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Conserved domains on  [gi|1487320837|ref|XP_026523803|]
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collagen alpha-1(III) chain [Notechis scutatus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1222-1454 2.21e-149

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: 452.95  E-value: 2.21e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837 1222 EILASLKSVNSQIENIISPDGSRKNPARNCRDLKFCHPELSSGEYWIDPNQGCKLDAIKVFCNMETGETCLSANPSSVPK 1301
Cdd:pfam01410    4 EVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKASIPR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837 1302 KNWWTSpgpEKKHIWFGETMNGGFQFSYGDPDLPEEVADVQLAFLRILSSRASQNITYHCKNSIAYMDEASGNVKRALKF 1381
Cdd:pfam01410   84 KNWWTK---ESKHVWFGEFMNGGSQFSYGVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKALLL 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1487320837 1382 MSSTDSEIKAEGNNKFTYTVLEDGCTKHTDEWSKTIFEYRTRKTMRLPVIDIAPFDIGASNQEFGVDVGPVCF 1454
Cdd:pfam01410  161 QGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 239-546 2.72e-30

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 125.79  E-value: 2.72e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  239 FPGLPGHKGPSGMPGMPGMKGHRGFDGKDGSKGDAGAPGLKGENGLPGENGSPGPMGPRGLPGERGRAGLPGTAGGRGND 318
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  319 GSpgaagqpgppgppgpsgfpgtpgfKGENGPAGPAGSSGPPGPKGDAgapgqpggsgppgpggrdgnpGAKGPPGAAGM 398
Cdd:NF038329   195 GP------------------------RGETGPAGEQGPAGPAGPDGEA---------------------GPAGEDGPAGP 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  399 PGapglSGARGPPGPSGTNGIPGQRGPSGEPGKNGGKGEPGPRGERGENGTPGSAGPPGEEGKagaPGQPGTNGIPGTAG 478
Cdd:NF038329   230 AG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK---DGQNGKDGLPGKDG 302

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1487320837  479 ERGAPGfrgpagpsgpggEKGAPGERGGPGSTGPRGAPGEPGRDGSPGLPgmrgltgSPGSPGVDGKP 546
Cdd:NF038329   303 KDGQNG------------KDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP-------APKTPEVPQKP 351
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 724-1046 3.36e-21

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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 98.44  E-value: 3.36e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  724 GERGASGNPGPKGEKGEPGSRGGDGTPGKDGVRGPVGSIGPPGPSGQSGDKGEPGPAgphgpsgprggpgdrgeqgppgp 803
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ----------------------- 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  804 agfpgapgqnGEPGGKGERGLPGERGESGPPGIAGPSGGPGAPGPAGSSGSKGERGSPGPPGASGFPGGRGLpgppgnng 883
Cdd:NF038329   174 ----------GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQ-------- 235

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  884 psgppgnagppgkdghsgppgstgpsgppggqgpkgepgvpGEKGPAGPKGNDGITGPSGNSGIPGPRGIVGLPGSRGPI 963
Cdd:NF038329   236 -----------------------------------------GPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  964 GSIGPSGPKGEDGKPGSNGSPGERGPPgpggppgingapgepGRDGNPGSDGLPGRDGSAGPKGDRGENGPAGVPGSPGH 1043
Cdd:NF038329   275 GKDGERGPVGPAGKDGQNGKDGLPGKD---------------GKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339


                   ...
gi 1487320837 1044 MGP 1046
Cdd:NF038329   340 PAP 342
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 33-89 1.81e-20

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


:

Pssm-ID: 278520  Cd Length: 57  Bit Score: 85.94  E-value: 1.81e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1487320837   33 CSHLGQLYSDRDVWKPEPCQICVCDSGSVLCDEIICEekELSCTNP--EIPFGECCPIC 89
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIICP--PLDCPNPrlEIPPGECCPVC 57
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 502-779 4.24e-16

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 82.65  E-value: 4.24e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  502 GERGGPGSTGPRGAPGEPGRDGSPGLPGMRGLTGSPGSPGVDGKPGPSGSPGESGRSGPPGPAGPRGQPGVMGFPGPKGN 581
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  582 EGSPGKNGERGGSGPPGGPGLPGKDGEPGGQGPPGPaggpgergeqgatGSPGFQGLPGPSGAPGESGKPGDPGPKGENG 661
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  662 LPGLPGGKGENGIPGERGAPGnaglpgarggpgpagpeggkgpggpvgppggmgppglqgMPGERGASGNPGPKGEKGEP 741
Cdd:NF038329   264 DRGEAGPDGPDGKDGERGPVG---------------------------------------PAGKDGQNGKDGLPGKDGKD 304

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1487320837  742 GSRGGDGTPGKDGVRGPVGSIGPPGPSGQSGDKGEPGP 779
Cdd:NF038329   305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 76-280 2.53e-12

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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 70.70  E-value: 2.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837   76 TNPEIPFGECCPICPNPTAVPPEKTVIRGPQGQKGDPGPPGRNGSPGIPGLPGDPGQPGPPGicQNCPDGTIfssqyGYD 155
Cdd:NF038329   143 TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG--EQGPAGPA-----GPD 215

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  156 VKAGPEPQIGtgGGFPGPPGPSGPPGPVGQPGSPGPHGYQGPPGEPGQSGAPGSPGPQGMIGPPGPSGKDGEPGRPGRPG 235
Cdd:NF038329   216 GEAGPAGEDG--PAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1487320837  236 ERGFPGLPGHKGPSGMPGMPGMKGHRGFDGKDGSKGDAGAPGLKG 280
Cdd:NF038329   294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 925-1170 1.18e-11

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 68.78  E-value: 1.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  925 GEKGPAGPKGNDGITGPSGNSGIPGPRGIVGLPGSRGPIGSIGPSGPKGEDGKPGsngspgergppgpggppgingapgE 1004
Cdd:NF038329   120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG------------------------P 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837 1005 PGRDGNPGSDGLPGRDGSAGPKGDRGENGPAGVPGSPGHMGPPGNAGAPGKSGERGhsgpagpagpagpagargapgpAG 1084
Cdd:NF038329   176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------------DG 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837 1085 ARGDKGEAGERGLNGMKGHRGfpgnpgspgpvgplgppgQSGSPGPAGARGPPGPSGSPGKDGRVGYAGPIGPPGPRGNR 1164
Cdd:NF038329   234 QQGPDGDPGPTGEDGPQGPDG------------------PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKD 295


                   ....*.
gi 1487320837 1165 GESGQA 1170
Cdd:NF038329   296 GLPGKD 301
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1222-1454 2.21e-149

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: 452.95  E-value: 2.21e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837 1222 EILASLKSVNSQIENIISPDGSRKNPARNCRDLKFCHPELSSGEYWIDPNQGCKLDAIKVFCNMETGETCLSANPSSVPK 1301
Cdd:pfam01410    4 EVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKASIPR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837 1302 KNWWTSpgpEKKHIWFGETMNGGFQFSYGDPDLPEEVADVQLAFLRILSSRASQNITYHCKNSIAYMDEASGNVKRALKF 1381
Cdd:pfam01410   84 KNWWTK---ESKHVWFGEFMNGGSQFSYGVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKALLL 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1487320837 1382 MSSTDSEIKAEGNNKFTYTVLEDGCTKHTDEWSKTIFEYRTRKTMRLPVIDIAPFDIGASNQEFGVDVGPVCF 1454
Cdd:pfam01410  161 QGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1221-1455 1.12e-137

