|
Name |
Accession |
Description |
Interval |
E-value |
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
709-989 |
1.78e-31 |
|
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: 129.25 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 709 GHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGKMGM 788
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 789 PGFPGVFGERGPPGLDGnpgelglpgppgvpgligdlgvlgPIGYPGPKGMKGLMGSVGepglKGDKGEQGVPGVSGDPG 868
Cdd:NF038329 197 RGETGPAGEQGPAGPAG------------------------PDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 869 FQGDKGSQGLPGFPGARGKPGPLGKVGDKGsigfpgppgpegfpgDIGPPGDNGPEGMKGKPGARGLPGPRGQLGPEGde 948
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDG---------------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG-- 311
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767958587 949 gpmgppgapgLEGQPGRKGFPGRPGLDGVKGEPGDPGRPGP 989
Cdd:NF038329 312 ----------LPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
691-889 |
6.89e-29 |
|
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: 121.55 E-value: 6.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 691 GDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGS 770
Cdd:NF038329 141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 771 DGERGLPGVPGkRGKMGMPGFPGVFGERGPPGLDGNPGELGLPGPPGVPGLIGDLGVLGPIGYPGPKGMKGLMGSVGEPG 850
Cdd:NF038329 221 AGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299
|
170 180 190
....*....|....*....|....*....|....*....
gi 767958587 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 ... |
625-837 |
1.04e-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: 96.90 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 625 GPPGPKGDCGLPGPPGLPGLPGIPGARGPRGPPGPYGNPGLPGPPGAKGQKGDPGLSPGKAHDGAKGDMGLPGLSGNPGP 704
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 705 PGRKGHKGYPGPAGHPGEQGQpGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRG 784
Cdd:NF038329 212 AGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767958587 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 |
2.80e-20 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 95.74 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 974 LDGVKGEPGDPGRPGPVGEQGFMGFIGLVGEPGIVGEKGDRGMMGPPGVPGPKGsmghpgmpggmgtpgEPGPQGPpgsr 1053
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------------EAGPQGP---- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 1054 gppgmRGAKGRRGPRGPDGPAGEQGSRGLKGPpgpqgrpgrpgqqgvAGERGHLGsrgfpgipgpsgpPGTKGLPGEPGP 1133
Cdd:NF038329 176 -----AGKDGEAGAKGPAGEKGPQGPRGETGP---------------AGEQGPAG-------------PAGPDGEAGPAG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 1134 QGPQGPIGPPGEMGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRGDPGPDG 1213
Cdd:NF038329 223 EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302
|
250 260 270
....*....|....*....|....*....|....*.
gi 767958587 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 ... |
844-1083 |
1.12e-19 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 93.82 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 844 GSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLGKVGDKGSIgfpgppgpegfpgdiGPPGDNGP 923
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKDGE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 924 EGMKGKPGARGLPGPRGQLGPEGDEGPMGPPGAPGLEGQPGRKGFPGRPGlDGVKGEPGDPGRPGPVGEQgfmgfiGLVG 1003
Cdd:NF038329 182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ------GPDG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 1004 EPGIVGEKGDRGMMGPPGVPGPKGSMGHPGMPGGMgtpgepgpqgppgsrgppgmrGAKGRRGPRGPDGPAGEQGSRGLK 1083
Cdd:NF038329 255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKD---------------------GQNGKDGLPGKDGKDGQNGKDGLP 313
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1048-1267 |
4.82e-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: 91.89 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 1048 GPPGSRGPPGMRGAKGRRGPRGPDGPAGEQGSRGLKGPPGPQGRPGRPGQQGVAGERGHLGSRGFPGIPGPSGPPGTKGL 1127
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 1128 PgepgpqgpqgpigppgemGPKGPPGAVGEPGLPGEAGMKGDLGPlGTPGEQGLIGQRGEPGLEGDSGPMGPDGLKGDRG 1207
Cdd:NF038329 206 Q------------------GPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 1208 DPGPDGEHGEKGQEGLMGEDgppGPPGVTGVRGPEGKSGKQGEKGRTGAKGAKGYQGQLG 1267
Cdd:NF038329 267 EAGPDGPDGKDGERGPVGPA---GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
869-1216 |
5.41e-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: 91.51 E-value: 5.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 869 FQGDKGSQGLPGFPGARGKPGPLGKVGDKGsigfpgppgpegFPGDIGPPGDNGPEGMKGKPGARGLPGPRGQLGPEGde 948
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETG------------PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG-- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 949 gpmgppgapglegQPGRKGFPGRPGLDGVKGEPGDPGRPGPVGEQGFMGFIGLVGEPGIVGEKGDrgmmgppgvpgpkgs 1028
Cdd:NF038329 181 -------------EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD--------------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 1029 mghpgmpggmgtpgepgpqgppgsrgppgmrGAKGRRGPRGPDGPAGEQGSRGlkgppgpqgrpgrpgqqgvagERGHLG 1108
Cdd:NF038329 233 -------------------------------GQQGPDGDPGPTGEDGPQGPDG---------------------PAGKDG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 1109 SRGFPGIPGPSgppgtkglpgepgpqgpqgpigppgemgpkGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEP 1188
Cdd:NF038329 261 PRGDRGEAGPD------------------------------GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD 310
|
330 340
....*....|....*....|....*...
gi 767958587 1189 GLEGDSGPMGPDGLKGDRGDPGPDGEHG 1216
Cdd:NF038329 311 GLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
274-605 |
1.89e-13 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 75.75 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 274 TATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAklsasnaldpmLPASVGGSTRTPRPAAA 353
Cdd:PHA03247 2636 NEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRA-----------ARPTVGSLTSLADPPPP 2704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 354 QPSQKITATKIPKSLPTKP-------SAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPaekPI 426
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPgpaaarqASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP---PR 2781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 427 QRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTeakitshASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPAT 506
Cdd:PHA03247 2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPA-------AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGG 2854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 507 MVPPTSGTS---TPRTAPAVPTPGSAPTGSKKPiGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPR-QPQP 582
Cdd:PHA03247 2855 SVAPGGDVRrrpPSRSPAAKPAAPARPPVRRLA-RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpQPPP 2933
|
330 340
....*....|....*....|...
gi 767958587 583 SQQTTPALVLAPAQFLSSSPRPT 605
Cdd:PHA03247 2934 PPPPRPQPPLAPTTDPAGAGEPS 2956
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
45-220 |
4.68e-13 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 68.92 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 45 DVDILQRLGLSWTKAGSPAPPGVIPFQSGFIFTQRARLQAPTGTVIPAALGTELALVLSLCSHRVNHAFLFAVRSQKRKL 124
Cdd:smart00210 1 GQDLLQVFDLPSLSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDAQNVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 125 QLGLQFLPGKTVVHL------GSRRSVAF-DLDMHDGRWHHLALELRGRTVTLVTACGQR-RVPVLLPFHrdPALDPGGS 196
Cdd:smart00210 81 QFGLEVDGRANTLLLryqgvdGKQHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIdSRPLDRPGQ--PPIDTDGI 158
|
170 180
....*....|....*....|....
