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Conserved domains on  [gi|1168715|sp|P31721|]
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RecName: Full=Complement C1q subcomponent subunit B; Flags: Precursor

Protein Classification

complement C1q tumor necrosis factor-related protein; cuticular collagen family protein( domain architecture ID 11117246)

complement C1q tumor necrosis factor-related protein (C1q/TNF) plays diverse and important roles in immune, endocrine, skeletal, neuronal, reproductive, sensory, and vascular systems| cuticular collagen family protein is a structural macromolecule of the extracellular matrix containing triple helix domains that form tight interactions and stabilize supramolecular aggregates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C1q super family cl23878
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 113-250 1.92e-47

C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system.


The actual alignment was detected with superfamily member smart00110:

Pssm-ID: 420072  Cd Length: 135  Bit Score: 154.00  E-value: 1.92e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168715     113 DYKATQKVAFSALRTvNSALRPNQAIRFEKVITNVNDNYEPRSGKFTCKVPGLYYFTYHASSRG-NLCVNIVRGRDRdrm 191
Cdd:smart00110   1 NYKAQPRSAFSVIRS-NRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGrNVKVSLMKNGIQ--- 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168715     192 qkVLTFCD-YAQNTFQVTTGGVVLKLEQEEVVHLQATDK-NSLLGVEGANSIFTGFLLFPD 250
Cdd:smart00110  77 --VMSTYDeYQKGLYDVASGGALLQLRQGDQVWLELPDEkNGLYAGEYVDSTFSGFLLFPD 135
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 31-64 5.62e-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: 48.26  E-value: 5.62e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1168715     31 GSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPG 64
Cdd:pfam01391  22 GPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 31-102 8.02e-06

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 46.44  E-value: 8.02e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168715    31 GSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPGLAGDHGELGEKGDAGIPGIPGKVGPKGPVGPKGAPGPP 102
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD 334
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 113-250 1.92e-47

Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.


Pssm-ID: 128420  Cd Length: 135  Bit Score: 154.00  E-value: 1.92e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168715     113 DYKATQKVAFSALRTvNSALRPNQAIRFEKVITNVNDNYEPRSGKFTCKVPGLYYFTYHASSRG-NLCVNIVRGRDRdrm 191
Cdd:smart00110   1 NYKAQPRSAFSVIRS-NRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGrNVKVSLMKNGIQ--- 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168715     192 qkVLTFCD-YAQNTFQVTTGGVVLKLEQEEVVHLQATDK-NSLLGVEGANSIFTGFLLFPD 250
Cdd:smart00110  77 --VMSTYDeYQKGLYDVASGGALLQLRQGDQVWLELPDEkNGLYAGEYVDSTFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 121-247 8.00e-43

C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system.


Pssm-ID: 395310 [Multi-domain]  Cd Length: 126  Bit Score: 141.65  E-value: 8.00e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168715    121 AFSALRTVNSALRPNQAIRFEKVITNVNDNYEPRSGKFTCKVPGLYYFTYHASS--RGNLCVNIVRGRdrdrmQKVLTFC 198
Cdd:pfam00386   1 AFSAGRTTGLTAPNEQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTvdGKSLYVSLVKNG-----QEVVSFY 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1168715    199 DYAQNT-FQVTTGGVVLKLEQEEVVHLQATDKNSLLGVEG-ANSIFTGFLL 247
Cdd:pfam00386  76 DQPQKGsLDVASGSVVLELQRGDEVWLQLTGYNGLYYDGSdTDSTFSGFLL 126
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 31-64 5.62e-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: 48.26  E-value: 5.62e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1168715     31 GSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPG 64
Cdd:pfam01391  22 GPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 34-92 7.91e-07

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: 49.52  E-value: 7.91e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 1168715    34 GIPGVPGIPGVPGSDGKPGTPGIKGEKGLPGLAGDHGELGEKGDAGIPGIPGKVGPKGP 92
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP 175
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 30-89 7.91e-07

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: 49.52  E-value: 7.91e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168715    30 TGSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPGLAGDHGELGEKGDAGIPG---------IPGKVGP 89
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGkdgqngkdgLPGKDGK 303
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 31-90 1.08e-06

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 49.13  E-value: 1.08e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168715    31 GSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPGLAGDHGELGEKGDAGIP------GIPGKVGPK 90
Cdd:NF038329 278 GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPgkdgkdGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 31-102 8.02e-06

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 46.44  E-value: 8.02e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168715    31 GSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPGLAGDHGELGEKGDAGIPGIPGKVGPKGPVGPKGAPGPP 102
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD 334
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 31-101 3.93e-05

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: 44.13  E-value: 3.93e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168715    31 GSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPGL-----AGDHGELGEKGDAGIPGIPGKVGPKGPVGPKGAPGP 101
Cdd:NF038329 198 GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 31-102 3.60e-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: 41.43  E-value: 3.60e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168715    31 GSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPGLAGDHGELGEKGDAGIPGIPGKVGPKGPVGPKGAPGPP 102
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 113-250 1.92e-47

Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.