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: 421.88  E-value: 1.12e-137
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  1221 GEILASLKSVNSQIENIISPDGSRKNPARNCRDLKFCHPELSSGEYWIDPNQGCKLDAIKVFCNMETGETCLSANPSSVP 1300
Cdd:smart00038    2 EEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETGETCVSPSPSSIP 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  1301 KKNWWTSpgpEKKHIWFGETMNGGFQFSYGDPDLPEeVADVQLAFLRILSSRASQNITYHCKNSIAYMDEASGNVKRALK 1380
Cdd:smart00038   82 RKTWYSG---KSKHVWFGETMNGGFKFSYGDSEGPP-VGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALR 157

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1487320837  1381 FMSSTDSEIKAEGNNKFTYTVLEDGCTKHTDEWSKTIFEYRTRKTMRLPVIDIAPFDIGASNQEFGVDVGPVCFL 1455
Cdd:smart00038  158 LRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 239-546 2.72e-30

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 125.79  E-value: 2.72e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  239 FPGLPGHKGPSGMPGMPGMKGHRGFDGKDGSKGDAGAPGLKGENGLPGENGSPGPMGPRGLPGERGRAGLPGTAGGRGND 318
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  319 GSpgaagqpgppgppgpsgfpgtpgfKGENGPAGPAGSSGPPGPKGDAgapgqpggsgppgpggrdgnpGAKGPPGAAGM 398
Cdd:NF038329   195 GP------------------------RGETGPAGEQGPAGPAGPDGEA---------------------GPAGEDGPAGP 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  399 PGapglSGARGPPGPSGTNGIPGQRGPSGEPGKNGGKGEPGPRGERGENGTPGSAGPPGEEGKagaPGQPGTNGIPGTAG 478
Cdd:NF038329   230 AG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK---DGQNGKDGLPGKDG 302

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1487320837  479 ERGAPGfrgpagpsgpggEKGAPGERGGPGSTGPRGAPGEPGRDGSPGLPgmrgltgSPGSPGVDGKP 546
Cdd:NF038329   303 KDGQNG------------KDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP-------APKTPEVPQKP 351
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 345-587 1.70e-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: 123.48  E-value: 1.70e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  345 KGENGPAGPAGSSGPPGPKGDAGAPGQPGGSGPpgpggrdgnpgaKGPPGAAGMPGAPGLSGARGPPGPSGTNGIPGQRG 424
Cdd:NF038329   119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGP------------PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  425 PSGEPGKNGGKGEPGPRGERGENGTPGSAGPPGEEGKAGAPGQPGtngiPGTAGERGAPGFRGPAGPSGPGGEKGAPGER 504
Cdd:NF038329   187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  505 GGPGSTGPRGAPGEPGRDGSPGLPGMRGLTGSPGSPGVDGKPGPSGSPGESGRSGPPGPAGPRgqpgvmGFPGPKGNEGS 584
Cdd:NF038329   263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD------GLPGKDGKDGQ 336


                   ...
gi 1487320837  585 PGK 587
Cdd:NF038329   337 PGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 193-468 5.01e-29

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 122.32  E-value: 5.01e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  193 GYQGPPGEPGQSGAPGSPGPQGMIGPPGPSGKDGEPGRPGRPGERGFPGLPGHKGPSGMPGMPGMKGHRGFDGKDGSKGD 272
Cdd:NF038329   126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  273 AGAPGLKGENGLPGENGSPGPMGPRGlPGERGRAGLPGTAggrgndgspgaagqpgppgppgpsgfpgtpgfkGENGPAG 352
Cdd:NF038329   206 QGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPT---------------------------------GEDGPQG 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  353 PAGSSGPPGPKGDagapgqpggsgppgpggrdgnpgakgpPGAAGMPGAPGLSGARGPPGPSGTNGIPGQRGPSGEPGKN 432
Cdd:NF038329   252 PDGPAGKDGPRGD---------------------------RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKD 304

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1487320837  433 GGKGEPGPRGERGENGTPGSAGPPGEEGKAGAPGQP 468
Cdd:NF038329   305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 331-557 3.93e-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: 110.38  E-value: 3.93e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  331 GPPGPSGFPGTPGFKGENGPAGPAGSSGPPGPKGDAGAPGQPGGSGPPGPGGRDGNPGAKGPPGAAGMPGAPGLSGARGP 410
Cdd:NF038329   126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  411 PGPSGTNGIPGQRGPSGEPGKNG--GKGEPGPRGERGENGTPGSAGPPGEEGKAGAPGQPGTNGIPGTAGERGapgfrgp 488
Cdd:NF038329   206 QGPAGPAGPDGEAGPAGEDGPAGpaGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG------- 278

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1487320837  489 agpsgpggEKGAPGERGGPGSTGPRGAPGEPGRDGSPGLPGMRGLTGSPGSPGVDGKPGPSGSPGESGR 557
Cdd:NF038329   279 --------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 178-475 3.52e-24

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 107.68  E-value: 3.52e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  178 GPPGPVGQPGSPGPHGYQGPPGEPGQSGAPGSPGPQGMIGPPGPSGKDGEPGRPGRPGERGFPGLPGHKGPSGMPGMPGM 257
Cdd:NF038329   132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  258 KGHRGFDGKDGSKGDAGAPGlkgenglPGENGSPGPMGPRGLPGERGRAGLPGTAGGRGNDgspgaagqpgppgppgpsg 337
Cdd:NF038329   212 AGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR------------------- 265

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  338 fpgtpgfkGENGPAGPAGSSGPPGPkgdagapgqpggsgppgpggrdgnpgaKGPPGAAGMPGAPGLSGARGPPGPSGTN 417
Cdd:NF038329   266 --------GEAGPDGPDGKDGERGP---------------------------VGPAGKDGQNGKDGLPGKDGKDGQNGKD 310

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1487320837  418 GIPGQRGPSGEPGKNggkGEPGPRGERGENGTPGSAGPPGEEGKAGAPGQPGTNGIPG 475
Cdd:NF038329   311 GLPGKDGKDGQPGKD---GLPGKDGKDGQPGKPAPKTPEVPQKPDTAPHTPKTPQIPG 365
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 724-1046 3.36e-21

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: 98.44  E-value: 3.36e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  724 GERGASGNPGPKGEKGEPGSRGGDGTPGKDGVRGPVGSIGPPGPSGQSGDKGEPGPAgphgpsgprggpgdrgeqgppgp 803
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ----------------------- 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  804 agfpgapgqnGEPGGKGERGLPGERGESGPPGIAGPSGGPGAPGPAGSSGSKGERGSPGPPGASGFPGGRGLpgppgnng 883
Cdd:NF038329   174 ----------GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQ-------- 235

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  884 psgppgnagppgkdghsgppgstgpsgppggqgpkgepgvpGEKGPAGPKGNDGITGPSGNSGIPGPRGIVGLPGSRGPI 963
Cdd:NF038329   236 -----------------------------------------GPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  964 GSIGPSGPKGEDGKPGSNGSPGERGPPgpggppgingapgepGRDGNPGSDGLPGRDGSAGPKGDRGENGPAGVPGSPGH 1043
Cdd:NF038329   275 GKDGERGPVGPAGKDGQNGKDGLPGKD---------------GKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339


