|
Name |
Accession |
Description |
Interval |
E-value |
| COLFI |
pfam01410 |
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1251-1486 |
3.22e-163 |
|
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.
Pssm-ID: 460199 Cd Length: 233 Bit Score: 490.32 E-value: 3.22e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 1251 HDAEVDATLKSLNNQIESIRSPEGSRKNPARTCRDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPAN 1330
Cdd:pfam01410 1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 1331 VPKKNWWSsksKEKKHIWFGETINGGFHFSYGDDNLAPNTANVQMTFLRLLSTEGSQNITYHCKNSIAYLDEAAGNLKKA 1410
Cdd:pfam01410 81 IPRKNWWT---KESKHVWFGEFMNGGSQFSYGVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 111118976 1411 LLIQGSNDVEIRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGPEQEFGVDIGPVCF 1486
Cdd:pfam01410 158 LLLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
|
|
| COLFI |
smart00038 |
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1252-1487 |
1.07e-151 |
|
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.
Pssm-ID: 197483 Cd Length: 232 Bit Score: 460.01 E-value: 1.07e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 1252 DAEVDATLKSLNNQIESIRSPEGSRKNPARTCRDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPANV 1331
Cdd:smart00038 1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETGETCVSPSPSSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 1332 PKKNWWSSKSKekkHIWFGETINGGFHFSYGDDNLAPnTANVQMTFLRLLSTEGSQNITYHCKNSIAYLDEAAGNLKKAL 1411
Cdd:smart00038 81 PRKTWYSGKSK---HVWFGETMNGGFKFSYGDSEGPP-VGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 111118976 1412 LIQGSNDVEIRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGPEQEFGVDIGPVCFL 1487
Cdd:smart00038 157 RLRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
801-1011 |
2.04e-34 |
|
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: 138.50 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 801 GEKGEVGPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAG---QKGDAGAPGPQGPSGAPGPQGP 877
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGpqgPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 878 TGVTGPKGARGAQGPPGATGFPGAAGRVGPPGSNGNP--------GPPGPPGPSGKDGPKGARGDSGPPGRAGEPGLQGP 949
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdgdpGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 111118976 950 AGPPGEKGEPGDDGPSGAEGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPG 1011
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
822-1056 |
3.79e-33 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 134.65 E-value: 3.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 822 GERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGA 901
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 902 AGRVGPPGSNGNPGPPGPPGPSGKDGPKGA-----RGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGL 976
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPagpagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 977 AGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASgdrgppgpvgppgltgpaGEPGREGSPGADGPPGRDGAAGVKG 1056
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLP------------------GKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
374-637 |
3.19e-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: 122.71 E-value: 3.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 374 KGEAGPTGARGPEGAQGPRGEPGTPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAgapgfpgprgppgpqgatGPLGPKG 453
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ------------------GPAGKDG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 454 QTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRGARGEPGGVGpigppgergaPGNRGFPGQDGLAGPKGAPGER 533
Cdd:NF038329 181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG----------PAGDGQQGPDGDPGPTGEDGPQ 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 534 GPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPsgapgedgrpgppgpqgaRGQPGVMGFPGPKGANGE 613
Cdd:NF038329 251 GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGK------------------DGLPGKDGKDGQNGKDGL 312
|
250 260
....*....|....*....|....
gi 111118976 614 PGKAGEKGLPGAPGLRGLPGKDGE 637
Cdd:NF038329 313 PGKDGKDGQPGKDGLPGKDGKDGQ 336
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
749-973 |
3.76e-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: 122.71 E-value: 3.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 749 QGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPAGSAGARGAPGERGETG 828
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 829 PPGPAGFAGPPGADGQPGAKGEQGEAG-----QKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAG 903
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 904 RVGPPGSNGNPGPPGPPGPSGKDGPKGARGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGP 973
Cdd:NF038329 282 PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKP 351
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
703-954 |
1.28e-28 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 121.17 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 703 FPGERGSPGAQGLQGPRGLPGTPGTDGPKGASGPAGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKD 782
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 783 GGRGLTGPIGPPgpaganGEKGEVGPPGPAGSAGARGAPGERGEtGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGA 862
Cdd:NF038329 195 GPRGETGPAGEQ------GPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 863 PGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGrvgppgsngnpgppgppgpsgKDGPKGARGDSGPPGRAG 942
Cdd:NF038329 268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG---------------------KDGLPGKDGKDGQPGKDG 326
|
250
....*....|..
gi 111118976 943 EPGLQGPAGPPG 954
Cdd:NF038329 327 LPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
650-877 |
1.28e-25 |
|
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: 111.92 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 650 AGERGEQGAPGPSGFQGLPGPPGPPGEGGKPGDQGVPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDG 729
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 730 PKGASGPAGPPGAQGPPGLQGMPGeRGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGltgpigppgpagANGEKGEVGPP 809
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG------------DRGEAGPDGPD 274
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 111118976 810 GPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGP 877
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
939-1134 |
4.86e-25 |
|
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: 109.99 E-value: 4.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 939 GRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGP 1018
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 1019 PGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGvKGDRGETGAVGAPGAPGPPGSPGPAGPTGKQGDRGEAGAQGPMG 1098
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
170 180 190
....*....|....*....|....*....|....*.
gi 111118976 1099 PSGPAGARGIQGPQGPRGDKGEAGEPGERGLKGHRG 1134
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
440-661 |
8.03e-25 |
|
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: 109.61 E-value: 8.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 440 PGPQGATGPLGPKGQTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRGARGEPGGVGPIGPPGERGAPGNRGFPG 519
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 520 QDGLAGPKGAPGERGPSGLAGPKGangdPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQP 599
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV 283
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 111118976 600 GVMGFPGPKGANGEPGKAGEKGLPGAPglrGLPGKDGETGAAGPPGPAGPAGERGEQGAPGP 661
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKD---GLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
856-1115 |
9.47e-25 |
|
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: 109.22 E-value: 9.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 856 QKGDAGAPGPQGPSGAPGPQGPtgvTGPKGARGAQGPPGATGFPGAAGRVGPPGSNGNPGPPGPPGPSGKDGPKGARGDS 935
Cdd:NF038329 112 QLKGDGEKGEPGPAGPAGPAGE---QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 936 GPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGLAGQrGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGD 1015
Cdd:NF038329 189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 1016 RGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGdrgetgavgapgapgppgspgpagPTGKQGDRGEAGAQG 1095
Cdd:NF038329 268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG------------------------KDGLPGKDGKDGQPG 323
|
250 260
....*....|....*....|
gi 111118976 1096 PMGPSGPAGARGIQGPQGPR 1115
Cdd:NF038329 324 KDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
463-732 |
1.06e-23 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 106.14 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 463 FKGEQGPKGEPGPAGPQGAPGPAGEEGKRGargepggvgpigppgERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPK 542
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETG---------------PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 543 GANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGapgedgrpgppgPQGARGQPGVMGFPGpKGANGEPGKAGEKGL 622
Cdd:NF038329 180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG------------EAGPAGEDGPAGPAG-DGQQGPDGDPGPTGE 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 623 PGAPGLRGLPGKDGETGAAGPPGPAGPAGERGEQGAPGPSGFqglpgppgppgeggkpgdQGVPGEAGAPGLVGPRGERG 702
Cdd:NF038329 247 DGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK------------------DGQNGKDGLPGKDGKDGQNG 308
|
250 260 270
....*....|....*....|....*....|
gi 111118976 703 FPGERGSPGAQGLQGPRGLPGTPGTDGPKG 732
Cdd:NF038329 309 KDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
652-895 |
1.42e-23 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 105.76 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 652 ERGEQGAPGPSGFQGLPGPPGPPGEGGKPGDQGVPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPK 731
Cdd:NF038329 118 EKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 732 GASGPAGPPGAQGPPGLQGMPGERGAAGIAGPKGD--RGDVGEKGPEGAPGKDGGRGLTGPigppgpagaNGEKGEVGPP 809
Cdd:NF038329 198 GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGK---------DGPRGDRGEA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 810 GPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGA 889
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVP 348
|
....*.
