 VGRQGLEGIAGPDGLPG 1448
Cdd:COG5164 237 TNPIERRGPERPEAAAL 253
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1146-1199 |
2.61e-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: 2.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 24251209 1146 MGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGP 1199
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 ... |
477-528 |
9.42e-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: 9.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 24251209 477 STHKP--PPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGS 528
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 ... |
1661-1859 |
2.00e-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: 2.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1661 EIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQKMVDGTYWVDPNLGCSSDTIEVSCNFThGGQTCLKPITAS-- 1738
Cdd:pfam01410 4 EVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFE-TGETCIYPTKASip 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1739 --------------------KVEF---------AISRVQMNFLHLLSSEVTQHITIHCLNMTVWQ-EGTGQTpaKQAVRF 1788
Cdd:pfam01410 83 rknwwtkeskhvwfgefmngGSQFsygvdgvgpSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMdQATGNL--KKALLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24251209 1789 RAWNGQIFEAGG--QFRPEVSMDGCKVQDGRWHQTLFTFRTQDPQQLPIISVDNLPPASSGKQYRLEVGPACF 1859
Cdd:pfam01410 161 QGSNDEEIRAEGnsRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
|
|
| COLFI |
smart00038 |
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1660-1860 |
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 24251209 1660 GEIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQKMVDGTYWVDPNLGCSSDTIEVSCNFThGGQTCLKPITAS- 1738
Cdd:smart00038 2 EEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFE-TGETCVSPSPSSi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1739 -----------------------KVEFAISR------VQMNFLHLLSSEVTQHITIHCLNMTVWQ-EGTGQTpaKQAVRF 1788
Cdd:smart00038 81 prktwysgkskhvwfgetmnggfKFSYGDSEgppvgvVQLTFLRLLSTEAHQNITYHCKNSVAYMdEATGNL--KKALRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24251209 1789 RAWNGQIFEAGGQFRP--EVSMDGCKVQDGRWHQTLFTFRTQDPQQLPIISVDNLPPASSGKQYRLEVGPACFL 1860
Cdd:smart00038 159 RGSNDVELSAEGNSKFtyEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1369-1598 |
3.44e-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: 3.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1369 EGVQGLRGKpGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEGIAGPDGlpg 1448
Cdd:NF038329 108 EGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG--- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1449 rdgqagqqgeqgDDGDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGtegrTGLPGNQGEPGSKGQP 1528
Cdd:NF038329 184 ------------AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGED 247
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1529 GDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLPGPKGDKGSRGDWG 1598
Cdd:NF038329 248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1355-1598 |
5.68e-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: 5.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1355 GDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGR 1434
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1435 QGLEGIAGPDGlpgrdgqagqqgeqgddgdpgPMGPAGKRGNPGVAGLPGAQGPPGfkgesglPGQLGPPGKRGTEGRTG 1514
Cdd:NF038329 197 RGETGPAGEQG---------------------PAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1515 LPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLPGPKGDKGSR 1594
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328
|
....
gi 24251209 1595 GDWG 1598
Cdd:NF038329 329 GKDG 332
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1328-1563 |
1.90e-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: 1.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1328 EKGEQGEDGKAegppGPPGDRGPVGDRGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGK 1407
Cdd:NF038329 118 EKGEPGPAGPA----GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1408 QGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEGIAGPDGlPGRDGQAGQQGEQGDDGDPGPMGPAGKRGNPGVAGLPGAQG 1487
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24251209 1488 PPGFKGESGLPgqlGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGP 1563
Cdd:NF038329 273 PDGKDGERGPV---GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
709-989 |
2.87e-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: 2.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 709 GHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGKMGM 788
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 789 PGFPGVFGERGPPGLDGnpgelglpgppgvpgligdlgvlgPIGYPGPKGMKGLMGSVGepglKGDKGEQGVPGVSGDPG 868
Cdd:NF038329 197 RGETGPAGEQGPAGPAG------------------------PDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 869 FQGDKGSQGLPGFPGARGKPGPLGKVGDKGsigfpgppgpegfpgDIGPPGDNGPEGMKGKPGARGLPGPRGQLGPEGde 948
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDG---------------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG-- 311
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 24251209 949 gpmgppgapgLEGQPGRKGFPGRPGLDGVKGEPGDPGRPGP 989
Cdd:NF038329 312 ----------LPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1183-1449 |
5.84e-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: 5.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1183 GQRGEPGLegdSGPMGPDGLKGDRGDPGPDGEHGEKGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQGEKGRTGAKGAKGY 1262
Cdd:NF038329 117 GEKGEPGP---AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1263 QGQLGEmgvpgdpgppgtPGPKGSRGSLGPTGAPGRMGAQGEPGLAGYDGhkgivgplgppgpkgeKGEQGEDGkaegpp 1342
Cdd:NF038329 194 QGPRGE------------TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------DGQQGPDG------ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1343 gppgdrgPVGDRGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGL 1422
Cdd:NF038329 240 -------DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL 312
|
250 260
....*....|....*....|....*..
gi 24251209 1423 QGLPGPRGVVGRQGLEGIAGPDGLPGR 1449
Cdd:NF038329 313 PGKDGKDGQPGKDGLPGKDGKDGQPGK 339
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
691-889 |
5.28e-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: 5.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 691 GDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGS 770
Cdd:NF038329 141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 771 DGERGLPGVPGkRGKMGMPGFPGVFGERGPPGLDGNPGELGLPGPPGVPGLIGDLGVLGPIGYPGPKGMKGLMGSVGEPG 850
Cdd:NF038329 221 AGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299
|
170 180 190
....*....|....*....|....*....|....*....
gi 24251209 851 LKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPG 889
Cdd:NF038329 300 KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1147-1405 |
2.57e-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: 2.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1147 GPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRGDPGPDGEHGEKGQEGLMGE 1226
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1227 dgppgppgvtgvRGPEGKSGKQGEKGRTGAKGAKGYQGQLGEMGVPGDPGppgtpgpkgsRGSLGPTGAPGRMGAQGEPG 1306
Cdd:NF038329 197 ------------RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ----------QGPDGDPGPTGEDGPQGPDG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1307 LAGYDGHKGIVGPLGPPGPKGEKGEQGEDGKAegppgppgdrGPVGDRGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGH 1386
Cdd:NF038329 255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPA----------GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324
|
250
....*....|....*....
gi 24251209 1387 PGPRGWPGPKGSKGAEGPK 1405
Cdd:NF038329 325 DGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1122-1416 |
8.05e-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: 8.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1122 PgtkglpgepgpqgpqgpigppgemGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDG 1201
Cdd:NF038329 128 A------------------------GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1202 LKGDRGDPGPDGEHGEKGQEGLMGEDgppgppgvtgvrGPEGKSGKQGEKGRTGAKGAKGyQGQLGEmgvpgdpgppgtp 1281
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPA------------GPAGPDGEAGPAGEDGPAGPAG-DGQQGP------------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1282 gpkgsRGSLGPTGAPGRMGAQGEPGLAGYDGHKGivgplgppgpkgEKGEQGEDGKAegppgppgdrgpvgdrGDRGEPG 1361
Cdd:NF038329 238 -----DGDPGPTGEDGPQGPDGPAGKDGPRGDRG------------EAGPDGPDGKD----------------GERGPVG 284
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 24251209 1362 DPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGR 1416
Cdd:NF038329 285 PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1060-1390 |
1.56e-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: 103.06 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1060 GAKGRRGPRGPDGPAGEQGSRGLKGPPGPQGRPGRPGQQGVAGERGHLGSRGFPGIPGPsgppgtkglpgepgpqgpqgp 1139
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP--------------------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1140 igppgeMGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGL--KGDRGDPGPDGEHGE 1217
Cdd:NF038329 176 ------AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGP 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1218 KGQEGLMGEDgppgppgvtgvrgpeGKSGKQGEKGRTGAKGakgyqgqlgemgvpgdpgppgtpgpkgSRGSLGPTGAPG 1297
Cdd:NF038329 250 QGPDGPAGKD---------------GPRGDRGEAGPDGPDG---------------------------KDGERGPVGPAG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1298 RMGAQGEPGLAGYDghkgivgplgppgpkgekGEQGEDGKAegppgppgdrgpvgdrgdrGEPGDPGYPGQEGVQGLRGK 1377
Cdd:NF038329 288 KDGQNGKDGLPGKD------------------GKDGQNGKD-------------------GLPGKDGKDGQPGKDGLPGK 330
|
330
....*....|...