                   ...
gi 1487320837 1044 MGP 1046
Cdd:NF038329   340 PAP 342
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 33-89 1.81e-20

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


Pssm-ID: 278520  Cd Length: 57  Bit Score: 85.94  E-value: 1.81e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1487320837   33 CSHLGQLYSDRDVWKPEPCQICVCDSGSVLCDEIICEekELSCTNP--EIPFGECCPIC 89
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIICP--PLDCPNPrlEIPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
33-89 7.05e-19

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 81.79  E-value: 7.05e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837    33 CSHLGQLYSDRDVWKPEPCQICVCDSGS-VLCDEIICeEKELSCTNPE--IPFGECCPIC 89
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGTtVLCDPVEC-PPPPDCPNPErvKPPGECCPRC 59
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 502-779 4.24e-16

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 82.65  E-value: 4.24e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  502 GERGGPGSTGPRGAPGEPGRDGSPGLPGMRGLTGSPGSPGVDGKPGPSGSPGESGRSGPPGPAGPRGQPGVMGFPGPKGN 581
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  582 EGSPGKNGERGGSGPPGGPGLPGKDGEPGGQGPPGPaggpgergeqgatGSPGFQGLPGPSGAPGESGKPGDPGPKGENG 661
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  662 LPGLPGGKGENGIPGERGAPGnaglpgarggpgpagpeggkgpggpvgppggmgppglqgMPGERGASGNPGPKGEKGEP 741
Cdd:NF038329   264 DRGEAGPDGPDGKDGERGPVG---------------------------------------PAGKDGQNGKDGLPGKDGKD 304

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1487320837  742 GSRGGDGTPGKDGVRGPVGSIGPPGPSGQSGDKGEPGP 779
Cdd:NF038329   305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 924-1150 3.02e-15

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: 79.95  E-value: 3.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  924 PGEKGPAGPKGNDGITGPSGNSGIPGPRGIVGLPGSRGPIGSIGPSGPKGEDGKPGSNGSPGERGPPGPGGPPGINGAPG 1003
Cdd:NF038329   128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837 1004 EPGRDGNPGSDGLPGRDGSAGPKGDrGENGPAGVPGSPGHMGPPGNAGAPGKSGERGhsgpagpagpagpagargapgpa 1083
Cdd:NF038329   208 PAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG----------------------- 263

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1487320837 1084 gargDKGEAGERGLNGMKGHRgfpgnpgspgpvgplgppgqsGSPGPAGARGPPGPSGSPGKDGRVG 1150
Cdd:NF038329   264 ----DRGEAGPDGPDGKDGER---------------------GPVGPAGKDGQNGKDGLPGKDGKDG 305
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 626-817 2.76e-13

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: 73.79  E-value: 2.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  626 EQGATGSPGFQGLPGPSGAPGESGKPGDPGPKGENGLPGLPGGKGENGIPGERGAPGNAGLPGARGGPGPAGPEGGKGPG 705
Cdd:NF038329   145 PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGED 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  706 GPVGPPGGMGPPGLQGmPGERGASGNPGPKGEKGEPGSRGGDGTPGKDGVRGPVGSIGPPGPSG---QSGDKGEPGPAGP 782
Cdd:NF038329   225 GPAGPAGDGQQGPDGD-PGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGkdgQNGKDGLPGKDGK 303

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1487320837  783 HGPSGPRGGPGDRGEQGPPGPAGFPGAPGQNGEPG 817
Cdd:NF038329   304 DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 626-835 7.99e-13

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: 72.25  E-value: 7.99e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  626 EQGATGSPGFQGLPGPSGAPGESGKPGDPGPKGENGLPGLPGGKGENGIPGERGAPGNAglpgarggpgpagpeGGKGPG 705
Cdd:NF038329   121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD---------------GEAGAK 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  706 GPVGPPGGMGPPGLQGMPGERGASGNPGPKGEKGEPGSR-----------GGDGTPGKDGVRGPVGSIGPPGPSGQSGDK 774
Cdd:NF038329   186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDgpagpagdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1487320837  775 GEPGPAGPHGPSGPRGGPGDRGEQGPPGPAGFPGAPGQNGEpggKGERGLPGERGESGPPG 835
Cdd:NF038329   266 GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQ---NGKDGLPGKDGKDGQPG 323
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 76-280 2.53e-12

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: 70.70  E-value: 2.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837   76 TNPEIPFGECCPICPNPTAVPPEKTVIRGPQGQKGDPGPPGRNGSPGIPGLPGDPGQPGPPGicQNCPDGTIfssqyGYD 155
Cdd:NF038329   143 TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG--EQGPAGPA-----GPD 215

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  156 VKAGPEPQIGtgGGFPGPPGPSGPPGPVGQPGSPGPHGYQGPPGEPGQSGAPGSPGPQGMIGPPGPSGKDGEPGRPGRPG 235
Cdd:NF038329   216 GEAGPAGEDG--PAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1487320837  236 ERGFPGLPGHKGPSGMPGMPGMKGHRGFDGKDGSKGDAGAPGLKG 280
Cdd:NF038329   294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 925-1170 1.18e-11

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 68.78  E-value: 1.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  925 GEKGPAGPKGNDGITGPSGNSGIPGPRGIVGLPGSRGPIGSIGPSGPKGEDGKPGsngspgergppgpggppgingapgE 1004
Cdd:NF038329   120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG------------------------P 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837 1005 PGRDGNPGSDGLPGRDGSAGPKGDRGENGPAGVPGSPGHMGPPGNAGAPGKSGERGhsgpagpagpagpagargapgpAG 1084
Cdd:NF038329   176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------------DG 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837 1085 ARGDKGEAGERGLNGMKGHRGfpgnpgspgpvgplgppgQSGSPGPAGARGPPGPSGSPGKDGRVGYAGPIGPPGPRGNR 1164
Cdd:NF038329   234 QQGPDGDPGPTGEDGPQGPDG------------------PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKD 295


                   ....*.
gi 1487320837 1165 GESGQA 1170
Cdd:NF038329   296 GLPGKD 301
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 955-1169 2.40e-09

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: 61.46  E-value: 2.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  955 GLPGSRGPIGSIGPSGPKGEDGKPGsngspgergppgpggppgingapgEPGRDGNPGSDGLPGRDGSAGPKGDRGENGP 1034
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRG------------------------ETGPAGPAGPPGPQGERGEKGPAGPQGEAGP 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837 1035 AGVPGSPGHMGPPGNAGAPGKSGERGHSGPAGPAGPAGPAGARGAPGPAGARGDKGEAG--ERGLNGMKGHRGFPGNPGS 1112
Cdd:NF038329   173 QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGP 252

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1487320837 1113 PGPVGPLGPPGQSGSPGPAGARGPPGPSGSPGKDGRVGYAGPIGPPGPRGNRGESGQ 1169
Cdd:NF038329   253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK 309
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
198-471 1.03e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 59.66  E-value: 1.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  198 PGEPGQSGAPGSPGPQGMIGPPGPSGKDGEPGRPGRPGERGFPGLPGHKGPSGMPGMPGMKGHRGFDGKDGSKGDAGAPG 277
Cdd:COG5164      6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  278 LKGENGLPGENGSPGPMGPRGLPGERGRAGLPGTAGGRGNDGSPGAAGQPGPPGPPGPSGFPGTPGFKGENGPAGPAGSS 357
Cdd:COG5164     86 NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGST 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  358 GPPGPKGDAGAPGQPGGsgppgpggrdgnpgakGPPGAAGMPGAPGLSGARGPPGPSGTNGIPGQRGPSGEPGKNGGKGE 437
Cdd:COG5164    166 TPPGPGGSTTPPDDGGS----------------TTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTG 229

