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Conserved domains on  [gi|49796|emb|CAA44741|]
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collagen-alpha-1 type X, partial [Mus musculus]

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 ...
 161-243 1.04e-40

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: 136.28  E-value: 1.04e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49796       161 GVTGMPVSAFTVILSKAYPAVGAPIPFDEILYNRQQHYDPRSGIFTCKIPGIYYFSYHVHVKGTHVWVGLYKNGTPTMYT 240
Cdd:smart00110   1 NYKAQPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMST 80


                   ...
gi 49796       241 YDE 243
Cdd:smart00110  81 YDE 83
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 5-99 1.23e-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: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49796       5 GYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGA---KGVPGHNGEAGPRGEPGIPGTKGPTGPPGVPGFPGS 81
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGErgeKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90
                 ....*....|....*...
gi 49796      82 KGDPGNPGAPGPAGIATK 99
Cdd:NF038329 197 RGETGPAGEQGPAGPAGP 214
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 161-243 1.04e-40

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: 136.28  E-value: 1.04e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49796       161 GVTGMPVSAFTVILSKAYPAVGAPIPFDEILYNRQQHYDPRSGIFTCKIPGIYYFSYHVHVKGTHVWVGLYKNGTPTMYT 240
Cdd:smart00110   1 NYKAQPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMST 80


                   ...
gi 49796       241 YDE 243
Cdd:smart00110  81 YDE 83
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 169-243 5.84e-29

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: 105.83  E-value: 5.84e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 49796      169 AFTVILSKAYPAVGA-PIPFDEILYNRQQHYDPRSGIFTCKIPGIYYFSYHVH-VKGTHVWVGLYKNGTPTMYTYDE 243
Cdd:pfam00386   1 AFSAGRTTGLTAPNEqPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQ 77
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 5-99 1.23e-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: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49796       5 GYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGA---KGVPGHNGEAGPRGEPGIPGTKGPTGPPGVPGFPGS 81
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGErgeKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90
                 ....*....|....*...
gi 49796      82 KGDPGNPGAPGPAGIATK 99
Cdd:NF038329 197 RGETGPAGEQGPAGPAGP 214
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1-108 2.89e-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: 59.53  E-value: 2.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49796       1 DGKTGYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHNGEAGPRGEPGIPGTKGPTGPPGVPGFPG 80
Cdd:NF038329 140 RGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAG 219

                         90       100
                 ....*....|....*....|....*...
gi 49796      81 SKGDPGNPGAPGPAGIATKGLNGPTGPP 108
Cdd:NF038329 220 PAGEDGPAGPAGDGQQGPDGDPGPTGED 247
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2-129 3.83e-09

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: 56.07  E-value: 3.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49796       2 GKTGYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHNGEAGPRGEPGIPGTKGPTGPPGVPGFPGS 81
Cdd:NF038329 123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGP 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 49796      82 KGDPGNPGAPGPAGIATKGLNGPTGPPGPPGPRGHSGEPGLPGPPGPP 129
Cdd:NF038329 203 AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQ 250
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1-95 1.56e-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: 54.53  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49796       1 DGKTGYPGEPGL--NGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHNGEAGPRGEPGIPGTKGPTGPPGVPGF 78
Cdd:NF038329 221 AGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGK 300

                         90
                 ....*....|....*..
gi 49796      79 PGSKGDPGNPGAPGPAG 95
Cdd:NF038329 301 DGKDGQNGKDGLPGKDG 317
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 5-61 9.65e-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: 44.79  E-value: 9.65e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 49796        5 GYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHNGEAGPRGEP 61
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1-111 1.14e-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: 45.67  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49796       1 DGKTGYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHNG--EAGPRGEPGIPGTKGPTGPPGVPGF 78
Cdd:NF038329 179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGK 258

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 49796      79 PGSKGDPGNPGAPGPAGIATKGLNGPTGP----------PGPP 111
Cdd:NF038329 259 DGPRGDRGEAGPDGPDGKDGERGPVGPAGkdgqngkdglPGKD 301
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 161-243 1.04e-40

