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Conserved domains on  [gi|1974326295|ref|XP_039189930|]
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collagen alpha-1(XXVI) chain isoform X4 [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 ...
 192-352 3.29e-27

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: 112.69  E-value: 3.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 192 RKPMGPVGLPGPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPGPRGYTGETGIPGPPGPPGPPASPNFPLTFQQGVLYS 271
Cdd:NF038329  152 PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 272 LQPNGEKeSPPGSSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGKKGEEGDRGAD 351
Cdd:NF038329  232 DGQQGPD-GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD 310


                  .
gi 1974326295 352 G 352
Cdd:NF038329  311 G 311
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
 51-121 8.75e-22

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: 88.25  E-value: 8.75e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1974326295  51 RHWCHYTVtrmVSCQVQNGSETVIQRVYQ----SCRWPGPCAnlvSYRTLIRPTYKIAYRTVTALEWRCCPGFTG 121
Cdd:pfam07546   1 RNVCAYKV---VSCVVVTGTESYVQPVYKpyltWCAGHRRCS---TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 192-352 3.29e-27

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: 112.69  E-value: 3.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 192 RKPMGPVGLPGPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPGPRGYTGETGIPGPPGPPGPPASPNFPLTFQQGVLYS 271
Cdd:NF038329  152 PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 272 LQPNGEKeSPPGSSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGKKGEEGDRGAD 351
Cdd:NF038329  232 DGQQGPD-GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD 310


                  .
gi 1974326295 352 G 352
Cdd:NF038329  311 G 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 196-353 3.00e-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: 106.91  E-value: 3.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 196 GPVGLPGPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPGPRGYTGETGipgppgpPGPPASPNFPLTfQQGVLYSLQPN 275
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG-------PQGEAGPQGPAG-KDGEAGAKGPA 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 276 GEK--ESPPGSSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGD--RGERGPAGQTGERGIKGFPGEPGKKGEEGDRGAD 351
Cdd:NF038329  189 GEKgpQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268


                  ..
gi 1974326295 352 GE 353
Cdd:NF038329  269 GP 270
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 208-356 1.07e-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: 99.59  E-value: 1.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 208 GLQGPKGEkGEIGERGPAGSPGQLGPPGPRGYTGETGipgppgppgppaspnfpltfQQGVLYSLQPNGEKeSPPGSSGP 287
Cdd:NF038329  109 GLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETG--------------------PAGPAGPPGPQGER-GEKGPAGP 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1974326295 288 KGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGKKGEEGDRGADGEGVQ 356
Cdd:NF038329  167 QGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQ 235
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
 51-121 8.75e-22

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: 88.25  E-value: 8.75e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1974326295  51 RHWCHYTVtrmVSCQVQNGSETVIQRVYQ----SCRWPGPCAnlvSYRTLIRPTYKIAYRTVTALEWRCCPGFTG 121
Cdd:pfam07546   1 RNVCAYKV---VSCVVVTGTESYVQPVYKpyltWCAGHRRCS---TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 192-345 1.50e-15

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: 78.02  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 192 RKPMGPVGLPGPTGRPGLQGPKGEKGEIGERG---PAGSPGQLGPPGPRGYTGETGIPGPPGPPGPPASPNFPLTFQQGV 268
Cdd:NF038329  167 QGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGetgPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGE 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 269 LYSLQPNGE-----------------------KESPPG------SSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRG 319
Cdd:NF038329  247 DGPQGPDGPagkdgprgdrgeagpdgpdgkdgERGPVGpagkdgQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326

                         170       180
                  ....*....|....*....|....*.
gi 1974326295 320 ERGPAGQTGErgikgfPGEPGKKGEE 345
Cdd:NF038329  327 LPGKDGKDGQ------PGKPAPKTPE 346
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 281-357 8.37e-15

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: 75.71  E-value: 8.37e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1974326295 281 PPGSSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGKKGEEGDRGADGEGVQQ 357
Cdd:NF038329  130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQ 206
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 289-344 1.03e-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: 59.81  E-value: 1.03e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1974326295 289 GAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGKKGE 344
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
196-352 2.32e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 56.19  E-value: 2.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 196 GPVGLPGPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPG------PRGYTGETGIPGPPGPPGPPASPNFPLTFQQGVL 269
Cdd:COG5164    55 TPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGntggttPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGST 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 270 YSLQPNGEKESPPGSSGPKGAPGPMGAPGVQGTPGSPGQ-----------PGLKGPKGDRGERGPAGQTGERGIKGFPGE 338
Cdd:COG5164   135 TPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSttppddggsttPPNKGETGTDIPTGGTPRQGPDGPVKKDDK 214

