|
Name |
Accession |
Description |
Interval |
E-value |
| COLFI |
pfam01410 |
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1251-1486 |
6.38e-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: 489.54 E-value: 6.38e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 1251 HDVEVDATLKSLNNQIESIRSPDGSRKNPARTCQDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPAT 1330
Cdd:pfam01410 1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 1331 VPRKNWWSsksKEKKHIWFGETMNGGFHFSYGDGNLAPNTANVQMTFLRLLSTEGSQNITYHCKNSVAYLDEVAGNLKKA 1410
Cdd:pfam01410 81 IPRKNWWT---KESKHVWFGEFMNGGSQFSYGVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767958757 1411 LLIQGSNDVEMRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGPEQEFGVDIGPVCF 1486
Cdd:pfam01410 158 LLLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
|
|
| COLFI |
smart00038 |
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1252-1487 |
2.21e-152 |
|
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: 461.55 E-value: 2.21e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 1252 DVEVDATLKSLNNQIESIRSPDGSRKNPARTCQDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPATV 1331
Cdd:smart00038 1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETGETCVSPSPSSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 1332 PRKNWWSSKSKekkHIWFGETMNGGFHFSYGDGNLAPnTANVQMTFLRLLSTEGSQNITYHCKNSVAYLDEVAGNLKKAL 1411
Cdd:smart00038 81 PRKTWYSGKSK---HVWFGETMNGGFKFSYGDSEGPP-VGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767958757 1412 LIQGSNDVEMRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGPEQEFGVDIGPVCFL 1487
Cdd:smart00038 157 RLRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
822-1056 |
2.43e-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: 138.11 E-value: 2.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 822 GERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGA 901
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 902 AGRVGPPGSNGNPGPAGPPGPAGKDGPKGA-----RGDSGPPGRAGDPGLQGPAGVPGEKGDPGDDGPSGSDGPPGPQGL 976
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPagpagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 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 ... |
703-949 |
1.26e-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: 123.86 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 703 FPGERGSPGAQGLQGPRGLPGTPGTDGPKGAAGPDGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKD 782
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 783 GGRGLTGPIGPPGPAGANGEKGEVGSPGPSGSTGARGaPGERGETGPPGPAGFAGPPGADGQPgakgdqGEAGQKGDAGA 862
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA------GKDGPRGDRGE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 863 PGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGsngnpgpagppgPAGKDGPKGARGDSGPPGRAG 942
Cdd:NF038329 268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG------------KDGKDGQPGKDGLPGKDGKDG 335
|
....*..
gi 1767958757 943 DPGLQGP 949
Cdd:NF038329 336 QPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
393-636 |
3.22e-27 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 116.93 E-value: 3.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 393 GEPGNPGSPGPAGASGNPGTDGIPGAKGSAGApgiagapgfpgprgppgpqgaTGPLGPKGQMGEPGIAGFKGEQGPKGE 472
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGP---------------------AGPPGPQGERGEKGPAGPQGEAGPQGP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 473 TGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGaPGERGPSGLAGPKGANGDPGRPG 552
Cdd:NF038329 176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 553 EPGLPGARGLTGRPGDAGPQGKVGPSGapgedgRPGPPGPQGARGQPGVMGFPGPKGANGEPGKAGEKGLAGAPGLRGLP 632
Cdd:NF038329 255 PAGKDGPRGDRGEAGPDGPDGKDGERG------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328
|
....
gi 1767958757 633 GKDG 636
Cdd:NF038329 329 GKDG 332
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
855-1115 |
8.93e-27 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 115.39 E-value: 8.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 855 GQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGsngnpgPAGPpgpAGKDGPKGARGD 934
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG------PQGP---AGKDGEAGAKGP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 935 SGPPGRAGDPGLQGPAGVPGEKGDPGDDGPSGSDGPPGPQGLAGQrGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASG 1014
Cdd:NF038329 188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 1015 DRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGdrgetgalgapgapgppgspgpagPTGKQGDRGEAGAQ 1094
Cdd:NF038329 267 EAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG------------------------KDGLPGKDGKDGQP 322
|
250 260
....*....|....*....|.
gi 1767958757 1095 GPMGPSGPAGARGIAGPQGPR 1115
Cdd:NF038329 323 GKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
650-907 |
6.78e-26 |
|
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: 112.69 E-value: 6.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 650 AGERGEQGAPGPSGFQGLPGPPGPPGEGGKQGDQGIPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDG 729
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 730 PKGAAGPDGPPGAQGPPGLQGMPGeRGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGltgpigppgpagANGEKGEVGSP 809
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG------------DRGEAGPDGPD 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 810 GPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGA 889
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTA 354
|
250
....*....|....*...
gi 1767958757 890 QGPPGATGFPGAAGRVGP 907
Cdd:NF038329 355 PHTPKTPQIPGQSKDVTP 372
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
440-661 |
1.67e-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: 111.54 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 440 PGPQGATGPLGPKGQMGEPGIAGFKGEQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPG 519
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 520 QDGLAGPKGAPGERGPSGLAGPKGangdPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQP 599
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV 283
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1767958757 600 GVMGFPGPKGANGEPGKAGEKGLAGAPglrGLPGKDGETGAAGPPGPSGPAGERGEQGAPGP 661
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKD---GLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| VWC |
pfam00093 |
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ... |
34-88 |
2.40e-25 |
|
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.
