|
Name |
Accession |
Description |
Interval |
E-value |
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
721-989 |
5.43e-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: 125.02 E-value: 5.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 721 GEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGKMGMPGFPGVFGERGP 800
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 801 PGLDGNPGELglpgppgvpgliGDLGVLGPIGYPGPKGMKGLMGSVGepglKGDKGEQGVPGVSGDPGFQGDKGSQGLPG 880
Cdd:NF038329 197 RGETGPAGEQ------------GPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 881 FPGARGKPGPLGKVGDKGsigfpgppgpegfpgDIGPPGDNGPEGMKGKPGARGLPGPRGQLGPEGdegpmgppgapgLE 960
Cdd:NF038329 261 PRGDRGEAGPDGPDGKDG---------------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG------------LP 313
|
250 260
....*....|....*....|....*....
gi 767958591 961 GQPGRKGFPGRPGLDGVKGEPGDPGRPGP 989
Cdd:NF038329 314 GKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
691-889 |
7.92e-28 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 118.47 E-value: 7.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 691 GDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGS 770
Cdd:NF038329 141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 771 DGERGLPGVPGkRGKMGMPGFPGVFGERGPPGLDGNPGELGLPGPPGVPGLIGDLGVLGPIGYPGPKGMKGLMGSVGEPG 850
Cdd:NF038329 221 AGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299
|
170 180 190
....*....|....*....|....*....|....*....
gi 767958591 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 ... |
1060-1315 |
2.05e-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: 101.91 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 1060 GAKGRRGPRGPDGPAGEQGSRGLKGPPGPQGRPGRPGQQGVAGERGHLGSRGFPGIPGPsgppgtkglpgepgpqgpqgp 1139
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP--------------------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 1140 igppgeMGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGL--KGDRGDPGPDGEHGE 1217
Cdd:NF038329 176 ------AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGP 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 1218 KGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQGEKGRTGAKGAKGYQGQLGEmgvpgdpgppgtpgpKGSRGSLGPTGAPG 1297
Cdd:NF038329 250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGK---------------DGKDGQNGKDGLPG 314
|
250
....*....|....*...
gi 767958591 1298 RMGAQGEPGLAGYDGHKG 1315
Cdd:NF038329 315 KDGKDGQPGKDGLPGKDG 332
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
625-837 |
4.76e-20 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 94.97 E-value: 4.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 625 GPPGPKGDCGLPGPPGLPGLPGIPGARGPRGPPGPYGNPGLPGPPGAKGQKGDPGLSPGKAHDGAKGDMGLPGLSGNPGP 704
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 705 PGRKGHKGYPGPAGHPGEQGQpGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRG 784
Cdd:NF038329 212 AGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767958591 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 |
2.57e-19 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 92.66 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 974 LDGVKGEPGDPGRPGPVGEQGFMGFIGLVGEPGIVGEKGDRGMMGPPGVPGPKGsmghpgmpggmgtpgEPGPQGPpgsr 1053
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------------EAGPQGP---- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 1054 gppgmRGAKGRRGPRGPDGPAGEQGSRGLKGPPGPQGRPGRPGQQGVAGERGHLGsrgfpgipgpsgppgtkglpgepgp 1133
Cdd:NF038329 176 -----AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG------------------------- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 1134 qgpQGPIGPPGEMGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRGDPGPDG 1213
Cdd:NF038329 226 ---PAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302
|
250 260 270
....*....|....*....|....*....|....*.
gi 767958591 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 |
6.71e-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: 91.12 E-value: 6.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 844 GSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLGKVGDKGSIgfpgppgpegfpgdiGPPGDNGP 923
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKDGE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 924 EGMKGKPGARGLPGPRGQLGPEGDEGPMGPPGAPGLEGQPGRKGFPGRPGlDGVKGEPGDPGRPGPVGEQgfmgfiGLVG 1003
Cdd:NF038329 182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ------GPDG 254
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767958591 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 ... |
869-1216 |
1.28e-17 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 87.27 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 869 FQGDKGSQGLPGFPGARGKPGPLGKVGDKGsigfpgppgpegFPGDIGPPGDNGPEGMKGKPGARGLPGPRGQLGPEGde 948
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETG------------PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG-- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 949 gpmgppgapglegQPGRKGFPGRPGLDGVKGEPGDPGRPGPVGEQGFMGFIGLVGEPGIVGEKGDrgmmgppgvpgpkgs 1028
Cdd:NF038329 181 -------------EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD--------------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 1029 mghpgmpggmgtpgepgpqgppgsrgppgmrGAKGRRGPRGPDGPAGEQGSRGlkgppgpqgrpgrpgqqgvagERGHLG 1108
Cdd:NF038329 233 -------------------------------GQQGPDGDPGPTGEDGPQGPDG---------------------PAGKDG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 1109 SRGFPGIPGPSgppgtkglpgepgpqgpqgpigppgemgpkGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEP 1188
Cdd:NF038329 261 PRGDRGEAGPD------------------------------GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD 310
|
330 340
....*....|....*....|....*...
gi 767958591 1189 GLEGDSGPMGPDGLKGDRGDPGPDGEHG 1216
Cdd:NF038329 311 GLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
274-605 |
3.58e-13 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 74.97 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 274 TATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPAAA 353
Cdd:PHA03247 2636 NEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHAL 2715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 354 QPSQKITatkiPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPaekPIQRNPGMP 433
Cdd:PHA03247 2716 VSATPLP----PGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP---PRRLTRPAV 2788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 434 RPPPPSTRPLPPTTSSSKKPIPTLARTeakitshASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSG 513
Cdd:PHA03247 2789 ASLSESRESLPSPWDPADPPAAVLAPA-------AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGD 2861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 514 TS---TPRTAPAVPTPGSAPTGSKKPiGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPR-QPQPSQQTTPA 589
Cdd:PHA03247 2862 VRrrpPSRSPAAKPAAPARPPVRRLA-RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpQPPPPPPPRPQ 2940
|
330
....*....|....*.
gi 767958591 590 LVLAPAQFLSSSPRPT 605
Cdd:PHA03247 2941 PPLAPTTDPAGAGEPS 2956
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
45-220 |
6.30e-13 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 68.54 E-value: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 45 DVDILQRLGLSWTKAGSPAPPGVIPFQSGFIFTQRARLQAPTGTVIPAALGTELALVLSLCSHRVNHAFLFAVRSQKRKL 124
Cdd:smart00210 1 GQDLLQVFDLPSLSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDAQNVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 125 QLGLQFLPGKTVVHL------GSRRSVAF-DLDMHDGRWHHLALELRGRTVTLVTACGQR-RVPVLLPFHrdPALDPGGS 196
Cdd:smart00210 81 QFGLEVDGRANTLLLryqgvdGKQHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIdSRPLDRPGQ--PPIDTDGI 158
|
170 180
....*....|....*....|....
