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Conserved domains on  [gi|1974326289|ref|XP_039189927|]
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collagen alpha-1(XXVI) chain isoform X2 [Crotalus tigris]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 190-381 3.55e-25

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: 107.30  E-value: 3.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 190 RKPMGPVGLPGPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPGPRGYTGETGIPGPPGPPGPPASPNfpltfQQGVLYS 269
Cdd:NF038329  152 PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAG-----PAGEDGP 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 270 LQPNGEKENGEsqlastvidtilAGLPGPRgapgpiglpgppgssGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGE 349
Cdd:NF038329  227 AGPAGDGQQGP------------DGDPGPT---------------GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGE 279

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1974326289 350 RGPAGQTGERGIKGFPGEPGKKGEEGDRGADG 381
Cdd:NF038329  280 RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
 51-119 9.27e-21

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


:

Pssm-ID: 462204  Cd Length: 69  Bit Score: 85.55  E-value: 9.27e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1974326289  51 RHWCHYTVtrmVSCQVQNGSETVIQRVYQ----SCRWPGPCANlVRTLIRPTYKIAYRTVTALEWRCCPGFTG 119
Cdd:pfam07546   1 RNVCAYKV---VSCVVVTGTESYVQPVYKpyltWCAGHRRCST-YRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 190-381 3.55e-25

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: 107.30  E-value: 3.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 190 RKPMGPVGLPGPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPGPRGYTGETGIPGPPGPPGPPASPNfpltfQQGVLYS 269
Cdd:NF038329  152 PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAG-----PAGEDGP 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 270 LQPNGEKENGEsqlastvidtilAGLPGPRgapgpiglpgppgssGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGE 349
Cdd:NF038329  227 AGPAGDGQQGP------------DGDPGPT---------------GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGE 279

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1974326289 350 RGPAGQTGERGIKGFPGEPGKKGEEGDRGADG 381
Cdd:NF038329  280 RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 194-382 4.25e-24

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: 104.22  E-value: 4.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 194 GPVGLPGPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPGPRGYTGETGipgppgppgpPASPNFPltfqqgvlyslqPN 273
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG----------EAGPQGP------------AG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 274 GEKENGESQLASTVIDTILAGLPGPRGAPGPIGLPGPPGSSGPKGAPGPMGAPGvQGTPGSPGQPGLKGPKGDRGERGPA 353
Cdd:NF038329  178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA 256

                         170       180
                  ....*....|....*....|....*....
gi 1974326289 354 GQTGERGIKGFPGEPGKKGEEGDRGADGE 382
Cdd:NF038329  257 GKDGPRGDRGEAGPDGPDGKDGERGPVGP 285
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
 51-119 9.27e-21

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


Pssm-ID: 462204  Cd Length: 69  Bit Score: 85.55  E-value: 9.27e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1974326289  51 RHWCHYTVtrmVSCQVQNGSETVIQRVYQ----SCRWPGPCANlVRTLIRPTYKIAYRTVTALEWRCCPGFTG 119
Cdd:pfam07546   1 RNVCAYKV---VSCVVVTGTESYVQPVYKpyltWCAGHRRCST-YRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 190-374 8.32e-19

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: 88.42  E-value: 8.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 190 RKPMGPVGLPGPTGRPGLQGPKGEKGEIGERG---PAGSPGQLGPPGPRGYTGETGipgppgppgPPASPNFPLTFQQGV 266
Cdd:NF038329  167 QGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGetgPAGEQGPAGPAGPDGEAGPAG---------EDGPAGPAGDGQQGP 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 267 LYSLQPNGEK-ENGESQLASTVIDTILAGLPGPRGAPGPIGLPGPPGSSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKG 345
Cdd:NF038329  238 DGDPGPTGEDgPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317

                         170       180
                  ....*....|....*....|....*....
gi 1974326289 346 DRGERGPAGQTGERGIKGFPGEPGKKGEE 374
Cdd:NF038329  318 KDGQPGKDGLPGKDGKDGQPGKPAPKTPE 346
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 206-385 8.63e-19