Pssm-ID: 278520 Cd Length: 57 Bit Score: 100.19 E-value: 2.40e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1767958757 34 CLQNGQRYKDKDVWKPSPCRICVCDTGNVLCDDIICEDPDCLNP--EIPFGECCPIC 88
Cdd:pfam00093 1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIICPPLDCPNPrlEIPPGECCPVC 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
463-732 |
5.52e-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: 5.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 463 FKGEQGPKGETGPAGPQGAPGPAGEEGKRGargepggagpigppgERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPK 542
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETG---------------PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 543 GANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGapgedgrpgppgPQGARGQPGVMGFPGpKGANGEPGKAGEKGL 622
Cdd:NF038329 180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG------------EAGPAGEDGPAGPAG-DGQQGPDGDPGPTGE 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 623 AGAPGLRGLPGKDGETGAAGPPGPSGPAGERGEQGAPGPSGFqglpgppgppgeggkqgdQGIPGEAGAPGLVGPRGERG 702
Cdd:NF038329 247 DGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK------------------DGQNGKDGLPGKDGKDGQNG 308
|
250 260 270
....*....|....*....|....*....|
gi 1767958757 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 ... |
939-1134 |
1.53e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 102.68 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 939 GRAGDPGLQGPAGVPGEKGDPGDDGPSGSDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGP 1018
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 1019 pgpvgppgltgpAGEPGREGSPGADGPPGRDGAAGVKGDRGETGALGAPGAPGPPGSpgpagptGKQGDRGEAGAQGPMG 1098
Cdd:NF038329 197 ------------RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDP-------GPTGEDGPQGPDGPAG 257
|
170 180 190
....*....|....*....|....*....|....*.
gi 1767958757 1099 PSGPAGARGIAGPQGPRGDKGESGEPGERGLKGHRG 1134
Cdd:NF038329 258 KDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
306-572 |
1.74e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 102.29 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 306 GVKGESGSPGENGSPGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPgpvgpaggpgfpgapgakgeaGPTGARGP 385
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ---------------------GEAGPQGP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 386 EGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPGiagapgfpgprgppgpqgATGPLGPKGQMGEPGiAGFKG 465
Cdd:NF038329 176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG------------------EAGPAGEDGPAGPAG-DGQQG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 466 EQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGAN 545
Cdd:NF038329 237 PDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKD 316
|
250 260
....*....|....*....|....*..
gi 1767958757 546 GDPGRPGEPGLPGARGLTGRPGDAGPQ 572
Cdd:NF038329 317 GKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| VWC |
smart00214 |
von Willebrand factor (vWF) type C domain; |
34-88 |
4.46e-21 |
|
von Willebrand factor (vWF) type C domain;
Pssm-ID: 214564 Cd Length: 59 Bit Score: 87.96 E-value: 4.46e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1767958757 34 CLQNGQRYKDKDVWKPSPCRICVCDTG-NVLCDDIICED-PDCLNPE--IPFGECCPIC 88
Cdd:smart00214 1 CVHNGRVYNDGETWKPDPCQICTCLDGtTVLCDPVECPPpPDCPNPErvKPPGECCPRC 59
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
255-490 |
3.26e-19 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 92.28 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 255 GEAGKPGKAGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERGR 334
Cdd:NF038329 123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGP 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 335 TGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPGaKGEAGPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDG 414
Cdd:NF038329 203 AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGD-PGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767958757 415 IPGAKGSAGAPGiagapgfpgprgppgpqgATGPLGPKGQMGEPGIAGFKGEQGPKGETGPAGPQGAPGPAGEEGK 490
Cdd:NF038329 282 PVGPAGKDGQNG------------------KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
225-426 |
1.89e-18 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 89.96 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 225 GTPGEPGEPGVSGPMGPRGPPGPAGKPGDDGEAGKPGKAGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGA 304
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 305 PGVKGESGSPGENGSPGPM-----GPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPGAKGEAGP 379
Cdd:NF038329 212 AGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1767958757 380 TGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPG 426
Cdd:NF038329 292 NGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
254-555 |
2.38e-17 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 86.50 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 254 DGEAGKPGKAGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERG 333
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 334 RTGPAGAAGARGNDGqpgpAGPPGPVGPAGGPGFPGAPGAKGEAGPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTD 413
Cdd:NF038329 196 PRGETGPAGEQGPAG----PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 414 GIPGAKGSAGAPgiagapgfpgprgppgpqgatgplgpkgqmgepGIAGFKGEQGPKGETGPAGPQGAPGPAGEEGKRGa 493
Cdd:NF038329 272 GPDGKDGERGPV---------------------------------GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG- 317
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1767958757 494 rgepggagpigppgERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPG 555
Cdd:NF038329 318 --------------KDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTAPHTPKTPQIPG 365
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
762-1012 |
6.48e-11 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 66.59 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 762 GPKGDRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGSPGPSGSTGARGAPGERGETGPPGPAGFAGPPGA 841
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 842 DGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKgARGAQGPPGATGF----PGAAGRVGPPGSNGNPGPA 917
Cdd:COG5164 87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPP-SGGSTTPPGDGGStppgPGSTGPGGSTTPPGDGGST 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 918 GPPGPAGKDGPKGARGDSGPP--GRAGDPGLQGPAGVPGEKGDPGDDGPSGSDGPPGPQGLAG----QRGIVGLPGQRGE 991
Cdd:COG5164 166 TPPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTgpkdQRPKTNPIERRGP 245
|
250 260
....*....|....*....|.