gi 24251209 1378 PGQQGQPGHPGPR 1390
Cdd:NF038329 331 DGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
625-837 |
4.39e-20 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 95.36 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 625 GPPGPKGDCGLPGPPGLPGLPGIPGARGPRGPPGPYGNPGLPGPPGAKGQKGDPGLSPGKAHDGAKGDMGLPGLSGNPGP 704
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 705 PGRKGHKGYPGPAGHPGEQGQpGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRG 784
Cdd:NF038329 212 AGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24251209 785 KMGMPGFPGVFGERGPPGLDGNPGELGLPGPPGVPGLIGDLGVLGPIGYPGPK 837
Cdd:NF038329 291 QNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
974-1249 |
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 24251209 974 LDGVKGEPGDPGRPGPVGEQGFMGFIGLVGEPGIVGEKGDRGMMGPPGVPGPKGsmghpgmpggmgtpgEPGPQGPpgsr 1053
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------------EAGPQGP---- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1054 gppgmRGAKGRRGPRGPDGPAGEQGSRGLKGPpgpqgrpgrpgqqgvAGERGHLGsrgfpgipgpsgpPGTKGLPGEPGP 1133
Cdd:NF038329 176 -----AGKDGEAGAKGPAGEKGPQGPRGETGP---------------AGEQGPAG-------------PAGPDGEAGPAG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1134 QGPQGPIGPPGEMGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRGDPGPDG 1213
Cdd:NF038329 223 EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302
|
250 260 270
....*....|....*....|....*....|....*.
gi 24251209 1214 EHGEKGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQG 1249
Cdd:NF038329 303 KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
844-1081 |
5.08e-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: 5.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 844 GSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLGKVGDKGSIgfpgppgpegfpgdiGPPGDNGP 923
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKDGE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 924 EGMKGKPGARGLPGPRGQLGPEGDEGPMGPPGAPGLEGQPGRKGFPGRPGlDGVKGEPGDPGRPGPVGEQgfmgfiGLVG 1003
Cdd:NF038329 182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ------GPDG 254
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24251209 1004 EPGIVGEKGDRGMMGPPGVPGPKGSMGHPGMPGGMGTPGEPGPQGPPGSRGPPGMRGAKGRRGPRGPDGPAGEQGSRG 1081
Cdd:NF038329 255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1463-1605 |
2.40e-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: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1463 GDPGPMGPAGKRGnpgvaglpgAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGL 1542
Cdd:NF038329 120 GEPGPAGPAGPAG---------EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24251209 1543 FGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLP--GPKGDKGSRGDWGLQGPRGP 1605
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGP 255
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
869-1216 |
6.54e-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: 6.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 869 FQGDKGSQGLPGFPGARGKPGPLGKVGDKGsigfpgppgpegFPGDIGPPGDNGPEGMKGKPGARGLPGPRGQLGPEGde 948
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETG------------PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG-- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 949 gpmgppgapglegQPGRKGFPGRPGLDGVKGEPGDPGRPGPVGEQGFMGFIGLVGEPGIVGEKGDrgmmgppgvpgpkgs 1028
Cdd:NF038329 181 -------------EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD--------------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1029 mghpgmpggmgtpgepgpqgppgsrgppgmrGAKGRRGPRGPDGPAGEQGSRGlkgppgpqgrpgrpgqqgvagERGHLG 1108
Cdd:NF038329 233 -------------------------------GQQGPDGDPGPTGEDGPQGPDG---------------------PAGKDG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1109 SRGFPGIPGPSgppgtkglpgepgpqgpqgpigppgemgpkGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEP 1188
Cdd:NF038329 261 PRGDRGEAGPD------------------------------GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD 310
|
330 340
....*....|....*....|....*...
gi 24251209 1189 GLEGDSGPMGPDGLKGDRGDPGPDGEHG 1216
Cdd:NF038329 311 GLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
274-605 |
4.44e-14 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 78.44 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 274 TATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAklsasnaldpmLPASVGGSTRTPRPAAA 353
Cdd:PHA03247 2636 NEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRA-----------ARPTVGSLTSLADPPPP 2704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 354 QPSQKITATKIPKSLPTKP-------SAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPaekPI 426
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPgpaaarqASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP---PR 2781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 427 QRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTeakitshASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPAT 506
Cdd:PHA03247 2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPA-------AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGG 2854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 507 MVPPTSGTS---TPRTAPAVPTPGSAPTGSKKPiGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPR-QPQP 582
Cdd:PHA03247 2855 SVAPGGDVRrrpPSRSPAAKPAAPARPPVRRLA-RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpQPPP 2933
|
330 340
....*....|....*....|...
gi 24251209 583 SQQTTPALVLAPAQFLSSSPRPT 605
Cdd:PHA03247 2934 PPPPRPQPPLAPTTDPAGAGEPS 2956
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
45-220 |
6.61e-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: 6.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 45 DVDILQRLGLSWTKAGSPAPPGVIPFQSGFIFTQRARLQAPTGTVIPAALGTELALVLSLCSHRVNHAFLFAVRSQKRKL 124
Cdd:smart00210 1 GQDLLQVFDLPSLSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDAQNVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 125 QLGLQFLPGKTVVHL------GSRRSVAF-DLDMHDGRWHHLALELRGRTVTLVTACGQR-RVPVLLPFHrdPALDPGGS 196
Cdd:smart00210 81 QFGLEVDGRANTLLLryqgvdGKQHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIdSRPLDRPGQ--PPIDTDGI 158
|
170 180
....*....|....*....|....
gi 24251209 197 FLFGKMNPHAVQFEGALCQFSIYP 220
Cdd:smart00210 159 EVRGAQAADRKPFQGDLQQLKIVC 182
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
281-608 |
1.02e-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: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 281 SLPAGR-GPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLlpaKLSASNALDPMLPASVggSTRTPRPAAAQPSqki 359
Cdd:pfam17823 98 SEPATReGAADGAASRALAAAASSSPSSAAQSLPAAIAALPSE---AFSAPRAAACRANASA--APRAAIAAASAPH--- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 360 TATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKS-------------ALPTQKQVPPTSRPVPARVSrpaekpi 426
Cdd:pfam17823 170 AASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPArgistaatatghpAAGTALAAVGNSSPAAGTVT------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 427 qrnpgmprppppstrplPPTTSSSKKPIPTLARTEAKITSHA-----SKPASARTSTHKPPPFTALSSSPAPTPGS-TRS 500
Cdd:pfam17823 243 -----------------AAVGTVTPAALATLAAAAGTVASAAgtinmGDPHARRLSPAKHMPSDTMARNPAAPMGAqAQG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 501 TRPPATMVPP---TSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSP 577
Cdd:pfam17823 306 PIIQVSTDQPvhnTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPSP 385
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 24251209 578 RqpQPSQQTT-PALVLAPAQF--------LSSSPRPTSSG 608
Cdd:pfam17823 386 L--LPTQGAAgPGILLAPEQVateatagtASAGPTPRSSG 423
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
275-631 |
1.43e-12 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 73.43 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 275 ATPALGSLPAG-RGPRGTVAPATPTKPQRTSPTNPhqhmaVGGPAQTPLLPAKLSASNALDPMLP--ASVGGSTRTPRPA 351
Cdd:PHA03247 2593 PQSARPRAPVDdRGDPRGPAPPSPLPPDTHAPDPP-----PPSPSPAANEPDPHPPPTVPPPERPrdDPAPGRVSRPRRA 2667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 352 AAQpsQKITATKIPKSLPTKPSAPST--SIVPIKSPHPTQKTAPSSFTksalPTQKQVPPTSRPVPARVSRPAE--KPIQ 427
Cdd:PHA03247 2668 RRL--GRAAQASSPPQRPRRRAARPTvgSLTSLADPPPPPPTPEPAPH----ALVSATPLPPGPAAARQASPALpaAPAP 2741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 428 RNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEA-----KITSHASKPASARTSTHKPP--PFTALSSSPAPTPGSTRS 500
Cdd:PHA03247 2742 PAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAagpprRLTRPAVASLSESRESLPSPwdPADPPAAVLAPAAALPPA 2821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 501 TRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKP-VPLRPGKAARDVPLSDLTTRPSP-- 577
Cdd:PHA03247 2822 ASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPaAPARPPVRRLARPAVSRSTESFAlp 2901
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 24251209 578 -----RQPQPSQQTTPALVLAPAQFLSSSPRPTSSGYSIFHLAgstPFPLLMGPPGPKG 631
