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Conserved domains on  [gi|56790315|ref|NP_954684|]
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collagen, type I, alpha 1a precursor [Danio rerio]

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 ...
 1210-1446 1.10e-156

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: 472.21  E-value: 1.10e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   1210 RDLEVDTTLKSLSQQIESIISPDGTKKNPARTCRDLKMCHPDWKSGEYWIDPDQGCNQDAIKVYCNMETGETCVNPTESA 1289
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKAS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   1290 IPKKNWYTskniKEKKHVWFGEAMTDGFQFEYGSEGSKPEDVNIQLTFLRLMSTEASQNITYHCKNSIAYMDQASGNLKK 1369
Cdd:pfam01410   81 IPRKNWWT----KESKHVWFGEFMNGGSQFSYGVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKK 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315   1370 ALLLQGSNEIEIRAEGNSRFTYSVTEDGCTSHTGAWGKTVIDYKTTKTSRLPIIDIAPMDVGAPNQEFGIEVGPVCF 1446
Cdd:pfam01410  157 ALLLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 626-861 3.45e-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: 113.46  E-value: 3.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   626 FQGLPGPQGATGEPGKSGEQGAPGEAGAPGPSGSRGDRGFPGERGAPGPAGPVGARGSPGSAGNDGAKGESGAAGAPGAQ 705
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   706 GPPGLQGMPGERGAAGLPGLKGDRGDQGAKGADGAagkdgirgmtGPIGPPGPAGAPGDKGESGAQGLVGPTGARGPPGE 785
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP----------AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56790315   786 RGETGAPGPAGFAGPPGADGLPGAKGEPGDNGAKGDAGAPGPAGATGAPGPQGPVGATGPKGARGAAGPPGATGFP 861
Cdd:NF038329  265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 469-724 9.89e-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: 112.31  E-value: 9.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   469 GERGAPGARGFPGADGAAGPRGAPGERggpgvvgpkgatgepGRNGEPGMPGSKGMTGSPGSPGPDGKTGPGGAPGQDGR 548
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGET---------------GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   549 PGPPGPVGARGQPGVMGFPGPKGAAGEAGKPGERGVMGAIGATGAPGKDGDvgapgapgpagpagerGEQGAAGPPGFQG 628
Cdd:NF038329  182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------------GQQGPDGDPGPTG 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   629 LPGPQGATGEPGKSGEQGAPGEAGAPGPSGSRGDRGFPGErgaPGPAGPVGARGSPGSAGNDGAKGESGAAGAPGAQGPP 708
Cdd:NF038329  246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP---AGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                         250
                  ....*....|....*.
gi 56790315   709 GLQGMPGERGAAGLPG 724
Cdd:NF038329  323 GKDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 784-1021 8.71e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 106.14  E-value: 8.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   784 GERGETGAPGPAGFAGPPGADGLPGAKGEPGDNGAKGDAGAPGPAGATGAPGPQGPVGATGPKGARGAAGPPGATGFPGA 863
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   864 AGRVgppgpsgnsgppgppgpagkeGQKGNRGETGPAGRTGEVGAAGPPGAPGEKGNpGAEGATGPAGIPGPQGIGGQRG 943
Cdd:NF038329  197 RGET---------------------GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDG 254

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56790315   944 IVGLPGQRGERGFPGLPGPSGEIGKQGPSGPSGERGPPGPMGPPGLAGPPGEPGREGTPGNEGSAGRDGAAGPKGDRG 1021
Cdd:NF038329  255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 336-579 5.92e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 100.75  E-value: 5.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   336 KGEVGPQGSRGAEGPQGARGEAGNPGPAGPAGPAGNNGADGAPGAKGAPGAPGIAGAPGFPGPRGPPGAAGAAGAPGPKG 415
Cdd:NF038329  119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   416 NTGEAGAPGAKGEAGAKGEAGAQGvQGPPGPPGEEGKRGPRGEPGAGGARGPTGERGAPGARGFPGADGAAGPRGAPGER 495
Cdd:NF038329  199 ETGPAGEQGPAGPAGPDGEAGPAG-EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   496 GGPGVVGPKGATGEPGRNGEPGMPGSKGMTGSPGSPGPDGKTgpggapgqdgrpgppgpvgarGQPGVMGFPGPKGAAGE 575
Cdd:NF038329  278 GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD---------------------GQPGKDGLPGKDGKDGQ 336


                  ....
gi 56790315   576 AGKP 579
Cdd:NF038329  337 PGKP 340
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 33-88 1.15e-21

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


:

Pssm-ID: 278520  Cd Length: 57  Bit Score: 89.41  E-value: 1.15e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 56790315     33 CTLDGQVYNDRDVWKPEPCQICVCDSGTVMCDEVICEDtSDCPNP--VIAHDECCPVC 88
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIICPP-LDCPNPrlEIPPGECCPVC 57
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 90-300 4.50e-20

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 94.97  E-value: 4.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315    90 DDDFQEPSVEGPRGSPGDKGERGPANPPGNDGIHEQSVLPVPTSHSGPAALGGNLSPQmsgGFDEKSSPMAVPGPMGPMG 169
Cdd:NF038329  107 DEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA---GPQGEAGPQGPAGKDGEAG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   170 PRGAPGPPGPSGPQGFTGPPGEPGEAGAPGPMGPRGAAGPPGKNGEDG--ESGKPGRPGERGPPGPQGARGFPGTPGLPG 247
Cdd:NF038329  184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 56790315   248 IKGHRGFSGLDGAKGDAGPAGPKGEPGAPGENGTPGAMGPRG------LPGERGRAGPP 300
Cdd:NF038329  264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGqngkdgLPGKDGKDGQP 322
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1048-1157 7.37e-11

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 66.08  E-value: 7.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  1048 GDRGETGPAGVPGPAGPSGPRGPSGPAGARGDKGETGEAGERGMKGHRGFTGMPGPPGPPGPSGESGPAGASGPAGPRGP 1127
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110
                  ....*....|....*....|....*....|
gi 56790315  1128 AGSAGSAGKDGMSGLPGPIGPPGPRGRNGE 1157
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1210-1446 1.10e-156

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: 472.21  E-value: 1.10e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   1210 RDLEVDTTLKSLSQQIESIISPDGTKKNPARTCRDLKMCHPDWKSGEYWIDPDQGCNQDAIKVYCNMETGETCVNPTESA 1289
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKAS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   1290 IPKKNWYTskniKEKKHVWFGEAMTDGFQFEYGSEGSKPEDVNIQLTFLRLMSTEASQNITYHCKNSIAYMDQASGNLKK 1369
Cdd:pfam01410   81 IPRKNWWT----KESKHVWFGEFMNGGSQFSYGVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKK 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315   1370 ALLLQGSNEIEIRAEGNSRFTYSVTEDGCTSHTGAWGKTVIDYKTTKTSRLPIIDIAPMDVGAPNQEFGIEVGPVCF 1446
Cdd:pfam01410  157 ALLLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1211-1447 1.17e-138

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: 424.57  E-value: 1.17e-138
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315    1211 DLEVDTTLKSLSQQIESIISPDGTKKNPARTCRDLKMCHPDWKSGEYWIDPDQGCNQDAIKVYCNMETGETCVNPTESAI 1290
Cdd:smart00038    1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETGETCVSPSPSSI 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315    1291 PKKNWYTSKNikekKHVWFGEAMTDGFQFEYGsEGSKPEDVNIQLTFLRLMSTEASQNITYHCKNSIAYMDQASGNLKKA 1370
Cdd:smart00038   81 PRKTWYSGKS----KHVWFGETMNGGFKFSYG-DSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKA 155

