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Conserved domains on  [gi|166064040|ref|NP_112440|]
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collagen alpha-1(II) chain isoform 1 preproprotein [Mus musculus]

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 ...
 1251-1486 1.61e-163

Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


:

Pssm-ID: 460199  Cd Length: 233  Bit Score: 491.09  E-value: 1.61e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  1251 HDVEVDATLKSLNNQIESIRSPDGSRKNPARTCQDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPAT 1330
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKAS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  1331 VPRKNWWSsksKEKKHIWFGETMNGGFHFSYGDGNLAPNTANVQMTFLRLLSTEGSQNITYHCKNSIAYLDEAAGNLKKA 1410
Cdd:pfam01410   81 IPRKNWWT---KESKHVWFGEFMNGGSQFSYGVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKA 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166064040  1411 LLIQGSNDVEMRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGAEQEFGVDIGPVCF 1486
Cdd:pfam01410  158 LLLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 801-1011 1.88e-34

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 138.50  E-value: 1.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  801 GEKGEVGPPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAG---QKGDAGAPGPQGPSGAPGPQGP 877
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGpqgPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  878 TGVTGPKGARGAQGPPGATGFPGAAGRVGPPGANGNP--------GPAGPPGPAGKDGPKGVRGDSGPPGRAGDPGLQGP 949
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdgdpGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166064040  950 AGAPGEKGEPGDDGPSGLDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPG 1011
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 393-636 5.59e-27

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 116.16  E-value: 5.59e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  393 GEPGNPGSPGPAGASGNPGTDGIPGAKGSAGApgiagapgfpgprgppgpqgaTGPLGPKGQAGEPGIAGFKGDQGPKGE 472
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGP---------------------AGPPGPQGERGEKGPAGPQGEAGPQGP 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  473 TGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGaPGERGPSGLTGPKGANGDPGRPG 552
Cdd:NF038329  176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDG 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  553 EPGLPGARGLTGRPGDAGPQGKVGPSGapgedgRPGPPGPQGARGQPGVMGFPGPKGANGEPGKAGEKGLAGAPGLRGLP 632
Cdd:NF038329  255 PAGKDGPRGDRGEAGPDGPDGKDGERG------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328


                  ....
gi 166064040  633 GKDG 636
Cdd:NF038329  329 GKDG 332
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 650-877 1.44e-26

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 114.62  E-value: 1.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  650 AGERGEQGAPGPSGFQGLPGPPGPPGEGGKQGDQGIPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDG 729
Cdd:NF038329  128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  730 PKGAAGPDGPPGAQGPPGLQGMPGeRGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGltgpigppgpagANGEKGEVGPP 809
Cdd:NF038329  208 PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG------------DRGEAGPDGPD 274

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166064040  810 GPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGP 877
Cdd:NF038329  275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 34-88 2.78e-25

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


:

Pssm-ID: 278520  Cd Length: 57  Bit Score: 99.81  E-value: 2.78e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 166064040    34 CLQNGQRYKDKDVWKPSSCRICVCDTGNVLCDDIICEDPDCLNP--EIPFGECCPIC 88
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIICPPLDCPNPrlEIPPGECCPVC 57
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 939-1134 4.64e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 110.38  E-value: 4.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  939 GRAGDPGLQGPAGAPGEKGEPGDDGPSGLDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGP 1018
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040 1019 PGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGvKGDRGETGALGAPGAPGPPGSPGPAGPTGKQGDRGEAGAQGPMG 1098
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 166064040 1099 PSGPAGARGIAGPQGPRGDKGESGEQGERGLKGHRG 1134
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 255-490 2.06e-19

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 93.05  E-value: 2.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  255 GEAGKPGKSGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERGR 334
Cdd:NF038329  123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGP 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  335 TGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPGaKGEAGPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDG 414
Cdd:NF038329  203 AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGD-PGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166064040  415 IPGAKGSAGAPGiagapgfpgprgppgpqgATGPLGPKGQAGEPGIAGFKGDQGPKGETGPAGPQGAPGPAGEEGK 490
Cdd:NF038329  282 PVGPAGKDGQNG------------------KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1251-1486 1.61e-163

Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 460199  Cd Length: 233  Bit Score: 491.09  E-value: 1.61e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  1251 HDVEVDATLKSLNNQIESIRSPDGSRKNPARTCQDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPAT 1330
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKAS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  1331 VPRKNWWSsksKEKKHIWFGETMNGGFHFSYGDGNLAPNTANVQMTFLRLLSTEGSQNITYHCKNSIAYLDEAAGNLKKA 1410
Cdd:pfam01410   81 IPRKNWWT---KESKHVWFGEFMNGGSQFSYGVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKA 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166064040  1411 LLIQGSNDVEMRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGAEQEFGVDIGPVCF 1486
Cdd:pfam01410  158 LLLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1252-1487 8.53e-153

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: 462.71  E-value: 8.53e-153
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040   1252 DVEVDATLKSLNNQIESIRSPDGSRKNPARTCQDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPATV 1331
Cdd:smart00038    1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETGETCVSPSPSSI 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040   1332 PRKNWWSSKSKekkHIWFGETMNGGFHFSYGDGNLAPnTANVQMTFLRLLSTEGSQNITYHCKNSIAYLDEAAGNLKKAL 1411
Cdd:smart00038   81 PRKTWYSGKSK---HVWFGETMNGGFKFSYGDSEGPP-VGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKAL 156

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166064040   1412 LIQGSNDVEMRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGAEQEFGVDIGPVCFL 1487
Cdd:smart00038  157 RLRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 801-1011 1.88e-34

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 138.50  E-value: 1.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  801 GEKGEVGPPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAG---QKGDAGAPGPQGPSGAPGPQGP 877
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGpqgPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  878 TGVTGPKGARGAQGPPGATGFPGAAGRVGPPGANGNP--------GPAGPPGPAGKDGPKGVRGDSGPPGRAGDPGLQGP 949
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdgdpGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166064040  950 AGAPGEKGEPGDDGPSGLDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPG 1011
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 822-1056 2.07e-33