gi 1767958757 992 RGFPGLPGPSGEPGKQGAPGA 1012
Cdd:COG5164 246 ERPEAAALPAELTALEAENRA 266
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
375-626 |
9.05e-10 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 63.13 E-value: 9.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 375 GEAGPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQ 454
Cdd:COG5164 10 GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 455 MGEPGIAGFKGEQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERG 534
Cdd:COG5164 90 TRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 535 PSGLAGPKGANGD--PGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQ-GARGQPGVMGFPGPKGAN 611
Cdd:COG5164 170 PGGSTTPPDDGGSttPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPkDQRPKTNPIERRGPERPE 249
|
250
....*....|....*
gi 1767958757 612 GEPGKAGEKGLAGAP 626
Cdd:COG5164 250 AAALPAELTALEAEN 264
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
804-860 |
1.35e-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: 49.41 E-value: 1.35e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1767958757 804 GEVGSPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDA 860
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
768-978 |
2.00e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 55.76 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 768 GDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGSPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGA 847
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 848 KGDQGEAGQKGDAGAP---GPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATgfPGAAGRVGPPGSNGNPGPAGPPGPAG 924
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPapaAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQP--PQAAQGASAPSPAADDPVPLPPEPDD 747
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1767958757 925 KDGPKGARGDSGPPGRAGDPGLQGPAGVPGEKGDP----GDDGPSGSDGPPGPQGLAG 978
Cdd:PRK07764 748 PPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEeemaEDDAPSMDDEDRRDAEEVA 805
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
261-317 |
1.18e-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: 46.72 E-value: 1.18e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1767958757 261 GKAGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGEN 317
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
377-569 |
1.81e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 49.60 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 377 AGPTGARGPEGAqGSRGEPGNPGSPGPAGASGNPGTDGipGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQMG 456
Cdd:PRK07764 595 AGGEGPPAPASS-GPPEEAARPAAPAAPAAPAAPAPAG--AAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 457 EPGIAGFKGEQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGErgPS 536
Cdd:PRK07764 672 KAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD--PP 749
|
170 180 190
....*....|....*....|....*....|...
gi 1767958757 537 GLAGPKGANGDPGRPGEPGLPGARGLTGRPGDA 569
Cdd:PRK07764 750 DPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 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 1767958757 508 ERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGAR 560
Cdd:pfam01391 5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
683-730 |
1.87e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 40.55 E-value: 1.87e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1767958757 683 QGIPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGP 730
Cdd:pfam01391 9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| GGGWT_bact |
NF040941 |
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ... |
1282-1319 |
5.96e-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: 5.96e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1767958757 1282 TCQDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMET 1319
Cdd:NF040941 1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTT 38
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
708-896 |
9.18e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.82 E-value: 9.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 708 GSPGAQGLQGPRGLPGTPGTDGPKGAAGPDGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGL 787
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 788 TGPIGPPGPAGANGEKGEVGSPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGeagqkGDAGAPGPQG 867
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPA-----ADDPVPLPPE 744
|
170 180
....*....|....*....|....*....
gi 1767958757 868 PSGAPGPQGPTGVTGPKGARGAQGPPGAT 896
Cdd:PRK07764 745 PDDPPDPAGAPAQPPPPPAPAPAAAPAAA 773
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COLFI |
pfam01410 |
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1251-1486 |
6.38e-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: 489.54 E-value: 6.38e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 1251 HDVEVDATLKSLNNQIESIRSPDGSRKNPARTCQDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPAT 1330
Cdd:pfam01410 1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 1331 VPRKNWWSsksKEKKHIWFGETMNGGFHFSYGDGNLAPNTANVQMTFLRLLSTEGSQNITYHCKNSVAYLDEVAGNLKKA 1410
Cdd:pfam01410 81 IPRKNWWT---KESKHVWFGEFMNGGSQFSYGVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767958757 1411 LLIQGSNDVEMRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGPEQEFGVDIGPVCF 1486
Cdd:pfam01410 158 LLLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
|
|
| COLFI |
smart00038 |
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1252-1487 |
2.21e-152 |
|
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: 461.55 E-value: 2.21e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 1252 DVEVDATLKSLNNQIESIRSPDGSRKNPARTCQDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPATV 1331
Cdd:smart00038 1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETGETCVSPSPSSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 1332 PRKNWWSSKSKekkHIWFGETMNGGFHFSYGDGNLAPnTANVQMTFLRLLSTEGSQNITYHCKNSVAYLDEVAGNLKKAL 1411
Cdd:smart00038 81 PRKTWYSGKSK---HVWFGETMNGGFKFSYGDSEGPP-VGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767958757 1412 LIQGSNDVEMRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGPEQEFGVDIGPVCFL 1487
Cdd:smart00038 157 RLRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
822-1056 |
2.43e-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: 138.11 E-value: 2.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 822 GERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGA 901
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 902 AGRVGPPGSNGNPGPAGPPGPAGKDGPKGA-----RGDSGPPGRAGDPGLQGPAGVPGEKGDPGDDGPSGSDGPPGPQGL 976
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPagpagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 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 ... |
703-949 |
1.26e-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: 123.86 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 703 FPGERGSPGAQGLQGPRGLPGTPGTDGPKGAAGPDGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKD 782
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 783 GGRGLTGPIGPPGPAGANGEKGEVGSPGPSGSTGARGaPGERGETGPPGPAGFAGPPGADGQPgakgdqGEAGQKGDAGA 862
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA------GKDGPRGDRGE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 863 PGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGsngnpgpagppgPAGKDGPKGARGDSGPPGRAG 942
Cdd:NF038329 268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG------------KDGKDGQPGKDGLPGKDGKDG 335
|
....*..
gi 1767958757 943 DPGLQGP 949
Cdd:NF038329 336 QPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
393-636 |
3.22e-27 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 116.93 E-value: 3.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 393 GEPGNPGSPGPAGASGNPGTDGIPGAKGSAGApgiagapgfpgprgppgpqgaTGPLGPKGQMGEPGIAGFKGEQGPKGE 472
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGP---------------------AGPPGPQGERGEKGPAGPQGEAGPQGP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 473 TGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGaPGERGPSGLAGPKGANGDPGRPG 552
Cdd:NF038329 176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 553 EPGLPGARGLTGRPGDAGPQGKVGPSGapgedgRPGPPGPQGARGQPGVMGFPGPKGANGEPGKAGEKGLAGAPGLRGLP 632
Cdd:NF038329 255 PAGKDGPRGDRGEAGPDGPDGKDGERG------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328
|
....