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315    1371 LLLQGSNEIEIRAEGNSRFTYSVTEDGCTSHTGAWGKTVIDYKTTKTSRLPIIDIAPMDVGAPNQEFGIEVGPVCFL 1447
Cdd:smart00038  156 LRLRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 626-861 3.45e-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: 113.46  E-value: 3.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   626 FQGLPGPQGATGEPGKSGEQGAPGEAGAPGPSGSRGDRGFPGERGAPGPAGPVGARGSPGSAGNDGAKGESGAAGAPGAQ 705
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   706 GPPGLQGMPGERGAAGLPGLKGDRGDQGAKGADGAagkdgirgmtGPIGPPGPAGAPGDKGESGAQGLVGPTGARGPPGE 785
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP----------AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56790315   786 RGETGAPGPAGFAGPPGADGLPGAKGEPGDNGAKGDAGAPGPAGATGAPGPQGPVGATGPKGARGAAGPPGATGFP 861
Cdd:NF038329  265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 469-724 9.89e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 112.31  E-value: 9.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   469 GERGAPGARGFPGADGAAGPRGAPGERggpgvvgpkgatgepGRNGEPGMPGSKGMTGSPGSPGPDGKTGPGGAPGQDGR 548
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGET---------------GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   549 PGPPGPVGARGQPGVMGFPGPKGAAGEAGKPGERGVMGAIGATGAPGKDGDvgapgapgpagpagerGEQGAAGPPGFQG 628
Cdd:NF038329  182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------------GQQGPDGDPGPTG 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   629 LPGPQGATGEPGKSGEQGAPGEAGAPGPSGSRGDRGFPGErgaPGPAGPVGARGSPGSAGNDGAKGESGAAGAPGAQGPP 708
Cdd:NF038329  246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP---AGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                         250
                  ....*....|....*.
gi 56790315   709 GLQGMPGERGAAGLPG 724
Cdd:NF038329  323 GKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 424-684 1.86e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.54  E-value: 1.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   424 GAKGEAGAKGEAGAQGVQgppgppgeegkrGPRGEPGAGGARGPTGERGAPGARGFPGADGAAGPRGAPGERGGPGVVGP 503
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQ------------GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   504 KGATGEPGRNGEPGMPGSKGMTGSPGSPGPDGKTGPGGapgqdgrPGPPGPVGARGQPGVMGFPGPKGAAGEAGKPGERG 583
Cdd:NF038329  185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAG-------EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAG 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   584 VMGAIGATGAPGKDGDVGAPGAPGPAGPAGERGEQGAAGPPGFQGLPGPQGATGEPGKSGEQGAPGEAGAPGPSGSRGDR 663
Cdd:NF038329  258 KDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337

                         250       260
                  ....*....|....*....|.
gi 56790315   664 GFPGERGAPGPAGPVGARGSP 684
Cdd:NF038329  338 GKPAPKTPEVPQKPDTAPHTP 358
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 565-839 6.17e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 109.99  E-value: 6.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   565 GFPGPKGAAGEAGKPGERGVMGAIGATGAPGKDGDVGAPGAPGPAGPAGERGEQGAAGPPGFQGLPGPQGATGEPGKSGE 644
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   645 QGAPGEAGAPGPSGSRGDRGFPGERGAPGPAGPVGargsPGSAGNDGAKGEsgaagapgaqgppglQGMPGERGAAGLPG 724
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGP---------------TGEDGPQGPDGPAG 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   725 LKGDRGDQgakgadgaagkdgirgmtgpigppgpagapGDKGESGAQGLVGPTGARGPPGERGETGAPGPAGFAGPPGAD 804
Cdd:NF038329  258 KDGPRGDR------------------------------GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN 307

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 56790315   805 GLPGAKGEPGDNGAKGDAGAPGPAGATGAPGPQGP 839
Cdd:NF038329  308 GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 418-648 7.41e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 109.61  E-value: 7.41e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   418 GEAGAPGAKGEAGAKGEAGAQGVQGPPGPPGEEGKRGPRGEPGAGGARGPTGERGAPGARGFPGADGAAGPRGAPGERGG 497
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   498 PGVVGPKGATGEPGRNGEPGMPGSKGMTGSPGSP--GPDGKTGPGGAPGQDGRPGPPGPVGARGQPGVMGFPGPKGAAGE 575
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGE 279

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56790315   576 AGKPGERGVMGAIGATGAPGKDgdvgapgapgpaGPAGERGEQGAAGPPGFQGLPGPQGATGEPGKSGEQGAP 648
Cdd:NF038329  280 RGPVGPAGKDGQNGKDGLPGKD------------GKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 665-866 6.94e-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: 106.53  E-value: 6.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   665 FPGERGAPGPAGPVGARGSPGSAGNDGAKGESGAAGAPGAQGPPGLQGMPGERGAAGLPGLKGDRGDQGAKGADGAAGKD 744
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   745 GIRGMTGPIGPPGPAGAPGDKGESGAQGLVGP--------TGARGPPGERGETGAPGPAGFAGPPGADGLPGAKGEPGDN 816
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPagpagdgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 56790315   817 GAKGDAGAPGPAGATGAPGPQGPVGATGPKGARGAAGPPGATGFPGAAGR 866
Cdd:NF038329  275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 747-973 7.46e-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: 106.53  E-value: 7.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   747 RGMTGPIGPPGPAGAPGDKGESGAQGLVGPTGARGPPGERGETGAPGPAGFAGPPGADGLPGAKGEPGDNGAKGDAGAPG 826
Cdd:NF038329  122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   827 PAGATGAPGPQGPVGATGPKGARGAAGPPGatgfPGAAGRVGPPGPSGNSGPPGPPGPAGKEGQKGNRGETGPAGRTGEv 906
Cdd:NF038329  202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK- 276

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315   907 gaagpPGAPGEKGNPGAEGATGPAGIPGPQGIGGQRGIVGLPGQRGERGFPGLPGPSGEIGKQGPSG 973
Cdd:NF038329  277 -----DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 784-1021 8.71e-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: 106.14  E-value: 8.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   784 GERGETGAPGPAGFAGPPGADGLPGAKGEPGDNGAKGDAGAPGPAGATGAPGPQGPVGATGPKGARGAAGPPGATGFPGA 863
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   864 AGRVgppgpsgnsgppgppgpagkeGQKGNRGETGPAGRTGEVGAAGPPGAPGEKGNpGAEGATGPAGIPGPQGIGGQRG 943
Cdd:NF038329  197 RGET---------------------GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDG 254

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56790315   944 IVGLPGQRGERGFPGLPGPSGEIGKQGPSGPSGERGPPGPMGPPGLAGPPGEPGREGTPGNEGSAGRDGAAGPKGDRG 1021
Cdd:NF038329  255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 520-808 2.16e-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: 101.91  E-value: 2.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   520 GSKGMTGSPGSPGPDGKTGPGGAPGQDGRPGPPGPVGARGQPGVMGFPGPKGAAGEAGKPGERGVMGAIGATGAPGKDgd 599
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ-- 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   600 vgapgapgpagpaGERGEQGAAGPPGFQGLPGPQGATGEPGKSGEQGAPGEaGAPGPSGSRGDRGFPGERGAPGPAGPVG 679
Cdd:NF038329  195 -------------GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDG 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   680 ARGSPGSAGNDGAKGESgaagapgaqgppglqgmpGERGAAGLPGLKGDRGDQgakgadgaagkdgirgmtgpigppgpa 759
Cdd:NF038329  261 PRGDRGEAGPDGPDGKD------------------GERGPVGPAGKDGQNGKD--------------------------- 295

