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Conserved domains on  [gi|1034660597|ref|XP_016869024|]
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scavenger receptor class A member 3 isoform X1 [Homo sapiens]

Protein Classification

collagen-like domain-containing protein( domain architecture ID 1903237)

collagen-like domain-containing protein such as collagens, which are extracellular structural proteins involved in formation of connective tissue structure

PubMed:  21421911|15837519

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 ...
 468-583 2.00e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 78.79  E-value: 2.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660597 468 KGDMGVKGPVGGRGPKGDPGSLGPLGPQGPQGQPGEAGPVGERGPVGPR---GFPGLKGSKGSFGTGGPRGQPGPKGDIG 544
Cdd:NF038329  128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAgkdGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034660597 545 PPGPEGPPGSPGPSGPQGKPGIA-----GKTGSPGQRGAMGPKG 583
Cdd:NF038329  208 PAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQG 251
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 468-583 2.00e-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: 78.79  E-value: 2.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660597 468 KGDMGVKGPVGGRGPKGDPGSLGPLGPQGPQGQPGEAGPVGERGPVGPR---GFPGLKGSKGSFGTGGPRGQPGPKGDIG 544
Cdd:NF038329  128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAgkdGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034660597 545 PPGPEGPPGSPGPSGPQGKPGIA-----GKTGSPGQRGAMGPKG 583
Cdd:NF038329  208 PAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQG 251
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 467-584 1.65e-13

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: 73.02  E-value: 1.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660597 467 FKGDMGVKGPVGGRGPKGDPGSLGPLGPQGPQGQPGEAGPVGERGPVGPRGFPGLKGSKGSFGTGGPRGQPGPKGDIGPP 546
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034660597 547 GPEGPPGSPGPSGPQGKPGIAGKTGSPGQRGAMGPKGE 584
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD 232
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 480-541 2.95e-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: 61.74  E-value: 2.95e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034660597 480 RGPKGDPGslgplgpqgpqgqpgEAGPVGERGPVGPRGFPGLKGSKGSFGTGGPRGQPGPKG 541
Cdd:pfam01391   9 PGPPGPPG---------------PPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 468-583 1.74e-11

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: 66.47  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660597 468 KGDMGVKGPVGGRGPKGDPGSLGPLGPQGPQGQPGEAGPVGERGPVGP-----------------------RGFPGLKGS 524
Cdd:NF038329  164 AGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPagpdgeagpagedgpagpagdgqQGPDGDPGP 243

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034660597 525 KGSFGTGGPRGQPG---PKGDIgppgpegppgspgpsgpqGKPGIAGKTGSPGQRGAMGPKG 583
Cdd:NF038329  244 TGEDGPQGPDGPAGkdgPRGDR------------------GEAGPDGPDGKDGERGPVGPAG 287
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 468-583 2.58e-11

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: 66.08  E-value: 2.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660597 468 KGDMGVKGPVGG--RGPKGDPGslgplgpqgPQGQPGEAGPVGERGPVGPRGFPGLKGSKGSFGTGGPRGQPGPKGdigp 545
Cdd:NF038329  221 AGEDGPAGPAGDgqQGPDGDPG---------PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG---- 287

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034660597 546 pgPEGPPGSPGPSGPQGKPGIAGKTGSPGQRGAMGPKG 583
Cdd:NF038329  288 --KDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 468-552 1.39e-04

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: 44.51  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660597 468 KGDMGVKGPVGGRGPKGDPGSLGPLGPQGPQGQPGEAGPVGERGPVGPRGFPGLKGSKGSFGTGGPRGQ----------- 536
Cdd:NF038329  238 DGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQngkdglpgkdg 317

                          90       100
                  ....*....|....*....|
gi 1034660597 537 ----PGPKGDIGPPGPEGPP 552
Cdd:NF038329  318 kdgqPGKDGLPGKDGKDGQP 337
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
469-581 5.92e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 39.63  E-value: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660597 469 GDMGVKGPV---GGRGPKGDPGSLGPLGPQGPQGQPGEAGPVGERGPVGPRGFPGLKGSK-----GSFGTGGPRGQ---- 536
Cdd:COG5164    67 GNQGATGPAqnqGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTtppsgGSTTPPGDGGStppg 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1034660597 537 ---PGPKGDIGPPGPEGPPGSpgpsgpqgkPGIAGKTGSPGQRGAMGP 581
Cdd:COG5164   147 pgsTGPGGSTTPPGDGGSTTP---------PGPGGSTTPPDDGGSTTP 185
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 468-583 2.00e-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: 78.79  E-value: 2.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660597 468 KGDMGVKGPVGGRGPKGDPGSLGPLGPQGPQGQPGEAGPVGERGPVGPR---GFPGLKGSKGSFGTGGPRGQPGPKGDIG 544
Cdd:NF038329  128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAgkdGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034660597 545 PPGPEGPPGSPGPSGPQGKPGIA-----GKTGSPGQRGAMGPKG 583
Cdd:NF038329  208 PAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQG 251
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 467-584 1.65e-13

