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Conserved domains on  [gi|1561678984|ref|XP_027622714|]
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collagen alpha-1(X) chain [Tupaia chinensis]

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 ...
 545-680 5.14e-68

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: 218.71  E-value: 5.14e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984  545 GVTGMPVSAFTVILSKAYPAIGAPIPFDKILYNRQQHYDPRTGIFTCRIPGIYYFSYHVHVKGTHVWVGLYKNGTPVMYT 624
Cdd:smart00110   1 NYKAQPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMST 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1561678984  625 YDEYAKGYLDQASGSAIIELTENDQVWLQLPNaESNGLYSSEYVHSSFSGFLVAPM 680
Cdd:smart00110  81 YDEYQKGLYDVASGGALLQLRQGDQVWLELPD-EKNGLYAGEYVDSTFSGFLLFPD 135
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 117-404 5.54e-22

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: 99.21  E-value: 5.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 117 PGERGPHGPKGDigpaglpgprgppgppgipgpagisvSGKPGQQGPTGAPGPRGFPGEKGAPGVRGANGQKGETGygap 196
Cdd:NF038329  128 AGPAGEQGPRGD--------------------------RGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG---- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 197 grpgerglpgpqgpmgppgppgvgKRGENGFPGQPGIKGDRGVPGErgpmgptgpqgppgargpegigkPGAAGTPGQPG 276
Cdd:NF038329  178 ------------------------KDGEAGAKGPAGEKGPQGPRGE-----------------------TGPAGEQGPAG 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 277 IPGAKGHPGTPGIAGPPGVPGFGKPGLPGLKGQRGPAGLPGGPGAKGEQGPVGHPGEPGLTGPPGNMGPQGPKGIPGNHG 356
Cdd:NF038329  211 PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1561678984 357 IPGAKGETGPVGPAGHPGAKGERGSPGVDGKPGYPGEPGLSGHKGNPG 404
Cdd:NF038329  291 QNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 545-680 5.14e-68

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: 218.71  E-value: 5.14e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984  545 GVTGMPVSAFTVILSKAYPAIGAPIPFDKILYNRQQHYDPRTGIFTCRIPGIYYFSYHVHVKGTHVWVGLYKNGTPVMYT 624
Cdd:smart00110   1 NYKAQPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMST 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1561678984  625 YDEYAKGYLDQASGSAIIELTENDQVWLQLPNaESNGLYSSEYVHSSFSGFLVAPM 680
Cdd:smart00110  81 YDEYQKGLYDVASGGALLQLRQGDQVWLELPD-EKNGLYAGEYVDSTFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 553-677 3.65e-52

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: 175.94  E-value: 3.65e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 553 AFTVILSKAYPAIGA-PIPFDKILYNRQQHYDPRTGIFTCRIPGIYYFSYHVH-VKGTHVWVGLYKNGTPVMYTYDEYAK 630
Cdd:pfam00386   1 AFSAGRTTGLTAPNEqPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQPQK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1561678984 631 GYLDQASGSAIIELTENDQVWLQLPNAesNGLYSSEY-VHSSFSGFLV 677
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLTGY--NGLYYDGSdTDSTFSGFLL 126
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 117-404 5.54e-22

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: 99.21  E-value: 5.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 117 PGERGPHGPKGDigpaglpgprgppgppgipgpagisvSGKPGQQGPTGAPGPRGFPGEKGAPGVRGANGQKGETGygap 196
Cdd:NF038329  128 AGPAGEQGPRGD--------------------------RGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG---- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 197 grpgerglpgpqgpmgppgppgvgKRGENGFPGQPGIKGDRGVPGErgpmgptgpqgppgargpegigkPGAAGTPGQPG 276
Cdd:NF038329  178 ------------------------KDGEAGAKGPAGEKGPQGPRGE-----------------------TGPAGEQGPAG 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 277 IPGAKGHPGTPGIAGPPGVPGFGKPGLPGLKGQRGPAGLPGGPGAKGEQGPVGHPGEPGLTGPPGNMGPQGPKGIPGNHG 356
Cdd:NF038329  211 PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1561678984 357 IPGAKGETGPVGPAGHPGAKGERGSPGVDGKPGYPGEPGLSGHKGNPG 404
Cdd:NF038329  291 QNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 223-449 7.84e-21

