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Conserved domains on  [gi|149040346|gb|EDL94384|]
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procollagen, type XVII, alpha 1 (predicted) [Rattus norvegicus]

Protein Classification

collagen-like domain-containing protein( domain architecture ID 1903237)

collagen-like domain-containing protein such as collagens, which are extracellular structural proteins involved in formation of connective tissue structure

PubMed:  21421911|15837519

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 574-812 1.26e-35

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: 141.97  E-value: 1.26e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  574 RGSPGPKGDTGSQGPkdRGLPGIPGTPGPLGHPGPEGPKGQKGSIGDPGMEGPIGQRGlagpmGPPGEPGPPGSGEKGDR 653
Cdd:NF038329  122 PGPAGPAGPAGEQGP--RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG-----KDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  654 GIAGEQGPRGLPGVPGSPGLRGTSGSPGPQGPPGSVGP-----QGLRGEVGLPGVKGDKGLVGPPGPKGDQGEKGPRGLT 728
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  729 GEPGIRGLPGAVGEPGAKGAMGPAGPDGQqgsRGEQGLTGMPGARgppgptgdpgkpgltGPQGPQGLPGTPGRPGTKGE 808
Cdd:NF038329  275 GKDGERGPVGPAGKDGQNGKDGLPGKDGK---DGQNGKDGLPGKD---------------GKDGQPGKDGLPGKDGKDGQ 336


                  ....
gi 149040346  809 PGAP 812
Cdd:NF038329  337 PGKP 340
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 574-812 1.26e-35

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: 141.97  E-value: 1.26e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  574 RGSPGPKGDTGSQGPkdRGLPGIPGTPGPLGHPGPEGPKGQKGSIGDPGMEGPIGQRGlagpmGPPGEPGPPGSGEKGDR 653
Cdd:NF038329  122 PGPAGPAGPAGEQGP--RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG-----KDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  654 GIAGEQGPRGLPGVPGSPGLRGTSGSPGPQGPPGSVGP-----QGLRGEVGLPGVKGDKGLVGPPGPKGDQGEKGPRGLT 728
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  729 GEPGIRGLPGAVGEPGAKGAMGPAGPDGQqgsRGEQGLTGMPGARgppgptgdpgkpgltGPQGPQGLPGTPGRPGTKGE 808
Cdd:NF038329  275 GKDGERGPVGPAGKDGQNGKDGLPGKDGK---DGQNGKDGLPGKD---------------GKDGQPGKDGLPGKDGKDGQ 336


                  ....
gi 149040346  809 PGAP 812
Cdd:NF038329  337 PGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 578-814 1.04e-34

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 139.27  E-value: 1.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  578 GPKGDTGSQGPkdRGLPGIPGTPGPLGHPGPEGPKGQKGSIGDPGMEGPIGQRGLAGPmgppgepgppgsgeKGDRGIAG 657
Cdd:NF038329  117 GEKGEPGPAGP--AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGP--------------QGPAGKDG 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  658 EQGPRGLPGVPGSPGLRGtsgspgPQGPPGSVGPQGLRGEVGLPGVKGDKGLVGPPG--PKGDQGEKGPRGLTGEPGIRG 735
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRG------ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDG 254

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149040346  736 LPGAVGEPGAKGAMGPAGPDGQQGSRGEQGLTGMPGARgppgptgdpGKPGLTGPQGPQGLPGTPGRPGTKGEPGAPGR 814
Cdd:NF038329  255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN---------GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 574-808 4.79e-29

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 122.32  E-value: 4.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  574 RGSPGPKGDTGSQGPK-DRGLPGIPGTPGPLGHPGPEGPKGQKGSIGDPGMEGPIGQRGLAGPMGPPGEPGppgsgEKGD 652
Cdd:NF038329  140 RGETGPAGPAGPPGPQgERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG-----PAGP 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  653 RGIAGEQGPRGLPGVPGS--------PGLRGTSGSPGPQGPPGSVGPQGLRGEVGLPGVKGDKGLVGPPGPKGDQGEKGP 724
Cdd:NF038329  215 DGEAGPAGEDGPAGPAGDgqqgpdgdPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGK 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  725 RGLTGEPGIRGLPGAVGEPGAKGAMGPAGPDGQQGSRGEQGLTGMPGARGPPGptgdpgkpgltgPQGPQGLPGTPGRPG 804
Cdd:NF038329  295 DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEV------------PQKPDTAPHTPKTPQ 362