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 56790315   760 gapgdkGESGAQGLVGPTGARGPPGERGETGAPGPAGFAGPPGADGLPG 808
Cdd:NF038329  296 ------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 336-579 5.92e-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: 100.75  E-value: 5.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   336 KGEVGPQGSRGAEGPQGARGEAGNPGPAGPAGPAGNNGADGAPGAKGAPGAPGIAGAPGFPGPRGPPGAAGAAGAPGPKG 415
Cdd:NF038329  119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   416 NTGEAGAPGAKGEAGAKGEAGAQGvQGPPGPPGEEGKRGPRGEPGAGGARGPTGERGAPGARGFPGADGAAGPRGAPGER 495
Cdd:NF038329  199 ETGPAGEQGPAGPAGPDGEAGPAG-EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   496 GGPGVVGPKGATGEPGRNGEPGMPGSKGMTGSPGSPGPDGKTgpggapgqdgrpgppgpvgarGQPGVMGFPGPKGAAGE 575
Cdd:NF038329  278 GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD---------------------GQPGKDGLPGKDGKDGQ 336


                  ....
gi 56790315   576 AGKP 579
Cdd:NF038329  337 PGKP 340
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 33-88 1.15e-21

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 89.41  E-value: 1.15e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 56790315     33 CTLDGQVYNDRDVWKPEPCQICVCDSGTVMCDEVICEDtSDCPNP--VIAHDECCPVC 88
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIICPP-LDCPNPrlEIPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
33-88 1.21e-21

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 89.50  E-value: 1.21e-21
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 56790315      33 CTLDGQVYNDRDVWKPEPCQICVCDSG-TVMCDEVICEDTSDCPNP--VIAHDECCPVC 88
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGtTVLCDPVECPPPPDCPNPerVKPPGECCPRC 59
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 90-300 4.50e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 94.97  E-value: 4.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315    90 DDDFQEPSVEGPRGSPGDKGERGPANPPGNDGIHEQSVLPVPTSHSGPAALGGNLSPQmsgGFDEKSSPMAVPGPMGPMG 169
Cdd:NF038329  107 DEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA---GPQGEAGPQGPAGKDGEAG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   170 PRGAPGPPGPSGPQGFTGPPGEPGEAGAPGPMGPRGAAGPPGKNGEDG--ESGKPGRPGERGPPGPQGARGFPGTPGLPG 247
Cdd:NF038329  184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 56790315   248 IKGHRGFSGLDGAKGDAGPAGPKGEPGAPGENGTPGAMGPRG------LPGERGRAGPP 300
Cdd:NF038329  264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGqngkdgLPGKDGKDGQP 322
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 138-387 4.51e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 91.89  E-value: 4.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   138 AALGGNLSPQMSGGFDEKSSPMAVPGPMGPMGPRGAPGPPGPSGPQGFTGPPGEPGEAGAPGPMGPRGAAGPPGKNGEDG 217
Cdd:NF038329  104 EELDEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   218 ESGKPGRPGERGPPGPQGARGFPGTPGLPGIKGHRGFSGLDGAKGDAGPaGPKGEPGAPGENGTPGAMGPRGLPGERGRA 297
Cdd:NF038329  184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   298 GPPGAAGARGNDGAAGAAGPPGPTGPAGPPGFpggpgsKGEVGPQGSRGAEGPQGARGEAGNPGPAGPAGPAGNNGADGA 377
Cdd:NF038329  263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGK------DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336

                         250
                  ....*....|
gi 56790315   378 PGaKGAPGAP 387
Cdd:NF038329  337 PG-KPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 888-1138 6.34e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 91.51  E-value: 6.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   888 EGQKGNRGETGPAGRTGEVGAAGPPGAPGEKGNPGAEGATGPAGIPGPQGIGGQRGIVGLPGQRGERGFPGLPGPSGEIG 967
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   968 KQGPSGPSGERGPPGPMGPPGLAGPPGEPGREGTPGN-----EGSAGRDGAAGPKGDRGETgpsgtpgapgppgaagpiG 1042
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPA------------------G 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  1043 PAGKTGDRGETGPAGVPGPAGPSGPRGPSGPAGARGDKGETGEAGERGMKGHRGFtgmpgppgppgpsgesgpAGASGPA 1122
Cdd:NF038329  258 KDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL------------------PGKDGKD 319

                         250
                  ....*....|....*.
gi 56790315  1123 GPRGPAGSAGSAGKDG 1138
Cdd:NF038329  320 GQPGKDGLPGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 180-388 1.37e-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: 90.35  E-value: 1.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   180 SGPQGFTGPPGEPGEAGAPGPMGPRGAAGPPGKNGEDGESGKPGRPGERGPPGPQGARGFPGTPGLPGIKGHRGFSGLDG 259
Cdd:NF038329  128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   260 AKGDAGPAGPKGEPGAPGENGTPGAM--GPRGLPGERGRAGPPGAAGARGNDGAAGAAGPPGPTGPAGPPGFPGGPGSKG 337
Cdd:NF038329  208 PAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 56790315   338 EVGPQGSRGAEGPQGARGEAGNPGPAGPAGPAGNNGADGAPGAKGAPGAPG 388
Cdd:NF038329  288 KDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 257-533 2.69e-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: 89.58  E-value: 2.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   257 LDGAKGDAGPAGPKGEPGAPGENGTPGAMGPRGLPGERGRAGPPGAAGARGNDGAAgaagppgptGPAGPPGFpggpgsK 336
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA---------GPQGPAGK------D 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   337 GEVGPQGSRGAEGPQGARGEAGNPGPAGPAGPAGNNGADGAPGAKGAPGAPGiagapgfpgprgppgaagaagaPGPKGN 416
Cdd:NF038329  180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------------DGQQGP 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   417 TGEAGAPGAKGEAGAKGEAGAQGvqgppgppgeegKRGPRGEPGAGGARGPTGERGAPGARGFPGADGAAGPRGAPGERG 496
Cdd:NF038329  238 DGDPGPTGEDGPQGPDGPAGKDG------------PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG 305

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 56790315   497 GPGVVGPKGATGEPGRNGEPGMPGSKGMTGSPGSPGP 533
Cdd:NF038329  306 QNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1048-1157 7.37e-11

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 66.08  E-value: 7.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  1048 GDRGETGPAGVPGPAGPSGPRGPSGPAGARGDKGETGEAGERGMKGHRGFTGMPGPPGPPGPSGESGPAGASGPAGPRGP 1127
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110
                  ....*....|....*....|....*....|
gi 56790315  1128 AGSAGSAGKDGMSGLPGPIGPPGPRGRNGE 1157
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 223-279 7.37e-09

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: 53.27  E-value: 7.37e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315    223 GRPGERGPPGPQGARGFPGTPGLPGIKGHRGFSGLDGAKGDAGPAGPKGEPGAPGEN 279
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
778-1070 7.63e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 56.58  E-value: 7.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  778 GARGPPGERGETGAPGPAGFAGPPGADGLPGAKGEPGDNGAKGDAGAPGPAGATGAPGPQGPVGATGPKGARGAAGPPGA 857
Cdd:COG5164    7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  858 TGFPGAAGRVGPPGPSGNSGPPGPPGPAGKEGQKGNRGETGPAGRTGEVGAAGPPGAPGEKGNPGAEGATGPAGIPGPQG 937
Cdd:COG5164   87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  938 IGGQRGIVGLPGQRGERGfpglPGPSGEIGKQGPSGPSGERGPPGPMGPPGlagppgepgreGTPGNEGSAGRDGAAGPK 1017
Cdd:COG5164  167 PPGPGGSTTPPDDGGSTT----PPNKGETGTDIPTGGTPRQGPDGPVKKDD-----------KNGKGNPPDDRGGKTGPK 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 56790315 1018 GDRGETGPSGTPGAPGPPGAAGPIGPAGKTGdrgeTGPAGVPGPAGPSGPRGP 1070
Cdd:COG5164  232 DQRPKTNPIERRGPERPEAAALPAELTALEA----ENRAANPEPATKTIPETT 280
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 766-822 1.39e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.41  E-value: 1.39e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315    766 GESGAQGLVGPTGARGPPGERGETGAPGPAGFAGPPGADGLPGAKGEPGDNGAKGDA 822
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 1241-1278 3.90e-06