gi 767958591 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 |
1.18e-10 |
|
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: 65.75 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 281 SLPAGR-GPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLlpaKLSASNALDPMLPASVggSTRTPRPAAAQPSqki 359
Cdd:pfam17823 98 SEPATReGAADGAASRALAAAASSSPSSAAQSLPAAIAALPSE---AFSAPRAAACRANASA--APRAAIAAASAPH--- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 360 TATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKS-------------ALPTQKQVPPTSRPVPARVSrpaekpi 426
Cdd:pfam17823 170 AASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPArgistaatatghpAAGTALAAVGNSSPAAGTVT------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 427 qrnpgmprppppstrplPPTTSSSKKPIPTLARTEAKITSHA-----SKPASARTSTHKPPPFTALSSSPAPTPGS-TRS 500
Cdd:pfam17823 243 -----------------AAVGTVTPAALATLAAAAGTVASAAgtinmGDPHARRLSPAKHMPSDTMARNPAAPMGAqAQG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 501 TRPPATMVPP---TSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSP 577
Cdd:pfam17823 306 PIIQVSTDQPvhnTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPSP 385
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 767958591 578 RqpQPSQQTT-PALVLAPAQF--------LSSSPRPTSSG 608
Cdd:pfam17823 386 L--LPTQGAAgPGILLAPEQVateatagtASAGPTPRSSG 423
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
691-747 |
7.32e-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: 44.41 E-value: 7.32e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767958591 691 GDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPV 747
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
697-752 |
1.15e-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: 44.02 E-value: 1.15e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 767958591 697 GLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGP 752
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| rad23 |
TIGR00601 |
UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
460-531 |
3.71e-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: 44.50 E-value: 3.71e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958591 460 TEAKITSHASKPASARTSTHKPPPFTALSSSPAPTpgstrSTRPPATMVPPTSGTSTPRT-APAVPTPGSAPT 531
Cdd:TIGR00601 80 GTGKVAPPAATPTSAPTPTPSPPASPASGMSAAPA-----SAVEEKSPSEESATATAPESpSTSVPSSGSDAA 147
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
136-204 |
6.40e-04 |
|
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: 41.25 E-value: 6.40e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958591 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 ... |
1146-1199 |
2.83e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.09 E-value: 2.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 767958591 1146 MGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGP 1199
Cdd:pfam01391 3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
721-989 |
5.43e-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: 125.02 E-value: 5.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 721 GEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGKMGMPGFPGVFGERGP 800
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 801 PGLDGNPGELglpgppgvpgliGDLGVLGPIGYPGPKGMKGLMGSVGepglKGDKGEQGVPGVSGDPGFQGDKGSQGLPG 880
Cdd:NF038329 197 RGETGPAGEQ------------GPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 881 FPGARGKPGPLGKVGDKGsigfpgppgpegfpgDIGPPGDNGPEGMKGKPGARGLPGPRGQLGPEGdegpmgppgapgLE 960
Cdd:NF038329 261 PRGDRGEAGPDGPDGKDG---------------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG------------LP 313
|
250 260
....*....|....*....|....*....
gi 767958591 961 GQPGRKGFPGRPGLDGVKGEPGDPGRPGP 989
Cdd:NF038329 314 GKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
691-889 |
7.92e-28 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 118.47 E-value: 7.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 691 GDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGS 770
Cdd:NF038329 141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 771 DGERGLPGVPGkRGKMGMPGFPGVFGERGPPGLDGNPGELGLPGPPGVPGLIGDLGVLGPIGYPGPKGMKGLMGSVGEPG 850
Cdd:NF038329 221 AGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299
|
170 180 190
....*....|....*....|....*....|....*....
gi 767958591 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 ... |
1060-1315 |
2.05e-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: 101.91 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 1060 GAKGRRGPRGPDGPAGEQGSRGLKGPPGPQGRPGRPGQQGVAGERGHLGSRGFPGIPGPsgppgtkglpgepgpqgpqgp 1139
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP--------------------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 1140 igppgeMGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGL--KGDRGDPGPDGEHGE 1217
Cdd:NF038329 176 ------AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGP 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 1218 KGQEGLMGEDGPPGPPGVTGVRGPEGKSGKQGEKGRTGAKGAKGYQGQLGEmgvpgdpgppgtpgpKGSRGSLGPTGAPG 1297
Cdd:NF038329 250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGK---------------DGKDGQNGKDGLPG 314
|
250
....*....|....*...
gi 767958591 1298 RMGAQGEPGLAGYDGHKG 1315
Cdd:NF038329 315 KDGKDGQPGKDGLPGKDG 332
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
625-837 |
4.76e-20 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 94.97 E-value: 4.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 625 GPPGPKGDCGLPGPPGLPGLPGIPGARGPRGPPGPYGNPGLPGPPGAKGQKGDPGLSPGKAHDGAKGDMGLPGLSGNPGP 704
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 705 PGRKGHKGYPGPAGHPGEQGQpGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRG 784
Cdd:NF038329 212 AGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767958591 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 |
2.57e-19 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 92.66 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 974 LDGVKGEPGDPGRPGPVGEQGFMGFIGLVGEPGIVGEKGDRGMMGPPGVPGPKGsmghpgmpggmgtpgEPGPQGPpgsr 1053
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------------EAGPQGP---- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 1054 gppgmRGAKGRRGPRGPDGPAGEQGSRGLKGPPGPQGRPGRPGQQGVAGERGHLGsrgfpgipgpsgppgtkglpgepgp 1133
Cdd:NF038329 176 -----AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG------------------------- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 1134 qgpQGPIGPPGEMGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRGDPGPDG 1213
Cdd:NF038329 226 ---PAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302
|
250 260 270
....*....|....*....|....*....|....*.
gi 767958591 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 |
6.71e-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: 91.12 E-value: 6.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 844 GSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLGKVGDKGSIgfpgppgpegfpgdiGPPGDNGP 923
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKDGE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 924 EGMKGKPGARGLPGPRGQLGPEGDEGPMGPPGAPGLEGQPGRKGFPGRPGlDGVKGEPGDPGRPGPVGEQgfmgfiGLVG 1003
Cdd:NF038329 182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ------GPDG 254
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767958591 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 ... |
869-1216 |
1.28e-17 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 87.27 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 869 FQGDKGSQGLPGFPGARGKPGPLGKVGDKGsigfpgppgpegFPGDIGPPGDNGPEGMKGKPGARGLPGPRGQLGPEGde 948
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETG------------PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG-- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 949 gpmgppgapglegQPGRKGFPGRPGLDGVKGEPGDPGRPGPVGEQGFMGFIGLVGEPGIVGEKGDrgmmgppgvpgpkgs 1028
Cdd:NF038329 181 -------------EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD--------------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 1029 mghpgmpggmgtpgepgpqgppgsrgppgmrGAKGRRGPRGPDGPAGEQGSRGlkgppgpqgrpgrpgqqgvagERGHLG 1108
Cdd:NF038329 233 -------------------------------GQQGPDGDPGPTGEDGPQGPDG---------------------PAGKDG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 1109 SRGFPGIPGPSgppgtkglpgepgpqgpqgpigppgemgpkGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEP 1188
Cdd:NF038329 261 PRGDRGEAGPD------------------------------GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD 310
|
330 340
....*....|....*....|....*...
gi 767958591 1189 GLEGDSGPMGPDGLKGDRGDPGPDGEHG 1216
Cdd:NF038329 311 GLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
274-605 |
3.58e-13 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 74.97 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 274 TATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPAAA 353
Cdd:PHA03247 2636 NEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHAL 2715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 354 QPSQKITatkiPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPaekPIQRNPGMP 433
Cdd:PHA03247 2716 VSATPLP----PGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP---PRRLTRPAV 2788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 434 RPPPPSTRPLPPTTSSSKKPIPTLARTeakitshASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSG 513
Cdd:PHA03247 2789 ASLSESRESLPSPWDPADPPAAVLAPA-------AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGD 2861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 514 TS---TPRTAPAVPTPGSAPTGSKKPiGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPR-QPQPSQQTTPA 589
Cdd:PHA03247 2862 VRrrpPSRSPAAKPAAPARPPVRRLA-RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpQPPPPPPPRPQ 2940
|
330
....*....|....*.
gi 767958591 590 LVLAPAQFLSSSPRPT 605
Cdd:PHA03247 2941 PPLAPTTDPAGAGEPS 2956
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
45-220 |
6.30e-13 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 68.54 E-value: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 45 DVDILQRLGLSWTKAGSPAPPGVIPFQSGFIFTQRARLQAPTGTVIPAALGTELALVLSLCSHRVNHAFLFAVRSQKRKL 124
Cdd:smart00210 1 GQDLLQVFDLPSLSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDAQNVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 125 QLGLQFLPGKTVVHL------GSRRSVAF-DLDMHDGRWHHLALELRGRTVTLVTACGQR-RVPVLLPFHrdPALDPGGS 196
Cdd:smart00210 81 QFGLEVDGRANTLLLryqgvdGKQHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIdSRPLDRPGQ--PPIDTDGI 158
|
170 180
....*....|....*....|....