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 135.42  E-value: 2.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  822 GERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGA 901
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  902 AGRVGPPGANGNPGPAGPPGPAGKDGPKGV-----RGDSGPPGRAGDPGLQGPAGAPGEKGEPGDDGPSGLDGPPGPQGL 976
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPagpagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  977 AGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASgdrgppgpvgppgltgpaGEPGREGSPGADGPPGRDGAAGVKG 1056
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLP------------------GKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 703-954 2.67e-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: 123.09  E-value: 2.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  703 FPGERGSPGAQGLQGPRGLPGTPGTDGPKGAAGPDGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKD 782
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  783 GGRGLTGPIGPPGPAGANGEKGEVGPPGPSGSTGARGaPGERGETGPPGPAGFAGPPGADGQPgakgdqGEAGQKGDAGA 862
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA------GKDGPRGDRGE 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  863 PGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGrvgppgangnpgpagppgpagKDGPKGVRGDSGPPGRAG 942
Cdd:NF038329  268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG---------------------KDGLPGKDGKDGQPGKDG 326

                         250
                  ....*....|..
gi 166064040  943 DPGLQGPAGAPG 954
Cdd:NF038329  327 LPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 393-636 5.59e-27

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 116.16  E-value: 5.59e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  393 GEPGNPGSPGPAGASGNPGTDGIPGAKGSAGApgiagapgfpgprgppgpqgaTGPLGPKGQAGEPGIAGFKGDQGPKGE 472
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGP---------------------AGPPGPQGERGEKGPAGPQGEAGPQGP 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  473 TGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGaPGERGPSGLTGPKGANGDPGRPG 552
Cdd:NF038329  176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDG 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  553 EPGLPGARGLTGRPGDAGPQGKVGPSGapgedgRPGPPGPQGARGQPGVMGFPGPKGANGEPGKAGEKGLAGAPGLRGLP 632
Cdd:NF038329  255 PAGKDGPRGDRGEAGPDGPDGKDGERG------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328


                  ....
gi 166064040  633 GKDG 636
Cdd:NF038329  329 GKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 650-877 1.44e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 114.62  E-value: 1.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  650 AGERGEQGAPGPSGFQGLPGPPGPPGEGGKQGDQGIPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDG 729
Cdd:NF038329  128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  730 PKGAAGPDGPPGAQGPPGLQGMPGeRGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGltgpigppgpagANGEKGEVGPP 809
Cdd:NF038329  208 PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG------------DRGEAGPDGPD 274

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166064040  810 GPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGP 877
Cdd:NF038329  275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 440-661 1.25e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.92  E-value: 1.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  440 PGPQGATGPLGPKGQAGEPGIAGFKGDQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPG 519
Cdd:NF038329  128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  520 QDGLAGPKGAPGERGPSGLTGPKGangdPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQP 599
Cdd:NF038329  208 PAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV 283

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166064040  600 GVMGFPGPKGANGEPGKAGEKGLAGAPglrGLPGKDGETGAAGPPGPSGPAGERGEQGAPGP 661
Cdd:NF038329  284 GPAGKDGQNGKDGLPGKDGKDGQNGKD---GLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 846-1115 1.48e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.92  E-value: 1.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  846 GAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGrvgppgangnpgpagPpgpAGK 925
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG---------------P---AGK 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  926 DGPKGVRGDSGPPGRAGDPGLQGPAGAPGEKGEPGDDGPSGLDGPPGPQGLAGQrGIVGLPGQRGERGFPGLPGPSGEPG 1005
Cdd:NF038329  179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAG 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040 1006 KQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGdrgetgalgapgapgppgspgpagPTGKQ 1085
Cdd:NF038329  258 KDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG------------------------KDGLP 313

                         250       260       270
                  ....*....|....*....|....*....|
gi 166064040 1086 GDRGEAGAQGPMGPSGPAGARGIAGPQGPR 1115
Cdd:NF038329  314 GKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 34-88 2.78e-25

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 99.81  E-value: 2.78e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 166064040    34 CLQNGQRYKDKDVWKPSSCRICVCDTGNVLCDDIICEDPDCLNP--EIPFGECCPIC 88
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIICPPLDCPNPrlEIPPGECCPVC 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 459-732 3.46e-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: 110.77  E-value: 3.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  459 GIAGFKGDqGPKGETGPAGPQGAPGPAGEEGKRGArgepggagpigpPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGL 538
Cdd:NF038329  109 GLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGE------------TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  539 TGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGaPGEDGRPGPPGPQGARGQPGVMGFPGPKGANGEPGKAG 618
Cdd:NF038329  176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG-EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDG 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  619 EKGLAGAPGLRGLPGKDGetgaagppgPSGPAGERGEQGAPGpsgfqglpgppgppgeggkqgDQGIPGEAGAPGLVGPR 698
Cdd:NF038329  255 PAGKDGPRGDRGEAGPDG---------PDGKDGERGPVGPAG---------------------KDGQNGKDGLPGKDGKD 304

                         250       260       270
                  ....*....|....*....|....*....|....
gi 166064040  699 GERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKG 732
Cdd:NF038329  305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 939-1134 4.64e-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: 4.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  939 GRAGDPGLQGPAGAPGEKGEPGDDGPSGLDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGP 1018
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040 1019 PGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGvKGDRGETGALGAPGAPGPPGSPGPAGPTGKQGDRGEAGAQGPMG 1098
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 166064040 1099 PSGPAGARGIAGPQGPRGDKGESGEQGERGLKGHRG 1134
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 359-579 1.84e-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: 108.45  E-value: 1.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  359 VGPAGGPGFPGAPGAKGEAGPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGAPGFPGPRG 438
Cdd:NF038329  125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  439 PPGPQGATGPLGPKGQAGEPGIAGFKGD--QGPKGETGPAGPQGAPGPAGEEGKRGARgepggagpiGPPGERGAPGNRG 516
Cdd:NF038329  205 EQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPR---------GDRGEAGPDGPDG 275