                  ....
gi 149040346  805 TKGE 808
Cdd:NF038329  363 IPGQ 366
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 702-985 8.82e-13

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 72.25  E-value: 8.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  702 GVKGDKGLVGPPGPKGDQGEKGPRGLTGEPGIRGLPGAVGEPGAKGAMGPAGPDGQQGSRGEQGLTGMPGARGPPGPTGD 781
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  782 PGKPGLTGPQGPQGLPGTPGRPGTKGEPGAPGRvmtsegssaitvpgppgppgamgppgppgtpgpagpaGLPGQQGPRG 861
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP-------------------------------------AGDGQQGPDG 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  862 EPGLAGDSflnsgssisevlSAQGVDfrgppgppgprgppgpsipgppgprgppgegvpgppgppgsfltdsetffsgpp 941
Cdd:NF038329  240 DPGPTGED------------GPQGPD------------------------------------------------------ 253

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 149040346  942 GPPGPPGPKGDQGDPGVPGTPGIPGglshgtssgtmyaqgPPGP 985
Cdd:NF038329  254 GPAGKDGPRGDRGEAGPDGPDGKDG---------------ERGP 282
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 711-765 9.46e-13

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: 64.05  E-value: 9.46e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 149040346   711 GPPGPKGDQGEKGPRGLTGEPGIRGLPGAVGEPGAKGAMGPAGPDGQQGSRGEQG 765
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
654-867 9.64e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 46.56  E-value: 9.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  654 GIAGEQGPRGLPGVPGSPGLRGTSGSPGPQGPPGSVGPQGLRGEVGLPGVKGDKGLVGPPG------PKGDQGEKGPRGL 727
Cdd:COG5164     7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGnqgatgPAQNQGGTTPAQN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  728 TGEPGIRGLPGAVGEPGAKGAMGPAGPDGQQGSRGEQGLTGMPGARGPPGPTGDPGKPGLTGPQGPQGLPGTPGRPGTKG 807
Cdd:COG5164    87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  808 EPGaPGRVMTSEGSSAITVPGPPGPPGAMGPPGPPGTPGPAGPAGLPGQQGPRGEPGLAG 867
Cdd:COG5164   167 PPG-PGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG 225
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 574-812 1.26e-35

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: 141.97  E-value: 1.26e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  574 RGSPGPKGDTGSQGPkdRGLPGIPGTPGPLGHPGPEGPKGQKGSIGDPGMEGPIGQRGlagpmGPPGEPGPPGSGEKGDR 653
Cdd:NF038329  122 PGPAGPAGPAGEQGP--RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG-----KDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  654 GIAGEQGPRGLPGVPGSPGLRGTSGSPGPQGPPGSVGP-----QGLRGEVGLPGVKGDKGLVGPPGPKGDQGEKGPRGLT 728
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  729 GEPGIRGLPGAVGEPGAKGAMGPAGPDGQqgsRGEQGLTGMPGARgppgptgdpgkpgltGPQGPQGLPGTPGRPGTKGE 808
Cdd:NF038329  275 GKDGERGPVGPAGKDGQNGKDGLPGKDGK---DGQNGKDGLPGKD---------------GKDGQPGKDGLPGKDGKDGQ 336


                  ....
gi 149040346  809 PGAP 812
Cdd:NF038329  337 PGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 578-814 1.04e-34

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 139.27  E-value: 1.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  578 GPKGDTGSQGPkdRGLPGIPGTPGPLGHPGPEGPKGQKGSIGDPGMEGPIGQRGLAGPmgppgepgppgsgeKGDRGIAG 657
Cdd:NF038329  117 GEKGEPGPAGP--AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGP--------------QGPAGKDG 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  658 EQGPRGLPGVPGSPGLRGtsgspgPQGPPGSVGPQGLRGEVGLPGVKGDKGLVGPPG--PKGDQGEKGPRGLTGEPGIRG 735
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRG------ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDG 254

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149040346  736 LPGAVGEPGAKGAMGPAGPDGQQGSRGEQGLTGMPGARgppgptgdpGKPGLTGPQGPQGLPGTPGRPGTKGEPGAPGR 814
Cdd:NF038329  255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN---------GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 574-808 4.79e-29