gi 111118976 890 QGPPGA 895
Cdd:NF038329 349 QKPDTA 354
|
|
| VWC |
pfam00093 |
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ... |
34-89 |
2.91e-23 |
|
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.
Pssm-ID: 278520 Cd Length: 57 Bit Score: 94.03 E-value: 2.91e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 111118976 34 CVQDGQRYNDKDVWKPEPCRICVCDTGTVLCDDIICEDVkDCLSP--EIPFGECCPIC 89
Cdd:pfam00093 1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIICPPL-DCPNPrlEIPPGECCPVC 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
521-779 |
3.32e-23 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 104.60 E-value: 3.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 521 DGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPG 600
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 601 VMGFPGPKGANGEPGKAGEKGLPGAPGLRGLPGKDGEtgaagppgpagpaGERGEQGAPGPsgfqglpgppgppgeggkp 680
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------------GQQGPDGDPGP------------------- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 681 gdQGVPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKGASGPAGPPGAQGPPGLQGMPGERGAAGI 760
Cdd:NF038329 244 --TGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321
|
250
....*....|....*....
gi 111118976 761 AGPKGDRGDVGEKGPEGAP 779
Cdd:NF038329 322 PGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
256-557 |
5.68e-23 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 103.83 E-value: 5.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 256 EAGKPGKAGERGPPGPQGARgfpgtpglpgvkghrgypGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERgrt 335
Cdd:NF038329 118 EKGEPGPAGPAGPAGEQGPR------------------GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA--- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 336 gpagaagargndgqpgpagppgpvgpaggpgfpgapgakGEAGPTGARGPEGAQGPRGEPGTPGSPGPAGASGNPGTDGI 415
Cdd:NF038329 177 ---------------------------------------GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 416 PGAKGSAGAPGIAGApgfpgprgppgpqgatgplGPKGQTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRGARG 495
Cdd:NF038329 218 AGPAGEDGPAGPAGD-------------------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 111118976 496 EPGGVGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPGLP 557
Cdd:NF038329 279 ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| VWC |
smart00214 |
von Willebrand factor (vWF) type C domain; |
34-89 |
7.47e-23 |
|
von Willebrand factor (vWF) type C domain;
Pssm-ID: 214564 Cd Length: 59 Bit Score: 92.96 E-value: 7.47e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 111118976 34 CVQDGQRYNDKDVWKPEPCRICVCDTG-TVLCDDIICEDVKDCLSPE--IPFGECCPIC 89
Cdd:smart00214 1 CVHNGRVYNDGETWKPDPCQICTCLDGtTVLCDPVECPPPPDCPNPErvKPPGECCPRC 59
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
213-426 |
2.40e-16 |
|
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: 83.42 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 213 GPAGAPGPQGFQGNPGEPGEPGVSGPMGPRGPPGPPGKPGDDGEAGKPGKAGERGPPGPQGARGFPGTPGLPGVKGHRGY 292
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 293 PGLDGAKGEAGAPGVKGESGSPGENGSpGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPG 372
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG 284
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 111118976 373 AKGEAGPTGARGPEGAQGPRGEPGTPGSPGPAGASGNPGTDGIPGAKGSAGAPG 426
Cdd:NF038329 285 PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
807-1012 |
1.81e-09 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 61.97 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 807 GPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGA 886
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 887 RGAQGPPGATGFPGAAGRVGPPGSNGNPGPPGPPGPSGKDGPKGARGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSG 966
Cdd:COG5164 87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 111118976 967 AEGPPGPQGLAGQRGiVGLPGQRGERGFPGLPGPSGEPGKQGAPGA 1012
Cdd:COG5164 167 PPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKK 211
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
804-860 |
1.31e-08 |
|
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: 52.50 E-value: 1.31e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 111118976 804 GEVGPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDA 860
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
686-897 |
1.31e-07 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 56.19 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 686 PGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKGASGPAGPPGAQGPPGLQGMPGERGAAGIAGPKG 765
Cdd:COG5164 6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 766 DRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGP------------------PGPAGSAGARGAPGERGET 827
Cdd:COG5164 86 NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPpsggsttppgdggstppgPGSTGPGGSTTPPGDGGST 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 111118976 828 GPPGPAGFAGPPGADGQ--PGAKGEQGEAGQKGDAGAPGPQGPSGAPG-------PQGPTGVTGPKGARGAQGPPGATG 897
Cdd:COG5164 166 TPPGPGGSTTPPDDGGSttPPNKGETGTDIPTGGTPRQGPDGPVKKDDkngkgnpPDDRGGKTGPKDQRPKTNPIERRG 244
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
852-1059 |
1.40e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 56.53 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 852 GEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGSNGNPGPPGPPGPSGKDGPKGA 931
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 932 RGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPG 1011
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 111118976 1012 ASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRG 1059
Cdd:PRK07764 750 DPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDED 797
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
78-330 |
1.67e-07 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 55.68 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 78 PEIPFGECCPICPTDLATASGQPGPKGQKGEPGDikdiVGPKGPPGPQGPAGEQGPRGDRGDKGEKGAPGPRGRDGEPGT 157
Cdd:NF038329 136 PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE----AGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 158 PGNPGPPGppgppgppglggnfaAQMAGGFDEKAGGAQLGVmqgpmgpmgprgppgpagapgpqgfQGNPGEPGEPGVSG 237
Cdd:NF038329 212 AGPDGEAG---------------PAGEDGPAGPAGDGQQGP-------------------------DGDPGPTGEDGPQG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 238 PMGPRGPPGPPGKPGDDGEAGKPGKAGERGPPGPQGARGFPGTPGLPGVKGHRGYPGLDgakgeaGAPGVKGESGSPGEN 317
Cdd:NF038329 252 PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD------GLPGKDGKDGQPGKD 325
|
250
....*....|...