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166064040  517 FPGQDGLAGPKGAPGERGPSGLTGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSG 579
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 306-557 2.01e-22

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 102.29  E-value: 2.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  306 GVKGESGSPGENGSPGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPgfpgapgakGEAGPTGARGP 385
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA---------GKDGEAGAKGP 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  386 EGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGApgfpgprgppgpqgatgplGPKGQAGEPGIAGFKG 465
Cdd:NF038329  188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------------------GQQGPDGDPGPTGEDG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  466 DQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLTGPKGAN 545
Cdd:NF038329  249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328

                         250
                  ....*....|..
gi 166064040  546 GDPGRPGEPGLP 557
Cdd:NF038329  329 GKDGKDGQPGKP 340
VWC smart00214
von Willebrand factor (vWF) type C domain;
34-88 7.47e-21

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 87.19  E-value: 7.47e-21
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 166064040     34 CLQNGQRYKDKDVWKPSSCRICVCDTG-NVLCDDIICED-PDCLNPE--IPFGECCPIC 88
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGtTVLCDPVECPPpPDCPNPErvKPPGECCPRC 59
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 255-490 2.06e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 93.05  E-value: 2.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  255 GEAGKPGKSGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERGR 334
Cdd:NF038329  123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGP 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  335 TGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPGaKGEAGPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDG 414
Cdd:NF038329  203 AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGD-PGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166064040  415 IPGAKGSAGAPGiagapgfpgprgppgpqgATGPLGPKGQAGEPGIAGFKGDQGPKGETGPAGPQGAPGPAGEEGK 490
Cdd:NF038329  282 PVGPAGKDGQNG------------------KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 225-426 3.36e-18

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 89.19  E-value: 3.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  225 GNPGEPGEPGVSGPMGPRGPPGPAGKPGDDGEAGKPGKSGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGA 304
Cdd:NF038329  132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  305 PGVKGESGSPGENGSPGPM-----GPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPGAKGEAGP 379
Cdd:NF038329  212 AGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 166064040  380 TGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPG 426
Cdd:NF038329  292 NGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 254-492 2.63e-17

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 86.50  E-value: 2.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  254 DGEAGKPGKSGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERG 333
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  334 RTGPAGAAGARGNDGqpgpAGPPGPVGPAGGPGFPGAPGAKGEAGPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTD 413
Cdd:NF038329  196 PRGETGPAGEQGPAG----PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  414 GIPGAKGSAGAPgiagapgfpgprgppGPQ---GATGPLGPKGQAGEPGIAGFKGDQGPKGETGPAGPQGAPGPAGEEGK 490
Cdd:NF038329  272 GPDGKDGERGPV---------------GPAgkdGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336


                  ..
gi 166064040  491 RG 492
Cdd:NF038329  337 PG 338
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
375-626 4.94e-10

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 63.90  E-value: 4.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  375 GEAGPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQ 454
Cdd:COG5164    10 GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  455 AGEPGIAGFKGDQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERG 534
Cdd:COG5164    90 TRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  535 PSGLTGPKGANGD--PGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQ-GARGQPGVMGFPGPKGAN 611
Cdd:COG5164   170 PGGSTTPPDDGGSttPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPkDQRPKTNPIERRGPERPE 249

                         250
                  ....*....|....*
gi 166064040  612 GEPGKAGEKGLAGAP 626
Cdd:COG5164   250 AAALPAELTALEAEN 264
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
762-1045 4.94e-10

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 63.90  E-value: 4.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  762 GPKGDRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPSGSTGARGAPGERGETGPPGPAGFAGPPGA 841
Cdd:COG5164     7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  842 DGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKgARGAQGPPGATGfpgaagrvgppGANGNPGPAGPPG 921
Cdd:COG5164    87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPP-SGGSTTPPGDGG-----------STPPGPGSTGPGG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  922 PAGKDGPKGVRGDSGPPGRAGDPGLQGPA--GAPGEKGEPGDDGPSGLDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPG 999
Cdd:COG5164   155 STTPPGDGGSTTPPGPGGSTTPPDDGGSTtpPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQR 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 166064040 1000 PSGEPGKQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGP 1045
Cdd:COG5164   235 PKTNPIERRGPERPEAAALPAELTALEAENRAANPEPATKTIPETT 280
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 804-860 6.53e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.57  E-value: 6.53e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 166064040   804 GEVGPPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDA 860
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 852-1059 7.52e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 53.84  E-value: 7.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  852 GEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGANGNPGPAGPPGPAGKDGPKGV 931
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  932 RGDSGPPGRAGDPGLQGPAGAPGEKGEPGDDGPSGLDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPG 1011
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 166064040 1012 ASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRG 1059
Cdd:PRK07764  750 DPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDED 797
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 261-317 1.60e-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: 1.60e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 166064040   261 GKSGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGEN 317
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 377-569 8.96e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 50.37  E-value: 8.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  377 AGPTGARGPEGAqGSRGEPGNPGSPGPAGASGNPGTDGipGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQAG 456
Cdd:PRK07764  595 AGGEGPPAPASS-GPPEEAARPAAPAAPAAPAAPAPAG--AAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA 671

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  457 EPGIAGFKGDQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGErgPS 536
Cdd:PRK07764  672 KAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD--PP 749

                         170       180       190
                  ....*....|....*....|....*....|...
gi 166064040  537 GLTGPKGANGDPGRPGEPGLPGARGLTGRPGDA 569
Cdd:PRK07764  750 DPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 508-560 1.99e-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: 43.25  E-value: 1.99e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 166064040   508 ERGAPGNRGFPGQDGLAGPKGAPGERGPSGLTGPKGANGDPGRPGEPGLPGAR 560
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 683-730 1.87e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 1.87e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 166064040   683 QGIPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGP 730
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 1282-1319 6.08e-04

fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 39.08  E-value: 6.08e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 166064040 1282 TCQDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMET 1319
Cdd:NF040941    1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTT 38
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 934-1133 1.01e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 43.74  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  934 DSGPPGRAGDPGLQGPAGAPGEKGEPGDDGPSGLDGPPGPQGLAGQRGIVGlpGQRGERGFPGLPGPSGEPGKQGAPGAS 1013
Cdd:PRK12678   83 AAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRER--GEAARRGAARKAGEGGEQPATEARADA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040 1014 GDRGPPGpvgppgltgpagEPGREGSPGADGPPGRDGAAGVKGDRGETGALGAPGAPGPPGSPGPAGPTGKQGDRGEAGA 1093
Cdd:PRK12678  161 AERTEEE------------ERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRG 228