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: 88.42  E-value: 8.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 206 GLQGPKGEkGEIGERGPAGSPGQLGPPGPRGYTGETGipgppgppgppaspnfpltfQQGVLYSLQPNGEkengesqlas 285
Cdd:NF038329  109 GLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETG--------------------PAGPAGPPGPQGE---------- 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 286 tvidtilAGLPGPrgapgpiglpgppgsSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFP 365
Cdd:NF038329  158 -------RGEKGP---------------AGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPD 215

                         170       180
                  ....*....|....*....|
gi 1974326289 366 GEPGKKGEEGDRGADGEGVQ 385
Cdd:NF038329  216 GEAGPAGEDGPAGPAGDGQQ 235
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 315-386 6.30e-14

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: 73.40  E-value: 6.30e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1974326289 315 GPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGKKGEEGDRGADGEGVQQ 386
Cdd:NF038329  135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQ 206
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 318-373 6.21e-12

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: 60.20  E-value: 6.21e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1974326289 318 GAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGKKGE 373
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
199-383 3.43e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 46.18  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 199 PGPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPGPRGYTGETGipgppgppgpPASPNFPLTFQQGvlySLQPNGEKEN 278
Cdd:COG5164     6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQ----------NQGSTTPAGNTGG---TRPAGNQGAT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 279 GESQLASTVIDTILAGLPGPRGAPGPIGLPGPPGSSGPKGAPGPMGAPGVQG--TPGSPGQPGLKGPKG----DRGERGP 352
Cdd:COG5164    73 GPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGstTPPSGGSTTPPGDGGstppGPGSTGP 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1974326289 353 AGQTGERGIKGFPGEPGKKGEEGDRGADGEG 383
Cdd:COG5164   153 GGSTTPPGDGGSTTPPGPGGSTTPPDDGGST 183
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 190-381 3.55e-25

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: 107.30  E-value: 3.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 190 RKPMGPVGLPGPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPGPRGYTGETGIPGPPGPPGPPASPNfpltfQQGVLYS 269
Cdd:NF038329  152 PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAG-----PAGEDGP 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 270 LQPNGEKENGEsqlastvidtilAGLPGPRgapgpiglpgppgssGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGE 349
Cdd:NF038329  227 AGPAGDGQQGP------------DGDPGPT---------------GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGE 279

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1974326289 350 RGPAGQTGERGIKGFPGEPGKKGEEGDRGADG 381
Cdd:NF038329  280 RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 194-382 4.25e-24

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: 104.22  E-value: 4.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 194 GPVGLPGPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPGPRGYTGETGipgppgppgpPASPNFPltfqqgvlyslqPN 273
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG----------EAGPQGP------------AG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 274 GEKENGESQLASTVIDTILAGLPGPRGAPGPIGLPGPPGSSGPKGAPGPMGAPGvQGTPGSPGQPGLKGPKGDRGERGPA 353
Cdd:NF038329  178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA 256

                         170       180
                  ....*....|....*....|....*....
gi 1974326289 354 GQTGERGIKGFPGEPGKKGEEGDRGADGE 382
Cdd:NF038329  257 GKDGPRGDRGEAGPDGPDGKDGERGPVGP 285
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
 51-119 9.27e-21

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


Pssm-ID: 462204  Cd Length: 69  Bit Score: 85.55  E-value: 9.27e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1974326289  51 RHWCHYTVtrmVSCQVQNGSETVIQRVYQ----SCRWPGPCANlVRTLIRPTYKIAYRTVTALEWRCCPGFTG 119
Cdd:pfam07546   1 RNVCAYKV---VSCVVVTGTESYVQPVYKpyltWCAGHRRCST-YRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 190-374 8.32e-19

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: 88.42  E-value: 8.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 190 RKPMGPVGLPGPTGRPGLQGPKGEKGEIGERG---PAGSPGQLGPPGPRGYTGETGipgppgppgPPASPNFPLTFQQGV 266
Cdd:NF038329  167 QGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGetgPAGEQGPAGPAGPDGEAGPAG---------EDGPAGPAGDGQQGP 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 267 LYSLQPNGEK-ENGESQLASTVIDTILAGLPGPRGAPGPIGLPGPPGSSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKG 345
Cdd:NF038329  238 DGDPGPTGEDgPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317

