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Conserved domains on  [gi|157820855|ref|NP_001100570|]
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collagen alpha-1(VIII) chain precursor [Rattus norvegicus]

Protein Classification

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 ...
 612-743 9.76e-65

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: 211.01  E-value: 9.76e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855   612 YEMPAFTAELTVPFPPVGAPVKFDKLLYNGRQNYNPQTGVFTCEVPGVYYFAYHVHCKGGNVWVALFKNNEPMMYTYDEY 691
Cdd:smart00110   5 QPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMSTYDEY 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 157820855   692 KKGFLDQASGSAVLLLRPGDRVFLQMPSEQaAGLYAGQYVHSSFSGYLLYPM 743
Cdd:smart00110  85 QKGLYDVASGGALLQLRQGDQVWLELPDEK-NGLYAGEYVDSTFSGFLLFPD 135
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 356-501 2.16e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 60.30  E-value: 2.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855 356 PGPKGDRGIGGVPGALGPRGEKGPVGAPGIGGPPGEPGLpgipgpmgppgaigfPGPKGEGGIVGPQGPPGPKGEPGLQG 435
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE---------------KGPAGPQGEAGPQGPAGKDGEAGAKG 186

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157820855 436 FPG---KPGFLGEVGPPGMRGLPGPIGPKGEAGHKGLPGLPGVPGLL--GPKGEPGIPGDQGLQGPPGIPG 501
Cdd:NF038329 187 PAGekgPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAG 257
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 612-743 9.76e-65

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: 211.01  E-value: 9.76e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855   612 YEMPAFTAELTVPFPPVGAPVKFDKLLYNGRQNYNPQTGVFTCEVPGVYYFAYHVHCKGGNVWVALFKNNEPMMYTYDEY 691
Cdd:smart00110   5 QPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMSTYDEY 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 157820855   692 KKGFLDQASGSAVLLLRPGDRVFLQMPSEQaAGLYAGQYVHSSFSGYLLYPM 743
Cdd:smart00110  85 QKGLYDVASGGALLQLRQGDQVWLELPDEK-NGLYAGEYVDSTFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 616-740 1.09e-50

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: 172.85  E-value: 1.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855  616 AFTAELTVPFP-PVGAPVKFDKLLYNGRQNYNPQTGVFTCEVPGVYYFAYHVH-CKGGNVWVALFKNNEPMMYTYDEYKK 693
Cdd:pfam00386   1 AFSAGRTTGLTaPNEQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQPQK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 157820855  694 GFLDQASGSAVLLLRPGDRVFLQMPSEQaaGLYAGQY-VHSSFSGYLL 740
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLTGYN--GLYYDGSdTDSTFSGFLL 126
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 356-501 2.16e-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: 60.30  E-value: 2.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855 356 PGPKGDRGIGGVPGALGPRGEKGPVGAPGIGGPPGEPGLpgipgpmgppgaigfPGPKGEGGIVGPQGPPGPKGEPGLQG 435
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE---------------KGPAGPQGEAGPQGPAGKDGEAGAKG 186

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157820855 436 FPG---KPGFLGEVGPPGMRGLPGPIGPKGEAGHKGLPGLPGVPGLL--GPKGEPGIPGDQGLQGPPGIPG 501
Cdd:NF038329 187 PAGekgPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAG 257
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 409-548 2.55e-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: 60.30  E-value: 2.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855 409 FPGPKGEGGIVGPQGPPGPKGEPGLQGFPGKPGFLGEVGPPGMRGLPGPIGPKGEAGHKGLPGLPGVPGLLGPKGEPGIP 488
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855 489 GDQGLQGPPGIPGIAGPSGPIGPPGIPGPKGEPGLPGPPGFPGVGKPGVAGLHGPPGKPG 548
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDG 254
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 447-501 1.93e-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: 45.56  E-value: 1.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157820855  447 GPPGMRGLPGPIGPKGEAGHKGLPGLPGVPGLLGPKGEPGIPGDQGLQGPPGIPG 501
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 273-476 1.46e-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: 47.98  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855 273 KPGVTGFPGPQGPLGKPGPPGEPGPQGLIGVPGVQGPPGMPG-------VGKPGQDGIPGQPGFPGGKGEQGLPGLPGPP 345
Cdd:NF038329 139 DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGeagakgpAGEKGPQGPRGETGPAGEQGPAGPAGPDGEA 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855 346 GLPGVGKPGFPGPKGDRGIGGVPGALGPRGEKGPVGAPGIGGPPGEPGLPGIPGPMGPPGAIGFPGPKGEGGIVGPQGPP 425
Cdd:NF038329 219 GPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLP 298