gi 1767958757 633 GKDG 636
Cdd:NF038329 329 GKDG 332
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
855-1115 |
8.93e-27 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 115.39 E-value: 8.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 855 GQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGsngnpgPAGPpgpAGKDGPKGARGD 934
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG------PQGP---AGKDGEAGAKGP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 935 SGPPGRAGDPGLQGPAGVPGEKGDPGDDGPSGSDGPPGPQGLAGQrGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASG 1014
Cdd:NF038329 188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 1015 DRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGdrgetgalgapgapgppgspgpagPTGKQGDRGEAGAQ 1094
Cdd:NF038329 267 EAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG------------------------KDGLPGKDGKDGQP 322
|
250 260
....*....|....*....|.
gi 1767958757 1095 GPMGPSGPAGARGIAGPQGPR 1115
Cdd:NF038329 323 GKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
650-907 |
6.78e-26 |
|
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: 112.69 E-value: 6.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 650 AGERGEQGAPGPSGFQGLPGPPGPPGEGGKQGDQGIPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDG 729
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 730 PKGAAGPDGPPGAQGPPGLQGMPGeRGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGltgpigppgpagANGEKGEVGSP 809
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG------------DRGEAGPDGPD 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 810 GPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGA 889
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTA 354
|
250
....*....|....*...
gi 1767958757 890 QGPPGATGFPGAAGRVGP 907
Cdd:NF038329 355 PHTPKTPQIPGQSKDVTP 372
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
440-661 |
1.67e-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: 111.54 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 440 PGPQGATGPLGPKGQMGEPGIAGFKGEQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPG 519
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 520 QDGLAGPKGAPGERGPSGLAGPKGangdPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQP 599
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV 283
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1767958757 600 GVMGFPGPKGANGEPGKAGEKGLAGAPglrGLPGKDGETGAAGPPGPSGPAGERGEQGAPGP 661
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKD---GLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| VWC |
pfam00093 |
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ... |
34-88 |
2.40e-25 |
|
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.
Pssm-ID: 278520 Cd Length: 57 Bit Score: 100.19 E-value: 2.40e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1767958757 34 CLQNGQRYKDKDVWKPSPCRICVCDTGNVLCDDIICEDPDCLNP--EIPFGECCPIC 88
Cdd:pfam00093 1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIICPPLDCPNPrlEIPPGECCPVC 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
463-732 |
5.52e-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: 5.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 463 FKGEQGPKGETGPAGPQGAPGPAGEEGKRGargepggagpigppgERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPK 542
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETG---------------PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 543 GANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGapgedgrpgppgPQGARGQPGVMGFPGpKGANGEPGKAGEKGL 622
Cdd:NF038329 180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG------------EAGPAGEDGPAGPAG-DGQQGPDGDPGPTGE 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 623 AGAPGLRGLPGKDGETGAAGPPGPSGPAGERGEQGAPGPSGFqglpgppgppgeggkqgdQGIPGEAGAPGLVGPRGERG 702
Cdd:NF038329 247 DGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK------------------DGQNGKDGLPGKDGKDGQNG 308
|
250 260 270
....*....|....*....|....*....|
gi 1767958757 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 ... |
939-1134 |
1.53e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 102.68 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 939 GRAGDPGLQGPAGVPGEKGDPGDDGPSGSDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGP 1018
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 1019 pgpvgppgltgpAGEPGREGSPGADGPPGRDGAAGVKGDRGETGALGAPGAPGPPGSpgpagptGKQGDRGEAGAQGPMG 1098
Cdd:NF038329 197 ------------RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDP-------GPTGEDGPQGPDGPAG 257
|
170 180 190
....*....|....*....|....*....|....*.
gi 1767958757 1099 PSGPAGARGIAGPQGPRGDKGESGEPGERGLKGHRG 1134
Cdd:NF038329 258 KDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
306-572 |
1.74e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 102.29 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 306 GVKGESGSPGENGSPGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPgpvgpaggpgfpgapgakgeaGPTGARGP 385
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ---------------------GEAGPQGP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 386 EGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPGiagapgfpgprgppgpqgATGPLGPKGQMGEPGiAGFKG 465
Cdd:NF038329 176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG------------------EAGPAGEDGPAGPAG-DGQQG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 466 EQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGAN 545
Cdd:NF038329 237 PDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKD 316
|
250 260
....*....|....*....|....*..