gi 111118976 318 GSPGPMGPRGLPG 330
Cdd:NF038329 326 GLPGKDGKDGQPG 338
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
261-317 |
4.20e-07 |
|
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: 48.26 E-value: 4.20e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 111118976 261 GKAGERGPPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGEN 317
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
445-695 |
1.90e-06 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 52.34 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 445 ATGPLGPKGQTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRGARGEPGGVgpigppgerGAPGNRGFPGQDGLA 524
Cdd:COG5164 8 KTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGT---------RPAGNQGATGPAQNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 525 GPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPGVMGF 604
Cdd:COG5164 79 GGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 605 PGPKGANGEPGKAGEKGLPGAPGlRGLPGKDGETGAAGPPGPAGPAGERGEQGAPGPSGFQGLPGPPGPPGEGGKPGDQG 684
Cdd:COG5164 159 PGDGGSTTPPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKT 237
|
250
....*....|.
gi 111118976 685 VPGEAGAPGLV 695
Cdd:COG5164 238 NPIERRGPERP 248
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
374-569 |
2.19e-06 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 52.30 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 374 KGEAGPTGARGPEGAQGPR--GEPGTPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAgapgfPGPRGPPGPQGATGPLGP 451
Cdd:PRK07764 592 PGAAGGEGPPAPASSGPPEeaARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVA-----APEHHPKHVAVPDASDGG 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 452 KGQTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRGARGEPGGVGPIGPPGERGAPGNRGFPGQDGLAGPKGAPG 531
Cdd:PRK07764 667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD 746
|
170 180 190
....*....|....*....|....*....|....*...
gi 111118976 532 ErgPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDA 569
Cdd:PRK07764 747 D--PPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
508-560 |
1.84e-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: 1.84e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 111118976 508 ERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGAR 560
Cdd:pfam01391 5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
928-1133 |
6.28e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 47.59 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 928 PKGARGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGLAGQRGIVGlpGQRGERGFPGLPGPSGEPGKQ 1007
Cdd:PRK12678 77 ARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRER--GEAARRGAARKAGEGGEQPAT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 1008 GAPGASGDRGPPGpvgppgltgpagEPGREGSPGADGPPGRDGAAGVKGDRGETGAVGAPGAPGPPGSPGPAGPTGKQGD 1087
Cdd:PRK12678 155 EARADAAERTEEE------------ERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRD 222
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 111118976 1088 RGEAGAQGPMGPSGPAGARGIQGPQGPRGDKGEAGEPGERGLKGHR 1133
Cdd:PRK12678 223 GGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRD 268
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
689-896 |
9.23e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 47.29 E-value: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 689 AGAPGLVGPRGERGfPGERGSPGAQGLQGPRGLPGTPGTDGPKGASGPAGPPGAQGPPGLQGMPGERGAAGIAGPKGDRG 768
Cdd:PRK07764 589 GPAPGAAGGEGPPA-PASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 769 DVGEKGPEGAPGKDGGRGltgpigppgpagangekGEVGPPGPAGSAGARGAPGERGETGPPGPAGFAGPPgadgqPGAK 848
Cdd:PRK07764 668 GWPAKAGGAAPAAPPPAP-----------------APAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQP-----PQAA 725
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 111118976 849 GEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGAT 896
Cdd:PRK07764 726 QGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAA 773
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1086-1195 |
1.11e-04 |
|
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: 46.44 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 1086 GDRGEAGAQGPMGPSGPAGARGIQGPQGPRGDKGEAGEPGERGLKGHRGFTGLQGLPGPPGPSGDQGASGPAGPSGPRGP 1165
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110
....*....|....*....|....*....|
gi 111118976 1166 PGPVGPSGKDGANGIPGPIGPPGPRGRSGE 1195
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
687-732 |
3.65e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.78 E-value: 3.65e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 111118976 687 GEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKG 732
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
|
|
| GGGWT_bact |
NF040941 |
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ... |
1282-1319 |
5.84e-04 |
|
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.
Pssm-ID: 468872 [Multi-domain] Cd Length: 46 Bit Score: 39.08 E-value: 5.84e-04
10 20 30
....*....|....*....|....*....|....*...
gi 111118976 1282 TCRDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMET 1319
Cdd:NF040941 1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTT 38
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1082-1128 |
5.15e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.70 E-value: 5.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 111118976 1082 TGKQGDRGEAGAQGPMGPSGPAGARGIQGPQGPRGDKGEAGEPGERG 1128
Cdd:pfam01391 9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COLFI |
pfam01410 |
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1251-1486 |
3.22e-163 |
|
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.
Pssm-ID: 460199 Cd Length: 233 Bit Score: 490.32 E-value: 3.22e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 1251 HDAEVDATLKSLNNQIESIRSPEGSRKNPARTCRDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPAN 1330
Cdd:pfam01410 1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 1331 VPKKNWWSsksKEKKHIWFGETINGGFHFSYGDDNLAPNTANVQMTFLRLLSTEGSQNITYHCKNSIAYLDEAAGNLKKA 1410
Cdd:pfam01410 81 IPRKNWWT---KESKHVWFGEFMNGGSQFSYGVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 111118976 1411 LLIQGSNDVEIRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGPEQEFGVDIGPVCF 1486
Cdd:pfam01410 158 LLLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
|
|
| COLFI |
smart00038 |
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1252-1487 |
1.07e-151 |
|
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.
Pssm-ID: 197483 Cd Length: 232 Bit Score: 460.01 E-value: 1.07e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 1252 DAEVDATLKSLNNQIESIRSPEGSRKNPARTCRDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPANV 1331
Cdd:smart00038 1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETGETCVSPSPSSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 1332 PKKNWWSSKSKekkHIWFGETINGGFHFSYGDDNLAPnTANVQMTFLRLLSTEGSQNITYHCKNSIAYLDEAAGNLKKAL 1411
Cdd:smart00038 81 PRKTWYSGKSK---HVWFGETMNGGFKFSYGDSEGPP-VGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 111118976 1412 LIQGSNDVEIRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGPEQEFGVDIGPVCFL 1487
Cdd:smart00038 157 RLRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
801-1011 |
2.04e-34 |
|
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: 138.50 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 801 GEKGEVGPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAG---QKGDAGAPGPQGPSGAPGPQGP 877
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGpqgPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 878 TGVTGPKGARGAQGPPGATGFPGAAGRVGPPGSNGNP--------GPPGPPGPSGKDGPKGARGDSGPPGRAGEPGLQGP 949
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdgdpGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 111118976 950 AGPPGEKGEPGDDGPSGAEGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPG 1011
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
822-1056 |
3.79e-33 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 134.65 E-value: 3.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 822 GERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGA 901
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 902 AGRVGPPGSNGNPGPPGPPGPSGKDGPKGA-----RGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGL 976
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPagpagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 977 AGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASgdrgppgpvgppgltgpaGEPGREGSPGADGPPGRDGAAGVKG 1056
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLP------------------GKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
374-637 |
3.19e-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: 122.71 E-value: 3.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 374 KGEAGPTGARGPEGAQGPRGEPGTPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAgapgfpgprgppgpqgatGPLGPKG 453
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ------------------GPAGKDG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 454 QTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRGARGEPGGVGpigppgergaPGNRGFPGQDGLAGPKGAPGER 533
Cdd:NF038329 181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG----------PAGDGQQGPDGDPGPTGEDGPQ 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 534 GPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPsgapgedgrpgppgpqgaRGQPGVMGFPGPKGANGE 613
Cdd:NF038329 251 GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGK------------------DGLPGKDGKDGQNGKDGL 312
|
250 260
....*....|....*....|....