gi 767958587 197 FLFGKMNPHAVQFEGALCQFSIYP 220
Cdd:smart00210 159 EVRGAQAADRKPFQGDLQQLKIVC 182
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
245-631 |
7.31e-12 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 70.74 E-value: 7.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 245 PLGPLFSQDSGRPFTFQSDLALLGLENLTTATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLP 324
Cdd:PHA03247 2561 PAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDP 2640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 325 AKLSASNALDPMLPASVGGSTRTPRPAAAQpsQKITATKIPKSLPTKPSAPST--SIVPIKSPHPTQKTAPSSFTksalP 402
Cdd:PHA03247 2641 HPPPTVPPPERPRDDPAPGRVSRPRRARRL--GRAAQASSPPQRPRRRAARPTvgSLTSLADPPPPPPTPEPAPH----A 2714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 403 TQKQVPPTSRPVPARVSRPAE--KPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEA-----KITSHASKPASAR 475
Cdd:PHA03247 2715 LVSATPLPPGPAAARQASPALpaAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAagpprRLTRPAVASLSES 2794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 476 TSTHKPP--PFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRK 553
Cdd:PHA03247 2795 RESLPSPwdPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAK 2874
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 554 P-VPLRPGKAARDVPLSDLTTRPSP-------RQPQPSQQTTPALVLAPAQFLSSSPRPTSSGYSIFHLAgstPFPLLMG 625
Cdd:PHA03247 2875 PaAPARPPVRRLARPAVSRSTESFAlppdqpeRPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLA---PTTDPAG 2951
|
....*.
gi 767958587 626 PPGPKG 631
Cdd:PHA03247 2952 AGEPSG 2957
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
283-780 |
5.38e-11 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 68.04 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 283 PAGRGPRGTVAPATPTKPQRTSPTNPhqhmAVGGPAQTPLLP-----AKLSASNALDP-------MLPASVGGSTRTPRP 350
Cdd:PHA03247 2498 PGGGGPPDPDAPPAPSRLAPAILPDE----PVGEPVHPRMLTwirglEELASDDAGDPppplppaAPPAAPDRSVPPPRP 2573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 351 AAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPtqkqvPPTSRPVPARVSRPAEKPIQRNP 430
Cdd:PHA03247 2574 APRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPD-----PPPPSPSPAANEPDPHPPPTVPP 2648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 431 GMPRPPPP------------STRPLPPTTSSSKKPIPTLAR-TEAKITSHASKPASARTSTHKPPPFTALSSSPaPTPGS 497
Cdd:PHA03247 2649 PERPRDDPapgrvsrprrarRLGRAAQASSPPQRPRRRAARpTVGSLTSLADPPPPPPTPEPAPHALVSATPLP-PGPAA 2727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 498 TRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASkkAGPKSSPRKPVPlRPGKAARDVPLSDLttrPSP 577
Cdd:PHA03247 2728 ARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPP--AAPAAGPPRRLT-RPAVASLSESRESL---PSP 2801
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 578 RQPQPSqqttPALVLAPAQFLSSSPRPTSsgysifhLAGSTPFPLLMGPPGPKGdcGLPGPPGLPGLPGIPGARGPRGPP 657
Cdd:PHA03247 2802 WDPADP----PAAVLAPAAALPPAASPAG-------PLPPPTSAQPTAPPPPPG--PPPPSLPLGGSVAPGGDVRRRPPS 2868
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 658 GPYGNPGLPGPPGAKGQKGDPGLSPgkahdgAKGDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGY 737
Cdd:PHA03247 2869 RSPAAKPAAPARPPVRRLARPAVSR------STESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 767958587 738 PGRQGLPGPVGDPGPKGSRGYIG--LPGLFGLPGSDGERGLPGVP 780
Cdd:PHA03247 2943 LAPTTDPAGAGEPSGAVPQPWLGalVPGRVAVPRFRVPQPAPSRE 2987
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
281-608 |
1.06e-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: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 281 SLPAGR-GPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLlpaKLSASNALDPMLPASVggSTRTPRPAAAQPSqki 359
Cdd:pfam17823 98 SEPATReGAADGAASRALAAAASSSPSSAAQSLPAAIAALPSE---AFSAPRAAACRANASA--APRAAIAAASAPH--- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 360 TATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKS-------------ALPTQKQVPPTSRPVPARVSrpaekpi 426
Cdd:pfam17823 170 AASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPArgistaatatghpAAGTALAAVGNSSPAAGTVT------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 427 qrnpgmprppppstrplPPTTSSSKKPIPTLARTEAKITSHA-----SKPASARTSTHKPPPFTALSSSPAPTPGS-TRS 500
Cdd:pfam17823 243 -----------------AAVGTVTPAALATLAAAAGTVASAAgtinmGDPHARRLSPAKHMPSDTMARNPAAPMGAqAQG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 501 TRPPATMVPP---TSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSP 577
Cdd:pfam17823 306 PIIQVSTDQPvhnTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPSP 385
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 767958587 578 RqpQPSQQTT-PALVLAPAQF--------LSSSPRPTSSG 608
Cdd:pfam17823 386 L--LPTQGAAgPGILLAPEQVateatagtASAGPTPRSSG 423
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
273-576 |
1.07e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 66.89 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 273 TTATPALgSLPAGRGPRGTVAPATPTKPqrTSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASvGGSTRTPRPAA 352
Cdd:PHA03247 2713 HALVSAT-PLPPGPAAARQASPALPAAP--APPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA-GPPRRLTRPAV 2788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 353 AQ-------------PSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPP--------TS 411
Cdd:PHA03247 2789 ASlsesreslpspwdPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPggdvrrrpPS 2868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 412 RPVPARVSRPAEKPIQRnpgmprpppPSTRPLPPTTSSSKKPIPTLARTEakitshaSKPASARTSTHKPPPFTALSSSP 491
Cdd:PHA03247 2869 RSPAAKPAAPARPPVRR---------LARPAVSRSTESFALPPDQPERPP-------QPQAPPPPQPQPQPPPPPQPQPP 2932
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 492 APTPGstrstRPPATMVPPTSGTSTPRTAPAVPTPgsaPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDL 571
Cdd:PHA03247 2933 PPPPP-----RPQPPLAPTTDPAGAGEPSGAVPQP---WLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRV 3004
|
....*
gi 767958587 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 |
1.51e-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: 59.54 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 271 NLTTATPA---LGSLPAGRGPRGTVAPATPTKPQRTSPTNphqhmAVGGP---AQTPLLPAKLSASNALDPML-PASVGG 343
Cdd:pfam05109 472 DVTSPTPAgttSGASPVTPSPSPRDNGTESKAPDMTSPTS-----AVTTPtpnATSPTPAVTTPTPNATSPTLgKTSPTS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 344 STRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPV---PARVSR 420
Cdd:pfam05109 547 AVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPVvtsPPKNAT 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 421 PAEKPIQRNPGMPRPPPPSTRPLP-------PTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKpppftALSSSPAP 493
Cdd:pfam05109 627 SAVTTGQHNITSSSTSSMSLRPSSisetlspSTSDNSTSHMPLLTSAHPTGGENITQVTPASTSTHH-----VSTSSPAP 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 494 TPGSTRSTRPP---ATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASkkAGPKSSPRKPVPLRPGKAARDVplSD 570
Cdd:pfam05109 702 RPGTTSQASGPgnsSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTS--TGGKANSTTGGKHTTGHGARTS--TE 777
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 767958587 571 LTTRPSPRQPQPSQQTTPALVLAPAQFLSSSPRPTSSGYSIFHLAGSTPFP 621
Cdd:pfam05109 778 PTTDYGGDSTTPRTRYNATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVP 828
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
272-607 |
1.58e-07 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 56.33 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 272 LTTATPALGSLPAGRGPRGTVAPATPTkpqrtSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPA 351
Cdd:PHA03307 50 LAAVTVVAGAAACDRFEPPTGPPPGPG-----TEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 352 AAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPiqrnpg 431
Cdd:PHA03307 125 SPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTP------ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 432 MPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHK------------PPPFTALSSSPAPTPGSTR 499
Cdd:PHA03307 199 PAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCgwgpenecplprPAPITLPTRIWEASGWNGP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 500 STRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKK-----PIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSdltTR 574
Cdd:PHA03307 279 SSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRAsssssSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSP---SR 355
|
330 340 350
....*....|....*....|....*....|...