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: 45.25  E-value: 3.90e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 56790315  1241 TCRDLKMCHPDWKSGEYWIDPDQGCNQDAIKVYCNMET 1278
Cdd:NF040941    1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTT 38
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
723-974 1.70e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 49.26  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  723 PGLKGDRGDQGAKGADGAAGKDGIRGMTGPIGPPGPAGAPGDKGESGAQGLVGPTGARGPPGERGETGAPGPAGFAGPPG 802
Cdd:COG5164    6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  803 ADGLPGAKGEPGDNGAKGDAGAPGPAGATGAPGPQGPVGATGPKgARGAAGPPGATGFPGAAGRVGPPGPSGNSGPPGPP 882
Cdd:COG5164   86 NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPP-SGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGS 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  883 GPAGKEGQKGNRGETGPAGRTGEVGAAGPPGAPGEKGNPGAEGATGPAGIPGPQGIGGQR-GIVGLPGQRGERGFPGLPG 961
Cdd:COG5164  165 TTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRgGKTGPKDQRPKTNPIERRG 244

                        250
                 ....*....|...
gi 56790315  962 PSGEIGKQGPSGP 974
Cdd:COG5164  245 PERPEAAALPAEL 257
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
454-694 9.14e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 46.95  E-value: 9.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  454 GPRGEPGAGGARGPTGERGAPGARGFPGADGAAGPRGAPGERGGPGVVGPKGATGEPGRNGEPGMPGSKGMTGSPGSPGP 533
Cdd:COG5164   13 DPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  534 DGKTGPGGAPGQDGRPGPPGPVGARGQPGVMGFPGP--KGAAGEAGKPGERGV-MGAIGATGAPGKDGDVGAPGAPGPAG 610
Cdd:COG5164   93 AGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPpsGGSTTPPGDGGSTPPgPGSTGPGGSTTPPGDGGSTTPPGPGG 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  611 PAGERGEQGAAGPP--GFQGLPGPQGATGEPGKSGEQGAPGEAGAPGPSGSRGDRGFP-GERGAPGPAGPVGARGSPGSA 687
Cdd:COG5164  173 STTPPDDGGSTTPPnkGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPkDQRPKTNPIERRGPERPEAAA 252


                 ....*..
gi 56790315  688 GNDGAKG 694
Cdd:COG5164  253 LPAELTA 259
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 106-300 5.09e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 5.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   106 GDKGERGPANPPGNDGIHEQSVLPVPTSHSGPAAlggnlsPQMSGGFDEKSSPMAVPGPMGPMGPRGAPGPPGPSGPQGF 185
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAA------PAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAS 663

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   186 TGPPGEPGEAGAPGPMGPRGAAGPPGKNGEDGESGKPGRPGERGPPGPQGARGFPGTPGLPGIKGHRGFSGLDGAKGDAG 265
Cdd:PRK07764  664 DGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPP 743

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 56790315   266 -PAGPKGEPGAPGENGTPGAMGPRGLPGERGRAGPP 300
Cdd:PRK07764  744 ePDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPP 779
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 457-523 5.86e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 5.86e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315    457 GEPGAGGARGPTGERGAPGARGFPGADGAAGPRGAPGerggpgvvgpkgATGEPGRNGEPGMPGSKG 523
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPG------------PPGPPGPPGPPGAPGAPG 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 774-866 7.39e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.21  E-value: 7.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   774 VGPTGARGPPGERGETGAPGPAGFAGPPGADGLPGAKGEPGDNGAKGDAGAPGPAGATGAPGPQGPVGATGPKGARGAAG 853
Cdd:PRK07764  625 AAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPA 704

                          90
                  ....*....|...
gi 56790315   854 PPGATGFPGAAGR 866
Cdd:PRK07764  705 PAATPPAGQADDP 717
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1047-1090 1.65e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 1.65e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 56790315   1047 TGDRGETGPAGVPGPAGPSGPRGPSGPAGARGDKGETGEAGERG 1090
Cdd:pfam01391   12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 420-624 2.10e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   420 AGAPGAKGEAGAKGEAGAQGVQgppgppgeegkrgPRGEPGAGGA-RGPTGERGAPGARGFPGADGAAGPRGAPGERGGP 498
Cdd:PRK07764  589 GPAPGAAGGEGPPAPASSGPPE-------------EAARPAAPAApAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPK 655

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   499 GVVGPKGATGEPGRNGEPGMPGSKGMTGSPGSPGPDGKTGPGGAPGQDGRPGPPGPVGARGQPgvmgfPGPKGAAGEAGK 578
Cdd:PRK07764  656 HVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPA-----AQPPQAAQGASA 730

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 56790315   579 PGERGVmGAIGATGAPGKDGDVGAPGAPGPAGPAGERGEQGAAGPP 624
Cdd:PRK07764  731 PSPAAD-DPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPP 775
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 439-495 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        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315    439 GVQGPPGPPGEEGKRGPRGEPGAGGARGPTGERGAPGARGFPGADGAAGPRGAPGER 495
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1210-1446 1.10e-156

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: 472.21  E-value: 1.10e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   1210 RDLEVDTTLKSLSQQIESIISPDGTKKNPARTCRDLKMCHPDWKSGEYWIDPDQGCNQDAIKVYCNMETGETCVNPTESA 1289
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKAS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   1290 IPKKNWYTskniKEKKHVWFGEAMTDGFQFEYGSEGSKPEDVNIQLTFLRLMSTEASQNITYHCKNSIAYMDQASGNLKK 1369
Cdd:pfam01410   81 IPRKNWWT----KESKHVWFGEFMNGGSQFSYGVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKK 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315   1370 ALLLQGSNEIEIRAEGNSRFTYSVTEDGCTSHTGAWGKTVIDYKTTKTSRLPIIDIAPMDVGAPNQEFGIEVGPVCF 1446
Cdd:pfam01410  157 ALLLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1211-1447 1.17e-138

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: 424.57  E-value: 1.17e-138
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315    1211 DLEVDTTLKSLSQQIESIISPDGTKKNPARTCRDLKMCHPDWKSGEYWIDPDQGCNQDAIKVYCNMETGETCVNPTESAI 1290
Cdd:smart00038    1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETGETCVSPSPSSI 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315    1291 PKKNWYTSKNikekKHVWFGEAMTDGFQFEYGsEGSKPEDVNIQLTFLRLMSTEASQNITYHCKNSIAYMDQASGNLKKA 1370
Cdd:smart00038   81 PRKTWYSGKS----KHVWFGETMNGGFKFSYG-DSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKA 155