gi 111118976 614 PGKAGEKGLPGAPGLRGLPGKDGE 637
Cdd:NF038329 313 PGKDGKDGQPGKDGLPGKDGKDGQ 336
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
749-973 |
3.76e-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: 122.71 E-value: 3.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 749 QGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPAGSAGARGAPGERGETG 828
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 829 PPGPAGFAGPPGADGQPGAKGEQGEAG-----QKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAG 903
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 904 RVGPPGSNGNPGPPGPPGPSGKDGPKGARGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGP 973
Cdd:NF038329 282 PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKP 351
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
703-954 |
1.28e-28 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 121.17 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 703 FPGERGSPGAQGLQGPRGLPGTPGTDGPKGASGPAGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKD 782
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 783 GGRGLTGPIGPPgpaganGEKGEVGPPGPAGSAGARGAPGERGEtGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGA 862
Cdd:NF038329 195 GPRGETGPAGEQ------GPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 863 PGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGrvgppgsngnpgppgppgpsgKDGPKGARGDSGPPGRAG 942
Cdd:NF038329 268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG---------------------KDGLPGKDGKDGQPGKDG 326
|
250
....*....|..
gi 111118976 943 EPGLQGPAGPPG 954
Cdd:NF038329 327 LPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
650-877 |
1.28e-25 |
|
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: 111.92 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 650 AGERGEQGAPGPSGFQGLPGPPGPPGEGGKPGDQGVPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDG 729
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 730 PKGASGPAGPPGAQGPPGLQGMPGeRGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGltgpigppgpagANGEKGEVGPP 809
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG------------DRGEAGPDGPD 274
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 111118976 810 GPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGP 877
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
939-1134 |
4.86e-25 |
|
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: 109.99 E-value: 4.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 939 GRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGP 1018
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 1019 PGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGvKGDRGETGAVGAPGAPGPPGSPGPAGPTGKQGDRGEAGAQGPMG 1098
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
170 180 190
....*....|....*....|....*....|....*.
gi 111118976 1099 PSGPAGARGIQGPQGPRGDKGEAGEPGERGLKGHRG 1134
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
440-661 |
8.03e-25 |
|
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: 109.61 E-value: 8.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 440 PGPQGATGPLGPKGQTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRGARGEPGGVGPIGPPGERGAPGNRGFPG 519
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 520 QDGLAGPKGAPGERGPSGLAGPKGangdPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQP 599
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV 283
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 111118976 600 GVMGFPGPKGANGEPGKAGEKGLPGAPglrGLPGKDGETGAAGPPGPAGPAGERGEQGAPGP 661
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKD---GLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
856-1115 |
9.47e-25 |
|
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: 109.22 E-value: 9.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 856 QKGDAGAPGPQGPSGAPGPQGPtgvTGPKGARGAQGPPGATGFPGAAGRVGPPGSNGNPGPPGPPGPSGKDGPKGARGDS 935
Cdd:NF038329 112 QLKGDGEKGEPGPAGPAGPAGE---QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 936 GPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGLAGQrGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGD 1015
Cdd:NF038329 189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 1016 RGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGdrgetgavgapgapgppgspgpagPTGKQGDRGEAGAQG 1095
Cdd:NF038329 268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG------------------------KDGLPGKDGKDGQPG 323
|
250 260
....*....|....*....|
gi 111118976 1096 PMGPSGPAGARGIQGPQGPR 1115
Cdd:NF038329 324 KDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
463-732 |
1.06e-23 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 106.14 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 463 FKGEQGPKGEPGPAGPQGAPGPAGEEGKRGargepggvgpigppgERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPK 542
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETG---------------PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 543 GANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGapgedgrpgppgPQGARGQPGVMGFPGpKGANGEPGKAGEKGL 622
Cdd:NF038329 180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG------------EAGPAGEDGPAGPAG-DGQQGPDGDPGPTGE 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 623 PGAPGLRGLPGKDGETGAAGPPGPAGPAGERGEQGAPGPSGFqglpgppgppgeggkpgdQGVPGEAGAPGLVGPRGERG 702
Cdd:NF038329 247 DGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK------------------DGQNGKDGLPGKDGKDGQNG 308
|
250 260 270
....*....|....*....|....*....|
gi 111118976 703 FPGERGSPGAQGLQGPRGLPGTPGTDGPKG 732
Cdd:NF038329 309 KDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
652-895 |
1.42e-23 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 105.76 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 652 ERGEQGAPGPSGFQGLPGPPGPPGEGGKPGDQGVPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPK 731
Cdd:NF038329 118 EKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 732 GASGPAGPPGAQGPPGLQGMPGERGAAGIAGPKGD--RGDVGEKGPEGAPGKDGGRGLTGPigppgpagaNGEKGEVGPP 809
Cdd:NF038329 198 GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGK---------DGPRGDRGEA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 810 GPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGA 889
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVP 348
|
....*.
gi 111118976 890 QGPPGA 895
Cdd:NF038329 349 QKPDTA 354
|
|
| VWC |
pfam00093 |
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ... |
34-89 |
2.91e-23 |
|
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.