gi 767958587 575 PSPRQPQPSQQTTPALVLAPAQFLSSSPRPTSS 607
Cdd:PHA03307 356 PPPPADPSSPRKRPRPSRAPSSPAASAGRPTRR 388
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
273-589 |
6.65e-07 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 54.00 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 273 TTATPALGSLPAGRGPRGTVAPATPTKPQRT-SPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPA 351
Cdd:pfam03154 191 TTQAATAGPTPSAPSVPPQGSPATSQPPNQTqSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPS 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 352 AAQPSQ------KITATKIPKSLPTKP----SAPSTSIVP----IKSPHPTQKTAPSSFTKSALPTQKqvPPTSRPV-PA 416
Cdd:pfam03154 271 LHGQMPpmphslQTGPSHMQHPVPPQPfpltPQSSQSQVPpgpsPAAPGQSQQRIHTPPSQSQLQSQQ--PPREQPLpPA 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 417 RVSRPAEKPiqrnpgmprppppstrplppttsSSKKPIPTLARTEA-KITSHASKPASARTSTHKPPP--FTALSSSPAP 493
Cdd:pfam03154 349 PLSMPHIKP-----------------------PPTTPIPQLPNPQShKHPPHLSGPSPFQMNSNLPPPpaLKPLSSLSTH 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 494 TPGSTRStrPPATMVPPTSGTSTPRTAPAVPT--PGSAPTGSKKPigSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDL 571
Cdd:pfam03154 406 HPPSAHP--PPLQLMPQSQQLPPPPAQPPVLTqsQSLPPPAASHP--PTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGP 481
|
330 340
....*....|....*....|
gi 767958587 572 TTRPSPRQP--QPSQQTTPA 589
Cdd:pfam03154 482 PTSTSSAMPgiQPPSSASVS 501
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
248-556 |
1.02e-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: 53.62 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 248 PLFSQDSGRPFTFQSDLALLGLENLTTATPALGSLPAGRGPRGTVAPATPTKPQRTS-PTNPH------QHMAVGGPAQT 320
Cdd:pfam03154 218 PNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQmPPMPHslqtgpSHMQHPVPPQP 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 321 PLLPAKLSASNALDPMLPASVGGSTRT-------PRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSP----HPTQ 389
Cdd:pfam03154 298 FPLTPQSSQSQVPPGPSPAAPGQSQQRihtppsqSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPqshkHPPH 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 390 KTAPSSFT-KSALPTQKQVPPTSRPVPARVSRPAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHA 468
Cdd:pfam03154 378 LSGPSPFQmNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVP 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 469 SKPASARTS--THKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTstprtAPAVPTPGSAPTGSKKPIGSEASKKAG 546
Cdd:pfam03154 458 SQSPFPQHPfvPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGP-----VPAAVSCPLPPVQIKEEALDEAEEPES 532
|
330
....*....|
gi 767958587 547 PKSSPRKPVP 556
Cdd:pfam03154 533 PPPPPRSPSP 542
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
277-588 |
1.91e-06 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 52.54 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 277 PALGslpAGRGPRGTVAPATPTkpqrtsptnphqhmAVGGPAQTPLLPAKLSASnaldPMLPASVGGSTRTPRPAAAQPS 356
Cdd:PRK07003 360 PAVT---GGGAPGGGVPARVAG--------------AVPAPGARAAAAVGASAV----PAVTAVTGAAGAALAPKAAAAA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 357 QKiTATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQRNpgmprpp 436
Cdd:PRK07003 419 AA-TRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAF------- 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 437 ppstrplppttsSSKKPIPTLARTEAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTR-----PPATMVPPT 511
Cdd:PRK07003 491 ------------EPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAAraggaAAALDVLRN 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 512 SG----TSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTT 587
Cdd:PRK07003 559 AGmrvsSDRGARAAAAAKPAAAPAAAPKPAAPRVAVQVPTPRARAATGDAPPNGAARAEQAAESRGAPPPWEDIPPDDYV 638
|
.
gi 767958587 588 P 588
Cdd:PRK07003 639 P 639
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
691-747 |
2.12e-06 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 45.95 E-value: 2.12e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767958587 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 |
3.33e-06 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 45.56 E-value: 3.33e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 767958587 697 GLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGP 752
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
264-536 |
3.99e-06 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 51.39 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 264 LALLGLENLTTAtpalGSLPAGRGPrGTVAPATPTKPQRTSPtnphqhmAVGGPAQTPLLPAKLSASNALDPMLPASVGG 343
Cdd:PRK07003 353 LRMLAFEPAVTG----GGAPGGGVP-ARVAGAVPAPGARAAA-------AVGASAVPAVTAVTGAAGAALAPKAAAAAAA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 344 STRTPRPAAAQPSQKITAT--KIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRP 421
Cdd:PRK07003 421 TRAEAPPAAPAPPATADRGddAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPS 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 422 AEKPIQRNPGMPRPPPPST---RPLPPTTSSSKKPIPTLARTEAKITSHAS-----KPASARTSTHKPPPFTALSSSPAP 493
Cdd:PRK07003 501 AATPAAVPDARAPAAASREdapAAAAPPAPEARPPTPAAAAPAARAGGAAAaldvlRNAGMRVSSDRGARAAAAAKPAAA 580
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767958587 494 TPGSTRSTRPPATMVPPTSG----TSTPRTAPAVPTPGSAPTGSKKP 536
Cdd:PRK07003 581 PAAAPKPAAPRVAVQVPTPRaraaTGDAPPNGAARAEQAAESRGAPP 627
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
237-548 |
4.65e-06 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 51.11 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 237 GQADTYQS--PLGPLFSQDSGRPFTFQSDLALLGLENLTTATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMAV 314
Cdd:pfam17823 105 GAADGAASraLAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 315 GGPAQTPLLPAKLSASNALDPMLPASvggSTRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPS 394
Cdd:pfam17823 185 ASSTTAASSAPTTAASSAPATLTPAR---GISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAG 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 395 SFTKSALPTQKQVPPTSRPVPARvSRP----AEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKIT---SH 467
Cdd:pfam17823 262 TVASAAGTINMGDPHARRLSPAK-HMPsdtmARNPAAPMGAQAQGPIIQVSTDQPVHNTAGEPTPSPSNTTLEPNtpkSV 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 468 ASKPASARTSTH---KPPpftalSSSPAPTPGSTRSTRPPATM-------VPPTSGTSTPRTAPAVPTPGSAPTGSKKPI 537
Cdd:pfam17823 341 ASTNLAVVTTTKaqaKEP-----SASPVPVLHTSMIPEVEATSpttqpspLLPTQGAAGPGILLAPEQVATEATAGTASA 415
|
330
....*....|.