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315    1371 LLLQGSNEIEIRAEGNSRFTYSVTEDGCTSHTGAWGKTVIDYKTTKTSRLPIIDIAPMDVGAPNQEFGIEVGPVCFL 1447
Cdd:smart00038  156 LRLRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 626-861 3.45e-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: 113.46  E-value: 3.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   626 FQGLPGPQGATGEPGKSGEQGAPGEAGAPGPSGSRGDRGFPGERGAPGPAGPVGARGSPGSAGNDGAKGESGAAGAPGAQ 705
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   706 GPPGLQGMPGERGAAGLPGLKGDRGDQGAKGADGAagkdgirgmtGPIGPPGPAGAPGDKGESGAQGLVGPTGARGPPGE 785
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP----------AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56790315   786 RGETGAPGPAGFAGPPGADGLPGAKGEPGDNGAKGDAGAPGPAGATGAPGPQGPVGATGPKGARGAAGPPGATGFP 861
Cdd:NF038329  265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 469-724 9.89e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 112.31  E-value: 9.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   469 GERGAPGARGFPGADGAAGPRGAPGERggpgvvgpkgatgepGRNGEPGMPGSKGMTGSPGSPGPDGKTGPGGAPGQDGR 548
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGET---------------GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   549 PGPPGPVGARGQPGVMGFPGPKGAAGEAGKPGERGVMGAIGATGAPGKDGDvgapgapgpagpagerGEQGAAGPPGFQG 628
Cdd:NF038329  182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------------GQQGPDGDPGPTG 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   629 LPGPQGATGEPGKSGEQGAPGEAGAPGPSGSRGDRGFPGErgaPGPAGPVGARGSPGSAGNDGAKGESGAAGAPGAQGPP 708
Cdd:NF038329  246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP---AGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                         250
                  ....*....|....*.
gi 56790315   709 GLQGMPGERGAAGLPG 724
Cdd:NF038329  323 GKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 424-684 1.86e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.54  E-value: 1.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   424 GAKGEAGAKGEAGAQGVQgppgppgeegkrGPRGEPGAGGARGPTGERGAPGARGFPGADGAAGPRGAPGERGGPGVVGP 503
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQ------------GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   504 KGATGEPGRNGEPGMPGSKGMTGSPGSPGPDGKTGPGGapgqdgrPGPPGPVGARGQPGVMGFPGPKGAAGEAGKPGERG 583
Cdd:NF038329  185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAG-------EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAG 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   584 VMGAIGATGAPGKDGDVGAPGAPGPAGPAGERGEQGAAGPPGFQGLPGPQGATGEPGKSGEQGAPGEAGAPGPSGSRGDR 663
Cdd:NF038329  258 KDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337

                         250       260
                  ....*....|....*....|.
gi 56790315   664 GFPGERGAPGPAGPVGARGSP 684
Cdd:NF038329  338 GKPAPKTPEVPQKPDTAPHTP 358
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 565-839 6.17e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 109.99  E-value: 6.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   565 GFPGPKGAAGEAGKPGERGVMGAIGATGAPGKDGDVGAPGAPGPAGPAGERGEQGAAGPPGFQGLPGPQGATGEPGKSGE 644
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   645 QGAPGEAGAPGPSGSRGDRGFPGERGAPGPAGPVGargsPGSAGNDGAKGEsgaagapgaqgppglQGMPGERGAAGLPG 724
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGP---------------TGEDGPQGPDGPAG 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   725 LKGDRGDQgakgadgaagkdgirgmtgpigppgpagapGDKGESGAQGLVGPTGARGPPGERGETGAPGPAGFAGPPGAD 804
Cdd:NF038329  258 KDGPRGDR------------------------------GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN 307

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 56790315   805 GLPGAKGEPGDNGAKGDAGAPGPAGATGAPGPQGP 839
Cdd:NF038329  308 GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 418-648 7.41e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 109.61  E-value: 7.41e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   418 GEAGAPGAKGEAGAKGEAGAQGVQGPPGPPGEEGKRGPRGEPGAGGARGPTGERGAPGARGFPGADGAAGPRGAPGERGG 497
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   498 PGVVGPKGATGEPGRNGEPGMPGSKGMTGSPGSP--GPDGKTGPGGAPGQDGRPGPPGPVGARGQPGVMGFPGPKGAAGE 575
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGE 279

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56790315   576 AGKPGERGVMGAIGATGAPGKDgdvgapgapgpaGPAGERGEQGAAGPPGFQGLPGPQGATGEPGKSGEQGAP 648
Cdd:NF038329  280 RGPVGPAGKDGQNGKDGLPGKD------------GKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 665-866 6.94e-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: 106.53  E-value: 6.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   665 FPGERGAPGPAGPVGARGSPGSAGNDGAKGESGAAGAPGAQGPPGLQGMPGERGAAGLPGLKGDRGDQGAKGADGAAGKD 744
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   745 GIRGMTGPIGPPGPAGAPGDKGESGAQGLVGP--------TGARGPPGERGETGAPGPAGFAGPPGADGLPGAKGEPGDN 816
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPagpagdgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 56790315   817 GAKGDAGAPGPAGATGAPGPQGPVGATGPKGARGAAGPPGATGFPGAAGR 866
Cdd:NF038329  275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 747-973 7.46e-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: 106.53  E-value: 7.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   747 RGMTGPIGPPGPAGAPGDKGESGAQGLVGPTGARGPPGERGETGAPGPAGFAGPPGADGLPGAKGEPGDNGAKGDAGAPG 826
Cdd:NF038329  122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   827 PAGATGAPGPQGPVGATGPKGARGAAGPPGatgfPGAAGRVGPPGPSGNSGPPGPPGPAGKEGQKGNRGETGPAGRTGEv 906
Cdd:NF038329  202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK- 276

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315   907 gaagpPGAPGEKGNPGAEGATGPAGIPGPQGIGGQRGIVGLPGQRGERGFPGLPGPSGEIGKQGPSG 973
Cdd:NF038329  277 -----DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 784-1021 8.71e-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: 106.14  E-value: 8.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   784 GERGETGAPGPAGFAGPPGADGLPGAKGEPGDNGAKGDAGAPGPAGATGAPGPQGPVGATGPKGARGAAGPPGATGFPGA 863
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   864 AGRVgppgpsgnsgppgppgpagkeGQKGNRGETGPAGRTGEVGAAGPPGAPGEKGNpGAEGATGPAGIPGPQGIGGQRG 943
Cdd:NF038329  197 RGET---------------------GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDG 254

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56790315   944 IVGLPGQRGERGFPGLPGPSGEIGKQGPSGPSGERGPPGPMGPPGLAGPPGEPGREGTPGNEGSAGRDGAAGPKGDRG 1021
Cdd:NF038329  255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 520-808 2.16e-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: 101.91  E-value: 2.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   520 GSKGMTGSPGSPGPDGKTGPGGAPGQDGRPGPPGPVGARGQPGVMGFPGPKGAAGEAGKPGERGVMGAIGATGAPGKDgd 599
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ-- 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   600 vgapgapgpagpaGERGEQGAAGPPGFQGLPGPQGATGEPGKSGEQGAPGEaGAPGPSGSRGDRGFPGERGAPGPAGPVG 679
Cdd:NF038329  195 -------------GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDG 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   680 ARGSPGSAGNDGAKGESgaagapgaqgppglqgmpGERGAAGLPGLKGDRGDQgakgadgaagkdgirgmtgpigppgpa 759
Cdd:NF038329  261 PRGDRGEAGPDGPDGKD------------------GERGPVGPAGKDGQNGKD--------------------------- 295