Pssm-ID: 278520 Cd Length: 57 Bit Score: 94.03 E-value: 2.91e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 111118976 34 CVQDGQRYNDKDVWKPEPCRICVCDTGTVLCDDIICEDVkDCLSP--EIPFGECCPIC 89
Cdd:pfam00093 1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIICPPL-DCPNPrlEIPPGECCPVC 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
521-779 |
3.32e-23 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 104.60 E-value: 3.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 521 DGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPG 600
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 601 VMGFPGPKGANGEPGKAGEKGLPGAPGLRGLPGKDGEtgaagppgpagpaGERGEQGAPGPsgfqglpgppgppgeggkp 680
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------------GQQGPDGDPGP------------------- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 681 gdQGVPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKGASGPAGPPGAQGPPGLQGMPGERGAAGI 760
Cdd:NF038329 244 --TGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321
|
250
....*....|....*....
gi 111118976 761 AGPKGDRGDVGEKGPEGAP 779
Cdd:NF038329 322 PGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
256-557 |
5.68e-23 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 103.83 E-value: 5.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 256 EAGKPGKAGERGPPGPQGARgfpgtpglpgvkghrgypGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERgrt 335
Cdd:NF038329 118 EKGEPGPAGPAGPAGEQGPR------------------GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA--- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 336 gpagaagargndgqpgpagppgpvgpaggpgfpgapgakGEAGPTGARGPEGAQGPRGEPGTPGSPGPAGASGNPGTDGI 415
Cdd:NF038329 177 ---------------------------------------GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 416 PGAKGSAGAPGIAGApgfpgprgppgpqgatgplGPKGQTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRGARG 495
Cdd:NF038329 218 AGPAGEDGPAGPAGD-------------------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 111118976 496 EPGGVGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPGLP 557
Cdd:NF038329 279 ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| VWC |
smart00214 |
von Willebrand factor (vWF) type C domain; |
34-89 |
7.47e-23 |
|
von Willebrand factor (vWF) type C domain;
Pssm-ID: 214564 Cd Length: 59 Bit Score: 92.96 E-value: 7.47e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 111118976 34 CVQDGQRYNDKDVWKPEPCRICVCDTG-TVLCDDIICEDVKDCLSPE--IPFGECCPIC 89
Cdd:smart00214 1 CVHNGRVYNDGETWKPDPCQICTCLDGtTVLCDPVECPPPPDCPNPErvKPPGECCPRC 59
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
213-426 |
2.40e-16 |
|
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: 83.42 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 213 GPAGAPGPQGFQGNPGEPGEPGVSGPMGPRGPPGPPGKPGDDGEAGKPGKAGERGPPGPQGARGFPGTPGLPGVKGHRGY 292
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 293 PGLDGAKGEAGAPGVKGESGSPGENGSpGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPG 372
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG 284
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 111118976 373 AKGEAGPTGARGPEGAQGPRGEPGTPGSPGPAGASGNPGTDGIPGAKGSAGAPG 426
Cdd:NF038329 285 PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
807-1012 |
1.81e-09 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 61.97 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 807 GPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGA 886
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 887 RGAQGPPGATGFPGAAGRVGPPGSNGNPGPPGPPGPSGKDGPKGARGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSG 966
Cdd:COG5164 87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 111118976 967 AEGPPGPQGLAGQRGiVGLPGQRGERGFPGLPGPSGEPGKQGAPGA 1012
Cdd:COG5164 167 PPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKK 211
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
752-1012 |
9.63e-09 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 59.66 E-value: 9.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 752 PGERGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPAGSAGARGAPGERGETGPPG 831
Cdd:COG5164 6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 832 PAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGpTGVTGPKGARGAQGPPGATGFPGAAgrVGPPGSN 911
Cdd:COG5164 86 NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPS-GGSTTPPGDGGSTPPGPGSTGPGGS--TTPPGDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 912 GNPGPPGPPGPSGKDGPKGArGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGLAG----QRGIVGLPG 987
Cdd:COG5164 163 GSTTPPGPGGSTTPPDDGGS-TTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTgpkdQRPKTNPIE 241
|
250 260
....*....|....*....|....*
gi 111118976 988 QRGERGFPGLPGPSGEPGKQGAPGA 1012
Cdd:COG5164 242 RRGPERPEAAALPAELTALEAENRA 266
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
804-860 |
1.31e-08 |
|
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: 52.50 E-value: 1.31e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 111118976 804 GEVGPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDA 860
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
686-897 |
1.31e-07 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 56.19 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 686 PGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKGASGPAGPPGAQGPPGLQGMPGERGAAGIAGPKG 765
Cdd:COG5164 6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 766 DRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGP------------------PGPAGSAGARGAPGERGET 827
Cdd:COG5164 86 NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPpsggsttppgdggstppgPGSTGPGGSTTPPGDGGST 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 111118976 828 GPPGPAGFAGPPGADGQ--PGAKGEQGEAGQKGDAGAPGPQGPSGAPG-------PQGPTGVTGPKGARGAQGPPGATG 897
Cdd:COG5164 166 TPPGPGGSTTPPDDGGSttPPNKGETGTDIPTGGTPRQGPDGPVKKDDkngkgnpPDDRGGKTGPKDQRPKTNPIERRG 244
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
852-1059 |
1.40e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 56.53 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 852 GEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGSNGNPGPPGPPGPSGKDGPKGA 931
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 932 RGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPG 1011
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 111118976 1012 ASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRG 1059
Cdd:PRK07764 750 DPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDED 797
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
768-976 |
1.56e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 56.15 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 768 GDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGA 847
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 848 KGEQGEAGQKGDAGAP---GPQGPSGAPGPQG-PTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGSNGNPGPPGPPGPS 923
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPapaAPAAPAGAAPAQPaPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 111118976 924 GKDGPKGARGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDgpsgAEGPPGPQGL 976
Cdd:PRK07764 750 DPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAED----DAPSMDDEDR 798
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
78-330 |
1.67e-07 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 55.68 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 78 PEIPFGECCPICPTDLATASGQPGPKGQKGEPGDikdiVGPKGPPGPQGPAGEQGPRGDRGDKGEKGAPGPRGRDGEPGT 157
Cdd:NF038329 136 PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE----AGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 158 PGNPGPPGppgppgppglggnfaAQMAGGFDEKAGGAQLGVmqgpmgpmgprgppgpagapgpqgfQGNPGEPGEPGVSG 237
Cdd:NF038329 212 AGPDGEAG---------------PAGEDGPAGPAGDGQQGP-------------------------DGDPGPTGEDGPQG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 238 PMGPRGPPGPPGKPGDDGEAGKPGKAGERGPPGPQGARGFPGTPGLPGVKGHRGYPGLDgakgeaGAPGVKGESGSPGEN 317
Cdd:NF038329 252 PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD------GLPGKDGKDGQPGKD 325
|
250
....*....|...
gi 111118976 318 GSPGPMGPRGLPG 330
Cdd:NF038329 326 GLPGKDGKDGQPG 338
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
810-865 |
2.84e-07 |
|
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: 48.64 E-value: 2.84e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 111118976 810 GPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGP 865
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
828-883 |
3.77e-07 |
|
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: 48.26 E-value: 3.77e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 111118976 828 GPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGP 883
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
261-317 |
4.20e-07 |
|
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: 48.26 E-value: 4.20e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 111118976 261 GKAGERGPPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGEN 317
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
807-863 |
5.01e-07 |
|
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: 47.87 E-value: 5.01e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 111118976 807 GPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAP 863
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
837-893 |
7.50e-07 |
|
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: 47.49 E-value: 7.50e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 111118976 837 GPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPP 893
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
801-980 |
1.16e-06 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 53.45 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 801 GEKGEVGPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPG--------AKGEQGEAGQKGDAGAPGP-QGPSGA 871
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAApaeasaapAPGVAAPEHHPKHVAVPDAsDGGDGW 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 872 PGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGSNGNPGPPGPPGPsgkdgPKGARGDSGPPGRAGEPGLQGPAG 951
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQ-----PPQAAQGASAPSPAADDPVPLPPE 744
|
170 180
....*....|....*....|....*....
