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Conserved domains on  [gi|56606098|ref|NP_001008524|]
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complement C1q subcomponent subunit C precursor [Rattus norvegicus]

Protein Classification

complement C1q domain-containing protein( domain architecture ID 10476615)

complement C1q domain-containing protein with an N-terminal collagen-like triple helix repeat domain similar to human C1q, which is a collagen-like hexameric glycoprotein, which associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 114-245 3.61e-56

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: 175.95  E-value: 3.61e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606098    114 YKQKHQSVFTVTRQTaQYPAANGLVKFNSAITNPQGDYNTNTGKFTCKVPGLYYFVHH-TSQTANLCVQLLLNNAKVTSF 192
Cdd:smart00110   2 YKAQPRSAFSVIRSN-RPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHvESKGRNVKVSLMKNGIQVMST 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 56606098    193 CDHMSN-SKQVSSGGVLLRLQRGDEVWLAVNDY-NGMVGTEGSDSVFSGFLLFPD 245
Cdd:smart00110  81 YDEYQKgLYDVASGGALLQLRQGDQVWLELPDEkNGLYAGEYVDSTFSGFLLFPD 135
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 34-82 4.00e-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: 51.34  E-value: 4.00e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 56606098    34 GIPGMPGLPGTPGKDGHDGLQGPKGEPGIPAIPGTQGPKGQKGEPGMPG 82
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 114-245 3.61e-56

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: 175.95  E-value: 3.61e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606098    114 YKQKHQSVFTVTRQTaQYPAANGLVKFNSAITNPQGDYNTNTGKFTCKVPGLYYFVHH-TSQTANLCVQLLLNNAKVTSF 192
Cdd:smart00110   2 YKAQPRSAFSVIRSN-RPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHvESKGRNVKVSLMKNGIQVMST 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 56606098    193 CDHMSN-SKQVSSGGVLLRLQRGDEVWLAVNDY-NGMVGTEGSDSVFSGFLLFPD 245
Cdd:smart00110  81 YDEYQKgLYDVASGGALLQLRQGDQVWLELPDEkNGLYAGEYVDSTFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 121-242 2.16e-47

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: 153.21  E-value: 2.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606098   121 VFTVTRQTAQYPAANGLVKFNSAITNPQGDYNTNTGKFTCKVPGLYYFVHHTSQ--TANLCVQLLLNNAKVTSFCDHMSN 198
Cdd:pfam00386   1 AFSAGRTTGLTAPNEQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTvdGKSLYVSLVKNGQEVVSFYDQPQK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 56606098   199 SK-QVSSGGVLLRLQRGDEVWLAVNDYNGMVGTEG-SDSVFSGFLL 242
Cdd:pfam00386  81 GSlDVASGSVVLELQRGDEVWLQLTGYNGLYYDGSdTDSTFSGFLL 126
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 34-82 4.00e-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: 51.34  E-value: 4.00e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 56606098    34 GIPGMPGLPGTPGKDGHDGLQGPKGEPGIPAIPGTQGPKGQKGEPGMPG 82
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-94 1.25e-08

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: 54.91  E-value: 1.25e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56606098   27 QANAGCYGIPGMPGLPGTPGKDGHDGLQGPKGEPGIPAIPGTQGPKGQKGEPGMPGHRGKNGPMGTSG 94
Cdd:NF038329 158 RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG 225
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 30-94 1.73e-08

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: 54.14  E-value: 1.73e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56606098   30 AGCYGIPGMPGLPGTPGKDGHDGLQGPKGEPGIPAIPGTQGPKGQKGEPGMPGHRGKNGPMGTSG 94
Cdd:NF038329 146 AGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG 210
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-94 2.16e-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: 47.98  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606098   27 QANAGCYGIPGMPGLPGTPGKDGhDGLQGPKGEPGIPAI---------PGTQGPKGQKGEPGMPGHRGK---NGPMGTSG 94
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEdgpqgpdgpAGKDGPRGDRGEAGPDGPDGKdgeRGPVGPAG 287
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-105 3.52e-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: 3.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606098   27 QANAGCYGIPGMPGLPGTPGKDGHDGLQGPKGEPGIPAIPGTQGPKGQKGEPGMPGH--RGKNGPMGTSGSPGDPGPRGP 104
Cdd:NF038329 173 QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDGPQGP 252


                 .
gi 56606098  105 P 105
Cdd:NF038329 253 D 253
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 30-81 6.41e-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: 43.36  E-value: 6.41e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 56606098   30 AGCYGIPGMPGLPGTPGKDGH---DGLQGPKGEPGIPAIPGTQGPKGQKGEPGMP 81
Cdd:NF038329 286 AGKDGQNGKDGLPGKDGKDGQngkDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 34-105 2.39e-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: 41.81  E-value: 2.39e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56606098   34 GIPGMPGLPGTPGKDGHDGLQGPKGEPGIPAIPGTQGPKGQKGEPGMPGHRGKNGPMGtsgspgdpgprgPP 105
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG------------PA 176
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 53-94 6.17e-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: 40.66  E-value: 6.17e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 56606098   53 LQGPKGEPGIPAIPGTQGPKGQKGEPGMPGHRGKNGPMGTSG 94
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG 156
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 114-245 3.61e-56

