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Conserved domains on  [gi|119829187|ref|NP_000485|]
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collagen alpha-1(XVII) chain [Homo sapiens]

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 ...
 508-807 2.32e-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: 141.20  E-value: 2.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187  508 SILPYGDSMDRIEKDRLqgmapaagADLDKiGLHsdsqeelwmfvrkKLMMEQENGNlRGSPGPKGDMGSPGPKGDRGFP 587
Cdd:NF038329   87 KIYKYLEERDKKLNSYL--------EELDE-GLQ-------------QLKGDGEKGE-PGPAGPAGPAGEQGPRGDRGET 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187  588 GTPGIPGPLGHPGPQGPKGQKGSVGDPGMEGPMGQRGREGPMGPRGEAGPPGS-GEKGERGAAgepgphgppgvpgsvGP 666
Cdd:NF038329  144 GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPrGETGPAGEQ---------------GP 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187  667 KgssgspgpqgppgpvGLQGLRGEVGLPGvKGDKGPMGPPGPKGDQGEKGPRGLTGEPGMRGLPGAVGEPGAKGAMGPAG 746
Cdd:NF038329  209 A---------------GPAGPDGEAGPAG-EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119829187  747 PDGHQGPRGEQGLTGMPGIRgppgpsgdpGKPGLTGPQGPQGLPGTPGRPGIKGEPGAPGK 807
Cdd:NF038329  273 PDGKDGERGPVGPAGKDGQN---------GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 508-807 2.32e-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: 141.20  E-value: 2.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187  508 SILPYGDSMDRIEKDRLqgmapaagADLDKiGLHsdsqeelwmfvrkKLMMEQENGNlRGSPGPKGDMGSPGPKGDRGFP 587
Cdd:NF038329   87 KIYKYLEERDKKLNSYL--------EELDE-GLQ-------------QLKGDGEKGE-PGPAGPAGPAGEQGPRGDRGET 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187  588 GTPGIPGPLGHPGPQGPKGQKGSVGDPGMEGPMGQRGREGPMGPRGEAGPPGS-GEKGERGAAgepgphgppgvpgsvGP 666
Cdd:NF038329  144 GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPrGETGPAGEQ---------------GP 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187  667 KgssgspgpqgppgpvGLQGLRGEVGLPGvKGDKGPMGPPGPKGDQGEKGPRGLTGEPGMRGLPGAVGEPGAKGAMGPAG 746
Cdd:NF038329  209 A---------------GPAGPDGEAGPAG-EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119829187  747 PDGHQGPRGEQGLTGMPGIRgppgpsgdpGKPGLTGPQGPQGLPGTPGRPGIKGEPGAPGK 807
Cdd:NF038329  273 PDGKDGERGPVGPAGKDGQN---------GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 579-635 1.77e-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: 63.28  E-value: 1.77e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 119829187   579 GPKGDRGFPGTPGIPGPLGHPGPQGPKGQKGSVGDPGMEGPMGQRGREGPMGPRGEA 635
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 684-975 1.56e-04

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: 46.05  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187  684 LQGLRGEVGLPGVKGDKGPmgppgpkgdQGEKGPRGLTGEPGMRGLPGAVGEPGAKGAMGPAGPDGHQGPRGEQGLTGMP 763
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGE---------QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187  764 GIRGPPGPSGDPGKPGLTGPQGPQGLPGTPGRPGIKGEPGAPGKivtsegssmltvpgppgppgamgppgppgapgpagp 843
Cdd:NF038329  186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP------------------------------------ 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187  844 aglpghqevlnlqgppgppgprgppgpsipgppgprgppgeglpgppgppgsflsnsetflsgppgppgppgpkgdqgpp 923
Cdd:NF038329      --------------------------------------------------------------------------------

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119829187  924 GPRGHQGEQGLpgfstsgsssfglnlqgppgpPGPQGPKGDKGDPGVPGALG 975
Cdd:NF038329  230 AGDGQQGPDGD---------------------PGPTGEDGPQGPDGPAGKDG 260
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 508-807 2.32e-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: 141.20  E-value: 2.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187  508 SILPYGDSMDRIEKDRLqgmapaagADLDKiGLHsdsqeelwmfvrkKLMMEQENGNlRGSPGPKGDMGSPGPKGDRGFP 587
Cdd:NF038329   87 KIYKYLEERDKKLNSYL--------EELDE-GLQ-------------QLKGDGEKGE-PGPAGPAGPAGEQGPRGDRGET 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187  588 GTPGIPGPLGHPGPQGPKGQKGSVGDPGMEGPMGQRGREGPMGPRGEAGPPGS-GEKGERGAAgepgphgppgvpgsvGP 666
Cdd:NF038329  144 GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPrGETGPAGEQ---------------GP 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187  667 KgssgspgpqgppgpvGLQGLRGEVGLPGvKGDKGPMGPPGPKGDQGEKGPRGLTGEPGMRGLPGAVGEPGAKGAMGPAG 746
Cdd:NF038329  209 A---------------GPAGPDGEAGPAG-EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119829187  747 PDGHQGPRGEQGLTGMPGIRgppgpsgdpGKPGLTGPQGPQGLPGTPGRPGIKGEPGAPGK 807
Cdd:NF038329  273 PDGKDGERGPVGPAGKDGQN---------GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 579-635 1.77e-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: 63.28  E-value: 1.77e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 119829187   579 GPKGDRGFPGTPGIPGPLGHPGPQGPKGQKGSVGDPGMEGPMGQRGREGPMGPRGEA 635
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 570-639 3.05e-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: 62.90  E-value: 3.05e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187   570 GPKGDMGSPGPKGDRGFPGTPGIPGPLGHPGPQGPKGQKGSVGDPgmegpmgqrgregpmGPRGEAGPPG 639
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPP---------------GPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 566-615 9.12e-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: 9.12e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 119829187   566 RGSPGPKGDMGSPGPKGDRGFPGTPGIPGPLGHPGPQGPKGQKGSVGDPG 615
Cdd:pfam01391    6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 565-619 1.84e-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: 60.59  E-value: 1.84e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 119829187   565 LRGSPGPKGDMGSPGPKGDRGFPGTPGIPGPLGHPGPQGPKGQKGSVGDPGMEGP 619
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 722-807 2.01e-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: 60.59  E-value: 2.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187   722 GEPGMRGLPGAVGEPGAKGAMGPAGPDGHQGPRGeqgltgmpgirgppgpsgdpgkpgltgPQGPQGLPGTPGRPGikgE 801
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPG---------------------------PPGPPGPPGPPGPPG---A 50