gi 111118976 952 PPGEKGEPGDDGPSGAEGPPGPQGLAGQR 980
Cdd:PRK07764 745 PDDPPDPAGAPAQPPPPPAPAPAAAPAAA 773
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
936-992 |
1.21e-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: 46.72 E-value: 1.21e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 111118976 936 GPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGLAGQRGIVGLPGQRGER 992
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
445-695 |
1.90e-06 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 52.34 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 445 ATGPLGPKGQTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRGARGEPGGVgpigppgerGAPGNRGFPGQDGLA 524
Cdd:COG5164 8 KTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGT---------RPAGNQGATGPAQNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 525 GPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPGVMGF 604
Cdd:COG5164 79 GGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 605 PGPKGANGEPGKAGEKGLPGAPGlRGLPGKDGETGAAGPPGPAGPAGERGEQGAPGPSGFQGLPGPPGPPGEGGKPGDQG 684
Cdd:COG5164 159 PGDGGSTTPPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKT 237
|
250
....*....|.
gi 111118976 685 VPGEAGAPGLV 695
Cdd:COG5164 238 NPIERRGPERP 248
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
816-872 |
2.18e-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: 2.18e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 111118976 816 GARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAP 872
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
374-569 |
2.19e-06 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 52.30 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 374 KGEAGPTGARGPEGAQGPR--GEPGTPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAgapgfPGPRGPPGPQGATGPLGP 451
Cdd:PRK07764 592 PGAAGGEGPPAPASSGPPEeaARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVA-----APEHHPKHVAVPDASDGG 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 452 KGQTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRGARGEPGGVGPIGPPGERGAPGNRGFPGQDGLAGPKGAPG 531
Cdd:PRK07764 667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD 746
|
170 180 190
....*....|....*....|....*....|....*...
gi 111118976 532 ErgPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDA 569
Cdd:PRK07764 747 D--PPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
927-981 |
5.83e-06 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 44.79 E-value: 5.83e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 111118976 927 GPKGARGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGLAGQRG 981
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
846-902 |
8.80e-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: 8.80e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 111118976 846 GAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAA 902
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
614-886 |
1.00e-05 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 50.03 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 614 PGKAGEKGLPGAPGLRGLPGKDGETGAAGPPGPAGPAGERG---EQGAPGPSGFQGLPGPPGPPGEGGKPGDQGVPGEAG 690
Cdd:COG5164 6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRpaqNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 691 APGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKGASGPAGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDV 770
Cdd:COG5164 86 NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGST 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 771 GEKGPEGAPGKDGGRGLTGPigppgpaganGEKGEVGPPGPAGSAgarGAPGERGETGPPGPAGFAGPPgaDGQPGAKGE 850
Cdd:COG5164 166 TPPGPGGSTTPPDDGGSTTP----------PNKGETGTDIPTGGT---PRQGPDGPVKKDDKNGKGNPP--DDRGGKTGP 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 111118976 851 QGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGA 886
Cdd:COG5164 231 KDQRPKTNPIERRGPERPEAAALPAELTALEAENRA 266
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
800-850 |
1.09e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 44.02 E-value: 1.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 111118976 800 NGEKGEVGPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGE 850
Cdd:pfam01391 6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
948-1004 |
1.34e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 44.02 E-value: 1.34e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 111118976 948 GPAGPPGEKGEPGDDGPSGAEGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEP 1004
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
264-320 |
1.78e-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: 1.78e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 111118976 264 GERGPPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSP 320
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
508-560 |
1.84e-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: 1.84e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 111118976 508 ERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGAR 560
Cdd:pfam01391 5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
374-425 |
3.88e-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: 3.88e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 111118976 374 KGEAGPTGARGPEGAQGPRGEPGTPGSPGPAGASGNPGTDGIPGAKGSAGAP 425
Cdd:pfam01391 6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
375-428 |
4.07e-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: 4.07e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 111118976 375 GEAGPTGARGPEGAQGPRGEPGTPGSPGPAGASGNPGTDGIPGAKGSAGAPGIA 428
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
471-661 |
5.60e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 47.67 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 471 GEPGPAGPQGAPGPAGEEGKRGARGEPGGVGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGR 550
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 551 PGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPGVMGFPGPKGANGEPGKAGEKGLPGAPGLRG 630
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749
|
170 180 190
....*....|....*....|....*....|.
gi 111118976 631 LPGKDGETGAAGPPGPAGPAGERGEQGAPGP 661
Cdd:PRK07764 750 DPAGAPAQPPPPPAPAPAAAPAAAPPPSPPS 780
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
928-1133 |
6.28e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 47.59 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 928 PKGARGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGLAGQRGIVGlpGQRGERGFPGLPGPSGEPGKQ 1007
Cdd:PRK12678 77 ARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRER--GEAARRGAARKAGEGGEQPAT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 1008 GAPGASGDRGPPGpvgppgltgpagEPGREGSPGADGPPGRDGAAGVKGDRGETGAVGAPGAPGPPGSPGPAGPTGKQGD 1087
Cdd:PRK12678 155 EARADAAERTEEE------------ERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRD 222
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 111118976 1088 RGEAGAQGPMGPSGPAGARGIQGPQGPRGDKGEAGEPGERGLKGHR 1133
Cdd:PRK12678 223 GGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRD 268
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
855-904 |
7.63e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 41.71 E-value: 7.63e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 111118976 855 GQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGR 904
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
447-493 |
7.94e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 41.71 E-value: 7.94e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 111118976 447 GPLGPKGQTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRGA 493
Cdd:pfam01391 7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
689-896 |
9.23e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 47.29 E-value: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 689 AGAPGLVGPRGERGfPGERGSPGAQGLQGPRGLPGTPGTDGPKGASGPAGPPGAQGPPGLQGMPGERGAAGIAGPKGDRG 768
Cdd:PRK07764 589 GPAPGAAGGEGPPA-PASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 769 DVGEKGPEGAPGKDGGRGltgpigppgpagangekGEVGPPGPAGSAGARGAPGERGETGPPGPAGFAGPPgadgqPGAK 848
Cdd:PRK07764 668 GWPAKAGGAAPAAPPPAP-----------------APAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQP-----PQAA 725
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 111118976 849 GEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGAT 896
Cdd:PRK07764 726 QGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAA 773
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1086-1195 |
1.11e-04 |
|
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: 46.44 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 1086 GDRGEAGAQGPMGPSGPAGARGIQGPQGPRGDKGEAGEPGERGLKGHRGFTGLQGLPGPPGPSGDQGASGPAGPSGPRGP 1165
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110
....*....|....*....|....*....|
gi 111118976 1166 PGPVGPSGKDGANGIPGPIGPPGPRGRSGE 1195
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
807-993 |
1.80e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.05 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 807 GPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPtgvtgpkgA 886
Cdd:PRK12678 61 GGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERR--------E 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 887 RGAQGPPGATGFPGAAGRVGPPGSNGNPGPPGPPGPSGKDGPKGARGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSG 966
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQG 212
|
170 180
....*....|....*....|....*..