                         170
                  ....*....|....
gi 1974326295 339 PGKKGEEGDRGADG 352
Cdd:COG5164   215 NGKGNPPDDRGGKT 228
PHA03378 PHA03378
EBNA-3B; Provisional
 183-334 3.62e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.13  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 183 PLANPGTALRKPMGPVGLPGPTGRPG-LQGPKGEKGEIgeRGPAGSPGQLGPPGPRGYTGETGIPGPPGPPGPPASPNfP 261
Cdd:PHA03378  687 IQWAPGTMQPPPRAPTPMRPPAAPPGrAQRPAAATGRA--RPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPG-R 763

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1974326295 262 LTFQQGVlyslqPNGEKESPPGSSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKG 334
Cdd:PHA03378  764 ARPPAAA-----PGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTG 831
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 192-352 3.29e-27

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: 112.69  E-value: 3.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 192 RKPMGPVGLPGPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPGPRGYTGETGIPGPPGPPGPPASPNFPLTFQQGVLYS 271
Cdd:NF038329  152 PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 272 LQPNGEKeSPPGSSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGKKGEEGDRGAD 351
Cdd:NF038329  232 DGQQGPD-GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD 310


                  .
gi 1974326295 352 G 352
Cdd:NF038329  311 G 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 196-353 3.00e-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: 106.91  E-value: 3.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 196 GPVGLPGPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPGPRGYTGETGipgppgpPGPPASPNFPLTfQQGVLYSLQPN 275
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG-------PQGEAGPQGPAG-KDGEAGAKGPA 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 276 GEK--ESPPGSSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGD--RGERGPAGQTGERGIKGFPGEPGKKGEEGDRGAD 351
Cdd:NF038329  189 GEKgpQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268


                  ..
gi 1974326295 352 GE 353
Cdd:NF038329  269 GP 270
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 208-356 1.07e-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: 99.59  E-value: 1.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 208 GLQGPKGEkGEIGERGPAGSPGQLGPPGPRGYTGETGipgppgppgppaspnfpltfQQGVLYSLQPNGEKeSPPGSSGP 287
Cdd:NF038329  109 GLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETG--------------------PAGPAGPPGPQGER-GEKGPAGP 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1974326295 288 KGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGKKGEEGDRGADGEGVQ 356
Cdd:NF038329  167 QGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQ 235
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
 51-121 8.75e-22

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: 88.25  E-value: 8.75e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1974326295  51 RHWCHYTVtrmVSCQVQNGSETVIQRVYQ----SCRWPGPCAnlvSYRTLIRPTYKIAYRTVTALEWRCCPGFTG 121
Cdd:pfam07546   1 RNVCAYKV---VSCVVVTGTESYVQPVYKpyltWCAGHRRCS---TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 192-345 1.50e-15

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: 78.02  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 192 RKPMGPVGLPGPTGRPGLQGPKGEKGEIGERG---PAGSPGQLGPPGPRGYTGETGIPGPPGPPGPPASPNFPLTFQQGV 268
Cdd:NF038329  167 QGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGetgPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGE 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 269 LYSLQPNGE-----------------------KESPPG------SSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRG 319
Cdd:NF038329  247 DGPQGPDGPagkdgprgdrgeagpdgpdgkdgERGPVGpagkdgQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326

                         170       180
                  ....*....|....*....|....*.
gi 1974326295 320 ERGPAGQTGErgikgfPGEPGKKGEE 345
Cdd:NF038329  327 LPGKDGKDGQ------PGKPAPKTPE 346
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 281-357 8.37e-15