                         170       180
                  ....*....|....*....|....*....
gi 1974326289 346 DRGERGPAGQTGERGIKGFPGEPGKKGEE 374
Cdd:NF038329  318 KDGQPGKDGLPGKDGKDGQPGKPAPKTPE 346
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 206-385 8.63e-19

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: 88.42  E-value: 8.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 206 GLQGPKGEkGEIGERGPAGSPGQLGPPGPRGYTGETGipgppgppgppaspnfpltfQQGVLYSLQPNGEkengesqlas 285
Cdd:NF038329  109 GLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETG--------------------PAGPAGPPGPQGE---------- 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 286 tvidtilAGLPGPrgapgpiglpgppgsSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFP 365
Cdd:NF038329  158 -------RGEKGP---------------AGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPD 215

                         170       180
                  ....*....|....*....|
gi 1974326289 366 GEPGKKGEEGDRGADGEGVQ 385
Cdd:NF038329  216 GEAGPAGEDGPAGPAGDGQQ 235
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 315-386 6.30e-14

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: 73.40  E-value: 6.30e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1974326289 315 GPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGKKGEEGDRGADGEGVQQ 386
Cdd:NF038329  135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQ 206
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 318-373 6.21e-12

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: 60.20  E-value: 6.21e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1974326289 318 GAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGKKGE 373
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 315-370 1.51e-11

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: 59.43  E-value: 1.51e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1974326289 315 GPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGK 370
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 321-377 2.37e-11

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: 58.66  E-value: 2.37e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1974326289 321 GPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGKKGEEGDR 377
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 315-368 1.98e-10

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: 55.96  E-value: 1.98e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1974326289 315 GPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEP 368
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 192-243 2.81e-10

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: 55.58  E-value: 2.81e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1974326289 192 PMGPVGLPGPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPGPRGYTGETGI 243
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 327-382 1.31e-09

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: 53.65  E-value: 1.31e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1974326289 327 GVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGKKGEEGDRGADGE 382
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 294-363 1.32e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.96  E-value: 1.32e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 294 GLPGPRgapgpiglpgppgssGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKG 363
Cdd:pfam01391   1 GPPGPP---------------GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 200-241 5.11e-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: 5.11e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1974326289 200 GPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPGPRGYTGET 241
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPP 42
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
199-383 3.43e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 46.18  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 199 PGPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPGPRGYTGETGipgppgppgpPASPNFPLTFQQGvlySLQPNGEKEN 278
Cdd:COG5164     6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQ----------NQGSTTPAGNTGG---TRPAGNQGAT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 279 GESQLASTVIDTILAGLPGPRGAPGPIGLPGPPGSSGPKGAPGPMGAPGVQG--TPGSPGQPGLKGPKG----DRGERGP 352
Cdd:COG5164    73 GPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGstTPPSGGSTTPPGDGGstppGPGSTGP 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1974326289 353 AGQTGERGIKGFPGEPGKKGEEGDRGADGEG 383
Cdd:COG5164   153 GGSTTPPGDGGSTTPPGPGGSTTPPDDGGST 183
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
194-381 5.99e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.41  E-value: 5.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 194 GPVGLPGPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPGPRGYTGETGIPGPPGPPGPPASPNFPLtfqqgvlyslqpN 273
Cdd:COG5164    55 TPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPD------------D 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326289 274 GEKENGESQLASTVIDTILAGLPGPrgapGPIGLPGPPGSSGPKGAPGPMGAPGVQGTPGSPGQ--PGLKGPKGDRGERG 351
Cdd:COG5164   123 GGSTTPPSGGSTTPPGDGGSTPPGP----GSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSttPPNKGETGTDIPTG 198

                         170       180       190
                  ....*....|....*....|....*....|
gi 1974326289 352 PAGQTGERGIKGFPGEPGKKGEEGDRGADG 381
Cdd:COG5164   199 GTPRQGPDGPVKKDDKNGKGNPPDDRGGKT 228
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 292-347 3.46e-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: 3.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1974326289 292 LAGLPGPRGAPGPIGLPGPPGSSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDR 347
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
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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