Pssm-ID: 128420  Cd Length: 135  Bit Score: 154.00  E-value: 1.92e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168715     113 DYKATQKVAFSALRTvNSALRPNQAIRFEKVITNVNDNYEPRSGKFTCKVPGLYYFTYHASSRG-NLCVNIVRGRDRdrm 191
Cdd:smart00110   1 NYKAQPRSAFSVIRS-NRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGrNVKVSLMKNGIQ--- 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168715     192 qkVLTFCD-YAQNTFQVTTGGVVLKLEQEEVVHLQATDK-NSLLGVEGANSIFTGFLLFPD 250
Cdd:smart00110  77 --VMSTYDeYQKGLYDVASGGALLQLRQGDQVWLELPDEkNGLYAGEYVDSTFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 121-247 8.00e-43

C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system.


Pssm-ID: 395310 [Multi-domain]  Cd Length: 126  Bit Score: 141.65  E-value: 8.00e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168715    121 AFSALRTVNSALRPNQAIRFEKVITNVNDNYEPRSGKFTCKVPGLYYFTYHASS--RGNLCVNIVRGRdrdrmQKVLTFC 198
Cdd:pfam00386   1 AFSAGRTTGLTAPNEQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTvdGKSLYVSLVKNG-----QEVVSFY 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1168715    199 DYAQNT-FQVTTGGVVLKLEQEEVVHLQATDKNSLLGVEG-ANSIFTGFLL 247
Cdd:pfam00386  76 DQPQKGsLDVASGSVVLELQRGDEVWLQLTGYNGLYYDGSdTDSTFSGFLL 126
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 31-64 5.62e-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: 48.26  E-value: 5.62e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1168715     31 GSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPG 64
Cdd:pfam01391  22 GPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 37-90 3.72e-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: 45.95  E-value: 3.72e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1168715     37 GVPGIPGVPGSDGKPGTPGIKGEKGLPGLAGDhgelgekgdAGIPGIPGKVGPK 90
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGE---------PGPPGPPGPPGPP 45
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 34-92 7.91e-07

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: 49.52  E-value: 7.91e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 1168715    34 GIPGVPGIPGVPGSDGKPGTPGIKGEKGLPGLAGDHGELGEKGDAGIPGIPGKVGPKGP 92
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP 175
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 30-89 7.91e-07

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: 49.52  E-value: 7.91e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168715    30 TGSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPGLAGDHGELGEKGDAGIPG---------IPGKVGP 89
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGkdgqngkdgLPGKDGK 303
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 31-90 1.08e-06

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 49.13  E-value: 1.08e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168715    31 GSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPGLAGDHGELGEKGDAGIP------GIPGKVGPK 90
Cdd:NF038329 278 GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPgkdgkdGQPGKPAPK 343
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 31-71 2.60e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 2.60e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1168715     31 GSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPGLAGDHGE 71
Cdd:pfam01391  16 GPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 30-67 6.47e-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: 42.48  E-value: 6.47e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1168715     30 TGSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPGLAG 67
Cdd:pfam01391  18 PGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 31-102 8.02e-06

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 46.44  E-value: 8.02e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168715    31 GSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPGLAGDHGELGEKGDAGIPGIPGKVGPKGPVGPKGAPGPP 102
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD 334
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 31-101 3.93e-05

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: 44.13  E-value: 3.93e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168715    31 GSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPGL-----AGDHGELGEKGDAGIPGIPGKVGPKGPVGPKGAPGP 101
Cdd:NF038329 198 GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 31-63 1.71e-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: 38.63  E-value: 1.71e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1168715     31 GSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLP 63
Cdd:pfam01391  25 GPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 31-102 3.60e-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: 41.43  E-value: 3.60e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168715    31 GSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPGLAGDHGELGEKGDAGIPGIPGKVGPKGPVGPKGAPGPP 102
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188
 
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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