gi 1767958757 546 GDPGRPGEPGLPGARGLTGRPGDAGPQ 572
Cdd:NF038329 317 GKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| VWC |
smart00214 |
von Willebrand factor (vWF) type C domain; |
34-88 |
4.46e-21 |
|
von Willebrand factor (vWF) type C domain;
Pssm-ID: 214564 Cd Length: 59 Bit Score: 87.96 E-value: 4.46e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1767958757 34 CLQNGQRYKDKDVWKPSPCRICVCDTG-NVLCDDIICED-PDCLNPE--IPFGECCPIC 88
Cdd:smart00214 1 CVHNGRVYNDGETWKPDPCQICTCLDGtTVLCDPVECPPpPDCPNPErvKPPGECCPRC 59
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
255-490 |
3.26e-19 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 92.28 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 255 GEAGKPGKAGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERGR 334
Cdd:NF038329 123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGP 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 335 TGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPGaKGEAGPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDG 414
Cdd:NF038329 203 AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGD-PGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767958757 415 IPGAKGSAGAPGiagapgfpgprgppgpqgATGPLGPKGQMGEPGIAGFKGEQGPKGETGPAGPQGAPGPAGEEGK 490
Cdd:NF038329 282 PVGPAGKDGQNG------------------KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
225-426 |
1.89e-18 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 89.96 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 225 GTPGEPGEPGVSGPMGPRGPPGPAGKPGDDGEAGKPGKAGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGA 304
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 305 PGVKGESGSPGENGSPGPM-----GPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPGAKGEAGP 379
Cdd:NF038329 212 AGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1767958757 380 TGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPG 426
Cdd:NF038329 292 NGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
254-555 |
2.38e-17 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 86.50 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 254 DGEAGKPGKAGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERG 333
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 334 RTGPAGAAGARGNDGqpgpAGPPGPVGPAGGPGFPGAPGAKGEAGPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTD 413
Cdd:NF038329 196 PRGETGPAGEQGPAG----PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 414 GIPGAKGSAGAPgiagapgfpgprgppgpqgatgplgpkgqmgepGIAGFKGEQGPKGETGPAGPQGAPGPAGEEGKRGa 493
Cdd:NF038329 272 GPDGKDGERGPV---------------------------------GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG- 317
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1767958757 494 rgepggagpigppgERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPG 555
Cdd:NF038329 318 --------------KDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTAPHTPKTPQIPG 365
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
762-1012 |
6.48e-11 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 66.59 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 762 GPKGDRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGSPGPSGSTGARGAPGERGETGPPGPAGFAGPPGA 841
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 842 DGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKgARGAQGPPGATGF----PGAAGRVGPPGSNGNPGPA 917
Cdd:COG5164 87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPP-SGGSTTPPGDGGStppgPGSTGPGGSTTPPGDGGST 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 918 GPPGPAGKDGPKGARGDSGPP--GRAGDPGLQGPAGVPGEKGDPGDDGPSGSDGPPGPQGLAG----QRGIVGLPGQRGE 991
Cdd:COG5164 166 TPPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTgpkdQRPKTNPIERRGP 245
|
250 260
....*....|....*....|.
gi 1767958757 992 RGFPGLPGPSGEPGKQGAPGA 1012
Cdd:COG5164 246 ERPEAAALPAELTALEAENRA 266
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
816-1060 |
4.12e-10 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 63.90 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 816 GARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGA 895
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 896 TGFPGAAGRVGPPGSNGNPGPAGPPGPAGKDGPKGARGDSGPPgragDPGLQGPAGVPGEK-GDPGDDGPSGSDGPPGPQ 974
Cdd:COG5164 87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPP----SGGSTTPPGDGGSTpPGPGSTGPGGSTTPPGDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 975 GLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGV 1054
Cdd:COG5164 163 GSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIER 242
|
....*.
gi 1767958757 1055 KGDRGE 1060
Cdd:COG5164 243 RGPERP 248
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
375-626 |
9.05e-10 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 63.13 E-value: 9.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 375 GEAGPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQ 454
Cdd:COG5164 10 GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 455 MGEPGIAGFKGEQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERG 534
Cdd:COG5164 90 TRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 535 PSGLAGPKGANGD--PGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQ-GARGQPGVMGFPGPKGAN 611
Cdd:COG5164 170 PGGSTTPPDDGGSttPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPkDQRPKTNPIERRGPERPE 249
|
250
....*....|....*
gi 1767958757 612 GEPGKAGEKGLAGAP 626
Cdd:COG5164 250 AAALPAELTALEAEN 264
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
861-1124 |
7.05e-08 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 56.96 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 861 GAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGSNGNPGPAGPPGPAGKDGPKGARGDSGPPGR 940
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 941 AGDPGLQGPAGVPGEKGDPGDDGPSGSDGPPGPQGLAGQRGivglPGQRGERGFPGLPGPSgePGKQGAPGASGDRGPPG 1020
Cdd:COG5164 87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT----PPSGGSTTPPGDGGST--PPGPGSTGPGGSTTPPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 1021 PVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRGETGALGAPGAPGPPGSPGPAGPTGKQGDRGEAGAQGPMGPS 1100
Cdd:COG5164 161 DGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPI 240
|
250 260
....*....|....*....|....
gi 1767958757 1101 GPAGARGIAGPQGPRGDKGESGEP 1124
Cdd:COG5164 241 ERRGPERPEAAALPAELTALEAEN 264
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
804-860 |
1.35e-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: 49.41 E-value: 1.35e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1767958757 804 GEVGSPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDA 860
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
768-978 |
2.00e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 55.76 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 768 GDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGSPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGA 847
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 848 KGDQGEAGQKGDAGAP---GPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATgfPGAAGRVGPPGSNGNPGPAGPPGPAG 924
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPapaAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQP--PQAAQGASAPSPAADDPVPLPPEPDD 747
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1767958757 925 KDGPKGARGDSGPPGRAGDPGLQGPAGVPGEKGDP----GDDGPSGSDGPPGPQGLAG 978
Cdd:PRK07764 748 PPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEeemaEDDAPSMDDEDRRDAEEVA 805
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
853-1059 |
4.12e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 54.99 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 853 EAGQKGDAGAPGPQGPSGAPGPQG------PTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGSNGNPGPAGPPGPAGKD 926
Cdd:PRK07764 585 EAVVGPAPGAAGGEGPPAPASSGPpeeaarPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASD 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 927 GPKGARGDSGPPGRAGDPGLQGPAGVPGEKGDPGDDGPSGSDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGK 1006
Cdd:PRK07764 665 GGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPE 744
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1767958757 1007 QGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRG 1059
Cdd:PRK07764 745 PDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDED 797
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
828-883 |
6.73e-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: 6.73e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1767958757 828 GPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGP 883
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
837-893 |
7.35e-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: 7.35e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1767958757 837 GPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPP 893
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
813-1010 |