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: 73.02  E-value: 1.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660597 467 FKGDMGVKGPVGGRGPKGDPGSLGPLGPQGPQGQPGEAGPVGERGPVGPRGFPGLKGSKGSFGTGGPRGQPGPKGDIGPP 546
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034660597 547 GPEGPPGSPGPSGPQGKPGIAGKTGSPGQRGAMGPKGE 584
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD 232
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 480-541 2.95e-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: 61.74  E-value: 2.95e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034660597 480 RGPKGDPGslgplgpqgpqgqpgEAGPVGERGPVGPRGFPGLKGSKGSFGTGGPRGQPGPKG 541
Cdd:pfam01391   9 PGPPGPPG---------------PPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 472-543 4.49e-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: 60.97  E-value: 4.49e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034660597 472 GVKGPVGGRGPKGDPGslgplgpqgpqgqpgEAGPVGERGPVGPRGFPGLKGSKGsfgtggPRGQPGPKGDI 543
Cdd:pfam01391   1 GPPGPPGPPGPPGPPG---------------PPGPPGPPGPPGPPGEPGPPGPPG------PPGPPGPPGAP 51
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 468-583 1.74e-11

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: 66.47  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660597 468 KGDMGVKGPVGGRGPKGDPGSLGPLGPQGPQGQPGEAGPVGERGPVGP-----------------------RGFPGLKGS 524
Cdd:NF038329  164 AGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPagpdgeagpagedgpagpagdgqQGPDGDPGP 243

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034660597 525 KGSFGTGGPRGQPG---PKGDIgppgpegppgspgpsgpqGKPGIAGKTGSPGQRGAMGPKG 583
Cdd:NF038329  244 TGEDGPQGPDGPAGkdgPRGDR------------------GEAGPDGPDGKDGERGPVGPAG 287
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 503-584 2.41e-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: 59.04  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660597 503 EAGPVGERGPVGPRGFPGLKGSKGSFGTGGPRGQPGPKGdigppgpegPpgspgpsgpqgkpgiagkTGSPGQRGAMGPK 582
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPG---------P------------------PGPPGPPGAPGAP 54


                  ..
gi 1034660597 583 GE 584
Cdd:pfam01391  55 GP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 468-583 2.58e-11

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: 66.08  E-value: 2.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660597 468 KGDMGVKGPVGG--RGPKGDPGslgplgpqgPQGQPGEAGPVGERGPVGPRGFPGLKGSKGSFGTGGPRGQPGPKGdigp 545
Cdd:NF038329  221 AGEDGPAGPAGDgqQGPDGDPG---------PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG---- 287

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034660597 546 pgPEGPPGSPGPSGPQGKPGIAGKTGSPGQRGAMGPKG 583
Cdd:NF038329  288 --KDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 505-584 1.20e-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: 57.12  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660597 505 GPVGERGPVGPRGFPGLKGSKGSfgtGGPRGQPGPKGdigppgpegppgspgpsgpqgkpgiagktgSPGQRGAMGPKGE 584
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGP---PGPPGPPGEPG------------------------------PPGPPGPPGPPGP 47
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 468-526 1.23e-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: 54.04  E-value: 1.23e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034660597 468 KGDMGVKGPVGGRGPKGDPGslgplgpqgpqgqpgEAGPVGERGPVGPRGFPGLKGSKG 526
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPG---------------EPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 468-552 1.39e-04

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: 44.51  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660597 468 KGDMGVKGPVGGRGPKGDPGSLGPLGPQGPQGQPGEAGPVGERGPVGPRGFPGLKGSKGSFGTGGPRGQ----------- 536
Cdd:NF038329  238 DGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQngkdglpgkdg 317

                          90       100
                  ....*....|....*....|
gi 1034660597 537 ----PGPKGDIGPPGPEGPP 552
Cdd:NF038329  318 kdgqPGKDGLPGKDGKDGQP 337
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
469-581 5.92e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 39.63  E-value: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660597 469 GDMGVKGPV---GGRGPKGDPGSLGPLGPQGPQGQPGEAGPVGERGPVGPRGFPGLKGSK-----GSFGTGGPRGQ---- 536
Cdd:COG5164    67 GNQGATGPAqnqGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTtppsgGSTTPPGDGGStppg 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1034660597 537 ---PGPKGDIGPPGPEGPPGSpgpsgpqgkPGIAGKTGSPGQRGAMGP 581
Cdd:COG5164   147 pgsTGPGGSTTPPGDGGSTTP---------PGPGGSTTPPDDGGSTTP 185
 
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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