Cdd:PHA03247 2902 pdqpeRPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLA---PTTDPAGAGEPSG 2957
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
283-780 |
7.92e-12 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 71.12 E-value: 7.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 283 PAGRGPRGTVAPATPTKPQRTSPTNPhqhmAVGGPAQTPLLP-----AKLSASNALDP-------MLPASVGGSTRTPRP 350
Cdd:PHA03247 2498 PGGGGPPDPDAPPAPSRLAPAILPDE----PVGEPVHPRMLTwirglEELASDDAGDPppplppaAPPAAPDRSVPPPRP 2573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 351 AAAQPSQKITATKIPKSLPTKPSAPSTsivPIKSPHPTQKTAPSSftksalPTQKQVPPTSRPVPARVSRPAEKPiqrnp 430
Cdd:PHA03247 2574 APRPSEPAVTSRARRPDAPPQSARPRA---PVDDRGDPRGPAPPS------PLPPDTHAPDPPPPSPSPAANEPD----- 2639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 431 GMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKPP--PFTALSSSPAPTPGSTRSTRPPATMV 508
Cdd:PHA03247 2640 PHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTvgSLTSLADPPPPPPTPEPAPHALVSAT 2719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 509 PPTSGTSTPRTA----PAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLR-----PGKAARDVPLSDLT----TRP 575
Cdd:PHA03247 2720 PLPPGPAAARQAspalPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAapaagPPRRLTRPAVASLSesreSLP 2799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 576 SPRQPQPSqqttPALVLAPAQFLSSSPRPTSsgysifhLAGSTPFPLLMGPPGPKGdcGLPGPPGLPGLPGIPGARGPRG 655
Cdd:PHA03247 2800 SPWDPADP----PAAVLAPAAALPPAASPAG-------PLPPPTSAQPTAPPPPPG--PPPPSLPLGGSVAPGGDVRRRP 2866
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 656 PPGPYGNPGLPGPPGAKGQKGDPGLSPgkahdgAKGDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAK 735
Cdd:PHA03247 2867 PSRSPAAKPAAPARPPVRRLARPAVSR------STESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ 2940
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24251209 736 GYPGRQGLPGPVGDPGPKGSRGYIG--LPGLFGLPGSDGERGLPGVP 780
Cdd:PHA03247 2941 PPLAPTTDPAGAGEPSGAVPQPWLGalVPGRVAVPRFRVPQPAPSRE 2987
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
273-576 |
1.83e-11 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 69.97 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 273 TTATPALgSLPAGRGPRGTVAPATPTKPqrTSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASvGGSTRTPRPAA 352
Cdd:PHA03247 2713 HALVSAT-PLPPGPAAARQASPALPAAP--APPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA-GPPRRLTRPAV 2788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 353 AQ-------------PSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPP--------TS 411
Cdd:PHA03247 2789 ASlsesreslpspwdPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPggdvrrrpPS 2868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 412 RPVPARVSRPAEKPIQRnpgmprpppPSTRPLPPTTSSSKKPIPTLARTEakitshaSKPASARTSTHKPPPFTALSSSP 491
Cdd:PHA03247 2869 RSPAAKPAAPARPPVRR---------LARPAVSRSTESFALPPDQPERPP-------QPQAPPPPQPQPQPPPPPQPQPP 2932
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 492 APTPGstrstRPPATMVPPTSGTSTPRTAPAVPTPgsaPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDL 571
Cdd:PHA03247 2933 PPPPP-----RPQPPLAPTTDPAGAGEPSGAVPQP---WLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRV 3004
|
....*
gi 24251209 572 TTRPS 576
Cdd:PHA03247 3005 SSWAS 3009
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1500-1630 |
9.89e-11 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 66.08 E-value: 9.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1500 QLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGIL 1579
Cdd:NF038329 112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 24251209 1580 GPSGLPGPKGDKGSRGDWGLQGPRGPPGPRGRPGPPGPPGGPIQLQQDDLG 1630
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG 242
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
271-626 |
2.41e-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: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 271 NLTTATPA---LGSLPAGRGPRGTVAPATPTKPQRTSPTNphqhmAVGGP---AQTPLLPAKLSASNALDPML-PASVGG 343
Cdd:pfam05109 472 DVTSPTPAgttSGASPVTPSPSPRDNGTESKAPDMTSPTS-----AVTTPtpnATSPTPAVTTPTPNATSPTLgKTSPTS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 344 STRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSsftksalpTQKQVPPTSRPVPARVSRPAE 423
Cdd:pfam05109 547 AVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGE--------TSPQANTTNHTLGGTSSTPVV 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 424 KPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIP---TLA-RTEAKITSH-----ASKPASARTSTHKPPPFTAL----SSS 490
Cdd:pfam05109 619 TSPPKNATSAVTTGQHNITSSSTSSMSLRPSSiseTLSpSTSDNSTSHmplltSAHPTGGENITQVTPASTSThhvsTSS 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 491 PAPTPGSTRSTRPP---ATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASkkAGPKSSPRKPVPLRPGKAARDVp 567
Cdd:pfam05109 699 PAPRPGTTSQASGPgnsSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTS--TGGKANSTTGGKHTTGHGARTS- 775
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 24251209 568 lSDLTTRPSPRQPQPSQQTTPALVLAPAQFLSSSPRPTSSGYSIFHLAGSTPFPLLMGP 626
Cdd:pfam05109 776 -TEPTTDYGGDSTTPRTRYNATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPTSQP 833
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
272-607 |
4.42e-08 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 58.64 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 272 LTTATPALGSLPAGRGPRGTVAPATPTkpqrtSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPA 351
Cdd:PHA03307 50 LAAVTVVAGAAACDRFEPPTGPPPGPG-----TEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 352 AAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKqVPPTSRPVParvSRPAEKPIQRNPG 431
Cdd:PHA03307 125 SPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSS-PEETARAPS---SPPAEPPPSTPPA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 432 MPRPPPPSTRPLPPTTSSSkkPIPTLARTEAKITSHASKPASARTSTHK------------PPPFTALSSSPAPTPGSTR 499
Cdd:PHA03307 201 AASPRPPRRSSPISASASS--PAPAPGRSAADDAGASSSDSSSSESSGCgwgpenecplprPAPITLPTRIWEASGWNGP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 500 STRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKK-----PIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSdltTR 574
Cdd:PHA03307 279 SSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRAsssssSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSP---SR 355
|
330 340 350
....*....|....*....|....*....|...
gi 24251209 575 PSPRQPQPSQQTTPALVLAPAQFLSSSPRPTSS 607
Cdd:PHA03307 356 PPPPADPSSPRKRPRPSRAPSSPAASAGRPTRR 388
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
237-589 |
5.47e-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: 58.24 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 237 GQADTYQSPLGPLFSQDSGRPFTFQSDLAllglenltTATPALGSLPAGRGPrgtvaPATPTKPQRTSPTNPHQHMAVGG 316
Cdd:pfam03154 169 TQPPVLQAQSGAASPPSPPPPGTTQAATA--------GPTPSAPSVPPQGSP-----ATSQPPNQTQSTAAPHTLIQQTP 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 317 PAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPAAAQPSQ------KITATKIPKSLPTKP----SAPSTSIVP----I 382
Cdd:pfam03154 236 TLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPpmphslQTGPSHMQHPVPPQPfpltPQSSQSQVPpgpsP 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 383 KSPHPTQKTAPSSFTKSALPTQKqvPPTSRPV-PARVSRPAEKPiqrnpgmprppppstrplppttsSSKKPIPTLARTE 461
Cdd:pfam03154 316 AAPGQSQQRIHTPPSQSQLQSQQ--PPREQPLpPAPLSMPHIKP-----------------------PPTTPIPQLPNPQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 462 A-KITSHASKPASARTSTHKPPP--FTALSSSPAPTPGSTRStrPPATMVPPTSGTSTPRTAPAVPT--PGSAPTGSKKP 536
Cdd:pfam03154 371 ShKHPPHLSGPSPFQMNSNLPPPpaLKPLSSLSTHHPPSAHP--PPLQLMPQSQQLPPPPAQPPVLTqsQSLPPPAASHP 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 24251209 537 igSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQP--QPSQQTTPA 589
Cdd:pfam03154 449 --PTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPgiQPPSSASVS 501
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
237-548 |
2.00e-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: 55.74 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 237 GQADTYQS--PLGPLFSQDSGRPFTFQSDLALLGLENLTTATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMAV 314
Cdd:pfam17823 105 GAADGAASraLAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 315 GGPAQTPLLPAKLSASNALDPMLPAS--VGGSTRTPRPAAAqpsqkiTATKipkSLPTKPSAPSTSIVPIKSPHP----T 388
Cdd:pfam17823 185 ASSTTAASSAPTTAASSAPATLTPARgiSTAATATGHPAAG------TALA---AVGNSSPAAGTVTAAVGTVTPaalaT 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 389 QKTAPSSFTKSALPTQKQVPPTSRPVPARvSRP----AEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKI 464
Cdd:pfam17823 256 LAAAAGTVASAAGTINMGDPHARRLSPAK-HMPsdtmARNPAAPMGAQAQGPIIQVSTDQPVHNTAGEPTPSPSNTTLEP 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 465 T---SHASKPASARTSTH---KPPpftalSSSPAPTPGSTRSTRPPATM-------VPPTSGTSTPRTAPAVPTPGSAPT 531
Cdd:pfam17823 335 NtpkSVASTNLAVVTTTKaqaKEP-----SASPVPVLHTSMIPEVEATSpttqpspLLPTQGAAGPGILLAPEQVATEAT 409
|
330
....*....|....*..