gi 767958591 197 FLFGKMNPHAVQFEGALCQFSIYP 220
Cdd:smart00210 159 EVRGAQAADRKPFQGDLQQLKIVC 182
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
245-631 |
1.31e-11 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 69.97 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 245 PLGPLFSQDSGRPFTFQSDLALLGLENLTTATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLP 324
Cdd:PHA03247 2561 PAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDP 2640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 325 AKLSASNALDPMLPASVGGSTRTPRPAAAQpsQKITATKIPKSLPTKPSAPST--SIVPIKSPHPTQKTAPSSFTksalP 402
Cdd:PHA03247 2641 HPPPTVPPPERPRDDPAPGRVSRPRRARRL--GRAAQASSPPQRPRRRAARPTvgSLTSLADPPPPPPTPEPAPH----A 2714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 403 TQKQVPPTSRPVPARVSRPAE--KPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEA-----KITSHASKPASAR 475
Cdd:PHA03247 2715 LVSATPLPPGPAAARQASPALpaAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAagpprRLTRPAVASLSES 2794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 476 TSTHKPP--PFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRK 553
Cdd:PHA03247 2795 RESLPSPwdPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAK 2874
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 554 P-VPLRPGKAARDVPLSDLTTRPSP-------RQPQPSQQTTPALVLAPAQFLSSSPRPTSSGYSIFHLAgstPFPLLMG 625
Cdd:PHA03247 2875 PaAPARPPVRRLARPAVSRSTESFAlppdqpeRPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLA---PTTDPAG 2951
|
....*.
gi 767958591 626 PPGPKG 631
Cdd:PHA03247 2952 AGEPSG 2957
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
283-780 |
1.01e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 66.89 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 283 PAGRGPRGTVAPATPTKPQRTSPTNPhqhmAVGGPAQTPLLP-----AKLSASNALDP-------MLPASVGGSTRTPRP 350
Cdd:PHA03247 2498 PGGGGPPDPDAPPAPSRLAPAILPDE----PVGEPVHPRMLTwirglEELASDDAGDPppplppaAPPAAPDRSVPPPRP 2573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 351 AAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPtqkqvPPTSRPVPARVSRPAEKPIQRNP 430
Cdd:PHA03247 2574 APRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPD-----PPPPSPSPAANEPDPHPPPTVPP 2648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 431 GMPRPPPPSTRPLPPTTSSSKKPIPTLAR-TEAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMV- 508
Cdd:PHA03247 2649 PERPRDDPAPGRVSRPRRARRLGRAAQASsPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAa 2728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 509 ----PPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSq 584
Cdd:PHA03247 2729 rqasPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADP- 2807
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 585 qttPALVLAPAQFLSSSPRPTSsgysifhLAGSTPFPLLMGPPGPKGdcGLPGPPGLPGLPGIPGARGPRGPPGPYGNPG 664
Cdd:PHA03247 2808 ---PAAVLAPAAALPPAASPAG-------PLPPPTSAQPTAPPPPPG--PPPPSLPLGGSVAPGGDVRRRPPSRSPAAKP 2875
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 665 LPGPPGAKGQKGDPGLSPgkahdgAKGDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLP 744
Cdd:PHA03247 2876 AAPARPPVRRLARPAVSR------STESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDP 2949
|
490 500 510
....*....|....*....|....*....|....*...
gi 767958591 745 GPVGDPGPKGSRGYIG--LPGLFGLPGSDGERGLPGVP 780
Cdd:PHA03247 2950 AGAGEPSGAVPQPWLGalVPGRVAVPRFRVPQPAPSRE 2987
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
281-608 |
1.18e-10 |
|
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: 65.75 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 281 SLPAGR-GPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLlpaKLSASNALDPMLPASVggSTRTPRPAAAQPSqki 359
Cdd:pfam17823 98 SEPATReGAADGAASRALAAAASSSPSSAAQSLPAAIAALPSE---AFSAPRAAACRANASA--APRAAIAAASAPH--- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 360 TATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKS-------------ALPTQKQVPPTSRPVPARVSrpaekpi 426
Cdd:pfam17823 170 AASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPArgistaatatghpAAGTALAAVGNSSPAAGTVT------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 427 qrnpgmprppppstrplPPTTSSSKKPIPTLARTEAKITSHA-----SKPASARTSTHKPPPFTALSSSPAPTPGS-TRS 500
Cdd:pfam17823 243 -----------------AAVGTVTPAALATLAAAAGTVASAAgtinmGDPHARRLSPAKHMPSDTMARNPAAPMGAqAQG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 501 TRPPATMVPP---TSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSP 577
Cdd:pfam17823 306 PIIQVSTDQPvhnTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPSP 385
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 767958591 578 RqpQPSQQTT-PALVLAPAQF--------LSSSPRPTSSG 608
Cdd:pfam17823 386 L--LPTQGAAgPGILLAPEQVateatagtASAGPTPRSSG 423
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
273-576 |
2.22e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 65.73 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 273 TTATPALgSLPAGRGPRGTVAPATPTKPqrTSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASvGGSTRTPRPAA 352
Cdd:PHA03247 2713 HALVSAT-PLPPGPAAARQASPALPAAP--APPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA-GPPRRLTRPAV 2788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 353 AQ-------------PSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPP--------TS 411
Cdd:PHA03247 2789 ASlsesreslpspwdPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPggdvrrrpPS 2868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 412 RPVPARVSRPAEKPIQRnpgmprpppPSTRPLPPTTSSSKKPIPTLARTEakitshaSKPASARTSTHKPPPFTALSSSP 491
Cdd:PHA03247 2869 RSPAAKPAAPARPPVRR---------LARPAVSRSTESFALPPDQPERPP-------QPQAPPPPQPQPQPPPPPQPQPP 2932
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 492 APTPGstrstRPPATMVPPTSGTSTPRTAPAVPTPgsaPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDL 571
Cdd:PHA03247 2933 PPPPP-----RPQPPLAPTTDPAGAGEPSGAVPQP---WLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRV 3004
|
....*
gi 767958591 572 TTRPS 576
Cdd:PHA03247 3005 SSWAS 3009
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
271-621 |
2.25e-08 |
|
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: 58.77 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 271 NLTTATPA---LGSLPAGRGPRGTVAPATPTKPQRTSPTNphqhmAVGGP---AQTPLLPAKLSASNALDPML-PASVGG 343
Cdd:pfam05109 472 DVTSPTPAgttSGASPVTPSPSPRDNGTESKAPDMTSPTS-----AVTTPtpnATSPTPAVTTPTPNATSPTLgKTSPTS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 344 STRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPV---PARVSR 420
Cdd:pfam05109 547 AVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPVvtsPPKNAT 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 421 PAEKPIQRNPGMPRPPPPSTRPLP-------PTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKpppftALSSSPAP 493
Cdd:pfam05109 627 SAVTTGQHNITSSSTSSMSLRPSSisetlspSTSDNSTSHMPLLTSAHPTGGENITQVTPASTSTHH-----VSTSSPAP 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 494 TPGSTRSTRPP---ATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASkkAGPKSSPRKPVPLRPGKAARDVplSD 570
Cdd:pfam05109 702 RPGTTSQASGPgnsSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTS--TGGKANSTTGGKHTTGHGARTS--TE 777
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 767958591 571 LTTRPSPRQPQPSQQTTPALVLAPAQFLSSSPRPTSSGYSIFHLAGSTPFP 621
Cdd:pfam05109 778 PTTDYGGDSTTPRTRYNATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVP 828
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
272-607 |
3.49e-07 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 55.18 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 272 LTTATPALGSLPAGRGPRGTVAPATPTkpqrtSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPA 351
Cdd:PHA03307 50 LAAVTVVAGAAACDRFEPPTGPPPGPG-----TEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 352 AAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPiqRNPG 431
Cdd:PHA03307 125 SPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTP--PAAA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 432 MPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASA--------RTSTHKPPPFTALSSSPAPTPGSTRSTRP 503
Cdd:PHA03307 203 SPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSgcgwgpenECPLPRPAPITLPTRIWEASGWNGPSSRP 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 504 PATMVPPTSGTSTPRTAPAVPTPGSAPTGSKK-----PIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSdltTRPSPR 578
Cdd:PHA03307 283 GPASSSSSPRERSPSPSPSSPGSGPAPSSPRAsssssSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSP---SRPPPP 359
|
330 340
....*....|....*....|....*....