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: 136.28  E-value: 1.04e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49796       161 GVTGMPVSAFTVILSKAYPAVGAPIPFDEILYNRQQHYDPRSGIFTCKIPGIYYFSYHVHVKGTHVWVGLYKNGTPTMYT 240
Cdd:smart00110   1 NYKAQPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMST 80


                   ...
gi 49796       241 YDE 243
Cdd:smart00110  81 YDE 83
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 169-243 5.84e-29

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: 105.83  E-value: 5.84e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 49796      169 AFTVILSKAYPAVGA-PIPFDEILYNRQQHYDPRSGIFTCKIPGIYYFSYHVH-VKGTHVWVGLYKNGTPTMYTYDE 243
Cdd:pfam00386   1 AFSAGRTTGLTAPNEqPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQ 77
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 5-99 1.23e-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: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49796       5 GYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGA---KGVPGHNGEAGPRGEPGIPGTKGPTGPPGVPGFPGS 81
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGErgeKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90
                 ....*....|....*...
gi 49796      82 KGDPGNPGAPGPAGIATK 99
Cdd:NF038329 197 RGETGPAGEQGPAGPAGP 214
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1-108 2.89e-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: 59.53  E-value: 2.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49796       1 DGKTGYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHNGEAGPRGEPGIPGTKGPTGPPGVPGFPG 80
Cdd:NF038329 140 RGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAG 219

                         90       100
                 ....*....|....*....|....*...
gi 49796      81 SKGDPGNPGAPGPAGIATKGLNGPTGPP 108
Cdd:NF038329 220 PAGEDGPAGPAGDGQQGPDGDPGPTGED 247
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2-129 3.83e-09

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: 56.07  E-value: 3.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49796       2 GKTGYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHNGEAGPRGEPGIPGTKGPTGPPGVPGFPGS 81
Cdd:NF038329 123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGP 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 49796      82 KGDPGNPGAPGPAGIATKGLNGPTGPPGPPGPRGHSGEPGLPGPPGPP 129
Cdd:NF038329 203 AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQ 250
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1-95 1.56e-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: 54.53  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49796       1 DGKTGYPGEPGL--NGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHNGEAGPRGEPGIPGTKGPTGPPGVPGF 78
Cdd:NF038329 221 AGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGK 300

                         90
                 ....*....|....*..
gi 49796      79 PGSKGDPGNPGAPGPAG 95
Cdd:NF038329 301 DGKDGQNGKDGLPGKDG 317
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 5-61 9.65e-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: 44.79  E-value: 9.65e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 49796        5 GYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHNGEAGPRGEP 61
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 8-62 2.25e-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: 2.25e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 49796        8 GEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHNGEAGPRGEPG 62
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1-111 1.14e-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: 45.67  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49796       1 DGKTGYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVPGHNG--EAGPRGEPGIPGTKGPTGPPGVPGF 78
Cdd:NF038329 179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGK 258

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 49796      79 PGSKGDPGNPGAPGPAGIATKGLNGPTGP----------PGPP 111
Cdd:NF038329 259 DGPRGDRGEAGPDGPDGKDGERGPVGPAGkdgqngkdglPGKD 301
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2-49 6.39e-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: 36.70  E-value: 6.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 49796        2 GKTGYPGEPGLNGPKGNPGLPGQKGDPGVGGTPGLRGPVGPVGAKGVP 49
Cdd:pfam01391  10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 23-94 1.16e-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: 1.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49796       23 GQKGDPGVGGTPGLRGPVGPVGAKGVPGHNGEAGPRGEPGIPGtkgptgppgvpgfpgSKGDPGNPGAPGPA 94
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPG---------------PPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 26-95 3.71e-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: 34.78  E-value: 3.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49796       26 GDPGVGGTPGLRGPVGPVGAKGVPGHNGEAGPRGEPGIPGtkgptgppgvpgfpgSKGDPGNPGAPGPAG 95
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPG---------------PPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 29-97 5.68e-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: 34.39  E-value: 5.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 49796       29 GVGGTPGLRGPVGPVGAKGVPGHNGEAGPRGEPGIPGtkgptgppgvpgfpgSKGDPGNPGAPGPAGIA 97
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPG---------------PPGPPGPPGPPGAPGAP 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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