gi 24251209 532 GSKKPIGSEASKKAGPK 548
Cdd:pfam17823 410 AGTASAGPTPRSSGDPK 426
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
248-556 |
2.55e-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: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 248 PLFSQDSGRPFTFQSDLALLGLENLTTATPALGSLPAGRGPRGTVAPATPTKPQRTS-PTNPH------QHMAVGGPAQT 320
Cdd:pfam03154 218 PNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQmPPMPHslqtgpSHMQHPVPPQP 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 321 PLLPAKLSASNALDPMLPASVGGSTRT-------PRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSP----HPTQ 389
Cdd:pfam03154 298 FPLTPQSSQSQVPPGPSPAAPGQSQQRihtppsqSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPqshkHPPH 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 390 KTAPSSFT-KSALPTQKQVPPTSRPVPARVSRPAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHA 468
Cdd:pfam03154 378 LSGPSPFQmNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVP 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 469 SKPASARTS--THKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTstprtAPAVPTPGSAPTGSKKPIGSEASKKAG 546
Cdd:pfam03154 458 SQSPFPQHPfvPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGP-----VPAAVSCPLPPVQIKEEALDEAEEPES 532
|
330
....*....|
gi 24251209 547 PKSSPRKPVP 556
Cdd:pfam03154 533 PPPPPRSPSP 542
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
277-588 |
4.85e-07 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 54.86 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 277 PALGslpAGRGPRGTVAPATPTkpqrtsptnphqhmAVGGPAQTPLLPAKLSASnaldPMLPASVGGSTRTPRPAAAQPS 356
Cdd:PRK07003 360 PAVT---GGGAPGGGVPARVAG--------------AVPAPGARAAAAVGASAV----PAVTAVTGAAGAALAPKAAAAA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 357 QKiTATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQRNpgmprpp 436
Cdd:PRK07003 419 AA-TRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAF------- 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 437 ppstrplppttsSSKKPIPTLARTEAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTR-----PPATMVPPT 511
Cdd:PRK07003 491 ------------EPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAAraggaAAALDVLRN 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 512 SG----TSTPRTAPAVPTPGSAPTGSKKPigseaskkagpkSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTT 587
Cdd:PRK07003 559 AGmrvsSDRGARAAAAAKPAAAPAAAPKP------------AAPRVAVQVPTPRARAATGDAPPNGAARAEQAAESRGAP 626
|
.
gi 24251209 588 P 588
Cdd:PRK07003 627 P 627
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
275-594 |
1.21e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.17 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 275 ATPALGSLPAGRG-PRGTVAPATPTKPQR-TSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPAA 352
Cdd:PHA03247 2731 ASPALPAAPAPPAvPAGPATPGGPARPARpPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 353 AQPSqkiTATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSAL---------PTQKQVPPT----SRPVPARVS 419
Cdd:PHA03247 2811 VLAP---AAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVapggdvrrrPPSRSPAAKpaapARPPVRRLA 2887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 420 RPA------------------EKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLA-RTEAKITSHASKPASARTSTHK 480
Cdd:PHA03247 2888 RPAvsrstesfalppdqperpPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLApTTDPAGAGEPSGAVPQPWLGAL 2967
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 481 PPPFTALSSSPAPTPGSTRSTrpPATMVPPTSGTSTPRTAP----------AVPTPGSAPTGSKKPIGSEASKKAGPKSS 550
Cdd:PHA03247 2968 VPGRVAVPRFRVPQPAPSREA--PASSTPPLTGHSLSRVSSwasslalheeTDPPPVSLKQTLWPPDDTEDSDADSLFDS 3045
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 24251209 551 PRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTTPALVLAP 594
Cdd:PHA03247 3046 DSERSDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSSQFGP 3089
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
268-614 |
2.42e-06 |
|
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: 52.61 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 268 GLENLTTATPALGSLPAGRGPRGTvAPAT--PTKPQRTSPTNPHQHMAVGGPAQTPLLPAkLSASNALDPMLPASVGGST 345
Cdd:pfam05109 375 GCENISGAFASNRTFDITVSGLGT-APKTliITRTATNATTTTHKVIFSKAPESTTTSPT-LNTTGFAAPNTTTGLPSST 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 346 RTPRPAAAQPSQKITATKIPKSLPTkPSAPSTSIVPIK-SPHPTQKTAPSSFTKSALPTQKQVPPT---SRPVPArVSRP 421
Cdd:pfam05109 453 HVPTNLTAPASTGPTVSTADVTSPT-PAGTTSGASPVTpSPSPRDNGTESKAPDMTSPTSAVTTPTpnaTSPTPA-VTTP 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 422 AEKPIQrnpgmprppppstrplppttssskkpiPTLARTEakitshaskPASARTSthkPPPftalsSSPAPTPGSTRST 501
Cdd:pfam05109 531 TPNATS---------------------------PTLGKTS---------PTSAVTT---PTP-----NATSPTPAVTTPT 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 502 rPPATMvpPTSGTSTPRTAPAVPTP-GSAPT-GSKKPIGSEASKKAGPKSSprKPVPLRPGKAArdvplsdlTTRPSPRQ 579
Cdd:pfam05109 567 -PNATI--PTLGKTSPTSAVTTPTPnATSPTvGETSPQANTTNHTLGGTSS--TPVVTSPPKNA--------TSAVTTGQ 633
|
330 340 350
....*....|....*....|....*....|....*
gi 24251209 580 PQPSQQTTPALVLAPAQfLSSSPRPTSSGYSIFHL 614
Cdd:pfam05109 634 HNITSSSTSSMSLRPSS-ISETLSPSTSDNSTSHM 667
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
691-747 |
6.00e-06 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 45.18 E-value: 6.00e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 24251209 691 GDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPV 747
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
459-618 |
6.41e-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: 51.11 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 459 RTEAKITSHA---SKPASaRTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTApAVPTPGSAptGSKK 535
Cdd:pfam17823 85 EVTAEHTPHGtdlSEPAT-REGAADGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAA-ACRANASA--APRA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 536 PIGSEASKKAG---PKSSPRKPVPLRPGKAARDVPLSDLTTRPS---PRQPQPSQQT---TPALVLAPAQFLSSSPRPTS 606
Cdd:pfam17823 161 AIAAASAPHAAspaPRTAASSTTAASSTTAASSAPTTAASSAPAtltPARGISTAATatgHPAAGTALAAVGNSSPAAGT 240
|
170
....*....|..
gi 24251209 607 SGYSIFHLAGST 618
Cdd:pfam17823 241 VTAAVGTVTPAA 252
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
697-752 |
9.42e-06 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 44.79 E-value: 9.42e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 24251209 697 GLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGP 752
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
350-586 |
9.82e-06 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 50.31 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 350 PAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSrPVPARVSRPAEKPIQRN 429
Cdd:PLN03209 324 PSQRVPPKESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYTAYEDLKPPTS-PIPTPPSSSPASSKSVD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 430 PGMPRPPPPSTRPLPPTTS-SSKKPIPTLARTEAKITSHA-------------SKPASARTSTHKPPPFTALSSSPAPTP 495
Cdd:PLN03209 403 AVAKPAEPDVVPSPGSASNvPEVEPAQVEAKKTRPLSPYAryedlkpptspspTAPTGVSPSVSSTSSVPAVPDTAPATA 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 496 GSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTT-- 573
Cdd:PLN03209 483 ATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQPKPRPLSPYTMye 562
|
250
....*....|....*
gi 24251209 574 --RPsPRQPQPSQQT 586
Cdd:PLN03209 563 dlKP-PTSPTPSPVL 576
|
|
| PHA03269 |
PHA03269 |
envelope glycoprotein C; Provisional |
448-556 |
1.50e-05 |
|
envelope glycoprotein C; Provisional
Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 49.73 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 448 SSSKKPIPTLARTEAkiTSHASKPASARTS--THKPPPFTALSSS------PAPTPGSTRSTRPPATMVPPTSGTSTPRt 519
Cdd:PHA03269 35 AATQKPDPAPAPHQA--ASRAPDPAVAPTSaaSRKPDLAQAPTPAasekfdPAPAPHQAASRAPDPAVAPQLAAAPKPD- 111
|
90 100 110
....*....|....*....|....*....|....*..