gi 767958587 538 GSEASKKAGPK 548
Cdd:pfam17823 416 GPTPRSSGDPK 426
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
275-594 |
5.19e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.48 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 275 ATPALGSLPAGRG-PRGTVAPATPTKPQR-TSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPAA 352
Cdd:PHA03247 2731 ASPALPAAPAPPAvPAGPATPGGPARPARpPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 353 AQPSqkiTATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSAL---------PTQKQVPPT----SRPVPARVS 419
Cdd:PHA03247 2811 VLAP---AAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVapggdvrrrPPSRSPAAKpaapARPPVRRLA 2887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 420 RPA------------------EKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLA-RTEAKITSHASKPASARTSTHK 480
Cdd:PHA03247 2888 RPAvsrstesfalppdqperpPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLApTTDPAGAGEPSGAVPQPWLGAL 2967
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 481 PPPFTALSSSPAPTPGSTRSTrpPATMVPPTSGTSTPRTAP----------AVPTPGSAPTGSKKPIGSEASKKAGPKSS 550
Cdd:PHA03247 2968 VPGRVAVPRFRVPQPAPSREA--PASSTPPLTGHSLSRVSSwasslalheeTDPPPVSLKQTLWPPDDTEDSDADSLFDS 3045
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 767958587 551 PRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTTPALVLAP 594
Cdd:PHA03247 3046 DSERSDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSSQFGP 3089
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
288-582 |
7.43e-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: 50.54 E-value: 7.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 288 PRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRT--------PRPAAAQPSQKI 359
Cdd:pfam03154 245 PHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSsqsqvppgPSPAAPGQSQQR 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 360 TATKIPKSLPTKPSAPSTSIVPiKSPHPTQKTAPSSFTksalPTQKQVPPTSRPVPARVSRPAEKPIQRNPGMPRPPPPS 439
Cdd:pfam03154 325 IHTPPSQSQLQSQQPPREQPLP-PAPLSMPHIKPPPTT----PIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 440 TRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRT 519
Cdd:pfam03154 400 SSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPS 479
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958587 520 APAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQP 582
Cdd:pfam03154 480 GPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSP 542
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
703-757 |
8.96e-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: 8.96e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 767958587 703 GPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRG 757
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
700-756 |
1.68e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 43.64 E-value: 1.68e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767958587 700 GNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSR 756
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
350-586 |
1.92e-05 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 49.15 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 350 PAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSrPVPARVSRPAEKPIQRN 429
Cdd:PLN03209 324 PSQRVPPKESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYTAYEDLKPPTS-PIPTPPSSSPASSKSVD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 430 PGMPRPPPPSTRPLPPTTS-SSKKPIPTLARTEAKITSHA-------------SKPASARTSTHKPPPFTALSSSPAPTP 495
Cdd:PLN03209 403 AVAKPAEPDVVPSPGSASNvPEVEPAQVEAKKTRPLSPYAryedlkpptspspTAPTGVSPSVSSTSSVPAVPDTAPATA 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 496 GSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTT-- 573
Cdd:PLN03209 483 ATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQPKPRPLSPYTMye 562
|
250
....*....|....*
gi 767958587 574 --RPsPRQPQPSQQT 586
Cdd:PLN03209 563 dlKP-PTSPTPSPVL 576
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
342-588 |
2.90e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 48.92 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 342 GGSTRTPRPAAA-QPSQKITATKIPkSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSR 420
Cdd:PTZ00449 555 GEVGKKPGPAKEhKPSKIPTLSKKP-EFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSP 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 421 PAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPI-PTLA-RTEAKITSHASKPASARTSTHKPPPFTALSSSPAP-TPGS 497
Cdd:PTZ00449 634 KRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFdPKFKeKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPeTPGT 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 498 TRSTRPPATMVPPT--SGTSTPRTAPAVPTPgSAPTGSKKPIGSEASKKAGPKSSPrkpvplRPGKAARDVPLSDLTTRP 575
Cdd:PTZ00449 714 PFTTPRPLPPKLPRdeEFPFEPIGDPDAEQP-DDIEFFTPPEEERTFFHETPADTP------LPDILAEEFKEEDIHAET 786
|
250 260
....*....|....*....|.
gi 767958587 576 S--------PRQPQPSQQTTP 588
Cdd:PTZ00449 787 GepdeamkrPDSPSEHEDKPP 807
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
268-614 |
3.09e-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: 48.76 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 268 GLENLTTATPALGSLPAGRGPRGTvAPAT--PTKPQRTSPTNPHQHMAVGGPAQTPLLPAkLSASNALDPMLPASVGGST 345
Cdd:pfam05109 375 GCENISGAFASNRTFDITVSGLGT-APKTliITRTATNATTTTHKVIFSKAPESTTTSPT-LNTTGFAAPNTTTGLPSST 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 346 RTPRPAAAQPSQKITATKIPKSLPTkPSAPSTSIVPIK-SPHPTQKTAPSSFTKSALPTQKQVPPT---SRPVPArVSRP 421
Cdd:pfam05109 453 HVPTNLTAPASTGPTVSTADVTSPT-PAGTTSGASPVTpSPSPRDNGTESKAPDMTSPTSAVTTPTpnaTSPTPA-VTTP 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 422 AEKPIQrnpgmprppppstrplppttssskkpiPTLARTEakitshaskPASARTSthkPPPftalsSSPAPTPGSTRST 501
Cdd:pfam05109 531 TPNATS---------------------------PTLGKTS---------PTSAVTT---PTP-----NATSPTPAVTTPT 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 502 rPPATMvpPTSGTSTPRTAPAVPTP-GSAPT-GSKKPIGSEASKKAGPKSSprKPVPLRPGKAArdvplsdlTTRPSPRQ 579
Cdd:pfam05109 567 -PNATI--PTLGKTSPTSAVTTPTPnATSPTvGETSPQANTTNHTLGGTSS--TPVVTSPPKNA--------TSAVTTGQ 633
|
330 340 350
....*....|....*....|....*....|....*
gi 767958587 580 PQPSQQTTPALVLAPAQfLSSSPRPTSSGYSIFHL 614
Cdd:pfam05109 634 HNITSSSTSSMSLRPSS-ISETLSPSTSDNSTSHM 667
|
|
| PHA03269 |
PHA03269 |
envelope glycoprotein C; Provisional |
448-556 |
3.79e-05 |
|
envelope glycoprotein C; Provisional
Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 48.19 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 448 SSSKKPIPTLARTEAkiTSHASKPASARTS--THKPPPFTALSSS------PAPTPGSTRSTRPPATMVPPTSGTSTPRt 519
Cdd:PHA03269 35 AATQKPDPAPAPHQA--ASRAPDPAVAPTSaaSRKPDLAQAPTPAasekfdPAPAPHQAASRAPDPAVAPQLAAAPKPD- 111
|
90 100 110
....*....|....*....|....*....|....*..