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 166064040 1094 QGPMGPSGPAGARGIAGPQGPRGDKGESGEQGERGLKGHR 1133
Cdd:PRK12678  229 RRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRD 268
PHA03169 PHA03169
hypothetical protein; Provisional
 698-878 2.50e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.27  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  698 RGERGFPGErGSPGAQGLQGPRGLPGTPGTDGPKGAAGPDGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEG 777
Cdd:PHA03169   81 HGEKEERGQ-GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSP 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  778 APGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPSGSTGARGAPGERG--ETGPPGPAGFAGPPGADGQPGAKGDQGEAG 855
Cdd:PHA03169  160 NQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPpdEPGEPQSPTPQQAPSPNTQQAVEHEDEPTE 239

                         170       180
                  ....*....|....*....|....
gi 166064040  856 -QKGDAGAPGPQGPSGAPGPQGPT 878
Cdd:PHA03169  240 pEREGPPFPGHRSHSYTVVGWKPS 263
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1251-1486 1.61e-163

Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 460199  Cd Length: 233  Bit Score: 491.09  E-value: 1.61e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  1251 HDVEVDATLKSLNNQIESIRSPDGSRKNPARTCQDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPAT 1330
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKAS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  1331 VPRKNWWSsksKEKKHIWFGETMNGGFHFSYGDGNLAPNTANVQMTFLRLLSTEGSQNITYHCKNSIAYLDEAAGNLKKA 1410
Cdd:pfam01410   81 IPRKNWWT---KESKHVWFGEFMNGGSQFSYGVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKA 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166064040  1411 LLIQGSNDVEMRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGAEQEFGVDIGPVCF 1486
Cdd:pfam01410  158 LLLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1252-1487 8.53e-153

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: 462.71  E-value: 8.53e-153
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040   1252 DVEVDATLKSLNNQIESIRSPDGSRKNPARTCQDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPATV 1331
Cdd:smart00038    1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETGETCVSPSPSSI 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040   1332 PRKNWWSSKSKekkHIWFGETMNGGFHFSYGDGNLAPnTANVQMTFLRLLSTEGSQNITYHCKNSIAYLDEAAGNLKKAL 1411
Cdd:smart00038   81 PRKTWYSGKSK---HVWFGETMNGGFKFSYGDSEGPP-VGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKAL 156

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166064040   1412 LIQGSNDVEMRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGAEQEFGVDIGPVCFL 1487
Cdd:smart00038  157 RLRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 801-1011 1.88e-34

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 138.50  E-value: 1.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  801 GEKGEVGPPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAG---QKGDAGAPGPQGPSGAPGPQGP 877
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGpqgPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  878 TGVTGPKGARGAQGPPGATGFPGAAGRVGPPGANGNP--------GPAGPPGPAGKDGPKGVRGDSGPPGRAGDPGLQGP 949
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdgdpGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166064040  950 AGAPGEKGEPGDDGPSGLDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPG 1011
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 822-1056 2.07e-33

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 135.42  E-value: 2.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  822 GERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGA 901
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  902 AGRVGPPGANGNPGPAGPPGPAGKDGPKGV-----RGDSGPPGRAGDPGLQGPAGAPGEKGEPGDDGPSGLDGPPGPQGL 976
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPagpagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  977 AGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASgdrgppgpvgppgltgpaGEPGREGSPGADGPPGRDGAAGVKG 1056
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLP------------------GKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 703-954 2.67e-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: 123.09  E-value: 2.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  703 FPGERGSPGAQGLQGPRGLPGTPGTDGPKGAAGPDGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKD 782
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  783 GGRGLTGPIGPPGPAGANGEKGEVGPPGPSGSTGARGaPGERGETGPPGPAGFAGPPGADGQPgakgdqGEAGQKGDAGA 862
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA------GKDGPRGDRGE 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  863 PGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGrvgppgangnpgpagppgpagKDGPKGVRGDSGPPGRAG 942
Cdd:NF038329  268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG---------------------KDGLPGKDGKDGQPGKDG 326

                         250
                  ....*....|..
gi 166064040  943 DPGLQGPAGAPG 954
Cdd:NF038329  327 LPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 393-636 5.59e-27

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 116.16  E-value: 5.59e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  393 GEPGNPGSPGPAGASGNPGTDGIPGAKGSAGApgiagapgfpgprgppgpqgaTGPLGPKGQAGEPGIAGFKGDQGPKGE 472
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGP---------------------AGPPGPQGERGEKGPAGPQGEAGPQGP 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  473 TGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGaPGERGPSGLTGPKGANGDPGRPG 552
Cdd:NF038329  176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDG 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  553 EPGLPGARGLTGRPGDAGPQGKVGPSGapgedgRPGPPGPQGARGQPGVMGFPGPKGANGEPGKAGEKGLAGAPGLRGLP 632
Cdd:NF038329  255 PAGKDGPRGDRGEAGPDGPDGKDGERG------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328


                  ....
gi 166064040  633 GKDG 636
Cdd:NF038329  329 GKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 650-877 1.44e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 114.62  E-value: 1.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  650 AGERGEQGAPGPSGFQGLPGPPGPPGEGGKQGDQGIPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDG 729
Cdd:NF038329  128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  730 PKGAAGPDGPPGAQGPPGLQGMPGeRGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGltgpigppgpagANGEKGEVGPP 809
Cdd:NF038329  208 PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG------------DRGEAGPDGPD 274