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1487320837  438 P-GPRGERGENGTPGSAGPPGEEGKAGAPGQPGTN 471
Cdd:COG5164    230 PkDQRPKTNPIERRGPERPEAAALPAELTALEAEN 264
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 412-468 1.05e-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: 49.80  E-value: 1.05e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1487320837  412 GPSGTNGIPGQRGPSGEPGKNGGKGEPGPRGERGENGTPGSAGPPGEEGKAGAPGQP 468
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 205-259 1.40e-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: 1.40e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1487320837  205 GAPGSPGPQGMIGPPGPSGKDGEPGRPGRPGERGFPGLPGHKGPSGMPGMPGMKG 259
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1018-1170 2.32e-06

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: 51.83  E-value: 2.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837 1018 GRDGSAGPKGDRGENGPAGVPGSPGHMGPPGNAGAPGKSGERGHSGPAGPAGPAGPAGARGAPGPAGARGDKGEAGERGL 1097
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1487320837 1098 NGMKGHRGFPGNPGSPGPVGPLGPPGQSGSPGPAGaRGPPGPSGSPGKDGRVGYAGPIGPPGPRGNRGESGQA 1170
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 350-525 1.50e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.60  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  350 PAGPAGSSGPPGPKGDAGAPGQPGGSGPPGPGGRDGNPGAKGPPGAAGMPGAPGLSGARGPPGPSGTNGIPGQRGPSGEP 429
Cdd:PRK07764   615 PAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA 694

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  430 GKNGGKGEPGPRgergengtPGSAGPPGEEGKAGAPGQPGTNGIPGTAGERGAPGFRGPAGPSGPGgekGAPGERGGPGS 509
Cdd:PRK07764   695 GAAPAQPAPAPA--------ATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPA---GAPAQPPPPPA 763

                          170
                   ....*....|....*.
gi 1487320837  510 TGPRGAPGEPGRDGSP 525
Cdd:PRK07764   764 PAPAAAPAAAPPPSPP 779
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1004-1059 3.30e-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: 3.30e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1487320837 1004 EPGRDGNPGSDGLPGRDGSAGPKGDRGENGPAGVPGSPGHMGPPGNAGAPGKSGER 1059
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 1250-1287 3.47e-05

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: 42.55  E-value: 3.47e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1487320837 1250 NCRDLKFCHPELSSGEYWIDPNQGCKLDAIKVFCNMET 1287
Cdd:NF040941     1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTT 38
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1222-1454 2.21e-149

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: 452.95  E-value: 2.21e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837 1222 EILASLKSVNSQIENIISPDGSRKNPARNCRDLKFCHPELSSGEYWIDPNQGCKLDAIKVFCNMETGETCLSANPSSVPK 1301
Cdd:pfam01410    4 EVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKASIPR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837 1302 KNWWTSpgpEKKHIWFGETMNGGFQFSYGDPDLPEEVADVQLAFLRILSSRASQNITYHCKNSIAYMDEASGNVKRALKF 1381
Cdd:pfam01410   84 KNWWTK---ESKHVWFGEFMNGGSQFSYGVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKALLL 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1487320837 1382 MSSTDSEIKAEGNNKFTYTVLEDGCTKHTDEWSKTIFEYRTRKTMRLPVIDIAPFDIGASNQEFGVDVGPVCF 1454
Cdd:pfam01410  161 QGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1221-1455 1.12e-137

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: 421.88  E-value: 1.12e-137
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  1221 GEILASLKSVNSQIENIISPDGSRKNPARNCRDLKFCHPELSSGEYWIDPNQGCKLDAIKVFCNMETGETCLSANPSSVP 1300
Cdd:smart00038    2 EEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETGETCVSPSPSSIP 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  1301 KKNWWTSpgpEKKHIWFGETMNGGFQFSYGDPDLPEeVADVQLAFLRILSSRASQNITYHCKNSIAYMDEASGNVKRALK 1380
Cdd:smart00038   82 RKTWYSG---KSKHVWFGETMNGGFKFSYGDSEGPP-VGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALR 157

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1487320837  1381 FMSSTDSEIKAEGNNKFTYTVLEDGCTKHTDEWSKTIFEYRTRKTMRLPVIDIAPFDIGASNQEFGVDVGPVCFL 1455
Cdd:smart00038  158 LRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 239-546 2.72e-30

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 125.79  E-value: 2.72e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  239 FPGLPGHKGPSGMPGMPGMKGHRGFDGKDGSKGDAGAPGLKGENGLPGENGSPGPMGPRGLPGERGRAGLPGTAGGRGND 318
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  319 GSpgaagqpgppgppgpsgfpgtpgfKGENGPAGPAGSSGPPGPKGDAgapgqpggsgppgpggrdgnpGAKGPPGAAGM 398
Cdd:NF038329   195 GP------------------------RGETGPAGEQGPAGPAGPDGEA---------------------GPAGEDGPAGP 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  399 PGapglSGARGPPGPSGTNGIPGQRGPSGEPGKNGGKGEPGPRGERGENGTPGSAGPPGEEGKagaPGQPGTNGIPGTAG 478
Cdd:NF038329   230 AG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK---DGQNGKDGLPGKDG 302

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1487320837  479 ERGAPGfrgpagpsgpggEKGAPGERGGPGSTGPRGAPGEPGRDGSPGLPgmrgltgSPGSPGVDGKP 546
Cdd:NF038329   303 KDGQNG------------KDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP-------APKTPEVPQKP 351
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 345-587 1.70e-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: 123.48  E-value: 1.70e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  345 KGENGPAGPAGSSGPPGPKGDAGAPGQPGGSGPpgpggrdgnpgaKGPPGAAGMPGAPGLSGARGPPGPSGTNGIPGQRG 424
Cdd:NF038329   119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGP------------PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  425 PSGEPGKNGGKGEPGPRGERGENGTPGSAGPPGEEGKAGAPGQPGtngiPGTAGERGAPGFRGPAGPSGPGGEKGAPGER 504
Cdd:NF038329   187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  505 GGPGSTGPRGAPGEPGRDGSPGLPGMRGLTGSPGSPGVDGKPGPSGSPGESGRSGPPGPAGPRgqpgvmGFPGPKGNEGS 584
Cdd:NF038329   263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD------GLPGKDGKDGQ 336


                   ...
gi 1487320837  585 PGK 587
Cdd:NF038329   337 PGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 193-468 5.01e-29

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 122.32  E-value: 5.01e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  193 GYQGPPGEPGQSGAPGSPGPQGMIGPPGPSGKDGEPGRPGRPGERGFPGLPGHKGPSGMPGMPGMKGHRGFDGKDGSKGD 272
Cdd:NF038329   126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  273 AGAPGLKGENGLPGENGSPGPMGPRGlPGERGRAGLPGTAggrgndgspgaagqpgppgppgpsgfpgtpgfkGENGPAG 352
Cdd:NF038329   206 QGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPT---------------------------------GEDGPQG 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  353 PAGSSGPPGPKGDagapgqpggsgppgpggrdgnpgakgpPGAAGMPGAPGLSGARGPPGPSGTNGIPGQRGPSGEPGKN 432
Cdd:NF038329   252 PDGPAGKDGPRGD---------------------------RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKD 304