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: 175.95  E-value: 3.61e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606098    114 YKQKHQSVFTVTRQTaQYPAANGLVKFNSAITNPQGDYNTNTGKFTCKVPGLYYFVHH-TSQTANLCVQLLLNNAKVTSF 192
Cdd:smart00110   2 YKAQPRSAFSVIRSN-RPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHvESKGRNVKVSLMKNGIQVMST 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 56606098    193 CDHMSN-SKQVSSGGVLLRLQRGDEVWLAVNDY-NGMVGTEGSDSVFSGFLLFPD 245
Cdd:smart00110  81 YDEYQKgLYDVASGGALLQLRQGDQVWLELPDEkNGLYAGEYVDSTFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 121-242 2.16e-47

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: 153.21  E-value: 2.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606098   121 VFTVTRQTAQYPAANGLVKFNSAITNPQGDYNTNTGKFTCKVPGLYYFVHHTSQ--TANLCVQLLLNNAKVTSFCDHMSN 198
Cdd:pfam00386   1 AFSAGRTTGLTAPNEQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTvdGKSLYVSLVKNGQEVVSFYDQPQK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 56606098   199 SK-QVSSGGVLLRLQRGDEVWLAVNDYNGMVGTEG-SDSVFSGFLL 242
Cdd:pfam00386  81 GSlDVASGSVVLELQRGDEVWLQLTGYNGLYYDGSdTDSTFSGFLL 126
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 34-82 4.00e-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: 51.34  E-value: 4.00e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 56606098    34 GIPGMPGLPGTPGKDGHDGLQGPKGEPGIPAIPGTQGPKGQKGEPGMPG 82
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-94 1.25e-08

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: 54.91  E-value: 1.25e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56606098   27 QANAGCYGIPGMPGLPGTPGKDGHDGLQGPKGEPGIPAIPGTQGPKGQKGEPGMPGHRGKNGPMGTSG 94
Cdd:NF038329 158 RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG 225
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 30-94 1.73e-08

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: 54.14  E-value: 1.73e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56606098   30 AGCYGIPGMPGLPGTPGKDGHDGLQGPKGEPGIPAIPGTQGPKGQKGEPGMPGHRGKNGPMGTSG 94
Cdd:NF038329 146 AGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG 210
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 46-94 2.10e-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: 49.41  E-value: 2.10e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 56606098    46 GKDGHDGLQGPKGEPGIPAIPGTQGPKGQKGEPGMPGHRGKNGPMGTSG 94
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 34-81 6.74e-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: 47.87  E-value: 6.74e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 56606098    34 GIPGMPGLPGTPGKDGHDGLQGPKGEPGIPAIPGTQGPKGQKGEPGMP 81
Cdd:pfam01391  10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-94 2.16e-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: 47.98  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606098   27 QANAGCYGIPGMPGLPGTPGKDGhDGLQGPKGEPGIPAI---------PGTQGPKGQKGEPGMPGHRGK---NGPMGTSG 94
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEdgpqgpdgpAGKDGPRGDRGEAGPDGPDGKdgeRGPVGPAG 287
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-105 3.52e-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: 3.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606098   27 QANAGCYGIPGMPGLPGTPGKDGHDGLQGPKGEPGIPAIPGTQGPKGQKGEPGMPGH--RGKNGPMGTSGSPGDPGPRGP 104
Cdd:NF038329 173 QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDGPQGP 252


                 .
gi 56606098  105 P 105
Cdd:NF038329 253 D 253
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 30-81 6.41e-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: 43.36  E-value: 6.41e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 56606098   30 AGCYGIPGMPGLPGTPGKDGH---DGLQGPKGEPGIPAIPGTQGPKGQKGEPGMP 81
Cdd:NF038329 286 AGKDGQNGKDGLPGKDGKDGQngkDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 34-105 2.39e-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: 41.81  E-value: 2.39e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56606098   34 GIPGMPGLPGTPGKDGHDGLQGPKGEPGIPAIPGTQGPKGQKGEPGMPGHRGKNGPMGtsgspgdpgprgPP 105
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG------------PA 176
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 53-94 6.17e-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: 40.66  E-value: 6.17e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 56606098   53 LQGPKGEPGIPAIPGTQGPKGQKGEPGMPGHRGKNGPMGTSG 94
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG 156
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 29-63 2.60e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.16  E-value: 2.60e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 56606098    29 NAGCYGIPGMPGLPGTPGKDGHDGLQGPKGEPGIP 63
Cdd:pfam01391  20 PPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
 
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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