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166064040  810 GPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGP 877
Cdd:NF038329  275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 440-661 1.25e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.92  E-value: 1.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  440 PGPQGATGPLGPKGQAGEPGIAGFKGDQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPG 519
Cdd:NF038329  128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  520 QDGLAGPKGAPGERGPSGLTGPKGangdPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQP 599
Cdd:NF038329  208 PAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV 283

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166064040  600 GVMGFPGPKGANGEPGKAGEKGLAGAPglrGLPGKDGETGAAGPPGPSGPAGERGEQGAPGP 661
Cdd:NF038329  284 GPAGKDGQNGKDGLPGKDGKDGQNGKD---GLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 846-1115 1.48e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.92  E-value: 1.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  846 GAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGrvgppgangnpgpagPpgpAGK 925
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG---------------P---AGK 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  926 DGPKGVRGDSGPPGRAGDPGLQGPAGAPGEKGEPGDDGPSGLDGPPGPQGLAGQrGIVGLPGQRGERGFPGLPGPSGEPG 1005
Cdd:NF038329  179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAG 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040 1006 KQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGdrgetgalgapgapgppgspgpagPTGKQ 1085
Cdd:NF038329  258 KDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG------------------------KDGLP 313

                         250       260       270
                  ....*....|....*....|....*....|
gi 166064040 1086 GDRGEAGAQGPMGPSGPAGARGIAGPQGPR 1115
Cdd:NF038329  314 GKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 34-88 2.78e-25

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 99.81  E-value: 2.78e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 166064040    34 CLQNGQRYKDKDVWKPSSCRICVCDTGNVLCDDIICEDPDCLNP--EIPFGECCPIC 88
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIICPPLDCPNPrlEIPPGECCPVC 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 459-732 3.46e-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: 110.77  E-value: 3.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  459 GIAGFKGDqGPKGETGPAGPQGAPGPAGEEGKRGArgepggagpigpPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGL 538
Cdd:NF038329  109 GLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGE------------TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  539 TGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGaPGEDGRPGPPGPQGARGQPGVMGFPGPKGANGEPGKAG 618
Cdd:NF038329  176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG-EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDG 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  619 EKGLAGAPGLRGLPGKDGetgaagppgPSGPAGERGEQGAPGpsgfqglpgppgppgeggkqgDQGIPGEAGAPGLVGPR 698
Cdd:NF038329  255 PAGKDGPRGDRGEAGPDG---------PDGKDGERGPVGPAG---------------------KDGQNGKDGLPGKDGKD 304

                         250       260       270
                  ....*....|....*....|....*....|....
gi 166064040  699 GERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKG 732
Cdd:NF038329  305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 939-1134 4.64e-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: 4.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  939 GRAGDPGLQGPAGAPGEKGEPGDDGPSGLDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGP 1018
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040 1019 PGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGvKGDRGETGALGAPGAPGPPGSPGPAGPTGKQGDRGEAGAQGPMG 1098
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 166064040 1099 PSGPAGARGIAGPQGPRGDKGESGEQGERGLKGHRG 1134
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 359-579 1.84e-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: 108.45  E-value: 1.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  359 VGPAGGPGFPGAPGAKGEAGPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGAPGFPGPRG 438
Cdd:NF038329  125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  439 PPGPQGATGPLGPKGQAGEPGIAGFKGD--QGPKGETGPAGPQGAPGPAGEEGKRGARgepggagpiGPPGERGAPGNRG 516
Cdd:NF038329  205 EQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPR---------GDRGEAGPDGPDG 275

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166064040  517 FPGQDGLAGPKGAPGERGPSGLTGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSG 579
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 306-557 2.01e-22

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 102.29  E-value: 2.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  306 GVKGESGSPGENGSPGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPgfpgapgakGEAGPTGARGP 385
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA---------GKDGEAGAKGP 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  386 EGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGApgfpgprgppgpqgatgplGPKGQAGEPGIAGFKG 465
Cdd:NF038329  188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------------------GQQGPDGDPGPTGEDG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  466 DQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLTGPKGAN 545
Cdd:NF038329  249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328

                         250
                  ....*....|..
gi 166064040  546 GDPGRPGEPGLP 557
Cdd:NF038329  329 GKDGKDGQPGKP 340
VWC smart00214
von Willebrand factor (vWF) type C domain;
34-88 7.47e-21

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 87.19  E-value: 7.47e-21
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 166064040     34 CLQNGQRYKDKDVWKPSSCRICVCDTG-NVLCDDIICED-PDCLNPE--IPFGECCPIC 88
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGtTVLCDPVECPPpPDCPNPErvKPPGECCPRC 59
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 255-490 2.06e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 93.05  E-value: 2.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  255 GEAGKPGKSGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERGR 334
Cdd:NF038329  123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGP 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  335 TGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPGaKGEAGPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDG 414
Cdd:NF038329  203 AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGD-PGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166064040  415 IPGAKGSAGAPGiagapgfpgprgppgpqgATGPLGPKGQAGEPGIAGFKGDQGPKGETGPAGPQGAPGPAGEEGK 490
Cdd:NF038329  282 PVGPAGKDGQNG------------------KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 225-426 3.36e-18

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 89.19  E-value: 3.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  225 GNPGEPGEPGVSGPMGPRGPPGPAGKPGDDGEAGKPGKSGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGA 304
Cdd:NF038329  132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  305 PGVKGESGSPGENGSPGPM-----GPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPGAKGEAGP 379
Cdd:NF038329  212 AGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 166064040  380 TGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPG 426
Cdd:NF038329  292 NGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 254-492 2.63e-17

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 86.50  E-value: 2.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  254 DGEAGKPGKSGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERG 333
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  334 RTGPAGAAGARGNDGqpgpAGPPGPVGPAGGPGFPGAPGAKGEAGPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTD 413
Cdd:NF038329  196 PRGETGPAGEQGPAG----PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  414 GIPGAKGSAGAPgiagapgfpgprgppGPQ---GATGPLGPKGQAGEPGIAGFKGDQGPKGETGPAGPQGAPGPAGEEGK 490
Cdd:NF038329  272 GPDGKDGERGPV---------------GPAgkdGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336