gi 24251209 520 aPAVPtPGSAPTgskkpiGSEASKKAGPKSSPRKPVP 556
Cdd:PHA03269 112 -AAEA-FTSAAQ------AHEAPADAGTSAASKKPDP 140
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
342-588 |
2.39e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 49.30 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 342 GGSTRTPRPAAA-QPSQKITATKIPkSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSR 420
Cdd:PTZ00449 555 GEVGKKPGPAKEhKPSKIPTLSKKP-EFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSP 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 421 PAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPI-PTLA-RTEAKITSHASKPASARTSTHKPPPFTALSSSPAP-TPGS 497
Cdd:PTZ00449 634 KRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFdPKFKeKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPeTPGT 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 498 TRSTRPPATMVPPT--SGTSTPRTAPAVPTPgSAPTGSKKPIGSEASKKAGPKSSPrkpvplRPGKAARDVPLSDLTTRP 575
Cdd:PTZ00449 714 PFTTPRPLPPKLPRdeEFPFEPIGDPDAEQP-DDIEFFTPPEEERTFFHETPADTP------LPDILAEEFKEEDIHAET 786
|
250 260
....*....|....*....|.
gi 24251209 576 S--------PRQPQPSQQTTP 588
Cdd:PTZ00449 787 GepdeamkrPDSPSEHEDKPP 807
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
703-757 |
2.44e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 43.64 E-value: 2.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 24251209 703 GPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRG 757
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| PHA03269 |
PHA03269 |
envelope glycoprotein C; Provisional |
399-531 |
3.07e-05 |
|
envelope glycoprotein C; Provisional
Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 48.96 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 399 SALPTQKQVPPTSRPVPARVSRPAEKPIQRnpgmprPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTST 478
Cdd:PHA03269 20 ANLNTNIPIPELHTSAATQKPDPAPAPHQA------ASRAPDPAVAPTSAASRKPDLAQAPTPAASEKFDPAPAPHQAAS 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 24251209 479 HKPPPFTALSSSPAPTPG-----STRSTRPPATMVPPTSgTSTPRTAPAVPTPGSAPT 531
Cdd:PHA03269 94 RAPDPAVAPQLAAAPKPDaaeafTSAAQAHEAPADAGTS-AASKKPDPAAHTQHSPPP 150
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
372-554 |
3.24e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 48.92 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 372 PSAPSTSIVPIKSP---------HPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQrnpgmprppppstrp 442
Cdd:PTZ00449 511 PEGPEASGLPPKAPgdkegeegeHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTL--------------- 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 443 lppttssSKKPiptlarTEAKITSHASKPASARTSTHkppPFTALSSSPAPTPgstrsTRPPATMVPPTSGTSTPRTAPA 522
Cdd:PTZ00449 576 -------SKKP------EFPKDPKHPKDPEEPKKPKR---PRSAQRPTRPKSP-----KLPELLDIPKSPKRPESPKSPK 634
|
170 180 190
....*....|....*....|....*....|..
gi 24251209 523 VPTPGSAPTGSKKPIGSEASKKAGPKSSPRKP 554
Cdd:PTZ00449 635 RPPPPQRPSSPERPEGPKIIKSPKPPKSPKPP 666
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
283-529 |
3.75e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 48.72 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 283 PAGRGprGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPAAaqpsqkitat 362
Cdd:PRK12323 365 PGQSG--GGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEA---------- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 363 kipksLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQRNPGMPRPPPPSTRP 442
Cdd:PRK12323 433 -----LAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 443 LPPTTSSSKKPIPTLArteAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPP---ATMVPPTSGTSTPRT 519
Cdd:PRK12323 508 SPAPAQPDAAPAGWVA---ESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPrasASGLPDMFDGDWPAL 584
|
250
....*....|
gi 24251209 520 APAVPTPGSA 529
Cdd:PRK12323 585 AARLPVRGLA 594
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
328-549 |
4.03e-05 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 48.01 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 328 SASNALDPMLPASVGGSTRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIkSPHPTQKTAPSSFTKSALpTQKQV 407
Cdd:PRK10905 33 SGEKSIDLAGNATDQANGVQPAPGTTSAEQTAGNTQQDVSLPPISSTPTQGQTPV-ATDGQQRVEVQGDLNNAL-TQPQN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 408 PPTSRPVPARVSRPAE----KPIQRNPGMPRPPPPStrplppttSSSKKPIPTLARTEAKItsHASKPASARTSTHKPPP 483
Cdd:PRK10905 111 QQQLNNVAVNSTLPTEpatvAPVRNGNASRQTAKTQ--------TAERPATTRPARKQAVI--EPKKPQATAKTEPKPVA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24251209 484 FTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKS 549
Cdd:PRK10905 181 QTPKRTEPAAPVASTKAPAATSTPAPKETATTAPVQTASPAQTTATPAAGGKTAGNVGSLKSAPSS 246
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
338-595 |
4.24e-05 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 48.52 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 338 PASVGGSTRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSfTKSALPTQ---KQVPPTSRPV 414
Cdd:PHA03378 553 PASTEPVHDQLLPAPGLGPLQIQPLTSPTTSQLASSAPSYAQTPWPVPHPSQTPEPPT-TQSHIPETsapRQWPMPLRPI 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 415 PARVSR-----------------PAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKP--IPTLARTEAKITSHASKPASAR 475
Cdd:PHA03378 632 PMRPLRmqpitfnvlvfptphqpPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIqwAPGTMQPPPRAPTPMRPPAAPP 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 476 TSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTpRTAPAVPTPGSAPTgskkpigseaskkagPKSSPRKPV 555
Cdd:PHA03378 712 GRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPG-RARPPAAAPGRARP---------------PAAAPGAPT 775
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 24251209 556 PLRPGKAArDVPLSDLTTRPSPrQPQPSQQTTPALVLAPA 595
Cdd:PHA03378 776 PQPPPQAP-PAPQQRPRGAPTP-QPPPQAGPTSMQLMPRA 813
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
700-756 |
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 24251209 700 GNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSR 756
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| DUF4045 |
pfam13254 |
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ... |
280-555 |
5.53e-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: 47.86 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 280 GSLPAGRGprGTVAPATPTKPQRTS-------PTNPHQHMAVGGPAQTPLLPAKLSASNAlDPMLPASvggsTRTPRPAA 352
Cdd:pfam13254 47 GSVAGPSG--SLSPGLSPTKLSREGspestsrPSSSHSEATIVRHSKDDERPSTPDEGFV-KPALPRH----SRSSSALS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 353 AQPSQKITAtkipkSLPTKPSAPSTSIVPiKSPHPTqktaPSSFTKSAL-----PTQKQVPPTSRPvPA----------- 416
Cdd:pfam13254 120 NTGSEEDSP-----SLPTSPPSPSKTMDP-KRWSPT----KSSWLESALnrpesPKPKAQPSQPAQ-PAwmkelnkirqs 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 417 -------RVSRPAEKP---IQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTlARTEAKITSHASKPASARTSTHKPPPFTA 486
Cdd:pfam13254 189 rasvdlgRPNSFKEVTpvgLMRSPAPGGHSKSPSVSGISADSSPTKEEPS-EEADTLSTDKEQSPAPTSASEPPPKTKEL 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24251209 487 LSSS---PAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSkKPIGSEASKKAGPKSSPRKPV 555
Cdd:pfam13254 268 PKDSeepAAPSKSAEASTEKKEPDTESSPETSSEKSAPSLLSPVSKASID-KPLSSPDRDPLSPKPKPQSPP 338
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
453-629 |
6.19e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 47.95 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 453 PIPTLARTEAKITSHASKPASA---RTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSA 529
Cdd:PRK12323 374 PATAAAAPVAQPAPAAAAPAAAapaPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 530 PTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAArdvplsdlttrpsprQPQPSQQTTPALVLAPAQFLSSSPRPTSSGY 609
Cdd:PRK12323 454 PAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAA---------------APAPADDDPPPWEELPPEFASPAPAQPDAAP 518
|
170 180
....*....|....*....|
gi 24251209 610 SIFHLAgSTPFPLLMGPPGP 629
Cdd:PRK12323 519 AGWVAE-SIPDPATADPDDA 537
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1463-1517 |
7.48e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 42.10 E-value: 7.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 24251209 1463 GDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPG 1517
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
727-783 |
1.08e-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: 1.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 24251209 727 GPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKR 783
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1481-1535 |
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 24251209 1481 GLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMG 1535
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
468-608 |
2.22e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 46.25 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 468 ASKPASARTSTHKPPPFTALSSSPAPTP--GSTRSTRPPATMVPPtsgtsTPRTAPAVPTPGSAPtgskkpigSEASKKA 545
Cdd:PRK14951 370 AEAAAPAEKKTPARPEAAAPAAAPVAQAaaAPAPAAAPAAAASAP-----AAPPAAAPPAPVAAP--------AAAAPAA 436
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24251209 546 GPKSSPRkPVPLRPGKAARDVP-LSDLTTRPSPRQPQPSQQTTPALVLAPAqflssSPRPTSSG 608
Cdd:PRK14951 437 APAAAPA-AVALAPAPPAQAAPeTVAIPVRVAPEPAVASAAPAPAAAPAAA-----RLTPTEEG 494
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
338-531 |
2.71e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 46.02 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 338 PASVGGSTRTPRPAAAQPSQKITATKIPKSL---PTKPSAPSTSIVPIKSPHPTQKTAPS--SFTKSALPTQKQV----- 407
Cdd:PRK12323 365 PGQSGGGAGPATAAAAPVAQPAPAAAAPAAAapaPAAPPAAPAAAPAAAAAARAVAAAPArrSPAPEALAAARQAsargp 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 408 ------PPTSRPVPARVSRPAEKPIQRNPGMpRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKP 481
Cdd:PRK12323 445 ggapapAPAPAAAPAAAARPAAAGPRPVAAA-AAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVA 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24251209 482 PPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPT 531
Cdd:PRK12323 524 ESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGL 573
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
360-606 |
3.05e-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: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 360 TATKIPKSLPTKPSAP---STSIVPIKSPHPTQKTAPS-------SFTKSALPTqkqvPPTSRPVPARVSRPAekpiqrn 429
Cdd:pfam17823 64 TAAPAPVTLTKGTSAAhlnSTEVTAEHTPHGTDLSEPAtregaadGAASRALAA----AASSSPSSAAQSLPA------- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 430 pgmprppppstrpLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHkpppftalSSSPAPTPGSTRSTRPPATMVP 509
Cdd:pfam17823 133 -------------AIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPH--------AASPAPRTAASSTTAASSTTAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 510 PTSGTSTPRTAPAVPTPGS----APTGSKKPIGSEASKKAGPKSsprkPVPLRPGKAARDVPLSDLTT------------ 573
Cdd:pfam17823 192 SSAPTTAASSAPATLTPARgistAATATGHPAAGTALAAVGNSS----PAAGTVTAAVGTVTPAALATlaaaagtvasaa 267
|
250 260 270
....*....|....*....|....*....|....*....