gi 767958587 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 ... |
727-783 |
4.27e-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: 42.48 E-value: 4.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767958587 727 GPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKR 783
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
372-554 |
4.62e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 48.15 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 372 PSAPSTSIVPIKSP---------HPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQrnpgmprppppstrp 442
Cdd:PTZ00449 511 PEGPEASGLPPKAPgdkegeegeHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTL--------------- 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 443 lppttssSKKPiptlarTEAKITSHASKPASARTSTHkppPFTALSSSPAPTPgstrsTRPPATMVPPTSGTSTPRTAPA 522
Cdd:PTZ00449 576 -------SKKP------EFPKDPKHPKDPEEPKKPKR---PRSAQRPTRPKSP-----KLPELLDIPKSPKRPESPKSPK 634
|
170 180 190
....*....|....*....|....*....|..
gi 767958587 523 VPTPGSAPTGSKKPIGSEASKKAGPKSSPRKP 554
Cdd:PTZ00449 635 RPPPPQRPSSPERPEGPKIIKSPKPPKSPKPP 666
|
|
| PHA03269 |
PHA03269 |
envelope glycoprotein C; Provisional |
399-531 |
5.16e-05 |
|
envelope glycoprotein C; Provisional
Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 47.80 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 399 SALPTQKQVPPTSRPVPARVSRPAEKPIQRnpgmprPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTST 478
Cdd:PHA03269 20 ANLNTNIPIPELHTSAATQKPDPAPAPHQA------ASRAPDPAVAPTSAASRKPDLAQAPTPAASEKFDPAPAPHQAAS 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767958587 479 HKPPPFTALSSSPAPTPG-----STRSTRPPATMVPPTSgTSTPRTAPAVPTPGSAPT 531
Cdd:PHA03269 94 RAPDPAVAPQLAAAPKPDaaeafTSAAQAHEAPADAGTS-AASKKPDPAAHTQHSPPP 150
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
283-529 |
6.65e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 47.56 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 283 PAGRGprGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPAAaqpsqkitat 362
Cdd:PRK12323 365 PGQSG--GGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEA---------- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 363 kipksLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQRNPGMPRPPPPSTRP 442
Cdd:PRK12323 433 -----LAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 443 LPPTTSSSKKPIPTLArteAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPP---ATMVPPTSGTSTPRT 519
Cdd:PRK12323 508 SPAPAQPDAAPAGWVA---ESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPrasASGLPDMFDGDWPAL 584
|
250
....*....|
gi 767958587 520 APAVPTPGSA 529
Cdd:PRK12323 585 AARLPVRGLA 594
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
328-549 |
7.08e-05 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 46.47 E-value: 7.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 328 SASNALDPMLPASVGGSTRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIkSPHPTQKTAPSSFTKSALpTQKQV 407
Cdd:PRK10905 33 SGEKSIDLAGNATDQANGVQPAPGTTSAEQTAGNTQQDVSLPPISSTPTQGQTPV-ATDGQQRVEVQGDLNNAL-TQPQN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 408 PPTSRPVPARVSRPAE----KPIQRNPGMPRPPPPStrplppttSSSKKPIPTLARTEAKItsHASKPASARTSTHKPPP 483
Cdd:PRK10905 111 QQQLNNVAVNSTLPTEpatvAPVRNGNASRQTAKTQ--------TAERPATTRPARKQAVI--EPKKPQATAKTEPKPVA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767958587 484 FTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKS 549
Cdd:PRK10905 181 QTPKRTEPAAPVASTKAPAATSTPAPKETATTAPVQTASPAQTTATPAAGGKTAGNVGSLKSAPSS 246
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
459-618 |
7.42e-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: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 459 RTEAKITSHA---SKPASaRTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTApAVPTPGSAptGSKK 535
Cdd:pfam17823 85 EVTAEHTPHGtdlSEPAT-REGAADGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAA-ACRANASA--APRA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 536 PIGSEASKKAG---PKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQT------TPALVLAPAQFLSSSPRPTS 606
Cdd:pfam17823 161 AIAAASAPHAAspaPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGISTaatatgHPAAGTALAAVGNSSPAAGT 240
|
170
....*....|..
gi 767958587 607 SGYSIFHLAGST 618
Cdd:pfam17823 241 VTAAVGTVTPAA 252
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
317-595 |
8.51e-05 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 47.37 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 317 PAQTPLLPAKLSASNALDPM----LPASVGGSTRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTA 392
Cdd:PHA03378 553 PASTEPVHDQLLPAPGLGPLqiqpLTSPTTSQLASSAPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIP 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 393 PSSFTKSALPTQkqvpPTSRPVPARVSRPAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPA 472
Cdd:PHA03378 633 MRPLRMQPITFN----VLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPA 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 473 SARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTpRTAPAVPTPGSAPTgskkpigseaskkagPKSSPR 552
Cdd:PHA03378 709 APPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPG-RARPPAAAPGRARP---------------PAAAPG 772
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 767958587 553 KPVPLRPGKAArDVPLSDLTTRPSPrQPQPSQQTTPALVLAPA 595
Cdd:PHA03378 773 APTPQPPPQAP-PAPQQRPRGAPTP-QPPPQAGPTSMQLMPRA 813
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
453-629 |
1.08e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 46.79 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 453 PIPTLARTEAKITSHASKPASA---RTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSA 529
Cdd:PRK12323 374 PATAAAAPVAQPAPAAAAPAAAapaPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 530 PTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAArdvplsdlttrpsprQPQPSQQTTPALVLAPAQFLSSSPRPTSSGY 609
Cdd:PRK12323 454 PAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAA---------------APAPADDDPPPWEELPPEFASPAPAQPDAAP 518
|
170 180
....*....|....*....|
gi 767958587 610 SIFHLAgSTPFPLLMGPPGP 629
Cdd:PRK12323 519 AGWVAE-SIPDPATADPDDA 537
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
688-736 |
2.23e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 40.55 E-value: 2.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767958587 688 GAKGDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKG 736
Cdd:pfam01391 7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| DUF4045 |
pfam13254 |
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ... |
280-555 |
2.91e-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: 45.16 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 280 GSLPAGRGprGTVAPATPTKPQRTS-------PTNPHQHMAVGGPAQTPLLPAKLSASNAlDPMLPASvggsTRTPRPAA 352
Cdd:pfam13254 47 GSVAGPSG--SLSPGLSPTKLSREGspestsrPSSSHSEATIVRHSKDDERPSTPDEGFV-KPALPRH----SRSSSALS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 353 AQPSQKITAtkipkSLPTKPSAPSTSIVPiKSPHPTqktaPSSFTKSAL-----PTQKQVPPTSRPvPA----------- 416
Cdd:pfam13254 120 NTGSEEDSP-----SLPTSPPSPSKTMDP-KRWSPT----KSSWLESALnrpesPKPKAQPSQPAQ-PAwmkelnkirqs 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 417 -------RVSRPAEKP---IQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTlARTEAKITSHASKPASARTSTHKPPPFTA 486
Cdd:pfam13254 189 rasvdlgRPNSFKEVTpvgLMRSPAPGGHSKSPSVSGISADSSPTKEEPS-EEADTLSTDKEQSPAPTSASEPPPKTKEL 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767958587 487 LSSS---PAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSkKPIGSEASKKAGPKSSPRKPV 555
Cdd:pfam13254 268 PKDSeepAAPSKSAEASTEKKEPDTESSPETSSEKSAPSLLSPVSKASID-KPLSSPDRDPLSPKPKPQSPP 338
|
|
| rad23 |
TIGR00601 |
UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
460-531 |
3.11e-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: 44.89 E-value: 3.11e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958587 460 TEAKITSHASKPASARTSTHKPPPFTALSSSPAPTpgstrSTRPPATMVPPTSGTSTPRT-APAVPTPGSAPT 531
Cdd:TIGR00601 80 GTGKVAPPAATPTSAPTPTPSPPASPASGMSAAPA-----SAVEEKSPSEESATATAPESpSTSVPSSGSDAA 147
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
338-533 |
3.61e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.87 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 338 PASVGGSTRTPRPAAAQPSQKITATKIPKSL---PTKPSAPSTSIVPIKSPHPTQKTAPS--SFTKSALPTQKQV----- 407