                  ..
gi 166064040  491 RG 492
Cdd:NF038329  337 PG 338
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
375-626 4.94e-10

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 63.90  E-value: 4.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  375 GEAGPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQ 454
Cdd:COG5164    10 GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  455 AGEPGIAGFKGDQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERG 534
Cdd:COG5164    90 TRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  535 PSGLTGPKGANGD--PGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQ-GARGQPGVMGFPGPKGAN 611
Cdd:COG5164   170 PGGSTTPPDDGGSttPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPkDQRPKTNPIERRGPERPE 249

                         250
                  ....*....|....*
gi 166064040  612 GEPGKAGEKGLAGAP 626
Cdd:COG5164   250 AAALPAELTALEAEN 264
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
762-1045 4.94e-10

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 63.90  E-value: 4.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  762 GPKGDRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPSGSTGARGAPGERGETGPPGPAGFAGPPGA 841
Cdd:COG5164     7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  842 DGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKgARGAQGPPGATGfpgaagrvgppGANGNPGPAGPPG 921
Cdd:COG5164    87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPP-SGGSTTPPGDGG-----------STPPGPGSTGPGG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  922 PAGKDGPKGVRGDSGPPGRAGDPGLQGPA--GAPGEKGEPGDDGPSGLDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPG 999
Cdd:COG5164   155 STTPPGDGGSTTPPGPGGSTTPPDDGGSTtpPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQR 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 166064040 1000 PSGEPGKQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGP 1045
Cdd:COG5164   235 PKTNPIERRGPERPEAAALPAELTALEAENRAANPEPATKTIPETT 280
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
816-1060 4.28e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 60.81  E-value: 4.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  816 GARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGA 895
Cdd:COG5164     7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  896 TGFPGAAGRVGPPGANGNPGPAGPPGPAGKDGPKGVRGDSGPPgragDPGLQGPAGAPGEK-GEPGDDGPSGLDGPPGPQ 974
Cdd:COG5164    87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPP----SGGSTTPPGDGGSTpPGPGSTGPGGSTTPPGDG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  975 GLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGV 1054
Cdd:COG5164   163 GSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIER 242


                  ....*.
gi 166064040 1055 KGDRGE 1060
Cdd:COG5164   243 RGPERP 248
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 804-860 6.53e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.57  E-value: 6.53e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 166064040   804 GEVGPPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDA 860
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
861-1123 3.46e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 54.65  E-value: 3.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  861 GAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGANGNPGPAGPPGPAGKDGPKGVRGDSGPPGR 940
Cdd:COG5164     7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  941 AGDPGLQGPAGAPGEKGEPGDDGPSGLDGPPGPQGLAGQRGivglPGQRGERGFPGLPGPSgePGKQGAPGASGDRGPPG 1020
Cdd:COG5164    87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT----PPSGGSTTPPGDGGST--PPGPGSTGPGGSTTPPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040 1021 PVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRGETGALGAPGAPGPPGSPGPAGPTGKQGDRGEAGAQGPMGPS 1100
Cdd:COG5164   161 DGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPI 240

                         250       260
                  ....*....|....*....|...
gi 166064040 1101 GPAGARGIAGPQGPRGDKGESGE 1123
Cdd:COG5164   241 ERRGPERPEAAALPAELTALEAE 263
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 807-863 5.01e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.87  E-value: 5.01e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 166064040   807 GPPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAP 863
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 828-883 6.73e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.49  E-value: 6.73e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 166064040   828 GPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGP 883
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 837-893 7.35e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.49  E-value: 7.35e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 166064040   837 GPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPP 893
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 852-1059 7.52e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 53.84  E-value: 7.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  852 GEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGANGNPGPAGPPGPAGKDGPKGV 931
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  932 RGDSGPPGRAGDPGLQGPAGAPGEKGEPGDDGPSGLDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPG 1011
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 166064040 1012 ASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRG 1059
Cdd:PRK07764  750 DPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDED 797
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 768-959 9.30e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 53.84  E-value: 9.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  768 GDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGA 847
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  848 KGDQGEAGQKGDAGAP---GPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATgfPGAAGRVGPPGANGNPGPAGPPGPAG 924
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPapaAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQP--PQAAQGASAPSPAADDPVPLPPEPDD 747

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 166064040  925 KDGPKGVRGDSGPPGRAGDPGLQGPAGAPGEKGEP 959
Cdd:PRK07764  748 PPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 261-317 1.60e-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: 1.60e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 166064040   261 GKSGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGEN 317
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 936-992 1.76e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.33  E-value: 1.76e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 166064040   936 GPPGRAGDPGLQGPAGAPGEKGEPGDDGPSGLDGPPGPQGLAGQRGIVGLPGQRGER 992
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 816-872 2.76e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.95  E-value: 2.76e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 166064040   816 GARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAP 872
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
445-661 7.01e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 50.41  E-value: 7.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  445 ATGPLGPKGQAGEPGIAGFKGDQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAgpigppgerGAPGNRGFPGQDGLA 524
Cdd:COG5164     8 KTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGT---------RPAGNQGATGPAQNQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  525 GPKGAPGERGPSGLTGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPGVMGF 604
Cdd:COG5164    79 GGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTP 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 166064040  605 PGPKGANGEPGKAGEKGLAGAPGlRGLPGKDGETGAAGPPGPSGPAGERGEQGAPGP 661
Cdd:COG5164   159 PGDGGSTTPPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDK 214
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 270-326 7.09e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.79  E-value: 7.09e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 166064040   270 GPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPR 326
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 377-569 8.96e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 50.37  E-value: 8.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  377 AGPTGARGPEGAqGSRGEPGNPGSPGPAGASGNPGTDGipGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQAG 456
Cdd:PRK07764  595 AGGEGPPAPASS-GPPEEAARPAAPAAPAAPAAPAPAG--AAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA 671