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 122.32  E-value: 4.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  574 RGSPGPKGDTGSQGPK-DRGLPGIPGTPGPLGHPGPEGPKGQKGSIGDPGMEGPIGQRGLAGPMGPPGEPGppgsgEKGD 652
Cdd:NF038329  140 RGETGPAGPAGPPGPQgERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG-----PAGP 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  653 RGIAGEQGPRGLPGVPGS--------PGLRGTSGSPGPQGPPGSVGPQGLRGEVGLPGVKGDKGLVGPPGPKGDQGEKGP 724
Cdd:NF038329  215 DGEAGPAGEDGPAGPAGDgqqgpdgdPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGK 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  725 RGLTGEPGIRGLPGAVGEPGAKGAMGPAGPDGQQGSRGEQGLTGMPGARGPPGptgdpgkpgltgPQGPQGLPGTPGRPG 804
Cdd:NF038329  295 DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEV------------PQKPDTAPHTPKTPQ 362


                  ....
gi 149040346  805 TKGE 808
Cdd:NF038329  363 IPGQ 366
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 702-985 8.82e-13

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 72.25  E-value: 8.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  702 GVKGDKGLVGPPGPKGDQGEKGPRGLTGEPGIRGLPGAVGEPGAKGAMGPAGPDGQQGSRGEQGLTGMPGARGPPGPTGD 781
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  782 PGKPGLTGPQGPQGLPGTPGRPGTKGEPGAPGRvmtsegssaitvpgppgppgamgppgppgtpgpagpaGLPGQQGPRG 861
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP-------------------------------------AGDGQQGPDG 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  862 EPGLAGDSflnsgssisevlSAQGVDfrgppgppgprgppgpsipgppgprgppgegvpgppgppgsfltdsetffsgpp 941
Cdd:NF038329  240 DPGPTGED------------GPQGPD------------------------------------------------------ 253

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 149040346  942 GPPGPPGPKGDQGDPGVPGTPGIPGglshgtssgtmyaqgPPGP 985
Cdd:NF038329  254 GPAGKDGPRGDRGEAGPDGPDGKDG---------------ERGP 282
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 711-765 9.46e-13

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: 64.05  E-value: 9.46e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 149040346   711 GPPGPKGDQGEKGPRGLTGEPGIRGLPGAVGEPGAKGAMGPAGPDGQQGSRGEQG 765
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 708-763 1.03e-12

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: 64.05  E-value: 1.03e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 149040346   708 GLVGPPGPKGDQGEKGPRGLTGEPGIRGLPGAVGEPGAKGAMGPAGPDGQQGSRGE 763
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 693-752 3.64e-12

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: 62.51  E-value: 3.64e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346   693 GLRGEVGLPGVKGDKGlvgPPGPKGDQGEKGPRGLTGEPGIRGLPGAVGEPGAKGAMGPA 752
Cdd:pfam01391    1 GPPGPPGPPGPPGPPG---PPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 702-757 5.38e-12

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: 62.13  E-value: 5.38e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 149040346   702 GVKGDKGLVGPPGPKGDQGEKGPRGLTGEPGIRGLPGAVGEPGAKGAMGPAGPDGQ 757
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 720-772 7.58e-12

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: 61.36  E-value: 7.58e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 149040346   720 GEKGPRGLTGEPGIRGLPGAVGEPGAKGAMGPAGPDGQQGSRGEQGLTGMPGA 772
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 741-812 4.15e-11

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: 59.43  E-value: 4.15e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149040346   741 GEPGAKGAMGPAGPDGQQGSRGEQGLTGMPGARgppgptgdpgkpgltGPQGPQGLPGTPGRPGTKGEPGAP 812
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEP---------------GPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 575-626 7.93e-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: 52.88  E-value: 7.93e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 149040346   575 GSPGPKGDTGSQGPkdRGLPGIPGTPGPLGHPGPEGPKGQKGSIGDPGMEGP 626
Cdd:pfam01391    1 GPPGPPGPPGPPGP--PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 750-813 9.94e-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: 52.88  E-value: 9.94e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149040346   750 GPAGPDGQQGSRGEQGLTGMPGARGPpgptgdpgkpglTGPQGPQGLPGTPGRPGTKGEPGAPG 813
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGP------------PGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 574-622 3.25e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 51.34  E-value: 3.25e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 149040346   574 RGSPGPKGDTGSQGPK-DRGLPGIPGTPGPLGHPGPEGPKGQKGSIGDPG 622
Cdd:pfam01391    6 PGPPGPPGPPGPPGPPgPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 657-745 3.38e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.26  E-value: 3.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346   657 GEQGPRGLPGVPGSPGLRGtsgspgPQgppgsvgpqglrgevglpgvkgdkglvGPPGPKGDQGEKGPRGLTGEPGIRGL 736
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPG------PP---------------------------GPPGPPGPPGEPGPPGPPGPPGPPGP 47


