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Conserved domains on  [gi|66472692|ref|NP_001018363|]
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complement C1q subcomponent subunit A precursor [Danio rerio]

Protein Classification

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 ...
 110-245 5.68e-29

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: 106.23  E-value: 5.68e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472692    110 KASEKPAFSVLRNEASQAQyKQPVTFNDKLSDANDDFQIKTGYFTCKVPGVYYFVFHASSEGRLCLRLKSTSAPPVsLSF 189
Cdd:smart00110   3 KAQPRSAFSVIRSNRPPPP-GQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQV-MST 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 66472692    190 CDFNSKSVSLVVSGGAVLTLLKGDKVWIEPFAGDGGVGQMPKrLYAVFNGFLIYRN 245
Cdd:smart00110  81 YDEYQKGLYDVASGGALLQLRQGDQVWLELPDEKNGLYAGEY-VDSTFSGFLLFPD 135
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 29-116 1.49e-10

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: 60.69  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472692   29 GRNGADGPNGRDGLPGPKGEKGEpalqvklssialeelKGDMGVRGPPGEPGLEGLMGAIGPRGPLGPAGPRGSSvGADG 108
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGE---------------TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD-GEAG 183


                 ....*...
gi 66472692  109 AKASEKPA 116
Cdd:NF038329 184 AKGPAGEK 191
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 110-245 5.68e-29

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: 106.23  E-value: 5.68e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472692    110 KASEKPAFSVLRNEASQAQyKQPVTFNDKLSDANDDFQIKTGYFTCKVPGVYYFVFHASSEGRLCLRLKSTSAPPVsLSF 189
Cdd:smart00110   3 KAQPRSAFSVIRSNRPPPP-GQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQV-MST 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 66472692    190 CDFNSKSVSLVVSGGAVLTLLKGDKVWIEPFAGDGGVGQMPKrLYAVFNGFLIYRN 245
Cdd:smart00110  81 YDEYQKGLYDVASGGALLQLRQGDQVWLELPDEKNGLYAGEY-VDSTFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 116-242 2.28e-27

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: 101.59  E-value: 2.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472692   116 AFSVLRNEASQAQYKQPVTFNDKLSDANDDFQIKTGYFTCKVPGVYYFVFHASSEGRLCLRLKSTSAPPVSLSFCDFNSK 195
Cdd:pfam00386   1 AFSAGRTTGLTAPNEQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDGKSLYVSLVKNGQEVVSFYDQPQK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 66472692   196 SVSLVVSGGAVLTLLKGDKVWIEPFaGDGGVGQMPKRLYAVFNGFLI 242
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLT-GYNGLYYDGSDTDSTFSGFLL 126
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 29-116 1.49e-10

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: 60.69  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472692   29 GRNGADGPNGRDGLPGPKGEKGEpalqvklssialeelKGDMGVRGPPGEPGLEGLMGAIGPRGPLGPAGPRGSSvGADG 108
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGE---------------TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD-GEAG 183


                 ....*...
gi 66472692  109 AKASEKPA 116
Cdd:NF038329 184 AKGPAGEK 191
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-116 1.26e-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: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472692   27 KHGRNGADGPNGRDGLPGPKGEKGEPALQVKLSSIALEELKGDMGVRGPPGEP--------GLEGLMGAIGPRGPLGPAG 98
Cdd:NF038329 178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqgpdGDPGPTGEDGPQGPDGPAG 257

                         90
                 ....*....|....*...
gi 66472692   99 PRGSSvGADGAKASEKPA 116
Cdd:NF038329 258 KDGPR-GDRGEAGPDGPD 274
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 29-108 1.86e-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: 1.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472692   29 GRNGADGPNGRDGLPGPKGEKGEPalqvklssialeelkGDMGVRGPPGEPGLEGLMGAIGPRGPLGPAGPRGSSvGADG 108
Cdd:NF038329 233 GQQGPDGDPGPTGEDGPQGPDGPA---------------GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN-GKDG 296
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 29-100 7.72e-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: 7.72e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66472692    29 GRNGADGPNGRDGLPGPKGEKGEPalqvklssialeelkGDMGVRGPPGEPGLEGLMGAIGPRGPLGPAGPR 100
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPP---------------GPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-110 8.30e-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: 49.13  E-value: 8.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472692   27 KHGRNGADGPNGRDGLPGPKGEKGEPalqvklssialeelkgdmGVRGPPGEPGLEglmGAIGPRGPLGPAGPRGSSvGA 106
Cdd:NF038329 252 PDGPAGKDGPRGDRGEAGPDGPDGKD------------------GERGPVGPAGKD---GQNGKDGLPGKDGKDGQN-GK 309