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  457 EPGIAGFKGDQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGErgPS 536
Cdd:PRK07764  672 KAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD--PP 749

                         170       180       190
                  ....*....|....*....|....*....|...
gi 166064040  537 GLTGPKGANGDPGRPGEPGLPGARGLTGRPGDA 569
Cdd:PRK07764  750 DPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 801-980 1.15e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.98  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  801 GEKGEVGPPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAG---------QKGDAGAPGPQGPSGA 871
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPApgvaapehhPKHVAVPDASDGGDGW 669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  872 PGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGANGNPGPAGPPGPagkdgPKGVRGDSGPPGRAGDPGLQGPAG 951
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQ-----PPQAAQGASAPSPAADDPVPLPPE 744

                         170       180
                  ....*....|....*....|....*....
gi 166064040  952 APGEKGEPGDDGPSGLDGPPGPQGLAGQR 980
Cdd:PRK07764  745 PDDPPDPAGAPAQPPPPPAPAPAAAPAAA 773
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 508-560 1.99e-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: 43.25  E-value: 1.99e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 166064040   508 ERGAPGNRGFPGQDGLAGPKGAPGERGPSGLTGPKGANGDPGRPGEPGLPGAR 560
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 930-986 2.75e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 2.75e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 166064040   930 GVRGDSGPPGRAGDPGLQGPAGAPGEKGEPGDDGPSGLDGPPGPQGLAGQRGIVGLP 986
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 374-425 2.78e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 2.78e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 166064040   374 KGEAGPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAP 425
Cdd:pfam01391    6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 948-1004 2.89e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 2.89e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 166064040   948 GPAGAPGEKGEPGDDGPSGLDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEP 1004
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 384-577 3.60e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.44  E-value: 3.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  384 GPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPlgPKGQAGEPGIAGF 463
Cdd:PRK07764  589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHH--PKHVAVPDASDGG 666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  464 KGDQGPKGETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGpkGAPGERGPSGLTGPKG 543
Cdd:PRK07764  667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGA--SAPSPAADDPVPLPPE 744

                         170       180       190
                  ....*....|....*....|....*....|....
gi 166064040  544 ANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGP 577
Cdd:PRK07764  745 PDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSP 778
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 800-849 3.88e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 3.88e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 166064040   800 NGEKGEVGPPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKG 849
Cdd:pfam01391    6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 927-981 4.28e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 4.28e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 166064040   927 GPKGVRGDSGPPGRAGDPGLQGPAGAPGEKGEPGDDGPSGLDGPPGPQGLAGQRG 981
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 276-332 5.20e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 5.20e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 166064040   276 GFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGER 332
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 801-847 5.31e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 5.31e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 166064040   801 GEKGEVGPPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGA 847
Cdd:pfam01391   10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 855-904 7.63e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 7.63e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 166064040   855 GQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGR 904
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 447-493 1.68e-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: 1.68e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 166064040   447 GPLGPKGQAGEPGIAGFKGDQGPKGETGPAGPQGAPGPAGEEGKRGA 493
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 683-730 1.87e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 1.87e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 166064040   683 QGIPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGP 730
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
 749-901 3.53e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 44.96  E-value: 3.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  749 QGMPGERGAAGIAGPKGDRGDVGEKGPEGApGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPSGSTGARGAPGERGETG 828
Cdd:PHA03169   81 HGEKEERGQGGPSGSGSESVGSPTPSPSGS-AEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSP 159

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166064040  829 PPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGvTGPKGARGAQGPPGATGFPGA 901
Cdd:PHA03169  160 NQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDE-PGEPQSPTPQQAPSPNTQQAV 231
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 513-569 3.54e-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: 3.54e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 166064040   513 GNRGFPGQDGLAGPKGAPGERGPSGLTGPKGANGDPGRPGEPGLPGARGLTGRPGDA 569
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 687-732 3.65e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 3.65e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 166064040   687 GEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKG 732
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 708-899 4.36e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  708 GSPGAQGLQGPRGLPGTPGTDGPKGAAGPDGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGL 787
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  788 TGPIGPPGPAGANGEKGEVGPPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQ- 866
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPp 749

                         170       180       190
                  ....*....|....*....|....*....|...
gi 166064040  867 GPSGAPGPQGPTGVTGPKGARGAQGPPGATGFP 899
Cdd:PRK07764  750 DPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 1282-1319 6.08e-04

fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 39.08  E-value: 6.08e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 166064040 1282 TCQDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMET 1319
Cdd:NF040941    1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTT 38
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 963-1013 7.05e-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: 7.05e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 166064040   963 GPSGLDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGAS 1013
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 934-1133 1.01e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 43.74  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  934 DSGPPGRAGDPGLQGPAGAPGEKGEPGDDGPSGLDGPPGPQGLAGQRGIVGlpGQRGERGFPGLPGPSGEPGKQGAPGAS 1013
Cdd:PRK12678   83 AAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRER--GEAARRGAARKAGEGGEQPATEARADA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040 1014 GDRGPPGpvgppgltgpagEPGREGSPGADGPPGRDGAAGVKGDRGETGALGAPGAPGPPGSPGPAGPTGKQGDRGEAGA 1093
Cdd:PRK12678  161 AERTEEE------------ERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRG 228

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 166064040 1094 QGPMGPSGPAGARGIAGPQGPRGDKGESGEQGERGLKGHR 1133
Cdd:PRK12678  229 RRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRD 268
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 812-902 1.01e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 43.52  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  812 SGSTGARGAPGerGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQG 891
Cdd:PRK14959  372 RPSGGGASAPS--GSAAEGPASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPAPSAAPSPRVPWDDAPPAPPRSGIP 449