gi 767958591 579 QPQPSQQTTPALVLAPAQFLSSSPRPTSS 607
Cdd:PHA03307 360 ADPSSPRKRPRPSRAPSSPAASAGRPTRR 388
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
248-556 |
2.02e-06 |
|
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: 52.46 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 248 PLFSQDSGRPFTFQSDLALLGLENLTTATPALGSLPAGRGPRGTVAPATPTKPQRTS-PTNPH------QHMAVGGPAQT 320
Cdd:pfam03154 218 PNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQmPPMPHslqtgpSHMQHPVPPQP 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 321 PLLPAKLSASNALDPMLPASVGGSTRT-------PRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSP----HPTQ 389
Cdd:pfam03154 298 FPLTPQSSQSQVPPGPSPAAPGQSQQRihtppsqSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPqshkHPPH 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 390 KTAPSSFT-KSALPTQKQVPPTSRPVPARVSRPAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHA 468
Cdd:pfam03154 378 LSGPSPFQmNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVP 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 469 SKPASARTS--THKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTstprtAPAVPTPGSAPTGSKKPIGSEASKKAG 546
Cdd:pfam03154 458 SQSPFPQHPfvPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGP-----VPAAVSCPLPPVQIKEEALDEAEEPES 532
|
330
....*....|
gi 767958591 547 PKSSPRKPVP 556
Cdd:pfam03154 533 PPPPPRSPSP 542
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
273-589 |
2.41e-06 |
|
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: 52.08 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 273 TTATPALGSLPAGRGPRGTVAPATPTKPQRT-SPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPA 351
Cdd:pfam03154 191 TTQAATAGPTPSAPSVPPQGSPATSQPPNQTqSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPS 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 352 AAQPSQ------KITATKIPKSLPTKP----SAPSTSIVP----IKSPHPTQKTAPSSFTKSALPTQKqvPPTSRPV-PA 416
Cdd:pfam03154 271 LHGQMPpmphslQTGPSHMQHPVPPQPfpltPQSSQSQVPpgpsPAAPGQSQQRIHTPPSQSQLQSQQ--PPREQPLpPA 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 417 RVSRPAEKPiqrnpgmprppppstrplppttsSSKKPIPTLARTEA-KITSHASKPASARTSTHKPPPFTALSSSPAPTP 495
Cdd:pfam03154 349 PLSMPHIKP-----------------------PPTTPIPQLPNPQShKHPPHLSGPSPFQMNSNLPPPPALKPLSSLSTH 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 496 GSTRSTRPPATMVPPTSGTSTPRTAPAVPT--PGSAPTGSKKPigSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTT 573
Cdd:pfam03154 406 HPPSAHPPPLQLMPQSQQLPPPPAQPPVLTqsQSLPPPAASHP--PTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPT 483
|
330
....*....|....*...
gi 767958591 574 RPSPRQP--QPSQQTTPA 589
Cdd:pfam03154 484 STSSAMPgiQPPSSASVS 501
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
277-588 |
2.57e-06 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 52.16 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 277 PALGslpAGRGPRGTVAPATPTkpqrtsptnphqhmAVGGPAQTPLLPAKLSASnaldPMLPASVGGSTRTPRPAAAQPS 356
Cdd:PRK07003 360 PAVT---GGGAPGGGVPARVAG--------------AVPAPGARAAAAVGASAV----PAVTAVTGAAGAALAPKAAAAA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 357 QKiTATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQRNpgmprpp 436
Cdd:PRK07003 419 AA-TRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAF------- 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 437 ppstrplppttsSSKKPIPTLARTEAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTR-----PPATMVPPT 511
Cdd:PRK07003 491 ------------EPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAAraggaAAALDVLRN 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 512 SG----TSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTT 587
Cdd:PRK07003 559 AGmrvsSDRGARAAAAAKPAAAPAAAPKPAAPRVAVQVPTPRARAATGDAPPNGAARAEQAAESRGAPPPWEDIPPDDYV 638
|
.
gi 767958591 588 P 588
Cdd:PRK07003 639 P 639
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
237-548 |
4.86e-06 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 50.73 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 237 GQADTYQS--PLGPLFSQDSGRPFTFQSDLALLGLENLTTATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMAV 314
Cdd:pfam17823 105 GAADGAASraLAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 315 GGPAQTPLLPAKLSASNALDPMLPASvggSTRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPS 394
Cdd:pfam17823 185 ASSTTAASSAPTTAASSAPATLTPAR---GISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAG 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 395 SFTKSALPTQKQVPPTSRPVPARvSRP----AEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKIT---SH 467
Cdd:pfam17823 262 TVASAAGTINMGDPHARRLSPAK-HMPsdtmARNPAAPMGAQAQGPIIQVSTDQPVHNTAGEPTPSPSNTTLEPNtpkSV 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 468 ASKPASARTSTH---KPPpftalSSSPAPTPGSTRSTRPPATM-------VPPTSGTSTPRTAPAVPTPGSAPTGSKKPI 537
Cdd:pfam17823 341 ASTNLAVVTTTKaqaKEP-----SASPVPVLHTSMIPEVEATSpttqpspLLPTQGAAGPGILLAPEQVATEATAGTASA 415
|
330
....*....|.