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: 75.71  E-value: 8.37e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1974326295 281 PPGSSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGKKGEEGDRGADGEGVQQ 357
Cdd:NF038329  130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQ 206
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 289-344 1.03e-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: 59.81  E-value: 1.03e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1974326295 289 GAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGKKGE 344
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 286-341 2.54e-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: 2.54e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1974326295 286 GPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGK 341
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 292-348 4.06e-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: 57.89  E-value: 4.06e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1974326295 292 GPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGKKGEEGDR 348
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 283-339 6.18e-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: 57.50  E-value: 6.18e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1974326295 283 GSSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEP 339
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 194-245 4.46e-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: 55.19  E-value: 4.46e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1974326295 194 PMGPVGLPGPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPGPRGYTGETGI 245
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 298-353 2.03e-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: 53.27  E-value: 2.03e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1974326295 298 GVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGKKGEEGDRGADGE 353
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 281-330 4.95e-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: 52.11  E-value: 4.95e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1974326295 281 PPGSSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGER 330
Cdd:pfam01391   8 PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
196-352 2.32e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 56.19  E-value: 2.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 196 GPVGLPGPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPG------PRGYTGETGIPGPPGPPGPPASPNFPLTFQQGVL 269
Cdd:COG5164    55 TPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGntggttPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGST 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 270 YSLQPNGEKESPPGSSGPKGAPGPMGAPGVQGTPGSPGQ-----------PGLKGPKGDRGERGPAGQTGERGIKGFPGE 338
Cdd:COG5164   135 TPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSttppddggsttPPNKGETGTDIPTGGTPRQGPDGPVKKDDK 214

                         170
                  ....*....|....
gi 1974326295 339 PGKKGEEGDRGADG 352
Cdd:COG5164   215 NGKGNPPDDRGGKT 228
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
196-354 3.70e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 48.87  E-value: 3.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 196 GPVGLPGPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPGPRGYTGETGIPGPPGPPGppaspnfpltfqqgvlyslqpN 275
Cdd:COG5164    37 RPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAG---------------------N 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 276 GEKESPPGSSGPKGAPGPMGAPGVQGTPGSPGQP--GLKGPKGDRGER-------GPAGQTGERGIKGFPGEPGKKGEEG 346
Cdd:COG5164    96 TGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGGSTppgpgstGPGGSTTPPGDGGSTTPPGPGGSTT 175


                  ....*...
gi 1974326295 347 DRGADGEG 354
Cdd:COG5164   176 PPDDGGST 183
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
201-354 9.26e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 47.72  E-value: 9.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 201 PGPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPGPRGYTGETGIPGPPGPPGppaspnfpltfQQGVLYSLQPNGEKES 280
Cdd:COG5164     6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAG-----------NTGGTRPAGNQGATGP 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1974326295 281 P--PGSSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGikgfPGEPGKKGEEGDRGADGEG 354
Cdd:COG5164    75 AqnQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT----PPSGGSTTPPGDGGSTPPG 146
PHA03378 PHA03378
EBNA-3B; Provisional
 183-334 3.62e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.13  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 183 PLANPGTALRKPMGPVGLPGPTGRPG-LQGPKGEKGEIgeRGPAGSPGQLGPPGPRGYTGETGIPGPPGPPGPPASPNfP 261
Cdd:PHA03378  687 IQWAPGTMQPPPRAPTPMRPPAAPPGrAQRPAAATGRA--RPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPG-R 763

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1974326295 262 LTFQQGVlyslqPNGEKESPPGSSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKG 334
Cdd:PHA03378  764 ARPPAAA-----PGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTG 831
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 202-297 1.28e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.70  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 202 GPTGRPGLQGPKGEKGEIGERGPAGSPGQLGPPGPRGYTGETgipgppgppgppaspnfpltfqqgvlyslqpngekesp 281
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPP-------------------------------------- 42

                          90
                  ....*....|....*.
gi 1974326295 282 pGSSGPKGAPGPMGAP 297
Cdd:pfam01391  43 -GPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 196-352 2.58e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.95  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 196 GPVGLPGPTGRPGLQGPKGEKG----EIGERGPAGSPGQLGPPGPRGYTGEtgiPGPPGPPGPPASPNfpltfqQGVLYS 271
Cdd:PHA03169   96 GSESVGSPTPSPSGSAEELASGlspeNTSGSSPESPASHSPPPSPPSHPGP---HEPAPPESHNPSPN------QQPSSF 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974326295 272 LQPNGEKESPPGsSGPKGAPGPMGAPGVQGTPGSPGQPGLKGPKGDRGERGPAGQTGERGIKGFPGEPGKKGEEGDRGAD 351
Cdd:PHA03169  167 LQPSHEDSPEEP-EPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGP 245


                  .
gi 1974326295 352 G 352
Cdd:PHA03169  246 P 246
 
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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