                 ....
gi 66472692  107 DGAK 110
Cdd:NF038329 310 DGLP 313
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 29-99 1.17e-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: 42.58  E-value: 1.17e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66472692   29 GRNGADGPNGRDGLPGPKGEKGEPalqvklssiALEELKGDMGVRGPPGEPGLEGLMGAIGPRGPLGPAGP 99
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQN---------GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 110-245 5.68e-29

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: 106.23  E-value: 5.68e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472692    110 KASEKPAFSVLRNEASQAQyKQPVTFNDKLSDANDDFQIKTGYFTCKVPGVYYFVFHASSEGRLCLRLKSTSAPPVsLSF 189
Cdd:smart00110   3 KAQPRSAFSVIRSNRPPPP-GQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQV-MST 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 66472692    190 CDFNSKSVSLVVSGGAVLTLLKGDKVWIEPFAGDGGVGQMPKrLYAVFNGFLIYRN 245
Cdd:smart00110  81 YDEYQKGLYDVASGGALLQLRQGDQVWLELPDEKNGLYAGEY-VDSTFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 116-242 2.28e-27

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: 101.59  E-value: 2.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472692   116 AFSVLRNEASQAQYKQPVTFNDKLSDANDDFQIKTGYFTCKVPGVYYFVFHASSEGRLCLRLKSTSAPPVSLSFCDFNSK 195
Cdd:pfam00386   1 AFSAGRTTGLTAPNEQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDGKSLYVSLVKNGQEVVSFYDQPQK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 66472692   196 SVSLVVSGGAVLTLLKGDKVWIEPFaGDGGVGQMPKRLYAVFNGFLI 242
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLT-GYNGLYYDGSDTDSTFSGFLL 126
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 29-116 1.49e-10

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: 60.69  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472692   29 GRNGADGPNGRDGLPGPKGEKGEpalqvklssialeelKGDMGVRGPPGEPGLEGLMGAIGPRGPLGPAGPRGSSvGADG 108
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGE---------------TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD-GEAG 183


                 ....*...
gi 66472692  109 AKASEKPA 116
Cdd:NF038329 184 AKGPAGEK 191
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-116 1.26e-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: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472692   27 KHGRNGADGPNGRDGLPGPKGEKGEPALQVKLSSIALEELKGDMGVRGPPGEP--------GLEGLMGAIGPRGPLGPAG 98
Cdd:NF038329 178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqgpdGDPGPTGEDGPQGPDGPAG 257

                         90
                 ....*....|....*...
gi 66472692   99 PRGSSvGADGAKASEKPA 116
Cdd:NF038329 258 KDGPR-GDRGEAGPDGPD 274
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 29-108 1.86e-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: 1.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472692   29 GRNGADGPNGRDGLPGPKGEKGEPalqvklssialeelkGDMGVRGPPGEPGLEGLMGAIGPRGPLGPAGPRGSSvGADG 108
Cdd:NF038329 233 GQQGPDGDPGPTGEDGPQGPDGPA---------------GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN-GKDG 296
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 29-100 7.72e-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: 7.72e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66472692    29 GRNGADGPNGRDGLPGPKGEKGEPalqvklssialeelkGDMGVRGPPGEPGLEGLMGAIGPRGPLGPAGPR 100
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPP---------------GPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 35-101 1.62e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.10  E-value: 1.62e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66472692    35 GPNGRDGLPGPKGEKGEPALQvklssialeelkGDMGVRGPPGEPGLEGLMGAIGPRGPLGPAGPRG 101
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPP------------GPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-110 8.30e-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: 49.13  E-value: 8.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472692   27 KHGRNGADGPNGRDGLPGPKGEKGEPalqvklssialeelkgdmGVRGPPGEPGLEglmGAIGPRGPLGPAGPRGSSvGA 106
Cdd:NF038329 252 PDGPAGKDGPRGDRGEAGPDGPDGKD------------------GERGPVGPAGKD---GQNGKDGLPGKDGKDGQN-GK 309


                 ....
gi 66472692  107 DGAK 110
Cdd:NF038329 310 DGLP 313
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 68-109 3.22e-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: 40.55  E-value: 3.22e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 66472692    68 GDMGVRGPPGEPGLEGLMGAIGPRGPLGPAGPRGsSVGADGA 109
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPG-PPGPPGP 41
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 29-99 1.17e-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: 42.58  E-value: 1.17e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66472692   29 GRNGADGPNGRDGLPGPKGEKGEPalqvklssiALEELKGDMGVRGPPGEPGLEGLMGAIGPRGPLGPAGP 99
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQN---------GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 67-110 1.10e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 1.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 66472692    67 KGDMGVRGPPGEPGLEGLMGAIGPRGPLGPAGPRGSSvGADGAK 110
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPP-GPPGPP 48
 
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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