gi 767958591 538 GSEASKKAGPK 548
Cdd:pfam17823 416 GPTPRSSGDPK 426
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
264-536 |
5.11e-06 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 51.00 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 264 LALLGLENLTTAtpalGSLPAGRGPrGTVAPATPTKPQRTSPtnphqhmAVGGPAQTPLLPAKLSASNALDPMLPASVGG 343
Cdd:PRK07003 353 LRMLAFEPAVTG----GGAPGGGVP-ARVAGAVPAPGARAAA-------AVGASAVPAVTAVTGAAGAALAPKAAAAAAA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 344 STRTPRPAAAQPSQKITAT--KIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRP 421
Cdd:PRK07003 421 TRAEAPPAAPAPPATADRGddAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPS 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 422 AEKPIQRNPGMPRPPPPST---RPLPPTTSSSKKPIPTLARTEAKITSHAS-----KPASARTSTHKPPPFTALSSSPAP 493
Cdd:PRK07003 501 AATPAAVPDARAPAAASREdapAAAAPPAPEARPPTPAAAAPAARAGGAAAaldvlRNAGMRVSSDRGARAAAAAKPAAA 580
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767958591 494 TPGSTRSTRPPATMVPPTSG----TSTPRTAPAVPTPGSAPTGSKKP 536
Cdd:PRK07003 581 PAAAPKPAAPRVAVQVPTPRaraaTGDAPPNGAARAEQAAESRGAPP 627
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
691-747 |
7.32e-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: 44.41 E-value: 7.32e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767958591 691 GDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPV 747
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
275-594 |
9.21e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.71 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 275 ATPALGSLPAGRG-PRGTVAPATPTKPQR-------TSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTR 346
Cdd:PHA03247 2731 ASPALPAAPAPPAvPAGPATPGGPARPARppttagpPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 347 TPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQ---------KTAPSSFTKSALPTQKQVPPTSRPVPAR 417
Cdd:PHA03247 2811 VLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGgsvapggdvRRRPPSRSPAAKPAAPARPPVRRLARPA 2890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 418 VSRPAE-------------KPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLA-RTEAKITSHASKPASARTSTHKPPP 483
Cdd:PHA03247 2891 VSRSTEsfalppdqperppQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLApTTDPAGAGEPSGAVPQPWLGALVPG 2970
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 484 FTALSSSPAPTPGSTRSTrpPATMVPPTSGTSTPRTAP----------AVPTPGSAPTGSKKPIGSEASKKAGPKSSPRK 553
Cdd:PHA03247 2971 RVAVPRFRVPQPAPSREA--PASSTPPLTGHSLSRVSSwasslalheeTDPPPVSLKQTLWPPDDTEDSDADSLFDSDSE 3048
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 767958591 554 PVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTTPALVLAP 594
Cdd:PHA03247 3049 RSDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSSQFGP 3089
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
697-752 |
1.15e-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: 44.02 E-value: 1.15e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 767958591 697 GLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGP 752
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
288-582 |
1.30e-05 |
|
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: 49.77 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 288 PRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRT--------PRPAAAQPSQKI 359
Cdd:pfam03154 245 PHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSsqsqvppgPSPAAPGQSQQR 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 360 TATKIPKSLPTKPSAPSTSIVPiKSPHPTQKTAPSSFTksalPTQKQVPPTSRPVPARVSRPAEKPIQRNPGMPRPPPPS 439
Cdd:pfam03154 325 IHTPPSQSQLQSQQPPREQPLP-PAPLSMPHIKPPPTT----PIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 440 TRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRT 519
Cdd:pfam03154 400 SSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPS 479
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958591 520 APAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQP 582
Cdd:pfam03154 480 GPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSP 542
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
350-586 |
2.42e-05 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 48.77 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 350 PAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSrPVPARVSRPAEKPIQRN 429
Cdd:PLN03209 324 PSQRVPPKESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYTAYEDLKPPTS-PIPTPPSSSPASSKSVD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 430 PGMPRPPPPSTRPLPPTTS-SSKKPIPTLARTEAKITSHA-------------SKPASARTSTHKPPPFTALSSSPAPTP 495
Cdd:PLN03209 403 AVAKPAEPDVVPSPGSASNvPEVEPAQVEAKKTRPLSPYAryedlkpptspspTAPTGVSPSVSSTSSVPAVPDTAPATA 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 496 GSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTT-- 573
Cdd:PLN03209 483 ATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQPKPRPLSPYTMye 562
|
250
....*....|....*
gi 767958591 574 --RPsPRQPQPSQQT 586
Cdd:PLN03209 563 dlKP-PTSPTPSPVL 576
|
|
| PHA03269 |
PHA03269 |
envelope glycoprotein C; Provisional |
448-556 |
2.82e-05 |
|
envelope glycoprotein C; Provisional
Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 48.57 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 448 SSSKKPIPTLARTEAkiTSHASKPASARTS--THKPPPFTALSSS------PAPTPGSTRSTRPPATMVPPTSGTSTPRt 519
Cdd:PHA03269 35 AATQKPDPAPAPHQA--ASRAPDPAVAPTSaaSRKPDLAQAPTPAasekfdPAPAPHQAASRAPDPAVAPQLAAAPKPD- 111
|
90 100 110
....*....|....*....|....*....|....*..
gi 767958591 520 aPAVPtPGSAPTgskkpiGSEASKKAGPKSSPRKPVP 556
Cdd:PHA03269 112 -AAEA-FTSAAQ------AHEAPADAGTSAASKKPDP 140
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
703-757 |
2.89e-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: 2.89e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 767958591 703 GPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRG 757
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
342-588 |
4.01e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 48.15 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 342 GGSTRTPRPAAA-QPSQKITATKIPkSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSR 420
Cdd:PTZ00449 555 GEVGKKPGPAKEhKPSKIPTLSKKP-EFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSP 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 421 PAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPI-PTLA-RTEAKITSHASKPASARTSTHKPPPFTALSSSPAP-TPGS 497
Cdd:PTZ00449 634 KRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFdPKFKeKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPeTPGT 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 498 TRSTRPPATMVPPT--SGTSTPRTAPAVPTPgSAPTGSKKPIGSEASKKAGPKSSPrkpvplRPGKAARDVPLSDLTTRP 575
Cdd:PTZ00449 714 PFTTPRPLPPKLPRdeEFPFEPIGDPDAEQP-DDIEFFTPPEEERTFFHETPADTP------LPDILAEEFKEEDIHAET 786
|
250 260
....*....|....*....|.
gi 767958591 576 S--------PRQPQPSQQTTP 588
Cdd:PTZ00449 787 GepdeamkrPDSPSEHEDKPP 807
|
|
| PHA03269 |
PHA03269 |
envelope glycoprotein C; Provisional |
399-531 |
4.04e-05 |
|
envelope glycoprotein C; Provisional
Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 47.80 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 399 SALPTQKQVPPTSRPVPARVSRPAEKPIQRnpgmprPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTST 478
Cdd:PHA03269 20 ANLNTNIPIPELHTSAATQKPDPAPAPHQA------ASRAPDPAVAPTSAASRKPDLAQAPTPAASEKFDPAPAPHQAAS 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767958591 479 HKPPPFTALSSSPAPTPG-----STRSTRPPATMVPPTSgTSTPRTAPAVPTPGSAPT 531
Cdd:PHA03269 94 RAPDPAVAPQLAAAPKPDaaeafTSAAQAHEAPADAGTS-AASKKPDPAAHTQHSPPP 150
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
268-614 |
5.15e-05 |
|
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: 47.99 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 268 GLENLTTATPALGSLPAGRGPRGTvAPAT--PTKPQRTSPTNPHQHMAVGGPAQTPLLPAkLSASNALDPMLPASVGGST 345
Cdd:pfam05109 375 GCENISGAFASNRTFDITVSGLGT-APKTliITRTATNATTTTHKVIFSKAPESTTTSPT-LNTTGFAAPNTTTGLPSST 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 346 RTPRPAAAQPSQKITATKIPKSLPTkPSAPSTSIVPIK-SPHPTQKTAPSSFTKSALPTQKQVPPT---SRPVPArVSRP 421
Cdd:pfam05109 453 HVPTNLTAPASTGPTVSTADVTSPT-PAGTTSGASPVTpSPSPRDNGTESKAPDMTSPTSAVTTPTpnaTSPTPA-VTTP 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 422 AEKPIQrnpgmprppppstrplppttssskkpiPTLARTEakitshaskPASARTSthkPPPftalsSSPAPTPGSTRST 501
Cdd:pfam05109 531 TPNATS---------------------------PTLGKTS---------PTSAVTT---PTP-----NATSPTPAVTTPT 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 502 rPPATMvpPTSGTSTPRTAPAVPTP-GSAPT-GSKKPIGSEASKKAGPKSSprKPVPLRPGKAArdvplsdlTTRPSPRQ 579
Cdd:pfam05109 567 -PNATI--PTLGKTSPTSAVTTPTPnATSPTvGETSPQANTTNHTLGGTSS--TPVVTSPPKNA--------TSAVTTGQ 633
|
330 340 350
....*....|....*....|....*....|....*
gi 767958591 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 ... |
700-756 |
5.42e-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: 5.42e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767958591 700 GNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSR 756
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
372-554 |
6.66e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 47.38 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 372 PSAPSTSIVPIKSP---------HPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQrnpgmprppppstrp 442
Cdd:PTZ00449 511 PEGPEASGLPPKAPgdkegeegeHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTL--------------- 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 443 lppttssSKKPiptlarTEAKITSHASKPASARTSTHkppPFTALSSSPAPTPgstrsTRPPATMVPPTSGTSTPRTAPA 522
Cdd:PTZ00449 576 -------SKKP------EFPKDPKHPKDPEEPKKPKR---PRSAQRPTRPKSP-----KLPELLDIPKSPKRPESPKSPK 634
|
170 180 190
....*....|....*....|....*....|..