                   ....*.
gi 119829187   802 PGAPGK 807
Cdd:pfam01391   51 PGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 566-614 5.70e-10

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: 56.35  E-value: 5.70e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 119829187   566 RGSPGPKGDMGSPGPKGDRGFPGTPGIPGPlghPGPQGPKGQKGSVGDP 614
Cdd:pfam01391   12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGP---PGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 686-756 3.77e-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: 54.04  E-value: 3.77e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119829187   686 GLRGEVGLPGVKgdkgpmgppgpkgdqGEKGPRGLTGEPGMRGLPGAVGEPGAKGAMGPAGPDGHQGPRGE 756
Cdd:pfam01391    1 GPPGPPGPPGPP---------------GPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 713-771 1.17e-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: 52.50  E-value: 1.17e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 119829187   713 GEKGPRGLTGEPGMRGLPGAVGEPGAKGAMGPAGPDGHQGPRGEQGLTGmpgirgppgP 771
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG---------A 50
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 557-813 3.20e-06

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: 51.93  E-value: 3.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187   557 MMEQENGNLRGSPGPKGDMGSPGPKGDRGfPGTPGIPGPLGHPG-PQGPKGQKGSVGDPGMEGP--MGQRGREGPMGPRG 633
Cdd:pfam09606  139 FPSQMSRVGRMQPGGQAGGMMQPSSGQPG-SGTPNQMGPNGGPGqGQAGGMNGGQQGPMGGQMPpqMGVPGMPGPADAGA 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187   634 EAG---------PPGSGEKGERGAAGEPGPHGPPGVPGSVGPKGSSGSPGPQGPPGPVGL-------------QGLRGEV 691
Cdd:pfam09606  218 QMGqqaqanggmNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQggpgqpmgppgqqPGAMPNV 297

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187   692 GLPGVKGDKGPMGPPGPKGDQGEKGPRGLTGEPGMRGLPGavGEPGAKGAMGPAGPdGHQGPRGEQGLTGM----PGIRG 767
Cdd:pfam09606  298 MSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQG--GQVVALGGLNHLET-WNPGNFGGLGANPMqrgqPGMMS 374

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 119829187   768 PPGPSGDPGKPGLTGPQG----PQGLPGTPGRPGIKGEPGAPGKIVTSEG 813
Cdd:pfam09606  375 SPSPVPGQQVRQVTPNQFmrqsPQPSVPSPQGPGSQPPQSHPGGMIPSPA 424
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 683-745 3.85e-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: 3.85e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119829187   683 GLQGLRGEVGLPGvkgdkgpmgppgpkgDQGEKGPRGLTGEPGMRGLPGAVGEPGAKGAMGPA 745
Cdd:pfam01391   10 GPPGPPGPPGPPG---------------PPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 606-649 1.49e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 1.49e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 119829187   606 GQKGSVGDPGMEGPMGQRGREGPMGPRGEAGPPGS-GEKGERGAA 649
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPpGPPGPPGPP 45
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 684-975 1.56e-04

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: 46.05  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187  684 LQGLRGEVGLPGVKGDKGPmgppgpkgdQGEKGPRGLTGEPGMRGLPGAVGEPGAKGAMGPAGPDGHQGPRGEQGLTGMP 763
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGE---------QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187  764 GIRGPPGPSGDPGKPGLTGPQGPQGLPGTPGRPGIKGEPGAPGKivtsegssmltvpgppgppgamgppgppgapgpagp 843
Cdd:NF038329  186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP------------------------------------ 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119829187  844 aglpghqevlnlqgppgppgprgppgpsipgppgprgppgeglpgppgppgsflsnsetflsgppgppgppgpkgdqgpp 923
Cdd:NF038329      --------------------------------------------------------------------------------

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119829187  924 GPRGHQGEQGLpgfstsgsssfglnlqgppgpPGPQGPKGDKGDPGVPGALG 975
Cdd:NF038329  230 AGDGQQGPDGD---------------------PGPTGEDGPQGPDGPAGKDG 260
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 683-741 3.78e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 3.78e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119829187   683 GLQGLRGEVGLPGVKGDkgpmgppgpkgdQGEKGPRGLTGEPGMRGLPGA---VGEPGAKGA 741
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGP------------PGPPGPPGEPGPPGPPGPPGPpgpPGAPGAPGP 56
Herpes_LP pfam03363
Herpesvirus leader protein;
552-607 4.19e-03

Herpesvirus leader protein;


Pssm-ID: 281372 [Multi-domain]  Cd Length: 174  Bit Score: 39.70  E-value: 4.19e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 119829187   552 VRKKLMMEQENGNLRGSPGpkgdmgspGPKGDRGFPGTPGIPGPLGhPGPQGPKGQ 607
Cdd:pfam03363   46 VRRRVLVQQEEEVVSGSPS--------GPRGDRSEGPGPARPGPPG-IGPEGPLGQ 92
 
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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