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1487320837  433 GGKGEPGPRGERGENGTPGSAGPPGEEGKAGAPGQP 468
Cdd:NF038329   305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 331-557 3.93e-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: 110.38  E-value: 3.93e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  331 GPPGPSGFPGTPGFKGENGPAGPAGSSGPPGPKGDAGAPGQPGGSGPPGPGGRDGNPGAKGPPGAAGMPGAPGLSGARGP 410
Cdd:NF038329   126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  411 PGPSGTNGIPGQRGPSGEPGKNG--GKGEPGPRGERGENGTPGSAGPPGEEGKAGAPGQPGTNGIPGTAGERGapgfrgp 488
Cdd:NF038329   206 QGPAGPAGPDGEAGPAGEDGPAGpaGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG------- 278

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1487320837  489 agpsgpggEKGAPGERGGPGSTGPRGAPGEPGRDGSPGLPGMRGLTGSPGSPGVDGKPGPSGSPGESGR 557
Cdd:NF038329   279 --------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 178-475 3.52e-24

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 107.68  E-value: 3.52e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  178 GPPGPVGQPGSPGPHGYQGPPGEPGQSGAPGSPGPQGMIGPPGPSGKDGEPGRPGRPGERGFPGLPGHKGPSGMPGMPGM 257
Cdd:NF038329   132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  258 KGHRGFDGKDGSKGDAGAPGlkgenglPGENGSPGPMGPRGLPGERGRAGLPGTAGGRGNDgspgaagqpgppgppgpsg 337
Cdd:NF038329   212 AGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR------------------- 265

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  338 fpgtpgfkGENGPAGPAGSSGPPGPkgdagapgqpggsgppgpggrdgnpgaKGPPGAAGMPGAPGLSGARGPPGPSGTN 417
Cdd:NF038329   266 --------GEAGPDGPDGKDGERGP---------------------------VGPAGKDGQNGKDGLPGKDGKDGQNGKD 310

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1487320837  418 GIPGQRGPSGEPGKNggkGEPGPRGERGENGTPGSAGPPGEEGKAGAPGQPGTNGIPG 475
Cdd:NF038329   311 GLPGKDGKDGQPGKD---GLPGKDGKDGQPGKPAPKTPEVPQKPDTAPHTPKTPQIPG 365
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 724-1046 3.36e-21

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: 98.44  E-value: 3.36e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  724 GERGASGNPGPKGEKGEPGSRGGDGTPGKDGVRGPVGSIGPPGPSGQSGDKGEPGPAgphgpsgprggpgdrgeqgppgp 803
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ----------------------- 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  804 agfpgapgqnGEPGGKGERGLPGERGESGPPGIAGPSGGPGAPGPAGSSGSKGERGSPGPPGASGFPGGRGLpgppgnng 883
Cdd:NF038329   174 ----------GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQ-------- 235

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  884 psgppgnagppgkdghsgppgstgpsgppggqgpkgepgvpGEKGPAGPKGNDGITGPSGNSGIPGPRGIVGLPGSRGPI 963
Cdd:NF038329   236 -----------------------------------------GPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  964 GSIGPSGPKGEDGKPGSNGSPGERGPPgpggppgingapgepGRDGNPGSDGLPGRDGSAGPKGDRGENGPAGVPGSPGH 1043
Cdd:NF038329   275 GKDGERGPVGPAGKDGQNGKDGLPGKD---------------GKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339


                   ...
gi 1487320837 1044 MGP 1046
Cdd:NF038329   340 PAP 342
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 33-89 1.81e-20

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


Pssm-ID: 278520  Cd Length: 57  Bit Score: 85.94  E-value: 1.81e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1487320837   33 CSHLGQLYSDRDVWKPEPCQICVCDSGSVLCDEIICEekELSCTNP--EIPFGECCPIC 89
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIICP--PLDCPNPrlEIPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
33-89 7.05e-19

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 81.79  E-value: 7.05e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837    33 CSHLGQLYSDRDVWKPEPCQICVCDSGS-VLCDEIICeEKELSCTNPE--IPFGECCPIC 89
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGTtVLCDPVEC-PPPPDCPNPErvKPPGECCPRC 59
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 502-779 4.24e-16

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 82.65  E-value: 4.24e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  502 GERGGPGSTGPRGAPGEPGRDGSPGLPGMRGLTGSPGSPGVDGKPGPSGSPGESGRSGPPGPAGPRGQPGVMGFPGPKGN 581
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  582 EGSPGKNGERGGSGPPGGPGLPGKDGEPGGQGPPGPaggpgergeqgatGSPGFQGLPGPSGAPGESGKPGDPGPKGENG 661
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  662 LPGLPGGKGENGIPGERGAPGnaglpgarggpgpagpeggkgpggpvgppggmgppglqgMPGERGASGNPGPKGEKGEP 741
Cdd:NF038329   264 DRGEAGPDGPDGKDGERGPVG---------------------------------------PAGKDGQNGKDGLPGKDGKD 304

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1487320837  742 GSRGGDGTPGKDGVRGPVGSIGPPGPSGQSGDKGEPGP 779
Cdd:NF038329   305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 924-1150 3.02e-15

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: 79.95  E-value: 3.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  924 PGEKGPAGPKGNDGITGPSGNSGIPGPRGIVGLPGSRGPIGSIGPSGPKGEDGKPGSNGSPGERGPPGPGGPPGINGAPG 1003
Cdd:NF038329   128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837 1004 EPGRDGNPGSDGLPGRDGSAGPKGDrGENGPAGVPGSPGHMGPPGNAGAPGKSGERGhsgpagpagpagpagargapgpa 1083
Cdd:NF038329   208 PAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG----------------------- 263

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1487320837 1084 gargDKGEAGERGLNGMKGHRgfpgnpgspgpvgplgppgqsGSPGPAGARGPPGPSGSPGKDGRVG 1150
Cdd:NF038329   264 ----DRGEAGPDGPDGKDGER---------------------GPVGPAGKDGQNGKDGLPGKDGKDG 305
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 626-817 2.76e-13

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: 73.79  E-value: 2.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  626 EQGATGSPGFQGLPGPSGAPGESGKPGDPGPKGENGLPGLPGGKGENGIPGERGAPGNAGLPGARGGPGPAGPEGGKGPG 705
Cdd:NF038329   145 PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGED 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  706 GPVGPPGGMGPPGLQGmPGERGASGNPGPKGEKGEPGSRGGDGTPGKDGVRGPVGSIGPPGPSG---QSGDKGEPGPAGP 782
Cdd:NF038329   225 GPAGPAGDGQQGPDGD-PGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGkdgQNGKDGLPGKDGK 303

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1487320837  783 HGPSGPRGGPGDRGEQGPPGPAGFPGAPGQNGEPG 817
Cdd:NF038329   304 DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 626-835 7.99e-13