gi 24251209 574 ------RPSPRQPQPSQQTtpalvlaPAQFLSSSPRPTS 606
Cdd:pfam17823 268 gtinmgDPHARRLSPAKHM-------PSDTMARNPAAPM 299
|
|
| rad23 |
TIGR00601 |
UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
460-531 |
3.23e-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: 3.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24251209 460 TEAKITSHASKPASARTSTHKPPPFTALSSSPAPTpgstrSTRPPATMVPPTSGTSTPRT-APAVPTPGSAPT 531
Cdd:TIGR00601 80 GTGKVAPPAATPTSAPTPTPSPPASPASGMSAAPA-----SAVEEKSPSEESATATAPESpSTSVPSSGSDAA 147
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1475-1529 |
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 24251209 1475 GNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPG 1529
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
1424-1598 |
4.64e-04 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 45.02 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1424 GLPGPRGVVGRQGLEGIAGPDGLPGRDGQAGQQGEQGDDGDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGP 1503
Cdd:COG5164 10 GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1504 PGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLF--GPKGPPGDIGfkgiQGPRGpPGLMGKEGIVGPLGILGP 1581
Cdd:COG5164 90 TRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGG----STPPG-PGSTGPGGSTTPPGDGGS 164
|
170
....*....|....*..
gi 24251209 1582 SGLPGPKGDKGSRGDWG 1598
Cdd:COG5164 165 TTPPGPGGSTTPPDDGG 181
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1379-1433 |
4.84e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.78 E-value: 4.84e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 24251209 1379 GQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVG 1433
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
453-632 |
4.87e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.31 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 453 PIPTLARTE-AKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAP---------- 521
Cdd:PHA03247 255 PAPPPVVGEgADRAPETARGATGPPPPPEAAAPNGAAAPPDGVWGAALAGAPLALPAPPDPPPPAPAGDAeeeddedgam 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 522 --AVPTP---GSAPTGSKK-------PIGSEASKKAGPKSSPRKPVPLRPGKAARDV-------PLSDLTTRPSPRQPQP 582
Cdd:PHA03247 335 evVSPLPrprQHYPLGFPKrrrptwtPPSSLEDLSAGRHHPKRASLPTRKRRSARHAatpfargPGGDDQTRPAAPVPAS 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24251209 583 SQQTTPALVLAPAQFLSSSPRPTSSGYSifhlAGSTPFPLLMGPPGPKGD 632
Cdd:PHA03247 415 VPTPAPTPVPASAPPPPATPLPSAEPGS----DDGPAPPPERQPPAPATE 460
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1382-1436 |
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 24251209 1382 GQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQG 1436
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1373-1429 |
5.35e-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: 5.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 24251209 1373 GLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPR 1429
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
688-736 |
5.73e-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: 5.73e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 24251209 688 GAKGDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKG 736
Cdd:pfam01391 7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
468-582 |
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 24251209 468 ASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVP--TPGSAPTGSKKPIGSEASKKA 545
Cdd:PRK07994 358 AFHPAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPlpETTSQLLAARQQLQRAQGATK 437
|
90 100 110
....*....|....*....|....*....|....*..
gi 24251209 546 GPKSSPRKPVPLRPGKAARDvPLSDLTTRPSPRQPQP 582
Cdd:PRK07994 438 AKKSEPAAASRARPVNSALE-RLASVRPAPSALEKAP 473
|
|
| Metaviral_G |
pfam09595 |
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. ... |
361-513 |
7.22e-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: 42.63 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 361 ATKIPKSLPTKPSAPSTSIVP---IKSPHPTQKTAPSSftkSALPTQKQVPPTSRPVPARVSRPAEKPIQRNPGMPRPPP 437
Cdd:pfam09595 31 ASLILIGESNKEAALIITDIIdinINKQHPEQEHHENP---PLNEAAKEAPSESEDAPDIDPNNQHPSQDRSEAPPLEPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 438 PSTRPLPPTTSSSkkpiPTLARTEAKITSHASKPASART----STHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSG 513
Cdd:pfam09595 108 AKTKPSEHEPANP----PDASNRLSPPDASTAAIREARTfrkpSTGKRNNPSSAQSDQSPPRANHEAIGRANPFAMSSTG 183
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1376-1430 |
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 24251209 1376 GKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRG 1430
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1502-1556 |
8.08e-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: 8.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 24251209 1502 GPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKG 1556
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| motB |
PRK12799 |
flagellar motor protein MotB; Reviewed |
463-606 |
8.85e-04 |
|
flagellar motor protein MotB; Reviewed
Pssm-ID: 183756 [Multi-domain] Cd Length: 421 Bit Score: 43.94 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 463 KITSHASKPASArtsthkPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGsapTGSKKPIGSEAS 542
Cdd:PRK12799 292 QIDTHGTVPVAA------VTPSSAVTQSSAITPSSAAIPSPAVIPSSVTTQSATTTQASAVALSS---AGVLPSDVTLPG 362
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24251209 543 KKAGPKSSPRKPVPlRPGKAARDVPLSDLTTRPSPRQPqpsqqtTPALVLAPAQflSSSPRPTS 606
Cdd:PRK12799 363 TVALPAAEPVNMQP-QPMSTTETQQSSTGNITSTANGP------TTSLPAAPAS--NIPVSPTS 417
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1364-1418 |
9.74e-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: 9.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 24251209 1364 GYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRG 1418
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
136-204 |
1.16e-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: 1.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24251209 136 VVHLGSRRSVAFDLD--MHDGRWHHLALELRGRTVTLVTaCGQRRVPVLLPfHRDPALDPGGSFLFGKMNP 204
Cdd:pfam02210 33 RYDLGSGPESLLSSGknLNDGQWHSVRVERNGNTLTLSV-DGQTVVSSLPP-GESLLLNLNGPLYLGGLPP 101
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1493-1549 |
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 24251209 1493 GESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPP 1549
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1385-1439 |
1.19e-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: 38.63 E-value: 1.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 24251209 1385 GHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEG 1439
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1478-1533 |
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 24251209 1478 GVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGE 1533
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
284-588 |
1.65e-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: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 284 AGRG--PRGTVAPATPTKPQRT------SPTNPHQHMAVGGPAQTPLLPAklSASNALDPMLPAS----VGGSTRTPRPA 351
Cdd:TIGR00927 97 VGRDeaTPSIAMENTPSPPRRTakitptTPKNNYSPTAAGTERVKEDTPA--TPSRALNHYISTSgrqrVKSYTPKPRGE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 352 AAQPSQKITATKIPKSLPT------KPSAPSTSIVPIKS----PHPTQKTAPSSFTKSALPTQ--KQVPPTSRPVPAR-- 417
Cdd:TIGR00927 175 VKSSSPTQTREKVRKYTPSplgrmvNSYAPSTFMTMPRShgitPRTTVKDSEITATYKMLETNpsKRTAGKTTPTPLKgm 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 418 -------VSRPAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKPPPFTALSSS 490
Cdd:TIGR00927 255 tdntptfLTREVETDLLTSPRSVVEKNTLTTPRRVESNSSTNHWGLVGKNNLTTPQGTVLEHTPATSEGQVTISIMTGSS 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 491 PAPTPGSTRSTRppatMVPPTSGTSTP--RTAPA-----VPTPGSAPTGSKKPigseaSKKAGPKSSPRKPVPLRPGKAA 563
Cdd:TIGR00927 335 PAETKASTAAWK----IRNPLSRTSAPavRIASAtfrglEKNPSTAPSTPATP-----RVRAVLTTQVHHCVVVKPAPAV 405
|
330 340
....*....|....*....|....*
gi 24251209 564 RDVPLSDLTTRPSPRQPQPSQQTTP 588
Cdd:TIGR00927 406 PTTPSPSLTTALFPEAPSPSPSALP 430
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
835-890 |
1.78e-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: 1.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 24251209 835 GPKGMKGLMGSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGP 890
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
1192-1448 |
1.83e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 43.09 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1192 GDSGPMGPDGLKGDRGDPGPDGEHGEKGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQGEKGRTGAKGAKGYQGQLGEMGV 1271
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1272 PGDPGPPGTPGPKGSRGSLGPTGAPGRMGAQGEPGLAGYDGHKGiVGPLGPPgpkgekGEQGEDGKAEGPPGPPGDRGPV 1351
Cdd:COG5164 87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPS-GGSTTPP------GDGGSTPPGPGSTGPGGSTTPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 1352 GDRGDRGEPGDPGYPGQEGVQGlRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGvqGLQGLPGPRGV 1431
Cdd:COG5164 160 GDGGSTTPPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGPKDQRPK 236
|
250
....*....|....*..