gi 111118976 967 AEGPPGPQGLAGQRGivGLPGQRGERG 993
Cdd:PRK12678 213 DRREERGRRDGGDRR--GRRRRRDRRD 237
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
807-1128 |
3.18e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 45.36 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 807 GPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPG--PQGPSGAPGPQGPTGVTGPK 884
Cdd:PRK07764 434 APAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAaaPAAPAAPAAPAGADDAATLR 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 885 GA--------------------RGAQ--GPPGAT---GF--PGAAGRVGPPGSNG------------------NPGPPGP 919
Cdd:PRK07764 514 ERwpeilaavpkrsrktwaillPEATvlGVRGDTlvlGFstGGLARRFASPGNAEvlvtalaeelggdwqveaVVGPAPG 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 920 PGPSGKDGPKGARGDSGPPGRAGEPGlqGPAGPPGEKGEPGDDGPSGAEGPPGPQGLAGQRGIVGLPGQRGERGFPGLPG 999
Cdd:PRK07764 594 AAGGEGPPAPASSGPPEEAARPAAPA--APAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 1000 PSGEPGKQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRGETGAVGAPGAPGPPGSPGPA 1079
Cdd:PRK07764 672 KAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDP 751
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 111118976 1080 GPTGKQGDRGEAGAQGPMGPSGPAGARGIQGPQGPRGDKGEAGEPGERG 1128
Cdd:PRK07764 752 AGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRD 800
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
471-541 |
3.21e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 40.17 E-value: 3.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 111118976 471 GEPGPAGPQGAPGPAGEEGKRGArgepggvgpigppgeRGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGP 541
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGP---------------PGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
513-569 |
3.24e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 40.17 E-value: 3.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 111118976 513 GNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDA 569
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
687-732 |
3.65e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.78 E-value: 3.65e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 111118976 687 GEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKG 732
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
|
|
| GGGWT_bact |
NF040941 |
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ... |
1282-1319 |
5.84e-04 |
|
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.
Pssm-ID: 468872 [Multi-domain] Cd Length: 46 Bit Score: 39.08 E-value: 5.84e-04
10 20 30
....*....|....*....|....*....|....*...
gi 111118976 1282 TCRDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMET 1319
Cdd:NF040941 1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTT 38
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
801-845 |
6.02e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.40 E-value: 6.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 111118976 801 GEKGEVGPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQP 845
Cdd:pfam01391 13 GPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK14959 |
PRK14959 |
DNA polymerase III subunits gamma and tau; Provisional |
814-902 |
7.62e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 43.90 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 814 SAGARGAPGerGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPP 893
Cdd:PRK14959 374 SGGGASAPS--GSAAEGPASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPAPSAAPSPRVPWDDAPPAPPRSGIPPR 451
|
....*....
gi 111118976 894 GATGFPGAA 902
Cdd:PRK14959 452 PAPRMPEAS 460
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
811-1127 |
8.37e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.82 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 811 PAGSAGARG--APGERGETGPPgPAGFAGPPGADGQPGAkgeqgeagqkgdAGAPGPQGPSGAPGPQGPTGVTGPKGARG 888
Cdd:PRK07764 365 PSASDDERGllARLERLERRLG-VAGGAGAPAAAAPSAA------------AAAPAAAPAPAAAAPAAAAAPAPAAAPQP 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 889 AQGPPgatgfPGAAGRVGPPGSNGNPGPPGPPGPSGKDGPKGARGDSGPPGRAGEPGLQGPAGPPGEKGEPgddgpSGAE 968
Cdd:PRK07764 432 APAPA-----PAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAP-----AAPA 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 969 GPPGPQGLAGQRG----IVGLPGQRGER---------------------GF--PGLPGPSGEPG---------------- 1005
Cdd:PRK07764 502 APAGADDAATLRErwpeILAAVPKRSRKtwaillpeatvlgvrgdtlvlGFstGGLARRFASPGnaevlvtalaeelggd 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 1006 -----KQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGD-RGETGAVGAPGAPGPPGSPGPA 1079
Cdd:PRK07764 582 wqveaVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEaSAAPAPGVAAPEHHPKHVAVPD 661
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 111118976 1080 GPTGKQGDRGEAGAQGPMGPSGPAGARGIQGPQGPRGDKGEAGEPGER 1127
Cdd:PRK07764 662 ASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATP 709
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
447-492 |
9.10e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 38.63 E-value: 9.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 111118976 447 GPLGPKGQTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRG 492
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
477-551 |
1.21e-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: 1.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 111118976 477 GPQGAPGPAGEEGKrgargepggvgpigppgeRGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRP 551
Cdd:pfam01391 1 GPPGPPGPPGPPGP------------------PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
749-897 |
1.26e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 43.04 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 749 QGMPGERGAAGIAGPKGDRGDVGEKGPEGApGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPAGSAGARGAPGERGETG 828
Cdd:PHA03169 81 HGEKEERGQGGPSGSGSESVGSPTPSPSGS-AEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSP 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 111118976 829 PPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATG 897
Cdd:PHA03169 160 NQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQ 228
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
257-305 |
2.00e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.86 E-value: 2.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 111118976 257 AGKPGKAGERGPPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAP 305
Cdd:pfam01391 9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
657-1053 |
3.14e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.28 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 657 GAPGPSGFQGLPGPPGPPGEGGKPGDQGVPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGtDGPKGASGP 736
Cdd:PRK07764 400 SAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPA-PAAAPEPTA 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 737 AGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPE--GAPGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPaGS 814
Cdd:PRK07764 479 APAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERWPEilAAVPKRSRKTWAILLPEATVLGVRGDTLVLGFSTG-GL 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 815 AGARGAPGE------------------RGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQG 876
Cdd:PRK07764 558 ARRFASPGNaevlvtalaeelggdwqvEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPA 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 877 PTGVTGPKGARGAQGPPGATGFPGAAGRVgppgsngnpgppgpPGPSGKDGPKGARGDSGPPGRAGEPGLQGPAGPPGEK 956
Cdd:PRK07764 638 EASAAPAPGVAAPEHHPKHVAVPDASDGG--------------DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAP 703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 957 GEPGDDGPSGAEGPPGPQGLAGQRGivGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGPPGPVGPPGLTGPAGEPG- 1035
Cdd:PRK07764 704 APAATPPAGQADDPAAQPPQAAQGA--SAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSe 781
|
410
....*....|....*...