8.40e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 53.84 E-value: 8.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 813 GSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQgeagqkgdAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGP 892
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAP--------APAGAAAAPAEASAAPAPGVAAPEHHPKHVAVP 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 893 PGATGFPGAAGRVGPPGSNGNPGPAGPPGPAGKDGPKGARGDSGPPGRAGDPGLQGPAGVPGEKGDPGDDGPSGSDG--- 969
Cdd:PRK07764 661 DASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDpvp 740
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1767958757 970 -PPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAP 1010
Cdd:PRK07764 741 lPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
807-863 |
1.08e-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: 47.10 E-value: 1.08e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1767958757 807 GSPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAP 863
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
261-317 |
1.18e-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: 46.72 E-value: 1.18e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1767958757 261 GKAGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGEN 317
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
816-872 |
2.76e-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: 2.76e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1767958757 816 GARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAP 872
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
445-661 |
4.15e-06 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 51.18 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 445 ATGPLGPKGQMGEPGIAGFKGEQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAgpigppgerGAPGNRGFPGQDGLA 524
Cdd:COG5164 8 KTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGT---------RPAGNQGATGPAQNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 525 GPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPGVMGF 604
Cdd:COG5164 79 GGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1767958757 605 PGPKGANGEPGKAGEKGLAGAPGlRGLPGKDGETGAAGPPGPSGPAGERGEQGAPGP 661
Cdd:COG5164 159 PGDGGSTTPPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDK 214
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
936-992 |
6.82e-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: 6.82e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1767958757 936 GPPGRAGDPGLQGPAGVPGEKGDPGDDGPSGSDGPPGPQGLAGQRGIVGLPGQRGER 992
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
846-902 |
1.17e-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: 1.17e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1767958757 846 GAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAA 902
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
377-569 |
1.81e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 49.60 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 377 AGPTGARGPEGAqGSRGEPGNPGSPGPAGASGNPGTDGipGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQMG 456
Cdd:PRK07764 595 AGGEGPPAPASS-GPPEEAARPAAPAAPAAPAAPAPAG--AAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 457 EPGIAGFKGEQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGErgPS 536
Cdd:PRK07764 672 KAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD--PP 749
|
170 180 190
....*....|....*....|....*....|...
gi 1767958757 537 GLAGPKGANGDPGRPGEPGLPGARGLTGRPGDA 569
Cdd:PRK07764 750 DPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 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 1767958757 508 ERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGAR 560
Cdd:pfam01391 5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
930-986 |
2.78e-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: 42.87 E-value: 2.78e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1767958757 930 GARGDSGPPGRAGDPGLQGPAGVPGEKGDPGDDGPSGSDGPPGPQGLAGQRGIVGLP 986
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
374-425 |
2.78e-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: 42.87 E-value: 2.78e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1767958757 374 KGEAGPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAP 425
Cdd:pfam01391 6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
864-909 |
4.86e-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: 4.86e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1767958757 864 GPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPG 909
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
|
|
| PRK14959 |
PRK14959 |
DNA polymerase III subunits gamma and tau; Provisional |
812-910 |
5.39e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 47.75 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 812 SGSTGARGAPGerGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQG 891
Cdd:PRK14959 372 RPSGGGASAPS--GSAAEGPASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPAPSAAPSPRVPWDDAPPAPPRSGIP 449
|
90
....*....|....*....
gi 1767958757 892 PPGATGFPGAAGRVGPPGS 910
Cdd:PRK14959 450 PRPAPRMPEASPVPGAPDS 468
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
948-1004 |
7.49e-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: 7.49e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1767958757 948 GPAGVPGEKGDPGDDGPSGSDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEP 1004
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
927-981 |
8.67e-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: 8.67e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1767958757 927 GPKGARGDSGPPGRAGDPGLQGPAGVPGEKGDPGDDGPSGSDGPPGPQGLAGQRG 981
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
800-849 |
9.29e-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: 9.29e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1767958757 800 NGEKGEVGSPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKG 849
Cdd:pfam01391 6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
264-320 |
1.12e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 41.33 E-value: 1.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1767958757 264 GERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSP 320
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
384-577 |
1.12e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 46.90 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 384 GPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPlgPKGQMGEPGIAGF 463
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHH--PKHVAVPDASDGG 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 464 KGEQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGpkGAPGERGPSGLAGPKG 543
Cdd:PRK07764 667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGA--SAPSPAADDPVPLPPE 744
|
170 180 190
....*....|....*....|....*....|....
gi 1767958757 544 ANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGP 577
Cdd:PRK07764 745 PDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSP 778
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
801-847 |
1.22e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 41.33 E-value: 1.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1767958757 801 GEKGEVGSPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGA 847
Cdd:pfam01391 10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
749-901 |
1.71e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 45.73 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 749 QGMPGERGAAGIAGPKGDRGDVGEKGPEGApGKDGGRGLTGPIGPPGPAGANGEKGEVGSPGPSGSTGARGAPGERGETG 828
Cdd:PHA03169 81 HGEKEERGQGGPSGSGSESVGSPTPSPSGS-AEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSP 159
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1767958757 829 PPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGvTGPKGARGAQGPPGATGFPGA 901
Cdd:PHA03169 160 NQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDE-PGEPQSPTPQQAPSPNTQQAV 231
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
683-730 |
1.87e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 40.55 E-value: 1.87e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1767958757 683 QGIPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGP 730
Cdd:pfam01391 9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 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 1767958757 513 GNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDA 569
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
807-993 |
3.27e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.28 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 807 GSPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPtgvtgpkgA 886
Cdd:PRK12678 61 GGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERR--------E 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 887 RGAQGPPGATGFPGAAGRVGPPGSNGNPGPAGPPGPAGKDGPKGARGDSGPPGRAGDPGLQGPAGVPGEKGDPGDDGPSG 966
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQG 212
|
170 180
....*....|....*....|....*..