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: 72.25  E-value: 7.99e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  626 EQGATGSPGFQGLPGPSGAPGESGKPGDPGPKGENGLPGLPGGKGENGIPGERGAPGNAglpgarggpgpagpeGGKGPG 705
Cdd:NF038329   121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD---------------GEAGAK 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  706 GPVGPPGGMGPPGLQGMPGERGASGNPGPKGEKGEPGSR-----------GGDGTPGKDGVRGPVGSIGPPGPSGQSGDK 774
Cdd:NF038329   186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDgpagpagdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1487320837  775 GEPGPAGPHGPSGPRGGPGDRGEQGPPGPAGFPGAPGQNGEpggKGERGLPGERGESGPPG 835
Cdd:NF038329   266 GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQ---NGKDGLPGKDGKDGQPG 323
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 76-280 2.53e-12

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: 70.70  E-value: 2.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837   76 TNPEIPFGECCPICPNPTAVPPEKTVIRGPQGQKGDPGPPGRNGSPGIPGLPGDPGQPGPPGicQNCPDGTIfssqyGYD 155
Cdd:NF038329   143 TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG--EQGPAGPA-----GPD 215

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  156 VKAGPEPQIGtgGGFPGPPGPSGPPGPVGQPGSPGPHGYQGPPGEPGQSGAPGSPGPQGMIGPPGPSGKDGEPGRPGRPG 235
Cdd:NF038329   216 GEAGPAGEDG--PAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1487320837  236 ERGFPGLPGHKGPSGMPGMPGMKGHRGFDGKDGSKGDAGAPGLKG 280
Cdd:NF038329   294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 925-1170 1.18e-11

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 68.78  E-value: 1.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  925 GEKGPAGPKGNDGITGPSGNSGIPGPRGIVGLPGSRGPIGSIGPSGPKGEDGKPGsngspgergppgpggppgingapgE 1004
Cdd:NF038329   120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG------------------------P 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837 1005 PGRDGNPGSDGLPGRDGSAGPKGDRGENGPAGVPGSPGHMGPPGNAGAPGKSGERGhsgpagpagpagpagargapgpAG 1084
Cdd:NF038329   176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------------DG 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837 1085 ARGDKGEAGERGLNGMKGHRGfpgnpgspgpvgplgppgQSGSPGPAGARGPPGPSGSPGKDGRVGYAGPIGPPGPRGNR 1164
Cdd:NF038329   234 QQGPDGDPGPTGEDGPQGPDG------------------PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKD 295


                   ....*.
gi 1487320837 1165 GESGQA 1170
Cdd:NF038329   296 GLPGKD 301
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 955-1169 2.40e-09

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: 61.46  E-value: 2.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  955 GLPGSRGPIGSIGPSGPKGEDGKPGsngspgergppgpggppgingapgEPGRDGNPGSDGLPGRDGSAGPKGDRGENGP 1034
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRG------------------------ETGPAGPAGPPGPQGERGEKGPAGPQGEAGP 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837 1035 AGVPGSPGHMGPPGNAGAPGKSGERGHSGPAGPAGPAGPAGARGAPGPAGARGDKGEAG--ERGLNGMKGHRGFPGNPGS 1112
Cdd:NF038329   173 QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGP 252

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1487320837 1113 PGPVGPLGPPGQSGSPGPAGARGPPGPSGSPGKDGRVGYAGPIGPPGPRGNRGESGQ 1169
Cdd:NF038329   253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK 309
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
198-471 1.03e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 59.66  E-value: 1.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  198 PGEPGQSGAPGSPGPQGMIGPPGPSGKDGEPGRPGRPGERGFPGLPGHKGPSGMPGMPGMKGHRGFDGKDGSKGDAGAPG 277
Cdd:COG5164      6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  278 LKGENGLPGENGSPGPMGPRGLPGERGRAGLPGTAGGRGNDGSPGAAGQPGPPGPPGPSGFPGTPGFKGENGPAGPAGSS 357
Cdd:COG5164     86 NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGST 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  358 GPPGPKGDAGAPGQPGGsgppgpggrdgnpgakGPPGAAGMPGAPGLSGARGPPGPSGTNGIPGQRGPSGEPGKNGGKGE 437
Cdd:COG5164    166 TPPGPGGSTTPPDDGGS----------------TTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTG 229

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1487320837  438 P-GPRGERGENGTPGSAGPPGEEGKAGAPGQPGTN 471
Cdd:COG5164    230 PkDQRPKTNPIERRGPERPEAAALPAELTALEAEN 264
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 412-468 1.05e-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: 49.80  E-value: 1.05e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1487320837  412 GPSGTNGIPGQRGPSGEPGKNGGKGEPGPRGERGENGTPGSAGPPGEEGKAGAPGQP 468
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
389-586 1.13e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 56.19  E-value: 1.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  389 AKGPPGAAGMPGAPGLSGARGPPGPSGTNGIPGQRGPSGEPGKNGGKGEPGPRGERGENGTPGSAGPPGEEGKAGAPGQP 468
Cdd:COG5164     26 STKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDG 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  469 GTNGIPGTAGERGAPGfRGPAGPSGPGGEKGAPGERG----GPGSTGPRGAPGEPGRDGSPGLPGMRGLTGSPGSPGVDG 544
Cdd:COG5164    106 GATGPPDDGGATGPPD-DGGSTTPPSGGSTTPPGDGGstppGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTT 184

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1487320837  545 KPGP--SGSPGESGRSGPPGPAGPRGQPGVMGFPGPKGNEGSPG 586
Cdd:COG5164    185 PPNKgeTGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKT 228
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 397-453 1.31e-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: 1.31e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1487320837  397 GMPGAPGLSGARGPPGPSGTNGIPGQRGPSGEPGKNGGKGEPGPRGERGENGTPGSA 453
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 205-259 1.40e-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: 1.40e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1487320837  205 GAPGSPGPQGMIGPPGPSGKDGEPGRPGRPGERGFPGLPGHKGPSGMPGMPGMKG 259
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 499-554 1.99e-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: 46.33  E-value: 1.99e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1487320837  499 GAPGERGGPGSTGPRGAPGEPGRDGSPGLPGMRGLTGSPGSPGVDGKPGPSGSPGE 554
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1018-1170 2.32e-06

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: 51.83  E-value: 2.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837 1018 GRDGSAGPKGDRGENGPAGVPGSPGHMGPPGNAGAPGKSGERGHSGPAGPAGPAGPAGARGAPGPAGARGDKGEAGERGL 1097
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1487320837 1098 NGMKGHRGFPGNPGSPGPVGPLGPPGQSGSPGPAGaRGPPGPSGSPGKDGRVGYAGPIGPPGPRGNRGESGQA 1170
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 421-475 2.38e-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: 2.38e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1487320837  421 GQRGPSGEPGKNGGKGEPGPRGERGENGTPGSAGPPGEEGKAGAPGQPGTNGIPG 475
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 193-248 2.50e-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: 2.50e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1487320837  193 GYQGPPGEPGQSGAPGSPGPQGMIGPPGPSGKDGEPGRPGRPGERGFPGLPGHKGP 248
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 502-556 3.35e-06

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.56  E-value: 3.35e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1487320837  502 GERGGPGSTGPRGAPGEPGRDGSPGLPGMRGLTGSPGSPGVDGKPGPSGSPGESG 556
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 427-483 3.81e-06

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.56  E-value: 3.81e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1487320837  427 GEPGKNGGKGEPGPRGERGENGTPGSAGPPGEEGKAGAPGQPGTNGIPGTAGERGAP 483
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 430-484 8.36e-06