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 56790315   760 gapgdkGESGAQGLVGPTGARGPPGERGETGAPGPAGFAGPPGADGLPG 808
Cdd:NF038329  296 ------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 336-579 5.92e-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: 100.75  E-value: 5.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   336 KGEVGPQGSRGAEGPQGARGEAGNPGPAGPAGPAGNNGADGAPGAKGAPGAPGIAGAPGFPGPRGPPGAAGAAGAPGPKG 415
Cdd:NF038329  119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   416 NTGEAGAPGAKGEAGAKGEAGAQGvQGPPGPPGEEGKRGPRGEPGAGGARGPTGERGAPGARGFPGADGAAGPRGAPGER 495
Cdd:NF038329  199 ETGPAGEQGPAGPAGPDGEAGPAG-EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   496 GGPGVVGPKGATGEPGRNGEPGMPGSKGMTGSPGSPGPDGKTgpggapgqdgrpgppgpvgarGQPGVMGFPGPKGAAGE 575
Cdd:NF038329  278 GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD---------------------GQPGKDGLPGKDGKDGQ 336


                  ....
gi 56790315   576 AGKP 579
Cdd:NF038329  337 PGKP 340
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 33-88 1.15e-21

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 89.41  E-value: 1.15e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 56790315     33 CTLDGQVYNDRDVWKPEPCQICVCDSGTVMCDEVICEDtSDCPNP--VIAHDECCPVC 88
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIICPP-LDCPNPrlEIPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
33-88 1.21e-21

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 89.50  E-value: 1.21e-21
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 56790315      33 CTLDGQVYNDRDVWKPEPCQICVCDSG-TVMCDEVICEDTSDCPNP--VIAHDECCPVC 88
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGtTVLCDPVECPPPPDCPNPerVKPPGECCPRC 59
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 90-300 4.50e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 94.97  E-value: 4.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315    90 DDDFQEPSVEGPRGSPGDKGERGPANPPGNDGIHEQSVLPVPTSHSGPAALGGNLSPQmsgGFDEKSSPMAVPGPMGPMG 169
Cdd:NF038329  107 DEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA---GPQGEAGPQGPAGKDGEAG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   170 PRGAPGPPGPSGPQGFTGPPGEPGEAGAPGPMGPRGAAGPPGKNGEDG--ESGKPGRPGERGPPGPQGARGFPGTPGLPG 247
Cdd:NF038329  184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 56790315   248 IKGHRGFSGLDGAKGDAGPAGPKGEPGAPGENGTPGAMGPRG------LPGERGRAGPP 300
Cdd:NF038329  264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGqngkdgLPGKDGKDGQP 322
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 138-387 4.51e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 91.89  E-value: 4.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   138 AALGGNLSPQMSGGFDEKSSPMAVPGPMGPMGPRGAPGPPGPSGPQGFTGPPGEPGEAGAPGPMGPRGAAGPPGKNGEDG 217
Cdd:NF038329  104 EELDEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   218 ESGKPGRPGERGPPGPQGARGFPGTPGLPGIKGHRGFSGLDGAKGDAGPaGPKGEPGAPGENGTPGAMGPRGLPGERGRA 297
Cdd:NF038329  184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   298 GPPGAAGARGNDGAAGAAGPPGPTGPAGPPGFpggpgsKGEVGPQGSRGAEGPQGARGEAGNPGPAGPAGPAGNNGADGA 377
Cdd:NF038329  263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGK------DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336

                         250
                  ....*....|
gi 56790315   378 PGaKGAPGAP 387
Cdd:NF038329  337 PG-KPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 888-1138 6.34e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 91.51  E-value: 6.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   888 EGQKGNRGETGPAGRTGEVGAAGPPGAPGEKGNPGAEGATGPAGIPGPQGIGGQRGIVGLPGQRGERGFPGLPGPSGEIG 967
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   968 KQGPSGPSGERGPPGPMGPPGLAGPPGEPGREGTPGN-----EGSAGRDGAAGPKGDRGETgpsgtpgapgppgaagpiG 1042
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPA------------------G 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  1043 PAGKTGDRGETGPAGVPGPAGPSGPRGPSGPAGARGDKGETGEAGERGMKGHRGFtgmpgppgppgpsgesgpAGASGPA 1122
Cdd:NF038329  258 KDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL------------------PGKDGKD 319

                         250
                  ....*....|....*.
gi 56790315  1123 GPRGPAGSAGSAGKDG 1138
Cdd:NF038329  320 GQPGKDGLPGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 180-388 1.37e-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: 90.35  E-value: 1.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   180 SGPQGFTGPPGEPGEAGAPGPMGPRGAAGPPGKNGEDGESGKPGRPGERGPPGPQGARGFPGTPGLPGIKGHRGFSGLDG 259
Cdd:NF038329  128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   260 AKGDAGPAGPKGEPGAPGENGTPGAM--GPRGLPGERGRAGPPGAAGARGNDGAAGAAGPPGPTGPAGPPGFPGGPGSKG 337
Cdd:NF038329  208 PAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 56790315   338 EVGPQGSRGAEGPQGARGEAGNPGPAGPAGPAGNNGADGAPGAKGAPGAPG 388
Cdd:NF038329  288 KDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 257-533 2.69e-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: 89.58  E-value: 2.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   257 LDGAKGDAGPAGPKGEPGAPGENGTPGAMGPRGLPGERGRAGPPGAAGARGNDGAAgaagppgptGPAGPPGFpggpgsK 336
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA---------GPQGPAGK------D 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   337 GEVGPQGSRGAEGPQGARGEAGNPGPAGPAGPAGNNGADGAPGAKGAPGAPGiagapgfpgprgppgaagaagaPGPKGN 416
Cdd:NF038329  180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----------------------DGQQGP 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   417 TGEAGAPGAKGEAGAKGEAGAQGvqgppgppgeegKRGPRGEPGAGGARGPTGERGAPGARGFPGADGAAGPRGAPGERG 496
Cdd:NF038329  238 DGDPGPTGEDGPQGPDGPAGKDG------------PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG 305

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 56790315   497 GPGVVGPKGATGEPGRNGEPGMPGSKGMTGSPGSPGP 533
Cdd:NF038329  306 QNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1048-1157 7.37e-11

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 66.08  E-value: 7.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  1048 GDRGETGPAGVPGPAGPSGPRGPSGPAGARGDKGETGEAGERGMKGHRGFTGMPGPPGPPGPSGESGPAGASGPAGPRGP 1127
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110
                  ....*....|....*....|....*....|
gi 56790315  1128 AGSAGSAGKDGMSGLPGPIGPPGPRGRNGE 1157
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 223-279 7.37e-09