gi 1767958757 967 SDGPPGPQGLAGQRGivGLPGQRGERG 993
Cdd:PRK12678 213 DRREERGRRDGGDRR--GRRRRRDRRD 237
|
|
| 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 1767958757 687 GEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKG 732
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
447-493 |
4.14e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.78 E-value: 4.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1767958757 447 GPLGPKGQMGEPGIAGFKGEQGPKGETGPAGPQGAPGPAGEEGKRGA 493
Cdd:pfam01391 7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
304-577 |
5.85e-04 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 44.25 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 304 APGVKGESGSPGENGSPGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPGAKGEAGPTGAR 383
Cdd:COG5164 5 GPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 384 GPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQMGEPGIAGF 463
Cdd:COG5164 85 QNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 464 KGEQGPKGETGPAGPQGAPGP-AGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFP--GQDGLAGPKGAPGERGPSGLAG 540
Cdd:COG5164 165 TTPPGPGGSTTPPDDGGSTTPpNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPpdDRGGKTGPKDQRPKTNPIERRG 244
|
250 260 270
....*....|....*....|....*....|....*..
gi 1767958757 541 PKGANGDPGrPGEPGLPGARGLTGRPGDAGPQGKVGP 577
Cdd:COG5164 245 PERPEAAAL-PAELTALEAENRAANPEPATKTIPETT 280
|
|
| GGGWT_bact |
NF040941 |
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ... |
1282-1319 |
5.96e-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: 5.96e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1767958757 1282 TCQDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMET 1319
Cdd:NF040941 1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTT 38
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
471-661 |
7.82e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.21 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 471 GETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGR 550
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 551 PGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPGVMGFPGPKGANGEPGKAGEKGLAGAPGLRG 630
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749
|
170 180 190
....*....|....*....|....*....|.
gi 1767958757 631 LPGKDGETGAAGPPGPSGPAGERGEQGAPGP 661
Cdd:PRK07764 750 DPAGAPAQPPPPPAPAPAAAPAAAPPPSPPS 780
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
928-1133 |
8.63e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.74 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 928 PKGARGDSGPPGRAGDPGLQGPAGVPGEKGDPGDDGPSGSDGPPGPQGLAGQRGIVGlpGQRGERGFPGLPGPSGEPGKQ 1007
Cdd:PRK12678 77 ARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRER--GEAARRGAARKAGEGGEQPAT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 1008 GAPGASGDRGPPGpvgppgltgpagEPGREGSPGADGPPGRDGAAGVKGDRGETGALGAPGAPGPPGSPGPAGPTGKQGD 1087
Cdd:PRK12678 155 EARADAAERTEEE------------ERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRD 222
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1767958757 1088 RGEAGAQGPMGPSGPAGARGIAGPQGPRGDKGESGEPGERGLKGHR 1133
Cdd:PRK12678 223 GGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRD 268
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
708-896 |
9.18e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.82 E-value: 9.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 708 GSPGAQGLQGPRGLPGTPGTDGPKGAAGPDGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGL 787
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 788 TGPIGPPGPAGANGEKGEVGSPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGeagqkGDAGAPGPQG 867
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPA-----ADDPVPLPPE 744
|
170 180
....*....|....*....|....*....
gi 1767958757 868 PSGAPGPQGPTGVTGPKGARGAQGPPGAT 896
Cdd:PRK07764 745 PDDPPDPAGAPAQPPPPPAPAPAAAPAAA 773
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
282-331 |
9.65e-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: 38.63 E-value: 9.65e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1767958757 282 GLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGE 331
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
|
|
| PPE |
COG5651 |
PPE-repeat protein [Function unknown]; |
810-987 |
1.05e-03 |
|
PPE-repeat protein [Function unknown];
Pssm-ID: 444372 [Multi-domain] Cd Length: 385 Bit Score: 43.34 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 810 GPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGA 889
Cdd:COG5651 206 NQVGIGGLNSGSGPIGLNSGPGNTGFAGTGAAAGAAAAAAAAAAAAGAGASAALASLAATLLNASSLGLAATAASSAATN 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 890 QGPPGATGFPGAAGRVGPPGSNGNPGPAGPPGPAGKDGPKGARGDSGPPGRAGDPGLQGPAGVPGEKGDPGDDGPSGSDG 969
Cdd:COG5651 286 LGLAGSPLGLAGGGAGAAAATGLGLGAGGAAGAAGATGAGAALGAGAAAAAAGAAAGAGAAAAAAAGGAGGGGGGALGAG 365
|
170
....*....|....*...
gi 1767958757 970 PPGPQGLAGQRGIVGLPG 987
Cdd:COG5651 366 GGGGSAGAAAGAASGGGA 383
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
805-1059 |
1.10e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 805 EVGSPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEagqkgDAGAPGPQGPSGAPGPQGPTGVTGPK 884
Cdd:PHA03307 96 APASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSP-----GPPPAASPPAAGASPAAVASDAASSR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 885 G-ARGAQGPPGATGFPGAAGRVGPPGSNGNPGPAGPPG-------PAGKDGPKGARGDSGPPGRAGDPGL--QGPAGVPG 954
Cdd:PHA03307 171 QaALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRrsspisaSASSPAPAPGRSAADDAGASSSDSSssESSGCGWG 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 955 EKGDPGDDGPSGSDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGA-SGDRGPPGPVGPPGLTGPAGE 1033
Cdd:PHA03307 251 PENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPApSSPRASSSSSSSRESSSSSTS 330
|
250 260
....*....|....*....|....*.