Cdd:PRK12323 365 PGQSGGGAGPATAAAAPVAQPAPAAAAPAAAapaPAAPPAAPAAAPAAAAAARAVAAAPArrSPAPEALAAARQAsargp 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 408 ------PPTSRPVPARVSRPAEKPIQRNPGMpRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKP 481
Cdd:PRK12323 445 ggapapAPAPAAAPAAAARPAAAGPRPVAAA-AAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVA 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767958587 482 PPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGS 533
Cdd:PRK12323 524 ESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPD 575
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
468-588 |
3.86e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 44.71 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 468 ASKPASARTSTHKPPPFTALSSSPAPTP--GSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKA 545
Cdd:PRK14951 370 AEAAAPAEKKTPARPEAAAPAAAPVAQAaaAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAP 449
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 767958587 546 GPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTTP 588
Cdd:PRK14951 450 APPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTE 492
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
468-582 |
6.50e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 44.09 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 468 ASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVP--TPGSAPTGSKKPIGSEASKKA 545
Cdd:PRK07994 358 AFHPAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPlpETTSQLLAARQQLQRAQGATK 437
|
90 100 110
....*....|....*....|....*....|....*..
gi 767958587 546 GPKSSPRKPVPLRPGKAARDvPLSDLTTRPSPRQPQP 582
Cdd:PRK07994 438 AKKSEPAAASRARPVNSALE-RLASVRPAPSALEKAP 473
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
136-204 |
6.64e-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: 6.64e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958587 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 ... |
835-890 |
6.97e-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: 6.97e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 767958587 835 GPKGMKGLMGSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGP 890
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1146-1199 |
1.02e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 38.63 E-value: 1.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 767958587 1146 MGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGP 1199
Cdd:pfam01391 3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| motB |
PRK12799 |
flagellar motor protein MotB; Reviewed |
463-606 |
1.19e-03 |
|
flagellar motor protein MotB; Reviewed
Pssm-ID: 183756 [Multi-domain] Cd Length: 421 Bit Score: 43.17 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 463 KITSHASKPASArtsthkPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGsapTGSKKPIGSEAS 542
Cdd:PRK12799 292 QIDTHGTVPVAA------VTPSSAVTQSSAITPSSAAIPSPAVIPSSVTTQSATTTQASAVALSS---AGVLPSDVTLPG 362
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958587 543 KKAGPKSSPRKPVPlRPGKAARDVPLSDLTTRPSPRQPqpsqqtTPALVLAPAQflSSSPRPTS 606
Cdd:PRK12799 363 TVALPAAEPVNMQP-QPMSTTETQQSSTGNITSTANGP------TTSLPAAPAS--NIPVSPTS 417
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
736-790 |
1.42e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 38.24 E-value: 1.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 767958587 736 GYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGKMGMPG 790
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
453-632 |
1.46e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.39 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 453 PIPTLARTE-AKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAP---------- 521
Cdd:PHA03247 255 PAPPPVVGEgADRAPETARGATGPPPPPEAAAPNGAAAPPDGVWGAALAGAPLALPAPPDPPPPAPAGDAeeeddedgam 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 522 --AVPTP---GSAPTGSKK-------PIGSEASKKAGPKSSPRKPVPLRPGKAARDV-------PLSDLTTRPSPRQPQP 582
Cdd:PHA03247 335 evVSPLPrprQHYPLGFPKrrrptwtPPSSLEDLSAGRHHPKRASLPTRKRRSARHAatpfargPGGDDQTRPAAPVPAS 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767958587 583 SQQTTPALVLAPAQFLSSSPRPTSSGYSifhlAGSTPFPLLMGPPGPKGD 632
Cdd:PHA03247 415 VPTPAPTPVPASAPPPPATPLPSAEPGS----DDGPAPPPERQPPAPATE 460
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
284-588 |
1.49e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 43.06 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 284 AGRG--PRGTVAPATPTKPQRT------SPTNPHQHMAVGGPAQTPLLPAklSASNALDPMLPAS----VGGSTRTPRPA 351
Cdd:TIGR00927 97 VGRDeaTPSIAMENTPSPPRRTakitptTPKNNYSPTAAGTERVKEDTPA--TPSRALNHYISTSgrqrVKSYTPKPRGE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 352 AAQPSQKITATKIPKSLPT------KPSAPSTSIVPIKS----PHPTQKTAPSSFTKSALPTQ--KQVPPTSRPVPAR-- 417
Cdd:TIGR00927 175 VKSSSPTQTREKVRKYTPSplgrmvNSYAPSTFMTMPRShgitPRTTVKDSEITATYKMLETNpsKRTAGKTTPTPLKgm 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 418 -------VSRPAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKPPPFTALSSS 490
Cdd:TIGR00927 255 tdntptfLTREVETDLLTSPRSVVEKNTLTTPRRVESNSSTNHWGLVGKNNLTTPQGTVLEHTPATSEGQVTISIMTGSS 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 491 PAPTPGSTRSTRppatMVPPTSGTSTP--RTAPA-----VPTPGSAPTGSKKPigseaSKKAGPKSSPRKPVPLRPGKAA 563
Cdd:TIGR00927 335 PAETKASTAAWK----IRNPLSRTSAPavRIASAtfrglEKNPSTAPSTPATP-----RVRAVLTTQVHHCVVVKPAPAV 405
|
330 340
....*....|....*....|....*
gi 767958587 564 RDVPLSDLTTRPSPRQPQPSQQTTP 588
Cdd:TIGR00927 406 PTTPSPSLTTALFPEAPSPSPSALP 430
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
456-597 |
1.59e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 42.84 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 456 TLARTEAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATmvpPTSGTSTPRTAPAVPTPGSAPTGSKK 535
Cdd:PRK14971 363 TQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSA---PQSATQPAGTPPTVSVDPPAAVPVNP 439
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767958587 536 PIGSEASKKAGPKSSPRKPVPLRPGKAARdvplsdLTTRPSPRQPQPSQQTTPALVLAPAQF 597
Cdd:PRK14971 440 PSTAPQAVRPAQFKEEKKIPVSKVSSLGP------STLRPIQEKAEQATGNIKEAPTGTQKE 495
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
847-899 |
1.74e-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: 37.86 E-value: 1.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 767958587 847 GEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLGKVGDKGS 899
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
916-990 |
1.78e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.86 E-value: 1.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958587 916 GPPGDNGPEGMKGKPGARGLPGPRGQLGPegdegpmgppgapglegqPGRKGFPGRPGLDGVKGEPGDPGRPGPV 990
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGP------------------PGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
393-589 |
1.94e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.56 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 393 PSSFTKSALPTQKQVPPTSRPVPARVS-RPAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKP 471
Cdd:PRK12323 365 PGQSGGGAGPATAAAAPVAQPAPAAAApAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGP 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 472 ASARTSTHKPPPFTAlSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAP-----------AVPTPGSAPTGSKKPIGSE 540
Cdd:PRK12323 445 GGAPAPAPAPAAAPA-AAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADddpppweelppEFASPAPAQPDAAPAGWVA 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767958587 541 ASKKAGPKSSPRKPVP-LRPGKAARDVPLSDLTTRP--SPRQPQPSQQTTPA 589
Cdd:PRK12323 524 ESIPDPATADPDDAFEtLAPAPAAAPAPRAAAATEPvvAPRPPRASASGLPD 575
|
|
| PRK14954 |
PRK14954 |
DNA polymerase III subunits gamma and tau; Provisional |
481-546 |
2.03e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184918 [Multi-domain] Cd Length: 620 Bit Score: 42.62 E-value: 2.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767958587 481 PPPFTALSSSPAPTpGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAG 546
Cdd:PRK14954 396 EPDLPQPDRHPGPA-KPEAPGARPAELPSPASAPTPEQQPPVARSAPLPPSPQASAPRNVASGKPG 460
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
476-564 |
2.84e-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: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 476 TSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPV 555
Cdd:PRK12270 39 GSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVT 118
|
....*....