gi 111118976 1036 REGSPGADGPPGRDGAAG 1053
Cdd:PRK07764 782 EEEMAEDDAPSMDDEDRR 799
|
|
| PPE |
COG5651 |
PPE-repeat protein [Function unknown]; |
810-986 |
4.26e-03 |
|
PPE-repeat protein [Function unknown];
Pssm-ID: 444372 [Multi-domain] Cd Length: 385 Bit Score: 41.42 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 810 GPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGAR-- 887
Cdd:COG5651 206 NQVGIGGLNSGSGPIGLNSGPGNTGFAGTGAAAGAAAAAAAAAAAAGAGASAALASLAATLLNASSLGLAATAASSAAtn 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 888 -GAQGPPGATGFPGAAGRVGPPGSNGNPGPPGPPGPSGKDGPKGARGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSG 966
Cdd:COG5651 286 lGLAGSPLGLAGGGAGAAAATGLGLGAGGAAGAAGATGAGAALGAGAAAAAAGAAAGAGAAAAAAAGGAGGGGGGALGAG 365
|
170 180
....*....|....*....|
gi 111118976 967 AEGPPGPQGLAGQRGIVGLP 986
Cdd:COG5651 366 GGGGSAGAAAGAASGGGAAA 385
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
755-975 |
4.68e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 41.11 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 755 RGAAGIAGPKGDrgDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPAGSA-----GARGAPGERGETGP 829
Cdd:PHA03169 38 GTAARAAKPAPP--APTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGsesvgSPTPSPSGSAEELA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 830 PGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPgaagrvgppg 909
Cdd:PHA03169 116 SGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEP---------- 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 111118976 910 sngnpgppgppGPSGKDGPKGARGDSGPPgragepglqgPAGPPGEKGEPGDDGPSGAEGPPGPQG 975
Cdd:PHA03169 186 -----------EPDSPGPPQSETPTSSPP----------PQSPPDEPGEPQSPTPQQAPSPNTQQA 230
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
698-878 |
4.81e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 41.11 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 698 RGERGFPGErGSPGAQGLQGPRGLPGTPGTDGPKGASGPAGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEG 777
Cdd:PHA03169 81 HGEKEERGQ-GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 778 APGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPAGSAGARGAPGERG--ETGPPGPAGFAGPPGADGQPGAKGEQGEAG 855
Cdd:PHA03169 160 NQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPpdEPGEPQSPTPQQAPSPNTQQAVEHEDEPTE 239
|
170 180
....*....|....*....|....
gi 111118976 856 -QKGDAGAPGPQGPSGAPGPQGPT 878
Cdd:PHA03169 240 pEREGPPFPGHRSHSYTVVGWKPS 263
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1082-1128 |
5.15e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.70 E-value: 5.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 111118976 1082 TGKQGDRGEAGAQGPMGPSGPAGARGIQGPQGPRGDKGEAGEPGERG 1128
Cdd:pfam01391 9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
804-1115 |
5.40e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.51 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 804 GEVGPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGP 883
Cdd:PRK07764 395 AAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAP 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 884 KGARGAQGPPGATGFPGAAGRVGPPGSNGNPGPPGPPGPSGKD------------------------------------- 926
Cdd:PRK07764 475 EPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERWPeilaavpkrsrktwaillpeatvlgvrgdtlvlgfst 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 927 --------GPKGAR--------------------GDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGLAG 978
Cdd:PRK07764 555 gglarrfaSPGNAEvlvtalaeelggdwqveavvGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAA 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 979 QRGIVGLPGQRGERGFPGLPGPSGEP----GKQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGV 1054
Cdd:PRK07764 635 APAEASAAPAPGVAAPEHHPKHVAVPdasdGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQA 714
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 111118976 1055 KGDRGETGAVGAPGAPGPPGSPGPAGPTGKQGDRGEAGAQGPMGPSGPAGARGIQGPQGPR 1115
Cdd:PRK07764 715 DDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPP 775
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
682-725 |
5.91e-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: 5.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 111118976 682 DQGVPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTP 725
Cdd:pfam01391 14 PPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
549-617 |
6.09e-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: 6.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 111118976 549 GRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGedgrpgppgpqgARGQPGVMGFPGPKGANGEPGKA 617
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPG------------PPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
379-632 |
6.25e-03 |
|
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.
Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 41.15 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 379 PTGARGPEGAQGPRGEPGTPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGAPGFPGPRGPPGPQGATG----------- 447
Cdd:pfam09606 164 GQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQqmggapnqvam 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 448 ---PLGPKGQTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRGARGEPGGVGPIGPPGERgaPGNRGFPGQDGLA 524
Cdd:pfam09606 244 qqqQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQ--QQTRQQQQQQGGN 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 525 GPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPGVMGF 604
Cdd:pfam09606 322 HPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSV 401
|
250 260
....*....|....*....|....*...
gi 111118976 605 PGPKGANGEPGKAGEKGLPGAPGLRGLP 632
Cdd:pfam09606 402 PSPQGPGSQPPQSHPGGMIPSPALIPSP 429
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
965-1134 |
6.64e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 41.04 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 965 SGAEGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGspgadG 1044
Cdd:PRK12678 60 GGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRER-----G 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111118976 1045 PPGRDGAAGVKGDRGETGAVGAPGAPGPPGSPGPAGPTGKQGDRGEAGAQGPMGPSGPAGARGIQGPQGPRGDKGEAGEP 1124
Cdd:PRK12678 135 EAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDR 214
|
170
....*....|
gi 111118976 1125 GERGLKGHRG 1134
Cdd:PRK12678 215 REERGRRDGG 224
|
|
| VWC_out |
smart00215 |
von Willebrand factor (vWF) type C domain; |
34-87 |
8.85e-03 |
|
von Willebrand factor (vWF) type C domain;
Pssm-ID: 214565 Cd Length: 67 Bit Score: 36.39 E-value: 8.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 111118976 34 CVQDGQRYNDKDVWKpEPCRICVCDTGTVLCDDIIC---EDVKDCLSPEIPFGECCP 87
Cdd:smart00215 1 CWNNGSYYPPGAKWD-DDCNRCTCLNGRVSCTKVWCgpkPCLLHNLSGECPLGQGCV 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
762-833 |
9.40e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 35.93 E-value: 9.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 111118976 762 GPKGDRGDVGEKGPEGAPGKDGGRGltgpigppgpagangEKGEVGPPGPAGSAGARGAPGERGETGPPGPA 833
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPG---------------PPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| |