                          90
                  ....*....|.
gi 166064040  892 PPGATGFPGAA 902
Cdd:PRK14959  450 PRPAPRMPEAS 460
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 801-845 1.08e-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: 1.08e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 166064040   801 GEKGEVGPPGPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQP 845
Cdd:pfam01391   13 GPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
34-86 1.73e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 38.31  E-value: 1.73e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 166064040     34 CLQNGQRYKDKDVWKpSSCRICVCDTGNVLCDDIICEDPDC----LNPEIPFGECCP 86
Cdd:smart00215    1 CWNNGSYYPPGAKWD-DDCNRCTCLNGRVSCTKVWCGPKPCllhnLSGECPLGQGCV 56
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 471-661 1.78e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  471 GETGPAGPQGAPGPAGEEGKRGARGEPGGAGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLTGPKGANGDPGR 550
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  551 PGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPGVMGFPGPKGANGEPGKAGEKGLAGAPGLRG 630
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749

                         170       180       190
                  ....*....|....*....|....*....|.
gi 166064040  631 LPGKDGETGAAGPPGPSGPAGERGEQGAPGP 661
Cdd:PRK07764  750 DPAGAPAQPPPPPAPAPAAAPAAAPPPSPPS 780
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 471-541 2.00e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 2.00e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166064040   471 GETGPAGPQGAPGPAGEEGKRGArgepggagpigppgeRGAPGNRGFPGQDGLAGPKGAPGERGPSGLTGP 541
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGP---------------PGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
 698-878 2.50e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.27  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  698 RGERGFPGErGSPGAQGLQGPRGLPGTPGTDGPKGAAGPDGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEG 777
Cdd:PHA03169   81 HGEKEERGQ-GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSP 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  778 APGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPSGSTGARGAPGERG--ETGPPGPAGFAGPPGADGQPGAKGDQGEAG 855
Cdd:PHA03169  160 NQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPpdEPGEPQSPTPQQAPSPNTQQAVEHEDEPTE 239

                         170       180
                  ....*....|....*....|....
gi 166064040  856 -QKGDAGAPGPQGPSGAPGPQGPT 878
Cdd:PHA03169  240 pEREGPPFPGHRSHSYTVVGWKPS 263
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 381-427 3.00e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.47  E-value: 3.00e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 166064040   381 GARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAGAPGI 427
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 447-492 3.15e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 3.15e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 166064040   447 GPLGPKGQAGEPGIAGFKGDQGPKGETGPAGPQGAPGPAGEEGKRG 492
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
PPE COG5651
PPE-repeat protein [Function unknown];
810-987 3.46e-03

PPE-repeat protein [Function unknown];


Pssm-ID: 444372 [Multi-domain]  Cd Length: 385  Bit Score: 41.42  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  810 GPSGSTGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGA 889
Cdd:COG5651   206 NQVGIGGLNSGSGPIGLNSGPGNTGFAGTGAAAGAAAAAAAAAAAAGAGASAALASLAATLLNASSLGLAATAASSAATN 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  890 QGPPGATGFPGAAGRVGPPGANGNPGPAGPPGPAGKDGPKGVRGDSGPPGRAGDPGLQGPAGAPGEKGEPGDDGPSGLDG 969
Cdd:COG5651   286 LGLAGSPLGLAGGGAGAAAATGLGLGAGGAAGAAGATGAGAALGAGAAAAAAGAAAGAGAAAAAAAGGAGGGGGGALGAG 365

                         170
                  ....*....|....*...
gi 166064040  970 PPGPQGLAGQRGIVGLPG 987
Cdd:COG5651   366 GGGGSAGAAAGAASGGGA 383
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
298-577 3.51e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 41.55  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  298 AKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPGAKGEA 377
Cdd:COG5164     5 GPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  378 GPTGARGPEGAQGSRGEPGNPGSPGPAGASGNPGTDGIPGAKGSAG------------APGIAGAPGFPGPRGPPGPQGA 445
Cdd:COG5164    85 QNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSggsttppgdggsTPPGPGSTGPGGSTTPPGDGGS 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  446 TGPLGPKGQAGEPGIAGF-----KGDQGPKGETGPAGPQGAPGPAGEEGKRGARGEPggagpigppgergapgnrgfPGQ 520
Cdd:COG5164   165 TTPPGPGGSTTPPDDGGSttppnKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPP--------------------DDR 224

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 166064040  521 DGLAGPKGAPGERGPSGLTGPKGANGDPGrPGEPGLPGARGLTGRPGDAGPQGKVGP 577
Cdd:COG5164   225 GGKTGPKDQRPKTNPIERRGPERPEAAAL-PAELTALEAENRAANPEPATKTIPETT 280
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 477-551 3.72e-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: 3.72e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166064040   477 GPQGAPGPAGEEGKrgargepggagpigppgeRGAPGNRGFPGQDGLAGPKGAPGERGPSGLTGPKGANGDPGRP 551
Cdd:pfam01391    1 GPPGPPGPPGPPGP------------------PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 684-893 5.83e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  684 GIPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKGAAGPDGPPGAQGPPGLQGMPGERGAAgiAGP 763
Cdd:PRK07764  589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAS--DGG 666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  764 KGDRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGA-NGEKGEVGPPGPSGSTGARGAPGERGETGPPGPAGFAGPPGAD 842
Cdd:PRK07764  667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPApAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD 746

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 166064040  843 GQPGAKGDQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPP 893
Cdd:PRK07764  747 DPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDED 797
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 549-617 6.15e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 6.15e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166064040   549 GRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGedgrpgppgpqgARGQPGVMGFPGPKGANGEPGKA 617
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPG------------PPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 984-1126 6.78e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.72  E-value: 6.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166064040  984 GLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRGETGA 1063
Cdd:PHA03169   90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQP 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166064040 1064 LGAPGAPGPPGSPGPAGPTGKQGDRGEAGAQGPMGPSGPAGARGIAGPQGPRGDKGESGEQGE 1126
Cdd:PHA03169  170 SHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVE 232
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 255-302 7.49e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 7.49e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 166064040   255 GEAGKPGKSGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEA 302
Cdd:pfam01391   10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
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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