                   ....*....
gi 149040346   737 PGAVGEPGA 745
Cdd:pfam01391   48 PGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 574-621 4.07e-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: 48.26  E-value: 4.07e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 149040346   574 RGSPGPKGDTGSQGPKdrGLPGIPGTPGPLGHPGPEGPKGQKGSIGDP 621
Cdd:pfam01391   12 PGPPGPPGPPGPPGPP--GPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 607-671 1.93e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 1.93e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149040346   607 GPEGPKGQKGSIGDPGMEGPIGQRGlagpmgppgepgppgsgEKGDRGIAGEQGPRGLPGVPGSP 671
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPG-----------------PPGPPGEPGPPGPPGPPGPPGPP 48
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 759-813 8.24e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 8.24e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 149040346   759 GSRGEQGLTGMPGARGPPGPTGDPGKPGLTGPQGPQGLPGTPGRPGTKGEPGAPG 813
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
654-867 9.64e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 46.56  E-value: 9.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  654 GIAGEQGPRGLPGVPGSPGLRGTSGSPGPQGPPGSVGPQGLRGEVGLPGVKGDKGLVGPPG------PKGDQGEKGPRGL 727
Cdd:COG5164     7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGnqgatgPAQNQGGTTPAQN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  728 TGEPGIRGLPGAVGEPGAKGAMGPAGPDGQQGSRGEQGLTGMPGARGPPGPTGDPGKPGLTGPQGPQGLPGTPGRPGTKG 807
Cdd:COG5164    87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346  808 EPGaPGRVMTSEGSSAITVPGPPGPPGAMGPPGPPGTPGPAGPAGLPGQQGPRGEPGLAG 867
Cdd:COG5164   167 PPG-PGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG 225
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 584-658 1.10e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 1.10e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149040346   584 GSQGPkdRGLPGIPGTPGPLGHPGPEGPKGQKGSIGDPGMEGPIGQRGLagpmgppgepgppgsgeKGDRGIAGE 658
Cdd:pfam01391    1 GPPGP--PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP-----------------PGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 598-676 2.90e-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: 2.90e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149040346   598 GTPGPLGHPGPEGPKGQKGSIGDPGMEGPigqrglagpmgppgepgppgsgekgdrgiageQGPRGLPGVPGSPGLRGT 676
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGP--------------------------------PGEPGPPGPPGPPGPPGP 47
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 565-864 2.43e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 42.30  E-value: 2.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346   565 MTEQENGNLRGSPGPKGDTGSQGPKDRGLPGIPGTPGPLGHPGPEGPKGQKGSIGDPGMEGPIGQRGLAGPMGPPGEPGP 644
Cdd:pfam09606  139 FPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQ 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346   645 PGSGEKGDRGIAGEQGPRGLPGVPGS---PGLRGTSGSPGPQGPPGSVGPQGLrgevglPGVKGDKGLVGPPGPKGDQGE 721
Cdd:pfam09606  219 MGQQAQANGGMNPQQMGGAPNQVAMQqqqPQQQGQQSQLGMGINQMQQMPQGV------GGGAGQGGPGQPMGPPGQQPG 292

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149040346   722 KGPRGLTGepgirGLPGAVGEPGAKGAMGPAGPDGQQGSRGEQGLTGMPGARGPPGPTGDPGKPGLTGPQGPQGLPGT-P 800
Cdd:pfam09606  293 AMPNVMSI-----GDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMqR 367

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149040346   801 GRPGTKGEPG-APGRVMTSegssaitvpgpPGPPGAMGPPGPPGTPGPAGpaglPGQQGPRGEPG 864
Cdd:pfam09606  368 GQPGMMSSPSpVPGQQVRQ-----------VTPNQFMRQSPQPSVPSPQG----PGSQPPQSHPG 417
 
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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