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: 95.74  E-value: 7.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 223 GENGFPGQPGIKGDRGVPGERGPMGPTGPQGPPGARGPEG-IGKPGAAGTPGQPGIPGAKGHPGTPGIAGPPGVPG-FGK 300
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGpQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGpAGE 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 301 PGLPGLKGQRGPAGLPGGPGAKGEQGPvGHPGEPGLTGPPGNMGPQGPKGIPGNHGIPGAKGETGPVGPAGHPGAKGERG 380
Cdd:NF038329  206 QGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG 284

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561678984 381 SPGVDG---KPGYPGEPGLSGHKGNPGLPGPKGDpgvggppglpgpvgpagaKGVPGHNGEAGPRGAPGIPG 449
Cdd:NF038329  285 PAGKDGqngKDGLPGKDGKDGQNGKDGLPGKDGK------------------DGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 156-507 8.20e-16

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: 80.33  E-value: 8.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 156 GKPGQQGPTGAPGPRGFPGEKGAPGVRGANGQKGETG-YGAPGRPGErglpgpqgpmgppgppgVGKRGENGFPGQPGIK 234
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGpQGERGEKGP-----------------AGPQGEAGPQGPAGKD 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 235 GDRGVPGERGpmgptgpqgppgARGPEGI-GKPGAAGTPGQPGIPGAKGHPGTPGIAGPPGVPGFGKPGlpglkgqrgpa 313
Cdd:NF038329  180 GEAGAKGPAG------------EKGPQGPrGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQG----------- 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 314 glpggpgAKGEQGPVGHPGEPGLTGPPGNMGPQGPKGIPGNHGIPGAKGETGPVGPAGHPGAKGERGSPGVDGKPGYPGE 393
Cdd:NF038329  237 -------PDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 394 PGLSGHKGNPGLpgpkgdpgvggppglpgpvgpagakgvPGHNGEAGPRGAPGIPGtrgpigppgipgfpgskgdpgnpg 473
Cdd:NF038329  310 DGLPGKDGKDGQ---------------------------PGKDGLPGKDGKDGQPG------------------------ 338

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1561678984 474 ppgpagiatkglngptgppgppgprghtgqpgLP 507
Cdd:NF038329  339 --------------------------------KP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 106-370 1.28e-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: 70.32  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 106 GKPGVPGLPGKPGERGPHGPKgdigpaglpgprgppgppgipgpagisvsGKPGQQGPTGAPGPRGFPGEKGAPGVRGAN 185
Cdd:NF038329  168 GEAGPQGPAGKDGEAGAKGPA-----------------------------GEKGPQGPRGETGPAGEQGPAGPAGPDGEA 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 186 GQKGETgyGAPGRPGERGLPGPQGPMGPPGPPGVGKRGENGFPGQPGIKGDRGVPGERgpmgptgpqgppgargpegiGK 265
Cdd:NF038329  219 GPAGED--GPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD--------------------GK 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 266 PGAAGTPGQPGIPGAKGHPGTPGIAGPPGVPgfGKPGLPGLKGQrgpaglPGGPGAKGEQGPVGHPGEPGLTGPPGNMGP 345
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQN--GKDGLPGKDGK------DGQPGKDGLPGKDGKDGQPGKPAPKTPEVP 348

                         250       260
                  ....*....|....*....|....*
gi 1561678984 346 QGPKGIPGNHGIPGAKGETGPVGPA 370
Cdd:NF038329  349 QKPDTAPHTPKTPQIPGQSKDVTPA 373
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 347-403 1.12e-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: 43.25  E-value: 1.12e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1561678984 347 GPKGIPGNHGIPGAKGETGPVGPAGHPGAKGERGSPGVDGKPGYPGEPGLSGHKGNP 403
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 239-394 4.37e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 4.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 239 VPGERGPMGPTGPQGPPGARGPEGIGKPGAAGTPGQPGIPGAKGHPGTPGIAGPPGVPGFGKPGLP--GLKGQRGPAGLP 316
Cdd:PRK07764  588 VGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHpkHVAVPDASDGGD 667

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1561678984 317 GGPGAKGEQGPVGHPGEPGLTGPPGNMGPQGPKGIPGNHGIPGAKGETGPVGPAGHPGAKGERGSPGVDGKPGYPGEP 394
Cdd:PRK07764  668 GWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEP 745
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 545-680 5.14e-68