gi 767958591 523 VPTPGSAPTGSKKPIGSEASKKAGPKSSPRKP 554
Cdd:PTZ00449 635 RPPPPQRPSSPERPEGPKIIKSPKPPKSPKPP 666
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
459-618 |
6.83e-05 |
|
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: 47.26 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 459 RTEAKITSHA---SKPASaRTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTApAVPTPGSAptGSKK 535
Cdd:pfam17823 85 EVTAEHTPHGtdlSEPAT-REGAADGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAA-ACRANASA--APRA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 536 PIGSEASKKAG---PKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQT------TPALVLAPAQFLSSSPRPTS 606
Cdd:pfam17823 161 AIAAASAPHAAspaPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGISTaatatgHPAAGTALAAVGNSSPAAGT 240
|
170
....*....|..
gi 767958591 607 SGYSIFHLAGST 618
Cdd:pfam17823 241 VTAAVGTVTPAA 252
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
283-529 |
7.37e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 47.18 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 283 PAGRGprGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPAAaqpsqkitat 362
Cdd:PRK12323 365 PGQSG--GGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEA---------- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 363 kipksLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQRNPGMPRPPPPSTRP 442
Cdd:PRK12323 433 -----LAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 443 LPPTTSSSKKPIPTLArteAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPP---ATMVPPTSGTSTPRT 519
Cdd:PRK12323 508 SPAPAQPDAAPAGWVA---ESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPrasASGLPDMFDGDWPAL 584
|
250
....*....|
gi 767958591 520 APAVPTPGSA 529
Cdd:PRK12323 585 AARLPVRGLA 594
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
328-549 |
1.01e-04 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 46.08 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 328 SASNALDPMLPASVGGSTRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIkSPHPTQKTAPSSFTKSALpTQKQV 407
Cdd:PRK10905 33 SGEKSIDLAGNATDQANGVQPAPGTTSAEQTAGNTQQDVSLPPISSTPTQGQTPV-ATDGQQRVEVQGDLNNAL-TQPQN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 408 PPTSRPVPARVSRPAE----KPIQRNPGMPRPPPPStrplppttSSSKKPIPTLARTEAKItsHASKPASARTSTHKPPP 483
Cdd:PRK10905 111 QQQLNNVAVNSTLPTEpatvAPVRNGNASRQTAKTQ--------TAERPATTRPARKQAVI--EPKKPQATAKTEPKPVA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767958591 484 FTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKS 549
Cdd:PRK10905 181 QTPKRTEPAAPVASTKAPAATSTPAPKETATTAPVQTASPAQTTATPAAGGKTAGNVGSLKSAPSS 246
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
727-783 |
1.26e-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: 40.94 E-value: 1.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767958591 727 GPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKR 783
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
453-629 |
1.29e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 46.41 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 453 PIPTLARTEAKITSHASKPASA---RTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSA 529
Cdd:PRK12323 374 PATAAAAPVAQPAPAAAAPAAAapaPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 530 PTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAArdvplsdlttrpsprQPQPSQQTTPALVLAPAQFLSSSPRPTSSGY 609
Cdd:PRK12323 454 PAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAA---------------APAPADDDPPPWEELPPEFASPAPAQPDAAP 518
|
170 180
....*....|....*....|
gi 767958591 610 SIFHLAgSTPFPLLMGPPGP 629
Cdd:PRK12323 519 AGWVAE-SIPDPATADPDDA 537
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
317-595 |
1.33e-04 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 46.60 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 317 PAQTPLLPAKLSASNALDPM----LPASVGGSTRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTA 392
Cdd:PHA03378 553 PASTEPVHDQLLPAPGLGPLqiqpLTSPTTSQLASSAPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIP 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 393 PSSFTKSALPTQkqvpPTSRPVPARVSRPAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPA 472
Cdd:PHA03378 633 MRPLRMQPITFN----VLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPA 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 473 SARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTpRTAPAVPTPGSAPTgskkpigseaskkagPKSSPR 552
Cdd:PHA03378 709 APPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPG-RARPPAAAPGRARP---------------PAAAPG 772
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 767958591 553 KPVPLRPGKAArDVPLSDLTTRPSPrQPQPSQQTTPALVLAPA 595
Cdd:PHA03378 773 APTPQPPPQAP-PAPQQRPRGAPTP-QPPPQAGPTSMQLMPRA 813
|
|
| rad23 |
TIGR00601 |
UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
460-531 |
3.71e-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: 44.50 E-value: 3.71e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958591 460 TEAKITSHASKPASARTSTHKPPPFTALSSSPAPTpgstrSTRPPATMVPPTSGTSTPRT-APAVPTPGSAPT 531
Cdd:TIGR00601 80 GTGKVAPPAATPTSAPTPTPSPPASPASGMSAAPA-----SAVEEKSPSEESATATAPESpSTSVPSSGSDAA 147
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
468-588 |
4.04e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 44.71 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 468 ASKPASARTSTHKPPPFTALSSSPAPTP--GSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKA 545
Cdd:PRK14951 370 AEAAAPAEKKTPARPEAAAPAAAPVAQAaaAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAP 449
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 767958591 546 GPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTTP 588
Cdd:PRK14951 450 APPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTE 492
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
338-531 |
4.22e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.87 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 338 PASVGGSTRTPRPAAAQPSQKITATKIPKSL---PTKPSAPSTSIVPIKSPHPTQKTAPS--SFTKSALPTQKQV----- 407
Cdd:PRK12323 365 PGQSGGGAGPATAAAAPVAQPAPAAAAPAAAapaPAAPPAAPAAAPAAAAAARAVAAAPArrSPAPEALAAARQAsargp 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 408 ------PPTSRPVPARVSRPAEKPIQRNPGMpRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKP 481
Cdd:PRK12323 445 ggapapAPAPAAAPAAAARPAAAGPRPVAAA-AAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVA 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767958591 482 PPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPT 531
Cdd:PRK12323 524 ESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGL 573
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
468-582 |
6.03e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 44.09 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 468 ASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVP--TPGSAPTGSKKPIGSEASKKA 545
Cdd:PRK07994 358 AFHPAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPlpETTSQLLAARQQLQRAQGATK 437
|
90 100 110
....*....|....*....|....*....|....*..