gi 24251209 1432 VGRQGLEGIAGPDGLPG 1448
Cdd:COG5164 237 TNPIERRGPERPEAAAL 253
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
452-629 |
1.94e-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: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 452 KPIPTLART-EAKITSHASKPASARTSTHKP-PPFTALS-----SSPAPTPGSTRSTRPPatmvpPTSGTSTPRTAPAVP 524
Cdd:PLN03209 340 KPVPTKPVTpEAPSPPIEEEPPQPKAVVPRPlSPYTAYEdlkppTSPIPTPPSSSPASSK-----SVDAVAKPAEPDVVP 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 525 TPGSAPTGSKKPIGSEASKKAGPKS---------SPRKPVPlrpgKAARDVPLSDLTTRPSPRQPQPSQQTTPALVLAPA 595
Cdd:PLN03209 415 SPGSASNVPEVEPAQVEAKKTRPLSpyaryedlkPPTSPSP----TAPTGVSPSVSSTSSVPAVPDTAPATAATDAAAPP 490
|
170 180 190
....*....|....*....|....*....|....*
gi 24251209 596 qflSSSPRPTSSGYSIFHLAGST-PFPLLMGPPGP 629
Cdd:PLN03209 491 ---PANMRPLSPYAVYDDLKPPTsPSPAAPVGKVA 522
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1520-1575 |
2.04e-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: 2.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 24251209 1520 GEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGP 1575
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
456-597 |
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 24251209 456 TLARTEAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATmvpPTSGTSTPRTAPAVPTPGSAPTGSKK 535
Cdd:PRK14971 363 TQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSA---PQSATQPAGTPPTVSVDPPAAVPVNP 439
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24251209 536 PIGSEASKKAGPKSSPRKPVPLRPGKAARdvplsdLTTRPSPRQPQPSQQTTPALVLAPAQF 597
Cdd:PRK14971 440 PSTAPQAVRPAQFKEEKKIPVSKVSSLGP------STLRPIQEKAEQATGNIKEAPTGTQKE 495
|
|
| PRK14954 |
PRK14954 |
DNA polymerase III subunits gamma and tau; Provisional |
481-546 |
2.22e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184918 [Multi-domain] Cd Length: 620 Bit Score: 43.01 E-value: 2.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24251209 481 PPPFTALSSSPAPTpGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAG 546
Cdd:PRK14954 396 EPDLPQPDRHPGPA-KPEAPGARPAELPSPASAPTPEQQPPVARSAPLPPSPQASAPRNVASGKPG 460
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1146-1199 |
2.61e-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: 2.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 24251209 1146 MGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGP 1199
Cdd:pfam01391 3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1511-1565 |
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 24251209 1511 GRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPG 1565
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
500-610 |
3.35e-03 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 41.85 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 500 STRP--PATmVPPTSGTSTPRTAPAVPTPGSAPTG----------SKKPigsEASKKAGPKSSPRKPVPLRPGKAARDVP 567
Cdd:PRK10905 121 STLPtePAT-VAPVRNGNASRQTAKTQTAERPATTrparkqaviePKKP---QATAKTEPKPVAQTPKRTEPAAPVASTK 196
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 24251209 568 LSDLTTRPsprQPQPSQQTTPALVLAPAQflsSSPRPTSSGYS 610
Cdd:PRK10905 197 APAATSTP---APKETATTAPVQTASPAQ---TTATPAAGGKT 233
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
452-560 |
3.42e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 452 KPIPTLARTEAKITSHASKPASARTSTHKPPPFTAL--SSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSA 529
Cdd:PHA03247 375 PKRASLPTRKRRSARHAATPFARGPGGDDQTRPAAPvpASVPTPAPTPVPASAPPPPATPLPSAEPGSDDGPAPPPERQP 454
|
90 100 110
....*....|....*....|....*....|....
gi 24251209 530 PTGSK---KPIGSEASKKAGPKSSPRKPvPLRPG 560
Cdd:PHA03247 455 PAPATepaPDDPDDATRKALDALRERRP-PEPPG 487
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
736-790 |
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 50
....*....|....*....|....*....|....*....|....*....|....*
gi 24251209 736 GYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGKMGMPG 790
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1354-1397 |
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 24251209 1354 RGDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKG 1397
Cdd:pfam01391 12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
476-564 |
3.60e-03 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 42.57 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 476 TSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPV 555
Cdd:PRK12270 39 GSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVT 118
|
....*....
gi 24251209 556 PLRpGKAAR 564
Cdd:PRK12270 119 PLR-GAAAA 126
|
|
| TALPID3 |
pfam15324 |
Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for ... |
501-632 |
3.74e-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: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 501 TRPPATMVP-PTSGTSTPRTAPaVPTPGSAPTGSKKPIGSEASKKAGPKSSPRkpvplrpgkaardvpLSDLTTRPSP-R 578
Cdd:pfam15324 966 EPPVAASVPgDLPTKETLLPTP-VPTPQPTPPCSPPSPLKEPSPVKTPDSSPC---------------VSEHDFFPVKeI 1029
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24251209 579 QPQPSQQTTPA--LVLAPAQFLSSSPR------PTSSGYSIFHLAGSTPfpllmGPPGPKGD 632
Cdd:pfam15324 1030 PPEKGADTGPAvsLVITPTVTPIATPPpaatptPPLSENSIDKLKSPSP-----ELPKPWED 1086
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
274-523 |
3.80e-03 |
|
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: 41.87 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 274 TATPALGSLPAGRGprgTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAklSASNALDPMlpasvggsTRTPRPAAA 353
Cdd:pfam17823 219 TGHPAAGTALAAVG---NSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAA--GTINMGDPH--------ARRLSPAKH 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 354 QPSQKITATKIPKSLP--------TKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRpvpARVSRPAEKP 425
Cdd:pfam17823 286 MPSDTMARNPAAPMGAqaqgpiiqVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTTTK---AQAKEPSASP 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 426 IqrnpgmpRPPPPSTRPLPPTTSSSKKPIPTLArteakiTSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPA 505
Cdd:pfam17823 363 V-------PVLHTSMIPEVEATSPTTQPSPLLP------TQGAAGPGILLAPEQVATEATAGTASAGPTPRSSGDPKTLA 429
|
250 260
....*....|....*....|....*
gi 24251209 506 TMV--PPTSG-----TSTPRTAPAV 523
Cdd:pfam17823 430 MAScqLSTQGqylvvTTDPLTPALV 454
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1355-1411 |
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 24251209 1355 GDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKA 1411
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
847-899 |
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 24251209 847 GEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLGKVGDKGS 899
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1532-1587 |
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 24251209 1532 GEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLGILGPSGLPGP 1587
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
372-633 |
4.39e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.08 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 372 PSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQRNPGMPRPPPPSTRPLPPTTSSSK 451
Cdd:PHA03307 63 DRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 452 KPIPTLARTEAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGStrstrPPATMVPPTSGTSTPRTAPAVPTPGSAPT 531
Cdd:PHA03307 143 SPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSS-----PPAEPPPSTPPAAASPRPPRRSSPISASA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 532 GSKKPigseaskkAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTTPALVLAPAQFLSSSPRPTSSgysi 611
Cdd:PHA03307 218 SSPAP--------APGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPA---- 285
|
250 260
....*....|....*....|..