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: 218.71  E-value: 5.14e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984  545 GVTGMPVSAFTVILSKAYPAIGAPIPFDKILYNRQQHYDPRTGIFTCRIPGIYYFSYHVHVKGTHVWVGLYKNGTPVMYT 624
Cdd:smart00110   1 NYKAQPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMST 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1561678984  625 YDEYAKGYLDQASGSAIIELTENDQVWLQLPNaESNGLYSSEYVHSSFSGFLVAPM 680
Cdd:smart00110  81 YDEYQKGLYDVASGGALLQLRQGDQVWLELPD-EKNGLYAGEYVDSTFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 553-677 3.65e-52

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: 175.94  E-value: 3.65e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 553 AFTVILSKAYPAIGA-PIPFDKILYNRQQHYDPRTGIFTCRIPGIYYFSYHVH-VKGTHVWVGLYKNGTPVMYTYDEYAK 630
Cdd:pfam00386   1 AFSAGRTTGLTAPNEqPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQPQK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1561678984 631 GYLDQASGSAIIELTENDQVWLQLPNAesNGLYSSEY-VHSSFSGFLV 677
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLTGY--NGLYYDGSdTDSTFSGFLL 126
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 117-404 5.54e-22

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: 99.21  E-value: 5.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 117 PGERGPHGPKGDigpaglpgprgppgppgipgpagisvSGKPGQQGPTGAPGPRGFPGEKGAPGVRGANGQKGETGygap 196
Cdd:NF038329  128 AGPAGEQGPRGD--------------------------RGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG---- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 197 grpgerglpgpqgpmgppgppgvgKRGENGFPGQPGIKGDRGVPGErgpmgptgpqgppgargpegigkPGAAGTPGQPG 276
Cdd:NF038329  178 ------------------------KDGEAGAKGPAGEKGPQGPRGE-----------------------TGPAGEQGPAG 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 277 IPGAKGHPGTPGIAGPPGVPGFGKPGLPGLKGQRGPAGLPGGPGAKGEQGPVGHPGEPGLTGPPGNMGPQGPKGIPGNHG 356
Cdd:NF038329  211 PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1561678984 357 IPGAKGETGPVGPAGHPGAKGERGSPGVDGKPGYPGEPGLSGHKGNPG 404
Cdd:NF038329  291 QNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 223-449 7.84e-21

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: 95.74  E-value: 7.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 223 GENGFPGQPGIKGDRGVPGERGPMGPTGPQGPPGARGPEG-IGKPGAAGTPGQPGIPGAKGHPGTPGIAGPPGVPG-FGK 300
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGpQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGpAGE 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 301 PGLPGLKGQRGPAGLPGGPGAKGEQGPvGHPGEPGLTGPPGNMGPQGPKGIPGNHGIPGAKGETGPVGPAGHPGAKGERG 380
Cdd:NF038329  206 QGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG 284

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561678984 381 SPGVDG---KPGYPGEPGLSGHKGNPGLPGPKGDpgvggppglpgpvgpagaKGVPGHNGEAGPRGAPGIPG 449
Cdd:NF038329  285 PAGKDGqngKDGLPGKDGKDGQNGKDGLPGKDGK------------------DGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 156-507 8.20e-16

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: 80.33  E-value: 8.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 156 GKPGQQGPTGAPGPRGFPGEKGAPGVRGANGQKGETG-YGAPGRPGErglpgpqgpmgppgppgVGKRGENGFPGQPGIK 234
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGpQGERGEKGP-----------------AGPQGEAGPQGPAGKD 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 235 GDRGVPGERGpmgptgpqgppgARGPEGI-GKPGAAGTPGQPGIPGAKGHPGTPGIAGPPGVPGFGKPGlpglkgqrgpa 313
Cdd:NF038329  180 GEAGAKGPAG------------EKGPQGPrGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQG----------- 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 314 glpggpgAKGEQGPVGHPGEPGLTGPPGNMGPQGPKGIPGNHGIPGAKGETGPVGPAGHPGAKGERGSPGVDGKPGYPGE 393
Cdd:NF038329  237 -------PDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 394 PGLSGHKGNPGLpgpkgdpgvggppglpgpvgpagakgvPGHNGEAGPRGAPGIPGtrgpigppgipgfpgskgdpgnpg 473
Cdd:NF038329  310 DGLPGKDGKDGQ---------------------------PGKDGLPGKDGKDGQPG------------------------ 338