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.41  E-value: 8.36e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1487320837  430 GKNGGKGEPGPRGERGENGTPGSAGPPGEEGKAGAPGQPGTNGIPGTAGERGAPG 484
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 350-525 1.50e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.60  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  350 PAGPAGSSGPPGPKGDAGAPGQPGGSGPPGPGGRDGNPGAKGPPGAAGMPGAPGLSGARGPPGPSGTNGIPGQRGPSGEP 429
Cdd:PRK07764   615 PAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA 694

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  430 GKNGGKGEPGPRgergengtPGSAGPPGEEGKAGAPGQPGTNGIPGTAGERGAPGFRGPAGPSGPGgekGAPGERGGPGS 509
Cdd:PRK07764   695 GAAPAQPAPAPA--------ATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPA---GAPAQPPPPPA 763

                          170
                   ....*....|....*.
gi 1487320837  510 TGPRGAPGEPGRDGSP 525
Cdd:PRK07764   764 PAPAAAPAAAPPPSPP 779
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 232-288 1.51e-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: 1.51e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1487320837  232 GRPGERGFPGLPGHKGPSGMPGMPGMKGHRGFDGKDGSKGDAGAPGLKGENGLPGEN 288
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 389-554 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 1487320837  389 AKGPPGAAGMPGAPGLSGARGPPGPSGTNGIPGQ----RGPSGEPGKNGGKGEPGPRGERGENGTPGSAGPPGEEGKAGA 464
Cdd:PRK07764   605 SSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEasaaPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPA 684

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  465 PGQPGTNGIPGTAGERGAPGFRGPAGPSGPGGEKGA-PGERGGPGSTGPRGAPGEPGRDGSPGLPGMRGLTGSPGSPGVD 543
Cdd:PRK07764   685 PAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQpPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAP 764

                          170
                   ....*....|.
gi 1487320837  544 GKPGPSGSPGE 554
Cdd:PRK07764   765 APAAAPAAAPP 775
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 350-558 2.48e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 49.01  E-value: 2.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  350 PAGPAGSSGPPGPKGDAGAPGQPGGSGPPGPGGRDGNPGAKGPPGAAGMPGAPGLSGARGPPGPSGTNGIPGQRGPSGEP 429
Cdd:PHA03307   118 PPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPST 197

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  430 GKNGGKGEPGPRGERGENGTPGSAGPPGEEGKAGAPGQPGTNGIPGTAG-------ERGAPGFRGPAGPSGPGGEKGAPG 502
Cdd:PHA03307   198 PPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGcgwgpenECPLPRPAPITLPTRIWEASGWNG 277

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1487320837  503 ERGGPGSTGPRGAPGEPGRDGSPGLPGMRGLTGSPGSPGVDGKPGPSGSPGESGRS 558
Cdd:PHA03307   278 PSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSS 333
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1004-1059 3.30e-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: 3.30e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1487320837 1004 EPGRDGNPGSDGLPGRDGSAGPKGDRGENGPAGVPGSPGHMGPPGNAGAPGKSGER 1059
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 1250-1287 3.47e-05

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: 42.55  E-value: 3.47e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1487320837 1250 NCRDLKFCHPELSSGEYWIDPNQGCKLDAIKVFCNMET 1287
Cdd:NF040941     1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTT 38
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 247-303 3.61e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 3.61e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1487320837  247 GPSGMPGMPGMKGHRGFDGKDGSKGDAGAPGLKGENGLPGENGSPGPMGPRGLPGER 303
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 389-441 6.08e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 6.08e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1487320837  389 AKGPPGAAGMPGAPGLSGARGPPGPSGTNGIPGQRGPSGEPGKNGGKGEPGPR 441
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 724-780 1.30e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 1.30e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1487320837  724 GERGASGNPGPKGEKGEPGSRGGDGTPGKDGVRGPVGSIGPPGPSGQSGDKGEPGPA 780
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 346-555 1.85e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  346 GENGPAGPAGSSGPPGPKGDAGAPGQPGGSGPPGPGGRDGNPGAKGPPGAAGMPGAPGLSGARGPPGPSGTNGIPGQRGP 425
Cdd:PRK07764   589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDG 668

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  426 SGEPGKNGGKGEPGPRgergengtPGSAGPPGEEGKAGAPGQPGtngipGTAGERGAPGFRGPAGPSGPGGEKGAPGERG 505
Cdd:PRK07764   669 WPAKAGGAAPAAPPPA--------PAPAAPAAPAGAAPAQPAPA-----PAATPPAGQADDPAAQPPQAAQGASAPSPAA 735

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1487320837  506 GPGSTGPRGAPGEPGRDGSPGLPGMRGLTGSPGSPGVDGKPGPSGSPGES 555
Cdd:PRK07764   736 DDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEM 785
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 497-548 3.82e-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: 3.82e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1487320837  497 EKGAPGERGGPGSTGPRGAPGEPGRDGSPGLPGMRGLTGSPGSPGVDGKPGP 548
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 198-553 3.89e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 3.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  198 PGEPGQSGAPGSPGPQGMIGPPGPSGKDGEPGRPGRPGERGFPGLPGHKGPSGMPGMPGMKGhrgfdgkDGSKGDAGAPG 277
Cdd:PHA03307    99 SPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPA-------AVASDAASSRQ 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  278 LKGENGLPGENGSPGPMGPRGLPGERGRAGLPGTAGGRGNDGSPGAagqpgppgppgpsgfpgtpgfkGENGPAGPAGSS 357
Cdd:PHA03307   172 AALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASA----------------------SSPAPAPGRSAA 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  358 GPPGPKGDAGAPGQPGGSGPPGPGGRDGNPGAKGPPGAAGMPGAPGLSGARGpPGPSGTNGIPGQRGPSGEPGKNGGKGE 437
Cdd:PHA03307   230 DDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSR-PGPASSSSSPRERSPSPSPSSPGSGPA 308

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  438 PGPRGERGENGTPGSAGPPGEEGKAGAPGQPGTNgiPGTAGERGAPGFRGPAGPSGPGGEKGAPGERGGPGSTGPRG--- 514
Cdd:PHA03307   309 PSSPRASSSSSSSRESSSSSTSSSSESSRGAAVS--PGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGrpt 386

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1487320837  515 --------APGEPGRDGSPGLPGMRGLTGSPGSPGVDGKPGPSGSPG 553
Cdd:PHA03307   387 rrraraavAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYPLL 433
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 460-528 5.03e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 5.03e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1487320837  460 GKAGAPGQPGTNGIPGTAGERGAPGfrgpagpsgpggEKGAPGERGGPGSTGPRGAPGEPGRDGSPGLP 528
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPG------------PPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 389-558 6.07e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 6.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  389 AKGPPGAAGMPGAPGLSGARGPPGPSGTNGIPGQRGPSGEPGKNGGKGEPGPRGERGENGTPGSAGPPGEEGKAGAPGQP 468
Cdd:PRK07764   594 AAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKA 673

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  469 GTNGIPGTAGERGAPGFRGPAGPSGPGGEKGAPGERGGPGSTGPRGAPGEPGRDGSPGLPGMRGLTGSPGSPGVDGKPGP 548
Cdd:PRK07764   674 GGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAG 753