gi 24251209 612 fhlAGSTPFPLLMGPPGPKGDC 633
Cdd:PHA03307 286 ---SSSSSPRERSPSPSPSSPG 304
|
|
| KAR9 |
pfam08580 |
Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal ... |
376-630 |
4.46e-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: 41.74 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 376 STSIVPIKSPhptQKTAPSSFTKSALPTQKQVPPTSRP----VPARVSRPAEKPIQRNpgmprppppstrplppttssSK 451
Cdd:pfam08580 421 PATLVANKTP---GSSPPSSVIMTPVNKGSKTPSSRRGssfdFGSSSERVINSKLRRE--------------------SK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 452 KPIPTLARTEAKITSHASKPASARTSTHKPPPFTalSSSPAPTPGSTRSTRPPatmvPPTSGTStPRTAPAVPTPGSAPT 531
Cdd:pfam08580 478 LPQIASTLKQTKRPSKIPRASPNHSGFLSTPSNT--ATSETPTPALRPPSRPQ----PPPPGNR-PRWNASTNTNDLDVG 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 532 GSKKPIgseaskkagpKSSPRKPVPLRpgkaardvplsdlTTRPSPRQPQPSQQTTPAlvlapaqflSSSPRPTSSGYSI 611
Cdd:pfam08580 551 HNFKPL----------TLTTPSPTPSR-------------SSRSSSTLPPVSPLSRDK---------SRSPAPTCRSVSR 598
|
250
....*....|....*....
gi 24251209 612 FHLAGSTPFPLLMGPPGPK 630
Cdd:pfam08580 599 ASRRRASRKPTRIGSPNSR 617
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
457-571 |
4.68e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 41.72 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 457 LARTEAKITS----HASKPASARTSTHKPPPftALSSSPAPTPGSTRSTRPP-ATMVPPTSGTSTPRTAPAVPTPGSAPT 531
Cdd:PRK14950 353 LAVIEALLVPvpapQPAKPTAAAPSPVRPTP--APSTRPKAAAAANIPPKEPvRETATPPPVPPRPVAPPVPHTPESAPK 430
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 24251209 532 GSKKPIGSEASKKAGPkssprkPVPLRPGKAARDVPLSDL 571
Cdd:PRK14950 431 LTRAAIPVDEKPKYTP------PAPPKEEEKALIADGDVL 464
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
283-629 |
4.96e-03 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 41.97 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 283 PAGRGPRGTVAPATPTKPQRTSPTNPHqhmavgGPAQTPLLP----AKLSASNALDPMLPASVGGSTRTPRPAAAQPSQK 358
Cdd:PHA03379 411 PTYGTPRPPVEKPRPEVPQSLETATSH------GSAQVPEPPpvhdLEPGPLHDQHSMAPCPVAQLPPGPLQDLEPGDQL 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 359 ITATKIPKSLPTKPSAPSTSIVPIKSPHPTQktAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQRNPGMPRPPPP 438
Cdd:PHA03379 485 PGVVQDGRPACAPVPAPAGPIVRPWEASLSQ--VPGVAFAPVMPQPMPVEPVPVPTVALERPVCPAPPLIAMQGPGETSG 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 439 STRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKP----PPFTALSSSPAPTpgsTRSTRPPATMVPPTSGT 514
Cdd:PHA03379 563 IVRVRERWRPAPWTPNPPRSPSQMSVRDRLARLRAEAQPYQASvevqPPQLTQVSPQQPM---EYPLEPEQQMFPGSPFS 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 515 STPRTAPAVPTPGSAPTGSKKPIGSEASKKA--GPKSSPRKPVPLRPGKAAR--DVPLSD-LTTRPSPRQPQPSQQTTPA 589
Cdd:PHA03379 640 QVADVMRAGGVPAMQPQYFDLPLQQPISQGAplAPLRASMGPVPPVPATQPQyfDIPLTEpINQGASAAHFLPQQPMEGP 719
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 24251209 590 LV----LAPAQFLSSSPRPTSSGYSIFHLAGSTPF----PLLMGPPGP 629
Cdd:PHA03379 720 LVperwMFQGATLSQSVRPGVAQSQYFDLPLTQPInhgaPAAHFLHQP 767
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
916-990 |
5.30e-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: 5.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24251209 916 GPPGDNGPEGMKGKPGARGLPGPRGQLGPegdegpmgppgapglegqPGRKGFPGRPGLDGVKGEPGDPGRPGPV 990
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGP------------------PGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| rad23 |
TIGR00601 |
UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
469-545 |
5.80e-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: 5.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24251209 469 SKPASARTSTHKPPPftalSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKA 545
Cdd:TIGR00601 75 SKPKTGTGKVAPPAA----TPTSAPTPTPSPPASPASGMSAAPASAVEEKSPSEESATATAPESPSTSVPSSGSDAA 147
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
334-590 |
5.97e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 41.61 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 334 DPML-------PASVGGSTRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPH---PTQKTAPSSFTKSALPT 403
Cdd:PRK10263 308 DPLLngapitePVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQtgePVIAPAPEGYPQQSQYA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 404 QKQVP---PTSRPVP-------------ARVSRPAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSH 467
Cdd:PRK10263 388 QPAVQynePLQQPVQpqqpyyapaaeqpAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQT 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 468 ASKPASARTSTHKPPPFTALSS-SPAPTPGSTRSTRPP------------------ATMVPPtsgTSTPRTAPAVPTPGS 528
Cdd:PRK10263 468 YQQPAAQEPLYQQPQPVEQQPVvEPEPVVEETKPARPPlyyfeeveekrarereqlAAWYQP---IPEPVKEPEPIKSSL 544
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24251209 529 APTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARD-VPLSDLTTRPSPRqPQPSQQTTPAL 590
Cdd:PRK10263 545 KAPSVAAVPPVEAAAAVSPLASGVKKATLATGAAATVaAPVFSLANSGGPR-PQVKEGIGPQL 606
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
472-593 |
8.35e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 40.95 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 472 ASARTSTHKPPPF------TALSSSPAPTPGSTRSTRPPAtmVPPTSGTST-PRTAPAVPTPGSAPTGSKKPIGSEASKK 544
Cdd:PRK14950 339 FQLRTTSYGQLPLelavieALLVPVPAPQPAKPTAAAPSP--VRPTPAPSTrPKAAAAANIPPKEPVRETATPPPVPPRP 416
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 24251209 545 AGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTTPALVLA 593
Cdd:PRK14950 417 VAPPVPHTPESAPKLTRAAIPVDEKPKYTPPAPPKEEEKALIADGDVLE 465
|
|
| PHA03377 |
PHA03377 |
EBNA-3C; Provisional |
366-619 |
8.74e-03 |
|
EBNA-3C; Provisional
Pssm-ID: 177614 [Multi-domain] Cd Length: 1000 Bit Score: 41.19 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 366 KSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQRNPGMPRPPPPSTRPLPP 445
Cdd:PHA03377 447 QSTPERPGPSDQPSVPVEPAHLTPVEHTTVILHQPPQSPPTVAIKPAPPPSRRRRGACVVYDDDIIEVIDVETTEEEESV 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 446 TTSSSKKPIPTLARTEAKITSHASKPASARTSTHKPP---PFTALSSSPAPTPGSTRSTRPPAtMVPPTSG--------T 514
Cdd:PHA03377 527 TQPAKPHRKVQDGFQRSGRRQKRATPPKVSPSDRGPPkasPPVMAPPSTGPRVMATPSTGPRD-MAPPSTGprqqakckD 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209 515 STPRTAPAVPTPGS-APTGSKKPIGSEASK-KAGPKSSPRKPVPLRPGKAARDVPlsDLTTRPSPRQPQPSQQTTPALVL 592
Cdd:PHA03377 606 GPPASGPHEKQPPSsAPRDMAPSVVRMFLReRLLEQSTGPKPKSFWEMRAGRDGS--GIQQEPSSRRQPATQSTPPRPSW 683
|
250 260
....*....|....*....|....*...
gi 24251209 593 APAQF-LSSSPRPTSSGYSIFHLAGSTP 619
Cdd:PHA03377 684 LPSVFvLPSVDAGRAQPSEESHLSSMSP 711
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1394-1448 |
8.76e-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: 36.32 E-value: 8.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 24251209 1394 GPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEGIAGPDGLPG 1448
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
760-809 |
8.85e-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: 8.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 24251209 760 GLPGLFGLPGSDGERGLPGVPGKRGKMGMPGFPGVFGERGPPGLDGNPGE 809
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
841-892 |
9.29e-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: 9.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 24251209 841 GLMGSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLG 892
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 ... |
477-528 |
9.42e-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: 9.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 24251209 477 STHKP--PPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGS 528
Cdd:cd21440 43 SLHKPkaPLQPPSVLSPSPMILSVSPSAPQSLVSSTGTGMGTTSAIPAVLSPGS 96
|
|
| |