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1561678984 474 ppgpagiatkglngptgppgppgprghtgqpgLP 507
Cdd:NF038329  339 --------------------------------KP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 106-370 1.28e-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: 70.32  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 106 GKPGVPGLPGKPGERGPHGPKgdigpaglpgprgppgppgipgpagisvsGKPGQQGPTGAPGPRGFPGEKGAPGVRGAN 185
Cdd:NF038329  168 GEAGPQGPAGKDGEAGAKGPA-----------------------------GEKGPQGPRGETGPAGEQGPAGPAGPDGEA 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 186 GQKGETgyGAPGRPGERGLPGPQGPMGPPGPPGVGKRGENGFPGQPGIKGDRGVPGERgpmgptgpqgppgargpegiGK 265
Cdd:NF038329  219 GPAGED--GPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD--------------------GK 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 266 PGAAGTPGQPGIPGAKGHPGTPGIAGPPGVPgfGKPGLPGLKGQrgpaglPGGPGAKGEQGPVGHPGEPGLTGPPGNMGP 345
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQN--GKDGLPGKDGK------DGQPGKDGLPGKDGKDGQPGKPAPKTPEVP 348

                         250       260
                  ....*....|....*....|....*
gi 1561678984 346 QGPKGIPGNHGIPGAKGETGPVGPA 370
Cdd:NF038329  349 QKPDTAPHTPKTPQIPGQSKDVTPA 373
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 347-403 1.12e-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: 43.25  E-value: 1.12e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1561678984 347 GPKGIPGNHGIPGAKGETGPVGPAGHPGAKGERGSPGVDGKPGYPGEPGLSGHKGNP 403
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 332-388 1.58e-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: 42.87  E-value: 1.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1561678984 332 GEPGLTGPPGNMGPQGPKGIPGNHGIPGAKGETGPVGPAGHPGAKGERGSPGVDGKP 388
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 335-394 2.59e-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: 39.40  E-value: 2.59e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 335 GLTGPPGNMGPQGPKGIPGNhgiPGAKGETGPVGPAGHPGAKGERGSPGVDGKPGYPGEP 394
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGP---PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 322-373 4.54e-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: 38.63  E-value: 4.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1561678984 322 KGEQGPVGHPGEPGLTGPPGNMGPQGPKGIPGNHGIPGAKGETGPVGPAGHP 373
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 257-402 9.75e-04

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 42.30  E-value: 9.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 257 ARGPEGIGKPGAAGTPGQPGIPGAKGHPGTPGIAGPP---GVPGFGKPGLPGLKGQRGPAGLPGGPGAKGEQGPVGHPGE 333
Cdd:pfam09606 165 QPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPpqmGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQ 244

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561678984 334 PGLTGPPGN-----MGPQGPKGIPGnhGIPGAKGETGPVGPAGHPGAKgergsPGVDGKPGYPGEPGLSGHKGN 402
Cdd:pfam09606 245 QQQPQQQGQqsqlgMGINQMQQMPQ--GVGGGAGQGGPGQPMGPPGQQ-----PGAMPNVMSIGDQNNYQQQQT 311
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 239-394 4.37e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 4.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561678984 239 VPGERGPMGPTGPQGPPGARGPEGIGKPGAAGTPGQPGIPGAKGHPGTPGIAGPPGVPGFGKPGLP--GLKGQRGPAGLP 316
Cdd:PRK07764  588 VGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHpkHVAVPDASDGGD 667

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1561678984 317 GGPGAKGEQGPVGHPGEPGLTGPPGNMGPQGPKGIPGNHGIPGAKGETGPVGPAGHPGAKGERGSPGVDGKPGYPGEP 394
Cdd:PRK07764  668 GWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEP 745
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 156-202 6.24e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.55  E-value: 6.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1561678984 156 GKPGQQGPTGAPGPRGFPGEKGAPGVRGANGQKGETgyGAPGRPGER 202
Cdd:pfam01391  13 GPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP--GAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 264-309 6.89e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.16  E-value: 6.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1561678984 264 GKPGAAGTPGQPGIPGAKGHPGTPGIAGPPGVPGF----GKPGLPGLKGQ 309
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPpgppGPPGPPGPPGA 50
 
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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