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: 53.27  E-value: 7.37e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315    223 GRPGERGPPGPQGARGFPGTPGLPGIKGHRGFSGLDGAKGDAGPAGPKGEPGAPGEN 279
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
778-1070 7.63e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 56.58  E-value: 7.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  778 GARGPPGERGETGAPGPAGFAGPPGADGLPGAKGEPGDNGAKGDAGAPGPAGATGAPGPQGPVGATGPKGARGAAGPPGA 857
Cdd:COG5164    7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  858 TGFPGAAGRVGPPGPSGNSGPPGPPGPAGKEGQKGNRGETGPAGRTGEVGAAGPPGAPGEKGNPGAEGATGPAGIPGPQG 937
Cdd:COG5164   87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  938 IGGQRGIVGLPGQRGERGfpglPGPSGEIGKQGPSGPSGERGPPGPMGPPGlagppgepgreGTPGNEGSAGRDGAAGPK 1017
Cdd:COG5164  167 PPGPGGSTTPPDDGGSTT----PPNKGETGTDIPTGGTPRQGPDGPVKKDD-----------KNGKGNPPDDRGGKTGPK 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 56790315 1018 GDRGETGPSGTPGAPGPPGAAGPIGPAGKTGdrgeTGPAGVPGPAGPSGPRGP 1070
Cdd:COG5164  232 DQRPKTNPIERRGPERPEAAALPAELTALEA----ENRAANPEPATKTIPETT 280
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 766-822 1.39e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.41  E-value: 1.39e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315    766 GESGAQGLVGPTGARGPPGERGETGAPGPAGFAGPPGADGLPGAKGEPGDNGAKGDA 822
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 781-836 2.12e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.03  E-value: 2.12e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 56790315    781 GPPGERGETGAPGPAGFAGPPGADGLPGAKGEPGDNGAKGDAGAPGPAGATGAPGP 836
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 790-845 2.85e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.64  E-value: 2.85e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 56790315    790 GAPGPAGFAGPPGADGLPGAKGEPGDNGAKGDAGAPGPAGATGAPGPQGPVGATGP 845
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 772-828 2.99e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.64  E-value: 2.99e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315    772 GLVGPTGARGPPGERGETGAPGPAGFAGPPGADGLPGAKGEPGDNGAKGDAGAPGPA 828
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 631-687 4.13e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.26  E-value: 4.13e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315    631 GPQGATGEPGKSGEQGAPGEAGAPGPSGSRGDRGFPGERGAPGPAGPVGARGSPGSA 687
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 193-247 4.93e-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: 4.93e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 56790315    193 GEAGAPGPMGPRGAAGPPGKNGEDGESGKPGRPGERGPPGPQGARGFPGTPGLPG 247
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 799-855 5.02e-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: 5.02e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315    799 GPPGADGLPGAKGEPGDNGAKGDAGAPGPAGATGAPGPQGPVGATGPKGARGAAGPP 855
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 199-253 5.07e-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: 5.07e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 56790315    199 GPMGPRGAAGPPGKNGEDGESGKPGRPGERGPPGPQGARGFPGTPGLPGIKGHRG 253
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 619-675 5.43e-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: 5.43e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315    619 GAAGPPGFQGLPGPQGATGEPGKSGEQGAPGEAGAPGPSGSRGDRGFPGERGAPGPA 675
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 622-678 7.58e-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: 7.58e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315    622 GPPGFQGLPGPQGATGEPGKSGEQGAPGEAGAPGPSGSRGDRGFPGERGAPGPAGPV 678
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 187-243 1.13e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.72  E-value: 1.13e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315    187 GPPGEPGEAGAPGPMGPRGAAGPPGKNGEDGESGKPGRPGERGPPGPQGARGFPGTP 243
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 637-692 1.54e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.72  E-value: 1.54e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 56790315    637 GEPGKSGEQGAPGEAGAPGPSGSRGDRGFPGERGAPGPAGPVGARGSPGSAGNDGA 692
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 793-849 3.27e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.56  E-value: 3.27e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315    793 GPAGFAGPPGADGLPGAKGEPGDNGAKGDAGAPGPAGATGAPGPQGPVGATGPKGAR 849
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 643-695 3.54e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.56  E-value: 3.54e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 56790315    643 GEQGAPGEAGAPGPSGSRGDRGFPGERGAPGPAGPVGARGSPGSAGNDGAKGE 695
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 1241-1278 3.90e-06

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: 45.25  E-value: 3.90e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 56790315  1241 TCRDLKMCHPDWKSGEYWIDPDQGCNQDAIKVYCNMET 1278
Cdd:NF040941    1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTT 38
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
723-974 1.70e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 49.26  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  723 PGLKGDRGDQGAKGADGAAGKDGIRGMTGPIGPPGPAGAPGDKGESGAQGLVGPTGARGPPGERGETGAPGPAGFAGPPG 802
Cdd:COG5164    6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  803 ADGLPGAKGEPGDNGAKGDAGAPGPAGATGAPGPQGPVGATGPKgARGAAGPPGATGFPGAAGRVGPPGPSGNSGPPGPP 882
Cdd:COG5164   86 NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPP-SGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGS 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  883 GPAGKEGQKGNRGETGPAGRTGEVGAAGPPGAPGEKGNPGAEGATGPAGIPGPQGIGGQR-GIVGLPGQRGERGFPGLPG 961
Cdd:COG5164  165 TTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRgGKTGPKDQRPKTNPIERRG 244

                        250
                 ....*....|...
gi 56790315  962 PSGEIGKQGPSGP 974
Cdd:COG5164  245 PERPEAAALPAEL 257
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
33-89 2.96e-05

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 43.32  E-value: 2.96e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315      33 CTLDGQVYNDRDVWKpEPCQICVCDSGTVMCDEVIC--------EDTSDCP--NPVIAHDECCPVCP 89
Cdd:smart00215    1 CWNNGSYYPPGAKWD-DDCNRCTCLNGRVSCTKVWCgpkpcllhNLSGECPlgQGCVPSLSDCLSSP 66
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
454-694 9.14e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 46.95  E-value: 9.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  454 GPRGEPGAGGARGPTGERGAPGARGFPGADGAAGPRGAPGERGGPGVVGPKGATGEPGRNGEPGMPGSKGMTGSPGSPGP 533
Cdd:COG5164   13 DPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  534 DGKTGPGGAPGQDGRPGPPGPVGARGQPGVMGFPGP--KGAAGEAGKPGERGV-MGAIGATGAPGKDGDVGAPGAPGPAG 610
Cdd:COG5164   93 AGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPpsGGSTTPPGDGGSTPPgPGSTGPGGSTTPPGDGGSTTPPGPGG 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315  611 PAGERGEQGAAGPP--GFQGLPGPQGATGEPGKSGEQGAPGEAGAPGPSGSRGDRGFP-GERGAPGPAGPVGARGSPGSA 687
Cdd:COG5164  173 STTPPDDGGSTTPPnkGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPkDQRPKTNPIERRGPERPEAAA 252


                 ....*..
gi 56790315  688 GNDGAKG 694
Cdd:COG5164  253 LPAELTA 259
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 186-231 2.83e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 2.83e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 56790315    186 TGPPGEPGEAGAPGPMGPRGAAGPPGKNGEDGESGKPGRPGERGPP 231
Cdd:pfam01391   12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 106-300 5.09e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 5.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   106 GDKGERGPANPPGNDGIHEQSVLPVPTSHSGPAAlggnlsPQMSGGFDEKSSPMAVPGPMGPMGPRGAPGPPGPSGPQGF 185
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAA------PAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAS 663

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   186 TGPPGEPGEAGAPGPMGPRGAAGPPGKNGEDGESGKPGRPGERGPPGPQGARGFPGTPGLPGIKGHRGFSGLDGAKGDAG 265
Cdd:PRK07764  664 DGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPP 743

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 56790315   266 -PAGPKGEPGAPGENGTPGAMGPRGLPGERGRAGPP 300
Cdd:PRK07764  744 ePDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPP 779
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 457-523 5.86e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 5.86e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315    457 GEPGAGGARGPTGERGAPGARGFPGADGAAGPRGAPGerggpgvvgpkgATGEPGRNGEPGMPGSKG 523
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPG------------PPGPPGPPGPPGAPGAPG 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 774-866 7.39e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.21  E-value: 7.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   774 VGPTGARGPPGERGETGAPGPAGFAGPPGADGLPGAKGEPGDNGAKGDAGAPGPAGATGAPGPQGPVGATGPKGARGAAG 853
Cdd:PRK07764  625 AAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPA 704