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157820855 426 GPKGEPGLQGFPGKPGFLGEVGPPGMRGLPGPIGPKGEAGhKGLPGLPGVP 476
Cdd:NF038329 299 GKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG-KPAPKTPEVP 348
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 146-497 1.89e-03

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 41.43  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855 146 KGKPGPQGYPG----IGKPGMPGMPGKPGAMGMPGAKGEIGPKGEIGPMGIPGPQGPPgphglpgigkpggpglpgqpga 221
Cdd:NF038329 119 KGEPGPAGPAGpageQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA---------------------- 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855 222 kgergpkgppgppglqgpkgekgfGMPGLPGLKGPpgmhgppgpvglpgvgkPGVTGFPGPQGPLGKPGPPGEPGPQGLI 301
Cdd:NF038329 177 ------------------------GKDGEAGAKGP-----------------AGEKGPQGPRGETGPAGEQGPAGPAGPD 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855 302 GVPGVQGPPGMPGVGKPGQDGIPGQPGFPGGKGEQGLPGLpgppglpgvgkpgfPGPKGDRGIGGVPGALGPRGEkgpvg 381
Cdd:NF038329 216 GEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGP--------------AGKDGPRGDRGEAGPDGPDGK----- 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855 382 apgiggppgepglpgipgpmgppgaigfpgpkgeggivgpqgppgpkgepglQGFPGKPGFLGEVGPPGMRGLPGPIGPK 461
Cdd:NF038329 277 ----------------------------------------------------DGERGPVGPAGKDGQNGKDGLPGKDGKD 304

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 157820855 462 GEAGHKGLPGLPGVPGLLGPKGEPGIPGDQGLQGPP 497
Cdd:NF038329 305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 612-743 9.76e-65

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: 211.01  E-value: 9.76e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855   612 YEMPAFTAELTVPFPPVGAPVKFDKLLYNGRQNYNPQTGVFTCEVPGVYYFAYHVHCKGGNVWVALFKNNEPMMYTYDEY 691
Cdd:smart00110   5 QPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMSTYDEY 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 157820855   692 KKGFLDQASGSAVLLLRPGDRVFLQMPSEQaAGLYAGQYVHSSFSGYLLYPM 743
Cdd:smart00110  85 QKGLYDVASGGALLQLRQGDQVWLELPDEK-NGLYAGEYVDSTFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 616-740 1.09e-50

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: 172.85  E-value: 1.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855  616 AFTAELTVPFP-PVGAPVKFDKLLYNGRQNYNPQTGVFTCEVPGVYYFAYHVH-CKGGNVWVALFKNNEPMMYTYDEYKK 693
Cdd:pfam00386   1 AFSAGRTTGLTaPNEQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQPQK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 157820855  694 GFLDQASGSAVLLLRPGDRVFLQMPSEQaaGLYAGQY-VHSSFSGYLL 740
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLTGYN--GLYYDGSdTDSTFSGFLL 126
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 356-501 2.16e-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: 60.30  E-value: 2.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855 356 PGPKGDRGIGGVPGALGPRGEKGPVGAPGIGGPPGEPGLpgipgpmgppgaigfPGPKGEGGIVGPQGPPGPKGEPGLQG 435
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE---------------KGPAGPQGEAGPQGPAGKDGEAGAKG 186