gi 1767958757 1034 PGREGSPGADGPPGRDGAAGVKGDRG 1059
Cdd:PHA03307 331 SSSESSRGAAVSPGPSPSRSPSPSRP 356
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
471-541 |
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 1767958757 471 GETGPAGPQGAPGPAGEEGKRGArgepggagpigppgeRGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGP 541
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGP---------------PGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| 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 1767958757 477 GPQGAPGPAGEEGKRgargepggagpigppgerGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRP 551
Cdd:pfam01391 1 GPPGPPGPPGPPGPP------------------GPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
724-910 |
1.21e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.44 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 724 TPGTDGPKGAAGPDGPPGAQGPPGLQGMPGERGAAgiAGPKGDRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEK 803
Cdd:PRK07764 587 VVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAP--AAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASD 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 804 GEVGSPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKG-------DAGAPGPQGPSGAPGPQG 876
Cdd:PRK07764 665 GGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAqppqaaqGASAPSPAADDPVPLPPE 744
|
170 180 190
....*....|....*....|....*....|....
gi 1767958757 877 PTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGS 910
Cdd:PRK07764 745 PDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSP 778
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
801-845 |
2.19e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.86 E-value: 2.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1767958757 801 GEKGEVGSPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQP 845
Cdd:pfam01391 13 GPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
381-427 |
3.00e-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: 37.47 E-value: 3.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1767958757 381 GARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPGI 427
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
811-1127 |
3.01e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.28 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 811 PSGSTGARG--APGERGETGPPgPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQgptgvtgPKGARG 888
Cdd:PRK07764 365 PSASDDERGllARLERLERRLG-VAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQ-------PAPAPA 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 889 AQGPPGATGFPGAAGRVGPPGSNGNPGPAGPPGPAGKDGPKGARGDSGPPGRAGDPGLQGPAGVPGEKGDPGDDGPSGSd 968
Cdd:PRK07764 437 PAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRER- 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 969 gppGPQGLAGQRGIVG-----------LPGQRGER---GF--PGLPGPSGEPG---------------------KQGAPG 1011
Cdd:PRK07764 516 ---WPEILAAVPKRSRktwaillpeatVLGVRGDTlvlGFstGGLARRFASPGnaevlvtalaeelggdwqveaVVGPAP 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 1012 ASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGD-RGETGALGAPGAPGPPGSPGPAGPTGKQGDRGE 1090
Cdd:PRK07764 593 GAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEaSAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAK 672
|
330 340 350
....*....|....*....|....*....|....*..
gi 1767958757 1091 AGAQGPMGPSGPAGARGIAGPQGPRGDKGESGEPGER 1127
Cdd:PRK07764 673 AGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATP 709
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
783-993 |
5.37e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 41.43 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 783 GGRGLTGPIGPPGPAGANGEKGEVGSPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAkgdqGEAGQKGDAGA 862
Cdd:PRK12678 60 GGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEA----AQARERRERGE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 863 PGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGSNGNPGPAGPPGPAGKDGPKGARGDSGPPGRAG 942
Cdd:PRK12678 136 AARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRR 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1767958757 943 DPGLQGPAGVPGEKGDPGDDGPSGSDGPPGPQGLAGQRGIVGLPGQRGERG 993
Cdd:PRK12678 216 EERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRF 266
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
839-1127 |
5.78e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.12 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 839 PGADGQPGAKGDQGEA-----GQKGDAGAPGPQGPSGAPGPQGPTgVTGPKGARGAQGPPGATGFPGAAGR---VGPPGS 910
Cdd:PRK07764 365 PSASDDERGLLARLERlerrlGVAGGAGAPAAAAPSAAAAAPAAA-PAPAAAAPAAAAAPAPAAAPQPAPApapAPAPPS 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 911 NGNPGPAGPPGPAGKDGPKGARGDSGPPGRAGDPGLQGPAGVPGEKGDPGDDGPSGSDGPPGPQGLAGQRG----IVGLP 986
Cdd:PRK07764 444 PAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRErwpeILAAV 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 987 GQRGER---------------------GFP--------GLPG----------------------PSGEPGKQGAPGASGD 1015
Cdd:PRK07764 524 PKRSRKtwaillpeatvlgvrgdtlvlGFStgglarrfASPGnaevlvtalaeelggdwqveavVGPAPGAAGGEGPPAP 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 1016 RGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRGETGALGAPGAPGPPGSPGPAGPTGKQGDRGEAGAQG 1095
Cdd:PRK07764 604 ASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPP 683
|
330 340 350
....*....|....*....|....*....|...
gi 1767958757 1096 PMGPSGPAGARGIAGPQG-PRGDKGESGEPGER 1127
Cdd:PRK07764 684 APAPAAPAAPAGAAPAQPaPAPAATPPAGQADD 716
|
|
| VWC_out |
smart00215 |
von Willebrand factor (vWF) type C domain; |
34-86 |
5.97e-03 |
|
von Willebrand factor (vWF) type C domain;
Pssm-ID: 214565 Cd Length: 67 Bit Score: 36.77 E-value: 5.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1767958757 34 CLQNGQRYKDKDVWKPSpCRICVCDTGNVLCDDIICEDPDC----LNPEIPFGECCP 86
Cdd:smart00215 1 CWNNGSYYPPGAKWDDD-CNRCTCLNGRVSCTKVWCGPKPCllhnLSGECPLGQGCV 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
549-617 |
6.15e-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: 36.32 E-value: 6.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1767958757 549 GRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGedgrpgppgpqgARGQPGVMGFPGPKGANGEPGKA 617
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPG------------PPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
255-302 |
6.21e-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: 36.32 E-value: 6.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1767958757 255 GEAGKPGKAGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEA 302
Cdd:pfam01391 10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
684-893 |
7.27e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.12 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 684 GIPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKGAAGPDGPPGAQGPPGLQGMPGERGAAgiAGP 763
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAS--DGG 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767958757 764 KGDRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGA-NGEKGEVGSPGPSGSTGARGAPGERGETGPPGPAGFAGPPGAD 842
Cdd:PRK07764 667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPApAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD 746
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1767958757 843 GQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPP 893
Cdd:PRK07764 747 DPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDED 797
|
|
| |