gi 767958587 556 PLRpGKAAR 564
Cdd:PRK12270 119 PLR-GAAAA 126
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
450-630 |
3.19e-03 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 450 SKKPIPTLarTEAKITSHASKPASARTSThKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTS---GTSTPRTAPA---- 522
Cdd:PTZ00449 492 SKKKLAPI--EEEDSDKHDEPPEGPEASG-LPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGEtkeGEVGKKPGPAkehk 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 523 ---VPTPGSAPTGSKKPigseaskkagpkSSPRKPVplRPGKAARDVPLSDLTTRPSPRQPQ----------PSQQTTPA 589
Cdd:PTZ00449 569 pskIPTLSKKPEFPKDP------------KHPKDPE--EPKKPKRPRSAQRPTRPKSPKLPElldipkspkrPESPKSPK 634
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767958587 590 LVLAPAQflSSSPRPTSSGYSIfhlagSTPFPllmgPPGPK 630
Cdd:PTZ00449 635 RPPPPQR--PSSPERPEGPKII-----KSPKP----PKSPK 664
|
|
| KAR9 |
pfam08580 |
Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal ... |
376-630 |
3.26e-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: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 376 STSIVPIKSPhptQKTAPSSFTKSALPTQKQVPPTSRP----VPARVSRPAEKPIQRNpgmprppppstrplppttssSK 451
Cdd:pfam08580 421 PATLVANKTP---GSSPPSSVIMTPVNKGSKTPSSRRGssfdFGSSSERVINSKLRRE--------------------SK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 452 KPIPTLARTEAKITSHASKPASARTSTHKPPPFTalSSSPAPTPGSTRSTRPPatmvPPTSGTStPRTAPAVPTPGSAPT 531
Cdd:pfam08580 478 LPQIASTLKQTKRPSKIPRASPNHSGFLSTPSNT--ATSETPTPALRPPSRPQ----PPPPGNR-PRWNASTNTNDLDVG 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 532 GSKKPIgseaskkagpKSSPRKPVPLRpgkaardvplsdlTTRPSPRQPQPSQQTTPAlvlapaqflSSSPRPTSSGYSI 611
Cdd:pfam08580 551 HNFKPL----------TLTTPSPTPSR-------------SSRSSSTLPPVSPLSRDK---------SRSPAPTCRSVSR 598
|
250
....*....|....*....
gi 767958587 612 FHLAGSTPFPLLMGPPGPK 630
Cdd:pfam08580 599 ASRRRASRKPTRIGSPNSR 617
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
760-809 |
3.64e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.09 E-value: 3.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 767958587 760 GLPGLFGLPGSDGERGLPGVPGKRGKMGMPGFPGVFGERGPPGLDGNPGE 809
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
422-608 |
3.69e-03 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 41.84 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 422 AEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTH--KPPpftalsSSPAPTPGSTR 499
Cdd:PLN03209 321 AKIPSQRVPPKESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYTAYEdlKPP------TSPIPTPPSSS 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 500 STRPPatmvpPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPgkaardvplsdlTTRPSPRQ 579
Cdd:PLN03209 395 PASSK-----SVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYARYEDLKP------------PTSPSPTA 457
|
170 180
....*....|....*....|....*....
gi 767958587 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 ... |
841-892 |
3.75e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.09 E-value: 3.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767958587 841 GLMGSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLG 892
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
|
|
| Metaviral_G |
pfam09595 |
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. ... |
361-513 |
4.12e-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: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 361 ATKIPKSLPTKPSAPSTSIVP---IKSPHPTQKTAPSSftkSALPTQKQVPPTSRPVPARVSRPAEKPIQRNPGMPRPPP 437
Cdd:pfam09595 31 ASLILIGESNKEAALIITDIIdinINKQHPEQEHHENP---PLNEAAKEAPSESEDAPDIDPNNQHPSQDRSEAPPLEPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 438 PSTRPLPPTTSSSkkpiPTLARTEAKITSHASKPASART----STHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSG 513
Cdd:pfam09595 108 AKTKPSEHEPANP----PDASNRLSPPDASTAAIREARTfrkpSTGKRNNPSSAQSDQSPPRANHEAIGRANPFAMSSTG 183
|
|
| rad23 |
TIGR00601 |
UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
469-545 |
5.10e-03 |
|
UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273167 [Multi-domain] Cd Length: 378 Bit Score: 41.03 E-value: 5.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767958587 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 ... |
961-1010 |
5.62e-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: 5.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 767958587 961 GQPGRKGFPGRPGLDGVKGEPGDPGRPGPVGEQGFMGFIGLVGEPGIVGE 1010
Cdd:pfam01391 7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
838-894 |
6.27e-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: 6.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767958587 838 GMKGLMGSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLGKV 894
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
452-560 |
6.56e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 452 KPIPTLARTEAKITSHASKPASARTSTHKPPPFTAL--SSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSA 529
Cdd:PHA03247 375 PKRASLPTRKRRSARHAATPFARGPGGDDQTRPAAPvpASVPTPAPTPVPASAPPPPATPLPSAEPGSDDGPAPPPERQP 454
|
90 100 110
....*....|....*....|....*....|....