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157820855 436 FPG---KPGFLGEVGPPGMRGLPGPIGPKGEAGHKGLPGLPGVPGLL--GPKGEPGIPGDQGLQGPPGIPG 501
Cdd:NF038329 187 PAGekgPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAG 257
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 409-548 2.55e-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: 60.30  E-value: 2.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855 409 FPGPKGEGGIVGPQGPPGPKGEPGLQGFPGKPGFLGEVGPPGMRGLPGPIGPKGEAGHKGLPGLPGVPGLLGPKGEPGIP 488
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855 489 GDQGLQGPPGIPGIAGPSGPIGPPGIPGPKGEPGLPGPPGFPGVGKPGVAGLHGPPGKPG 548
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDG 254
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 447-501 1.93e-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: 45.56  E-value: 1.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157820855  447 GPPGMRGLPGPIGPKGEAGHKGLPGLPGVPGLLGPKGEPGIPGDQGLQGPPGIPG 501
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 273-476 1.46e-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: 47.98  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855 273 KPGVTGFPGPQGPLGKPGPPGEPGPQGLIGVPGVQGPPGMPG-------VGKPGQDGIPGQPGFPGGKGEQGLPGLPGPP 345
Cdd:NF038329 139 DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGeagakgpAGEKGPQGPRGETGPAGEQGPAGPAGPDGEA 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855 346 GLPGVGKPGFPGPKGDRGIGGVPGALGPRGEKGPVGAPGIGGPPGEPGLPGIPGPMGPPGAIGFPGPKGEGGIVGPQGPP 425
Cdd:NF038329 219 GPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLP 298

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157820855 426 GPKGEPGLQGFPGKPGFLGEVGPPGMRGLPGPIGPKGEAGhKGLPGLPGVP 476
Cdd:NF038329 299 GKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG-KPAPKTPEVP 348
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 438-492 1.83e-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: 42.48  E-value: 1.83e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157820855  438 GKPGFLGEVGPPGMRGLPGPIGPKGEAGHKGLPGLPGVPGLLGPKGEPGIPGDQG 492
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 433-481 1.02e-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: 37.86  E-value: 1.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 157820855  433 LQGFPGKPGFLGEVGPPGMRGLPGPIGPKGEAGHKGLPGLPGVPGLLGP 481
Cdd:pfam01391   8 PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 146-497 1.89e-03

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 41.43  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855 146 KGKPGPQGYPG----IGKPGMPGMPGKPGAMGMPGAKGEIGPKGEIGPMGIPGPQGPPgphglpgigkpggpglpgqpga 221
Cdd:NF038329 119 KGEPGPAGPAGpageQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA---------------------- 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855 222 kgergpkgppgppglqgpkgekgfGMPGLPGLKGPpgmhgppgpvglpgvgkPGVTGFPGPQGPLGKPGPPGEPGPQGLI 301
Cdd:NF038329 177 ------------------------GKDGEAGAKGP-----------------AGEKGPQGPRGETGPAGEQGPAGPAGPD 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855 302 GVPGVQGPPGMPGVGKPGQDGIPGQPGFPGGKGEQGLPGLpgppglpgvgkpgfPGPKGDRGIGGVPGALGPRGEkgpvg 381
Cdd:NF038329 216 GEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGP--------------AGKDGPRGDRGEAGPDGPDGK----- 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820855 382 apgiggppgepglpgipgpmgppgaigfpgpkgeggivgpqgppgpkgepglQGFPGKPGFLGEVGPPGMRGLPGPIGPK 461
Cdd:NF038329 277 ----------------------------------------------------DGERGPVGPAGKDGQNGKDGLPGKDGKD 304

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 157820855 462 GEAGHKGLPGLPGVPGLLGPKGEPGIPGDQGLQGPP 497
Cdd:NF038329 305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
 
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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