gi 767958591 546 GPKSSPRKPVPLRPGKAARDvPLSDLTTRPSPRQPQP 582
Cdd:PRK07994 438 AKKSEPAAASRARPVNSALE-RLASVRPAPSALEKAP 473
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
688-738 |
6.34e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.01 E-value: 6.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767958591 688 GAKGDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYP 738
Cdd:pfam01391 7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
136-204 |
6.40e-04 |
|
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: 41.25 E-value: 6.40e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958591 136 VVHLGSRRSVAFDLD--MHDGRWHHLALELRGRTVTLVTaCGQRRVPVLLPfHRDPALDPGGSFLFGKMNP 204
Cdd:pfam02210 33 RYDLGSGPESLLSSGknLNDGQWHSVRVERNGNTLTLSV-DGQTVVSSLPP-GESLLLNLNGPLYLGGLPP 101
|
|
| DUF4045 |
pfam13254 |
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ... |
280-555 |
8.15e-04 |
|
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: 43.62 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 280 GSLPAGRGprGTVAPATPTKPQRTS-------PTNPHQHMAVGGPAQTPLLPAKLSASNAlDPMLPASvggsTRTPRPAA 352
Cdd:pfam13254 47 GSVAGPSG--SLSPGLSPTKLSREGspestsrPSSSHSEATIVRHSKDDERPSTPDEGFV-KPALPRH----SRSSSALS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 353 AQPSQKITAtkipkSLPTKPSAPSTSIVPiKSPHPTqktaPSSFTKSAL-----PTQKQVPPTSRPvPA----------- 416
Cdd:pfam13254 120 NTGSEEDSP-----SLPTSPPSPSKTMDP-KRWSPT----KSSWLESALnrpesPKPKAQPSQPAQ-PAwmkelnkirqs 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 417 -------RVSRPAEKP---IQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTlARTEAKITSHASKPASARTSTHKPPPFTA 486
Cdd:pfam13254 189 rasvdlgRPNSFKEVTpvgLMRSPAPGGHSKSPSVSGISADSSPTKEEPS-EEADTLSTDKEQSPAPTSASEPPPKTKEL 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767958591 487 LSSS---PAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSkKPIGSEASKKAGPKSSPRKPV 555
Cdd:pfam13254 268 PKDSeepAAPSKSAEASTEKKEPDTESSPETSSEKSAPSLLSPVSKASID-KPLSSPDRDPLSPKPKPQSPP 338
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
456-597 |
1.52e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 42.84 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 456 TLARTEAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATmvpPTSGTSTPRTAPAVPTPGSAPTGSKK 535
Cdd:PRK14971 363 TQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSA---PQSATQPAGTPPTVSVDPPAAVPVNP 439
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767958591 536 PIGSEASKKAGPKSSPRKPVPLRPGKAARdvplsdLTTRPSPRQPQPSQQTTPALVLAPAQF 597
Cdd:PRK14971 440 PSTAPQAVRPAQFKEEKKIPVSKVSSLGP------STLRPIQEKAEQATGNIKEAPTGTQKE 495
|
|
| motB |
PRK12799 |
flagellar motor protein MotB; Reviewed |
463-606 |
1.58e-03 |
|
flagellar motor protein MotB; Reviewed
Pssm-ID: 183756 [Multi-domain] Cd Length: 421 Bit Score: 42.78 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 463 KITSHASKPASArtsthkPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGsapTGSKKPIGSEAS 542
Cdd:PRK12799 292 QIDTHGTVPVAA------VTPSSAVTQSSAITPSSAAIPSPAVIPSSVTTQSATTTQASAVALSS---AGVLPSDVTLPG 362
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958591 543 KKAGPKSSPRKPVPlRPGKAARDVPLSDLTTRPSPRQPqpsqqtTPALVLAPAQflSSSPRPTS 606
Cdd:PRK12799 363 TVALPAAEPVNMQP-QPMSTTETQQSSTGNITSTANGP------TTSLPAAPAS--NIPVSPTS 417
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
284-588 |
1.95e-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: 42.68 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 284 AGRG--PRGTVAPATPTKPQRT------SPTNPHQHMAVGGPAQTPLLPAklSASNALDPMLPAS----VGGSTRTPRPA 351
Cdd:TIGR00927 97 VGRDeaTPSIAMENTPSPPRRTakitptTPKNNYSPTAAGTERVKEDTPA--TPSRALNHYISTSgrqrVKSYTPKPRGE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 352 AAQPSQKITATKIPKSLPT------KPSAPSTSIVPIKS----PHPTQKTAPSSFTKSALPTQ--KQVPPTSRPVPAR-- 417
Cdd:TIGR00927 175 VKSSSPTQTREKVRKYTPSplgrmvNSYAPSTFMTMPRShgitPRTTVKDSEITATYKMLETNpsKRTAGKTTPTPLKgm 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 418 -------VSRPAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKPPPFTALSSS 490
Cdd:TIGR00927 255 tdntptfLTREVETDLLTSPRSVVEKNTLTTPRRVESNSSTNHWGLVGKNNLTTPQGTVLEHTPATSEGQVTISIMTGSS 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 491 PAPTPGSTRSTRppatMVPPTSGTSTP--RTAPA-----VPTPGSAPTGSKKPigseaSKKAGPKSSPRKPVPLRPGKAA 563
Cdd:TIGR00927 335 PAETKASTAAWK----IRNPLSRTSAPavRIASAtfrglEKNPSTAPSTPATP-----RVRAVLTTQVHHCVVVKPAPAV 405
|
330 340
....*....|....*....|....*
gi 767958591 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 |
1.97e-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: 1.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 767958591 835 GPKGMKGLMGSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGP 890
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| PRK14954 |
PRK14954 |
DNA polymerase III subunits gamma and tau; Provisional |
481-546 |
2.07e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184918 [Multi-domain] Cd Length: 620 Bit Score: 42.62 E-value: 2.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767958591 481 PPPFTALSSSPAPTpGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAG 546
Cdd:PRK14954 396 EPDLPQPDRHPGPA-KPEAPGARPAELPSPASAPTPEQQPPVARSAPLPPSPQASAPRNVASGKPG 460
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
393-589 |
2.14e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.56 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 393 PSSFTKSALPTQKQVPPTSRPVPARVS-RPAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKP 471
Cdd:PRK12323 365 PGQSGGGAGPATAAAAPVAQPAPAAAApAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGP 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 472 ASARTSTHKPPPFTAlSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAP-----------AVPTPGSAPTGSKKPIGSE 540
Cdd:PRK12323 445 GGAPAPAPAPAAAPA-AAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADddpppweelppEFASPAPAQPDAAPAGWVA 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767958591 541 ASKKAGPKSSPRKPVP-LRPGKAARDVPLSDLTTRP--SPRQPQPSQQTTPA 589
Cdd:PRK12323 524 ESIPDPATADPDDAFEtLAPAPAAAPAPRAAAATEPvvAPRPPRASASGLPD 575
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
453-632 |
2.22e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 453 PIPTLARTE-AKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAP---------- 521
Cdd:PHA03247 255 PAPPPVVGEgADRAPETARGATGPPPPPEAAAPNGAAAPPDGVWGAALAGAPLALPAPPDPPPPAPAGDAeeeddedgam 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 522 --AVPTP---GSAPTGSKK-------PIGSEASKKAGPKSSPRKPVPLRPGKAARDV-------PLSDLTTRPSPRQPQP 582
Cdd:PHA03247 335 evVSPLPrprQHYPLGFPKrrrptwtPPSSLEDLSAGRHHPKRASLPTRKRRSARHAatpfargPGGDDQTRPAAPVPAS 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767958591 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 ... |
1146-1199 |
2.83e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.09 E-value: 2.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 767958591 1146 MGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGP 1199
Cdd:pfam01391 3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
476-564 |
3.07e-03 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 42.18 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 476 TSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPV 555
Cdd:PRK12270 39 GSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVT 118
|
....*....
gi 767958591 556 PLRpGKAAR 564
Cdd:PRK12270 119 PLR-GAAAA 126
|
|
| KAR9 |
pfam08580 |
Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal ... |
376-630 |
3.13e-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: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 376 STSIVPIKSPhptQKTAPSSFTKSALPTQKQVPPTSRP----VPARVSRPAEKPIQRNpgmprppppstrplppttssSK 451
Cdd:pfam08580 421 PATLVANKTP---GSSPPSSVIMTPVNKGSKTPSSRRGssfdFGSSSERVINSKLRRE--------------------SK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 452 KPIPTLARTEAKITSHASKPASARTSTHKPPPFTalSSSPAPTPGSTRSTRPPatmvPPTSGTStPRTAPAVPTPGSAPT 531
Cdd:pfam08580 478 LPQIASTLKQTKRPSKIPRASPNHSGFLSTPSNT--ATSETPTPALRPPSRPQ----PPPPGNR-PRWNASTNTNDLDVG 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 532 GSKKPIgseaskkagpKSSPRKPVPLRpgkaardvplsdlTTRPSPRQPQPSQQTTPAlvlapaqflSSSPRPTSSGYSI 611
Cdd:pfam08580 551 HNFKPL----------TLTTPSPTPSR-------------SSRSSSTLPPVSPLSRDK---------SRSPAPTCRSVSR 598
|
250
....*....|....*....
