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Conserved domains on  [gi|61098164|ref|NP_780634|]
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complement C1q tumor necrosis factor-related protein 7 isoform b precursor [Mus musculus]

Protein Classification

complement C1q domain-containing protein( domain architecture ID 10448922)

complement C1q domain-containing protein may be involved in the regulation of the inflammatory network

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 149-273 1.95e-54

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: 172.47  E-value: 1.95e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61098164   149 AFSVGITTS-YPEERLPIIFNKVLFNEGEHYNPATGKFICAFPGIYYFSYDITLAN-KHLAIGLVHNGQYRIRTFDANT- 225
Cdd:pfam00386   1 AFSAGRTTGlTAPNEQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDgKSLYVSLVKNGQEVVSFYDQPQk 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 61098164   226 GNHDVASGSTVIYLQPEDEVWLEIFfnDQNGLFSDPGWADSLFSGFLL 273
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLT--GYNGLYYDGSDTDSTFSGFLL 126
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 56-137 1.35e-13

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 70.32  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61098164   56 GRIGLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPEGEKGEVGPAGPPGPKGDRGDQGDPGL 135
Cdd:NF038329 141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220


                 ..
gi 61098164  136 PG 137
Cdd:NF038329 221 AG 222
 
Name Accession Description Interval E-value
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 149-273 1.95e-54

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: 172.47  E-value: 1.95e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61098164   149 AFSVGITTS-YPEERLPIIFNKVLFNEGEHYNPATGKFICAFPGIYYFSYDITLAN-KHLAIGLVHNGQYRIRTFDANT- 225
Cdd:pfam00386   1 AFSAGRTTGlTAPNEQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDgKSLYVSLVKNGQEVVSFYDQPQk 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 61098164   226 GNHDVASGSTVIYLQPEDEVWLEIFfnDQNGLFSDPGWADSLFSGFLL 273
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLT--GYNGLYYDGSDTDSTFSGFLL 126
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 147-276 3.05e-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: 154.38  E-value: 3.05e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61098164    147 KSAFSVGITTSYPEERLPIIFNKVLFNEGEHYNPATGKFICAFPGIYYFSYDITLANKHLAIGLVHNGQYRIRTFDANT- 225
Cdd:smart00110   7 RSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMSTYDEYQk 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 61098164    226 GNHDVASGSTVIYLQPEDEVWLEIfFNDQNGLFSDpGWADSLFSGFLLYVD 276
Cdd:smart00110  87 GLYDVASGGALLQLRQGDQVWLEL-PDEKNGLYAG-EYVDSTFSGFLLFPD 135
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 56-137 1.35e-13

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 70.32  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61098164   56 GRIGLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPEGEKGEVGPAGPPGPKGDRGDQGDPGL 135
Cdd:NF038329 141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220


                 ..
gi 61098164  136 PG 137
Cdd:NF038329 221 AG 222
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 59-137 5.24e-12

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: 65.70  E-value: 5.24e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61098164   59 GLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPEGEKGEVGPAGPPGPKGDRGDQGDPGLPG 137
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 61-137 1.39e-11

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: 64.54  E-value: 1.39e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61098164   61 PGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPEGEKGEvgpagppGPKGDRGDQGDPGLPG 137
Cdd:NF038329 176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP-------AGDGQQGPDGDPGPTG 245
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 56-137 3.37e-11

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: 63.39  E-value: 3.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61098164   56 GRIGLPGRDGR--DGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGK---------KGPIGPEGEKGEVGPAGPPGPK 124
Cdd:NF038329 222 GEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPdgpdgkdgeRGPVGPAGKDGQNGKDGLPGKD 301

                         90
                 ....*....|...
gi 61098164  125 GDRGDQGDPGLPG 137
Cdd:NF038329 302 GKDGQNGKDGLPG 314
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 56-109 8.96e-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: 52.99  E-value: 8.96e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 61098164   56 GRIGLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPE 109
Cdd:NF038329 293 GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPE 346
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 59-108 1.21e-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: 47.49  E-value: 1.21e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 61098164    59 GLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGP 108
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
 59-137 2.31e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.18  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61098164   59 GLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLA-GEKGDQGETGKKGPIGPEGEKGEVGPAGPPGPKGDRGDQGDPGLPG 137
Cdd:PHA03169  90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENtSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQP 169
 
Name Accession Description Interval E-value
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 149-273 1.95e-54

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: 172.47  E-value: 1.95e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61098164   149 AFSVGITTS-YPEERLPIIFNKVLFNEGEHYNPATGKFICAFPGIYYFSYDITLAN-KHLAIGLVHNGQYRIRTFDANT- 225
Cdd:pfam00386   1 AFSAGRTTGlTAPNEQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDgKSLYVSLVKNGQEVVSFYDQPQk 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 61098164   226 GNHDVASGSTVIYLQPEDEVWLEIFfnDQNGLFSDPGWADSLFSGFLL 273
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLT--GYNGLYYDGSDTDSTFSGFLL 126
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 147-276 3.05e-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: 154.38  E-value: 3.05e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61098164    147 KSAFSVGITTSYPEERLPIIFNKVLFNEGEHYNPATGKFICAFPGIYYFSYDITLANKHLAIGLVHNGQYRIRTFDANT- 225
Cdd:smart00110   7 RSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMSTYDEYQk 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 61098164    226 GNHDVASGSTVIYLQPEDEVWLEIfFNDQNGLFSDpGWADSLFSGFLLYVD 276
Cdd:smart00110  87 GLYDVASGGALLQLRQGDQVWLEL-PDEKNGLYAG-EYVDSTFSGFLLFPD 135
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 56-137 1.35e-13

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 70.32  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61098164   56 GRIGLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPEGEKGEVGPAGPPGPKGDRGDQGDPGL 135
Cdd:NF038329 141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220


                 ..
gi 61098164  136 PG 137
Cdd:NF038329 221 AG 222
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 59-137 5.24e-12

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: 65.70  E-value: 5.24e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61098164   59 GLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPEGEKGEVGPAGPPGPKGDRGDQGDPGLPG 137
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 61-137 1.39e-11

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: 64.54  E-value: 1.39e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61098164   61 PGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPEGEKGEvgpagppGPKGDRGDQGDPGLPG 137
Cdd:NF038329 176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP-------AGDGQQGPDGDPGPTG 245
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 56-137 3.37e-11

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: 63.39  E-value: 3.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61098164   56 GRIGLPGRDGR--DGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGK---------KGPIGPEGEKGEVGPAGPPGPK 124
Cdd:NF038329 222 GEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPdgpdgkdgeRGPVGPAGKDGQNGKDGLPGKD 301

                         90
                 ....*....|...
gi 61098164  125 GDRGDQGDPGLPG 137
Cdd:NF038329 302 GKDGQNGKDGLPG 314
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 56-109 8.96e-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: 52.99  E-value: 8.96e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 61098164   56 GRIGLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPE 109
Cdd:NF038329 293 GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPE 346
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 59-108 1.21e-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: 47.49  E-value: 1.21e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 61098164    59 GLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGP 108
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 65-118 6.48e-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: 39.78  E-value: 6.48e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 61098164    65 GRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPEGEKGEvgpA 118
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA---P 51
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 74-137 8.13e-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: 39.78  E-value: 8.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61098164    74 GEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPEGEKGEvgpagppgpKGDRGDQGDPGLPG 137
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGP---------PGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 59-137 2.31e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.18  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61098164   59 GLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLA-GEKGDQGETGKKGPIGPEGEKGEVGPAGPPGPKGDRGDQGDPGLPG 137
Cdd:PHA03169  90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENtSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQP 169
 
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.
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