                          90
                  ....*....|...
gi 56790315   854 PPGATGFPGAAGR 866
Cdd:PRK07764  705 PAATPPAGQADDP 717
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 786-867 1.47e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 43.13  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   786 RGETGAPGPAGFAGPPGADGLPGAKGEPGDNGAKGDAGAPGPAGATGAPGPQGPVGATGPK---------------GARG 850
Cdd:PRK14959  373 PSGGGASAPSGSAAEGPASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPAPSAAPSPRvpwddappapprsgiPPRP 452

                          90
                  ....*....|....*..
gi 56790315   851 AAGPPGATGFPGAAGRV 867
Cdd:PRK14959  453 APRMPEASPVPGAPDSV 469
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1047-1090 1.65e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 1.65e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 56790315   1047 TGDRGETGPAGVPGPAGPSGPRGPSGPAGARGDKGETGEAGERG 1090
Cdd:pfam01391   12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 466-533 1.75e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 1.75e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56790315    466 GPTGERGAPGARGFPGADGAAGPRGAPGERggpgvvgpkgatGEPGRNGEPGMPGSKGMTGSPGSPGP 533
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPP------------GEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 420-624 2.10e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   420 AGAPGAKGEAGAKGEAGAQGVQgppgppgeegkrgPRGEPGAGGA-RGPTGERGAPGARGFPGADGAAGPRGAPGERGGP 498
Cdd:PRK07764  589 GPAPGAAGGEGPPAPASSGPPE-------------EAARPAAPAApAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPK 655

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   499 GVVGPKGATGEPGRNGEPGMPGSKGMTGSPGSPGPDGKTGPGGAPGQDGRPGPPGPVGARGQPgvmgfPGPKGAAGEAGK 578
Cdd:PRK07764  656 HVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPA-----AQPPQAAQGASA 730

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 56790315   579 PGERGVmGAIGATGAPGKDGDVGAPGAPGPAGPAGERGEQGAAGPP 624
Cdd:PRK07764  731 PSPAAD-DPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPP 775
PHA03247 PHA03247
large tegument protein UL36; Provisional
 89-300 2.38e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315    89 PDDDFQEPSVEGPRGSPGDKGERGPANPPGNDGIHEQSVLPVPTSHSGPAALGGNLSPQMSGGFDEKSSPMAVPGPMGPM 168
Cdd:PHA03247 2589 PDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRAR 2668

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   169 GPRGAPGPpgpsgpqgfTGPPGEPGEAGAPGPMGPRGA-AGPPGKNGEDGESGKPGRPGERGPPGPQGARG-FPGTPGLP 246
Cdd:PHA03247 2669 RLGRAAQA---------SSPPQRPRRRAARPTVGSLTSlADPPPPPPTPEPAPHALVSATPLPPGPAAARQaSPALPAAP 2739

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 56790315   247 GIKGhrgfsgldGAKGDAGPAGPKGEPGAPGENGTPGAMGPRGLPGERGRAGPP 300
Cdd:PHA03247 2740 APPA--------VPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTR 2785
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 340-688 2.61e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   340 GPQGSRGAEGPQGARGEAGNPGPAGPAGPAGNNGADGAPGAKGAPGAPGIAGAPGFPGPRGPPGAAGAAGAPGPKGNTGE 419
Cdd:PRK07764  397 AAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEP 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   420 AGAPGAKGEAGAKGEAGAQGVQGPPGPPGEEGKRGPRG----------------------EPGAGGARGPT---GERGAP 474
Cdd:PRK07764  477 TAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRErwpeilaavpkrsrktwaillpEATVLGVRGDTlvlGFSTGG 556

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   475 GARGFPGADGAAGPRGAPGERGGPGVVGPKGATGEPGRNGEPGMPGSKGMTGSPGSPGPDGKTGPGGAPGQDGRPGPPGP 554
Cdd:PRK07764  557 LARRFASPGNAEVLVTALAEELGGDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAP 636

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   555 VGARGQPGVMGFPGPKGAAGEAGKPGERGVMGAIGATGAPGKDGDVGAPGAPGPAGPAGERGEQGAAGPP-GFQGLPGPQ 633
Cdd:PRK07764  637 AEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAaTPPAGQADD 716

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 56790315   634 GATGEPGKSGEQGAPGEAGAPGPSGSRGDRGFPGERGAPGPAGPVGARGSPGSAG 688
Cdd:PRK07764  717 PAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPA 771
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 439-495 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        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 56790315    439 GVQGPPGPPGEEGKRGPRGEPGAGGARGPTGERGAPGARGFPGADGAAGPRGAPGER 495
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 452-662 3.34e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   452 KRGPRGEPGAGGARGPTGERGAPGARGFPGADGAAGPRGAPGERGGPGVVGPKGATGEPGRNGEPGMPG-SKGMTGSPGS 530
Cdd:PRK07764  593 GAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDaSDGGDGWPAK 672

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   531 PGPDGKTGPGGAPGQDGRPGppgpvgARGQPGVMGFPGPKGAAGEAGKPGERGVM---GAIGATGAPGKDGDVGAPGAPG 607
Cdd:PRK07764  673 AGGAAPAAPPPAPAPAAPAA------PAGAAPAQPAPAPAATPPAGQADDPAAQPpqaAQGASAPSPAADDPVPLPPEPD 746

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 56790315   608 PAGPAGERGEQGAAGPPGFQGlPGPQGATGEPGKSGEQGAPGEAGAPGPSGSRGD 662
Cdd:PRK07764  747 DPPDPAGAPAQPPPPPAPAPA-AAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRD 800
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 612-660 3.58e-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: 3.58e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 56790315    612 AGERGEQGAAGPPGFQGLPGPQGATGEPGKSGEQGAPGEAGAPGPSGSR 660
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 508-579 4.77e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.70  E-value: 4.77e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56790315    508 GEPGRNGEPGMPGSKGMTGSPGSPGPDGKTGPGGApgqdgrpgppgpvgaRGQPGVMGFPGPKGAAGEAGKP 579
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGP---------------PGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 452-519 5.64e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 5.64e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56790315    452 KRGPRGEPGAGGARGPTGERGAPGARGFPGADGAAGPRGAPGerggpgvvgpkgATGEPGRNGEPGMP 519
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPG------------PPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 259-300 8.04e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.93  E-value: 8.04e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 56790315    259 GAKGDAGPAGPKGEPGAPGENGTPGAMGPRGLPGERGRAGPP 300
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPP 42
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 376-695 9.01e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 9.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   376 GAPGAKGAPGAPGIAGAPGFPGPRGPPGAAGAAGAPGPKGNTGEAGAPGAKGEAGAKGEAGAQGVQGPPGPPGEEGKRGP 455
Cdd:PRK07764  400 SAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAA 479

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   456 RGEPGAGGARGPTGERGAPGARGFPGADGAAGPRGA--------PGERGGPGVVGPKGATGEPGRNGEPGM----PGSKG 523
Cdd:PRK07764  480 PAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERwpeilaavPKRSRKTWAILLPEATVLGVRGDTLVLgfstGGLAR 559

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   524 MTGSPGSP---------------------GPDGKTGPGGAPGQDGRPGPPGPVGARGQPGVMGFPGPKGAAGEAGKPGER 582
Cdd:PRK07764  560 RFASPGNAevlvtalaeelggdwqveavvGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEA 639

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56790315   583 GVMGAIGATGAPGKDGDVGAPGAPGPAGPAGERGEQGA-AGPPGFQGLPGPQGATGEPGKSGEQGAPGEAGAPGPSGSRG 661
Cdd:PRK07764  640 SAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAApAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAA 719

                         330       340       350
                  ....*....|....*....|....*....|....
gi 56790315   662 DRGFPGERGAPGPAGPVGARGSPGSAGNDGAKGE 695
Cdd:PRK07764  720 QPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAG 753
 
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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