gi 767958591 612 FHLAGSTPFPLLMGPPGPK 630
Cdd:pfam08580 599 ASRRRASRKPTRIGSPNSR 617
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
736-790 |
3.88e-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: 3.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 767958591 736 GYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGKMGMPG 790
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Metaviral_G |
pfam09595 |
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. ... |
361-513 |
4.19e-03 |
|
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: 39.94 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 361 ATKIPKSLPTKPSAPSTSIVP---IKSPHPTQKTAPSSftkSALPTQKQVPPTSRPVPARVSRPAEKPIQRNPGMPRPPP 437
Cdd:pfam09595 31 ASLILIGESNKEAALIITDIIdinINKQHPEQEHHENP---PLNEAAKEAPSESEDAPDIDPNNQHPSQDRSEAPPLEPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 438 PSTRPLPPTTSSSkkpiPTLARTEAKITSHASKPASART----STHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSG 513
Cdd:pfam09595 108 AKTKPSEHEPANP----PDASNRLSPPDASTAAIREARTfrkpSTGKRNNPSSAQSDQSPPRANHEAIGRANPFAMSSTG 183
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
422-608 |
4.39e-03 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 41.45 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 422 AEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTH--KPPpftalsSSPAPTPGSTR 499
Cdd:PLN03209 321 AKIPSQRVPPKESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYTAYEdlKPP------TSPIPTPPSSS 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 500 STRPPatmvpPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPgkaardvplsdlTTRPSPRQ 579
Cdd:PLN03209 395 PASSK-----SVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYARYEDLKP------------PTSPSPTA 457
|
170 180
....*....|....*....|....*....
gi 767958591 580 PQPSQQTTPALVLAPAQflSSSPRPTSSG 608
Cdd:PLN03209 458 PTGVSPSVSSTSSVPAV--PDTAPATAAT 484
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
847-899 |
4.63e-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: 4.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 767958591 847 GEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLGKVGDKGS 899
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
450-630 |
5.05e-03 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 450 SKKPIPTLarTEAKITSHASKPASARTSThKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTS---GTSTPRTAPA---- 522
Cdd:PTZ00449 492 SKKKLAPI--EEEDSDKHDEPPEGPEASG-LPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGEtkeGEVGKKPGPAkehk 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 523 ---VPTPGSAPTGSKKPigseaskkagpkSSPRKPVplRPGKAARDVPLSDLTTRPSPRQPQ----------PSQQTTPA 589
Cdd:PTZ00449 569 pskIPTLSKKPEFPKDP------------KHPKDPE--EPKKPKRPRSAQRPTRPKSPKLPElldipkspkrPESPKSPK 634
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767958591 590 LVLAPAQflSSSPRPTSSGYSIfhlagSTPFPllmgPPGPK 630
Cdd:PTZ00449 635 RPPPPQR--PSSPERPEGPKII-----KSPKP----PKSPK 664
|
|
| rad23 |
TIGR00601 |
UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
469-545 |
6.03e-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: 40.65 E-value: 6.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767958591 469 SKPASARTSTHKPPPftalSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKA 545
Cdd:TIGR00601 75 SKPKTGTGKVAPPAA----TPTSAPTPTPSPPASPASGMSAAPASAVEEKSPSEESATATAPESPSTSVPSSGSDAA 147
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
916-990 |
6.74e-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: 6.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958591 916 GPPGDNGPEGMKGKPGARGLPGPRGQLGPegdegpmgppgapglegqPGRKGFPGRPGLDGVKGEPGDPGRPGPV 990
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGP------------------PGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
360-606 |
6.79e-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: 40.71 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 360 TATKIPKSLPTKPSAP---STSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPT---SRPVPARVSRPAekpiqrnpgmp 433
Cdd:pfam17823 64 TAAPAPVTLTKGTSAAhlnSTEVTAEHTPHGTDLSEPATREGAADGAASRALAAaasSSPSSAAQSLPA----------- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 434 rppppstrpLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHkpppftalSSSPAPTPGSTRSTRPPATMVPPTSG 513
Cdd:pfam17823 133 ---------AIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPH--------AASPAPRTAASSTTAASSTTAASSAP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 514 TSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTT------------------RP 575
Cdd:pfam17823 196 TTAASSAPATLTPARGISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATlaaaagtvasaagtinmgDP 275
|
250 260 270
....*....|....*....|....*....|.
gi 767958591 576 SPRQPQPSQQTtpalvlaPAQFLSSSPRPTS 606
Cdd:pfam17823 276 HARRLSPAKHM-------PSDTMARNPAAPM 299
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
457-571 |
7.71e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 40.56 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 457 LARTEAKITSHASKPASARTSTHKPP--PFTALSSSPAPTPGSTRSTRPP-ATMVPPTSGTSTPRTAPAVPTPGSAPTGS 533
Cdd:PRK14950 353 LAVIEALLVPVPAPQPAKPTAAAPSPvrPTPAPSTRPKAAAAANIPPKEPvRETATPPPVPPRPVAPPVPHTPESAPKLT 432
|
90 100 110
....*....|....*....|....*....|....*...
gi 767958591 534 KKPIGSEASKKAGPkssprkPVPLRPGKAARDVPLSDL 571
Cdd:PRK14950 433 RAAIPVDEKPKYTP------PAPPKEEEKALIADGDVL 464
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
452-560 |
8.75e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.69 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 452 KPIPTLARTEAKITSHASKPASARTSTHKPPPFTAL--SSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSA 529
Cdd:PHA03247 375 PKRASLPTRKRRSARHAATPFARGPGGDDQTRPAAPvpASVPTPAPTPVPASAPPPPATPLPSAEPGSDDGPAPPPERQP 454
|
90 100 110
....*....|....*....|....*....|....
gi 767958591 530 PTGSK---KPIGSEASKKAGPKSSPRKPvPLRPG 560
Cdd:PHA03247 455 PAPATepaPDDPDDATRKALDALRERRP-PEPPG 487
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
275-429 |
9.43e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 40.23 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 275 ATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMavggPAQTPLLPAKLSASNALDPMLP-ASVGGSTRTPRPAAA 353
Cdd:PRK07994 369 EVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASA----PQQAPAVPLPETTSQLLAARQQlQRAQGATKAKKSEPA 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 354 QPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHP----TQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQRN 429
Cdd:PRK07994 445 AASRARPVNSALERLASVRPAPSALEKAPAKKEAyrwkATNPVEVKKEPVATPKALKKALEHEKTPELAAKLAAEAIERD 524
|
|
| TALPID3 |
pfam15324 |
Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for ... |
501-632 |
9.79e-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: 40.64 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958591 501 TRPPATMVP-PTSGTSTPRTAPaVPTPGSAPTGSKKPIGSEASKKAGPKSSPRkpvplrpgkaardvpLSDLTTRPSP-R 578
Cdd:pfam15324 966 EPPVAASVPgDLPTKETLLPTP-VPTPQPTPPCSPPSPLKEPSPVKTPDSSPC---------------VSEHDFFPVKeI 1029
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767958591 579 QPQPSQQTTPA--LVLAPAQFLSSSPR------PTSSGYSIFHLAGSTPfpllmGPPGPKGD 632
Cdd:pfam15324 1030 PPEKGADTGPAvsLVITPTVTPIATPPpaatptPPLSENSIDKLKSPSP-----ELPKPWED 1086
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
760-809 |
9.90e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 35.55 E-value: 9.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 767958591 760 GLPGLFGLPGSDGERGLPGVPGKRGKMGMPGFPGVFGERGPPGLDGNPGE 809
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
|
|
| |