gi 767958587 530 PTGSK---KPIGSEASKKAGPKSSPRKPvPLRPG 560
Cdd:PHA03247 455 PAPATepaPDDPDDATRKALDALRERRP-PEPPG 487
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
360-606 |
6.71e-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: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 360 TATKIPKSLPTKPSAP---STSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPT---SRPVPARVSRPAekpiqrnpgmp 433
Cdd:pfam17823 64 TAAPAPVTLTKGTSAAhlnSTEVTAEHTPHGTDLSEPATREGAADGAASRALAAaasSSPSSAAQSLPA----------- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 434 rppppstrpLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHkpppftalSSSPAPTPGSTRSTRPPATMVPPTSG 513
Cdd:pfam17823 133 ---------AIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPH--------AASPAPRTAASSTTAASSTTAASSAP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 514 TSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTT------------------RP 575
Cdd:pfam17823 196 TTAASSAPATLTPARGISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATlaaaagtvasaagtinmgDP 275
|
250 260 270
....*....|....*....|....*....|.
gi 767958587 576 SPRQPQPSQQTtpalvlaPAQFLSSSPRPTS 606
Cdd:pfam17823 276 HARRLSPAKHM-------PSDTMARNPAAPM 299
|
|
| TALPID3 |
pfam15324 |
Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for ... |
501-632 |
6.91e-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: 41.03 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 501 TRPPATMVP-PTSGTSTPRTAPaVPTPGSAPTGSKKPIGSEASKKAGPKSSPRkpvplrpgkaardvpLSDLTTRPSP-R 578
Cdd:pfam15324 966 EPPVAASVPgDLPTKETLLPTP-VPTPQPTPPCSPPSPLKEPSPVKTPDSSPC---------------VSEHDFFPVKeI 1029
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767958587 579 QPQPSQQTTPA--LVLAPAQFLSSSPR------PTSSGYSIFHLAGSTPfpllmGPPGPKGD 632
Cdd:pfam15324 1030 PPEKGADTGPAvsLVITPTVTPIATPPpaatptPPLSENSIDKLKSPSP-----ELPKPWED 1086
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
334-590 |
7.18e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 40.84 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 334 DPML-------PASVGGSTRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPH---PTQKTAPSSFTKSALPT 403
Cdd:PRK10263 308 DPLLngapitePVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQtgePVIAPAPEGYPQQSQYA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 404 QKQVP---PTSRPVP-------------ARVSRPAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSH 467
Cdd:PRK10263 388 QPAVQynePLQQPVQpqqpyyapaaeqpAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQT 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 468 ASKPASARTSTHKPPPFTALSS-SPAPTPGSTRSTRPP------------------ATMVPPtsgTSTPRTAPAVPTPGS 528
Cdd:PRK10263 468 YQQPAAQEPLYQQPQPVEQQPVvEPEPVVEETKPARPPlyyfeeveekrarereqlAAWYQP---IPEPVKEPEPIKSSL 544
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958587 529 APTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARD-VPLSDLTTRPSPRqPQPSQQTTPAL 590
Cdd:PRK10263 545 KAPSVAAVPPVEAAAAVSPLASGVKKATLATGAAATVaAPVFSLANSGGPR-PQVKEGIGPQL 606
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
500-610 |
7.24e-03 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 40.31 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 500 STRP--PATmVPPTSGTSTPRTAPAVPTPGSAPTG----------SKKPigsEASKKAGPKSSPRKPVPLRPGKAARDVP 567
Cdd:PRK10905 121 STLPtePAT-VAPVRNGNASRQTAKTQTAERPATTrparkqaviePKKP---QATAKTEPKPVAQTPKRTEPAAPVASTK 196
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 767958587 568 LSDLTTRPsprQPQPSQQTTPALVLAPAQflsSSPRPTSSGYS 610
Cdd:PRK10905 197 APAATSTP---APKETATTAPVQTASPAQ---TTATPAAGGKT 233
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
283-629 |
7.38e-03 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 40.81 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 283 PAGRGPRGTVAPATPTKPQRTSPTNPHqhmavgGPAQTPLLP----AKLSASNALDPMLPASVGGSTRTPRPAAAQPSQK 358
Cdd:PHA03379 411 PTYGTPRPPVEKPRPEVPQSLETATSH------GSAQVPEPPpvhdLEPGPLHDQHSMAPCPVAQLPPGPLQDLEPGDQL 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 359 ITATKIPKSLPTKPSAPSTSIVPIKSPHPTQktAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQRNPGMPRPPPP 438
Cdd:PHA03379 485 PGVVQDGRPACAPVPAPAGPIVRPWEASLSQ--VPGVAFAPVMPQPMPVEPVPVPTVALERPVCPAPPLIAMQGPGETSG 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 439 STRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKP----PPFTALSSSPAPTpgsTRSTRPPATMVPPTSGT 514
Cdd:PHA03379 563 IVRVRERWRPAPWTPNPPRSPSQMSVRDRLARLRAEAQPYQASvevqPPQLTQVSPQQPM---EYPLEPEQQMFPGSPFS 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 515 STPRTAPAVPTPGSAPTGSKKPIGSEASKKA--GPKSSPRKPVPLRPGKAAR--DVPLSD-LTTRPSPRQPQPSQQTTPA 589
Cdd:PHA03379 640 QVADVMRAGGVPAMQPQYFDLPLQQPISQGAplAPLRASMGPVPPVPATQPQyfDIPLTEpINQGASAAHFLPQQPMEGP 719
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 767958587 590 LV----LAPAQFLSSSPRPTSSGYSIFHLAGSTPF----PLLMGPPGP 629
Cdd:PHA03379 720 LVperwMFQGATLSQSVRPGVAQSQYFDLPLTQPInhgaPAAHFLHQP 767
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
457-571 |
7.76e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 40.56 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 457 LARTEAKITSHASKPASARTSTHKPP--PFTALSSSPAPTPGSTRSTRPP-ATMVPPTSGTSTPRTAPAVPTPGSAPTGS 533
Cdd:PRK14950 353 LAVIEALLVPVPAPQPAKPTAAAPSPvrPTPAPSTRPKAAAAANIPPKEPvRETATPPPVPPRPVAPPVPHTPESAPKLT 432
|
90 100 110
....*....|....*....|....*....|....*...
gi 767958587 534 KKPIGSEASKKAGPkssprkPVPLRPGKAARDVPLSDL 571
Cdd:PRK14950 433 RAAIPVDEKPKYTP------PAPPKEEEKALIADGDVL 464
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
372-633 |
8.54e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 40.92 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 372 PSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQRNPGMPRPPPPSTRPLPPTTSSSK 451
Cdd:PHA03307 63 DRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 452 KPIPTLARTEAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGStrstrPPATMVPPTSGTSTPRTAPAVPTPGSAPT 531
Cdd:PHA03307 143 SPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSS-----PPAEPPPSTPPAAASPRPPRRSSPISASA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958587 532 GSKKPigseaskkAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTTPALVLAPAQFLSSSPRPTSSgysi 611
Cdd:PHA03307 218 SSPAP--------APGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPA---- 285
|
250 260
....*....|....*....|..
gi 767958587 612 fhlAGSTPFPLLMGPPGPKGDC 633
Cdd:PHA03307 286 ---SSSSSPRERSPSPSPSSPG 304
|
|
| |