                          170
                   ....*....|
gi 1487320837  549 SGSPGESGRS 558
Cdd:PRK07764   754 APAQPPPPPA 763
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 253-310 7.24e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 7.24e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1487320837  253 GMPGMKGHRGFDGKDGSKGDAGAPGLKGEnglPGENGSPGPMGPRGLPGERGRAGLPG 310
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGP---PGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 391-523 7.96e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 43.90  E-value: 7.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  391 GPPGAAGMPG-APGLSGARGPPG---PSGTNGIPGQRGPSGEPGKNGGKGEPGPRgergengTPGSAGPPGEEGKAGAPG 466
Cdd:PRK14959   379 SAPSGSAAEGpASGGAATIPTPGtqgPQGTAPAAGMTPSSAAPATPAPSAAPSPR-------VPWDDAPPAPPRSGIPPR 451

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1487320837  467 qpGTNGIPGTAGERGAPgfrgpagpSGPGGEKGAPGERGGPGSTGPRGAPGEPGRDG 523
Cdd:PRK14959   452 --PAPRMPEASPVPGAP--------DSVASASDAPPTLGDPSDTAEHTPSGPRTWDG 498
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1015-1060 1.09e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 1.09e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1487320837 1015 GLPGRDGSAGPKGDRGENGPAGVPGSPGHMGPPGNAGAPGKSGERG 1060
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 268-317 1.46e-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: 1.46e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1487320837  268 GSKGDAGAPGLKGENGLPGENGSPGPMGPRGLPGERGRAGLPGTAGGRGN 317
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 427-548 1.55e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 43.13  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  427 GEPGKNGGKGEPGP-RGERGENGTPGSAGPpgeEGKAGAPGQPGTNGIPGTAGERGAPGFRGPAGPSGPggekgAPGERG 505
Cdd:PRK14959   376 GGASAPSGSAAEGPaSGGAATIPTPGTQGP---QGTAPAAGMTPSSAAPATPAPSAAPSPRVPWDDAPP-----APPRSG 447

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1487320837  506 GPgstgPRGAPGEPGRDGSPGLP-GMRGLTGSPGSPGVDGKPGP 548
Cdd:PRK14959   448 IP----PRPAPRMPEASPVPGAPdSVASASDAPPTLGDPSDTAE 487
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 199-414 1.77e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  199 GEPGQSGAPGSPGPQGMIGP-----PGPSGKDGEPGRPGRPGERGFPGLPGHKGPSGMPGMPGMKGHRGFDgkDGSKGDA 273
Cdd:PRK07764   590 PAPGAAGGEGPPAPASSGPPeeaarPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVP--DASDGGD 667

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  274 GAPGLKGENGLPGENGSPGPMGPRGLPGERGRAGLPGTAGGRGNDGSPGAAgqpgppgppgpsgfpgtpgfkgeNGPAGP 353
Cdd:PRK07764   668 GWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPA-----------------------AQPPQA 724

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1487320837  354 AGSSGPPGPKGDAGAPGQPGGSGPPGPGGRDGNPGAKGPPGAAGMPGAPGLSGARGPPGPS 414
Cdd:PRK07764   725 AQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEM 785
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 448-519 1.96e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 1.96e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1487320837  448 GTPGSAGPPGEEGKAGAPGQPGTNGIPGTAGERGAPgfrgpagpsgpggekGAPGERGGPGSTGPRGAPGEP 519
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPP---------------GPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 265-319 2.10e-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: 2.10e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1487320837  265 GKDGSKGDAGAPGLKGENGLPGENGSPGPMGPRGLPGERGRAGLPGTAGGRGNDG 319
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 400-598 2.30e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  400 GAPGLSGARGPPGPSGTNGIPGQR---GPSGEPGKNGGKGEPGPRGERGENGTPGSAGPPGEEGKAGAPGQPGTNGIPGT 476
Cdd:PRK07764   590 PAPGAAGGEGPPAPASSGPPEEAArpaAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  477 AGERGAPGfrgpagpsgpggekgAPGERGGPGSTGPRGAPGEPGRDGSPGLPgmrglTGSPGSPGVDGKPGPSGSPGESG 556
Cdd:PRK07764   670 PAKAGGAA---------------PAAPPPAPAPAAPAAPAGAAPAQPAPAPA-----ATPPAGQADDPAAQPPQAAQGAS 729

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1487320837  557 RSGPPGPAGPRGQPGVMGFPGPKGNEGSPGKNGERGGSGPPG 598
Cdd:PRK07764   730 APSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPA 771
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 720-767 2.99e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 2.99e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1487320837  720 QGMPGERGASGNPGPKGEKGEPGSRGGDGTPGKDGVRGPVGSIGPPGP 767
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 273-459 3.54e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 3.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  273 AGAPGLKGENGLPGENGSPGPMGPRGLPGERGRAGLPGTAGGRGNDGSPGAAGQPGPPGPPGPSGFPGTPGFKGENGPAG 352
Cdd:PRK07764   589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDG 668

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  353 PAGSSGPPGPKGDAGAPGQPGGSGPPGPGGR----DGNPGAKGPPGAAGMPGAPGLSGARGPPGPSGTNGIPGQRGPSGE 428
Cdd:PRK07764   669 WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAqpapAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDP 748

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1487320837  429 PGKNGGKGEPGPRGERGENGTPGSAGPPGEE 459
Cdd:PRK07764   749 PDPAGAPAQPPPPPAPAPAAAPAAAPPPSPP 779
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 722-772 3.57e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 3.57e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1487320837  722 MPGERGASGNPGPKGEKGEPGSRGGDGTPGKDGVRGPVGSIGPPGPSGQSG 772
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 349-429 3.90e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 3.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  349 GPAGPAGSSGPPGPKGdagapgqpggsgppgpggrdgnpgAKGPPGAAGMPGAPGLSGARGPPGPSGTNGIPGQRGPSGE 428
Cdd:pfam01391    1 GPPGPPGPPGPPGPPG------------------------PPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56


                   .
gi 1487320837  429 P 429
Cdd:pfam01391   57 P 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 301-522 5.50e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 5.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  301 GERGRAGLPGTAGGRGNdGSPGAAGQPGPPGPPGPSGFPGTPGFKGENGPA--GPAGSSGPPGPKGDAGAPGQPGGSGPP 378
Cdd:PRK07764   590 PAPGAAGGEGPPAPASS-GPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEAsaAPAPGVAAPEHHPKHVAVPDASDGGDG 668

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487320837  379 GPGGRDGNPGAKGPPGAAGMPGAPGLSGARGPPGPSGTNGIPGQRGPSGEPGKNGGKGEPGPRGERGENGTPGSAGPPGE 458
Cdd:PRK07764   669 WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDP 748

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1487320837  459 EGKAGAPGQPGTNGIPGTAGERGAPgfrgpAGPSGPGGEKGAPGERGGPGSTGPRGAPGEPGRD 522
Cdd:PRK07764   749 PDPAGAPAQPPPPPAPAPAAAPAAA-----PPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVAME 807
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
33-87 7.18e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 36.39  E-value: 7.18e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1487320837    33 CSHLGQLYSDRDVWKpEPCQICVCDSGSVLCDEIICEEKE--LSCTNPEIPFGECCP 87
Cdd:smart00215    1 CWNNGSYYPPGAKWD-DDCNRCTCLNGRVSCTKVWCGPKPclLHNLSGECPLGQGCV 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 924-971 8.75e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.93  E-value: 8.75e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1487320837  924 PGEKGPAGPKGNDGITGPSGNSGIPGPRGIVGLPGSRGPIGSIGPSGP 971
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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