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Conserved domains on  [gi|157817432|ref|NP_001102340|]
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scavenger receptor class A member 3 [Rattus norvegicus]

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 ...
 468-584 6.06e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 71.09  E-value: 6.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817432 468 KGDTGMKGPVGNKGPKGDPGSLGPPGPQGPQGQPGEPGPVGERGPAGPRGFPGLKGSKGSFGTGGPRGQPGPKGDVGPPG 547
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 157817432 548 PEGPPGSQgpsGPQGKPGISGKAGSPGQRGATGPKGE 584
Cdd:NF038329 199 ETGPAGEQ---GPAGPAGPDGEAGPAGEDGPAGPAGD 232
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 78-357 3.24e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 3.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817432    78 RKVDSLSEDISLAQSI--YNKKLVSMQENLQGLDPKALIncsfcREAEQLGQEIRKLQEELEGLQKMLLAQEVQLDQTSQ 155
Cdd:TIGR02168  200 RQLKSLERQAEKAERYkeLKAELRELELALLVLRLEELR-----EELEELQEELKEAEEELEELTAELQELEEKLEELRL 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817432   156 AHELLSTTSSQISQEMGTCSFSIHQVNQSLGLFLAQVRGWQATTAGMDISLKDLTQECYDVKAAVHQINFTVGQTAEWIH 235
Cdd:TIGR02168  275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817432   236 GIQRKTDEETLTLQKIVTDWQNYTRLFGGLRSTSAKTGEIVKTIQATLGASSQRISQNSESMHDLVLQVMGLQ-----LQ 310
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkleeAE 434

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 157817432   311 LDNISSFLDDHEENMHDLQYHtryaQNRTVERFESLEGRMASHEIEI 357
Cdd:TIGR02168  435 LKELQAELEELEEELEELQEE----LERLEEALEELREELEEAEQAL 477
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 468-584 6.06e-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: 71.09  E-value: 6.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817432 468 KGDTGMKGPVGNKGPKGDPGSLGPPGPQGPQGQPGEPGPVGERGPAGPRGFPGLKGSKGSFGTGGPRGQPGPKGDVGPPG 547
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 157817432 548 PEGPPGSQgpsGPQGKPGISGKAGSPGQRGATGPKGE 584
Cdd:NF038329 199 ETGPAGEQ---GPAGPAGPDGEAGPAGEDGPAGPAGD 232
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 508-584 1.69e-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: 62.51  E-value: 1.69e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157817432  508 GERGPAGPRGFPGLKGSKGSfgtGGPRGQPGPKgdvgppgpegppgsqgpsGPQGKPGISGKAGSPGQRGATGPKGE 584
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGP---PGPPGPPGPP------------------GEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 462-583 1.08e-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: 67.24  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817432 462 PGPRGFKGDTGMKGPVGNKGPKGDPGSLGPPGPQGPQGQPGEPGPVGERGPAGPRGFPGLKGSKGSFGTGGPRGQPGPKG 541
Cdd:NF038329 125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 157817432 542 DVGPPGPEGPPGSQGPSGPQGKPGIS-----GKAGSPGQRGATGPKG 583
Cdd:NF038329 205 EQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQG 251
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 467-584 2.00e-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: 2.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817432 467 FKGDTGMKGPVGNKGPKGDPGSLGPPGPQGPQgqpgepgpvGERGPAGPRGFPGLKGSKGSFGTGGPRGQPGPKgdvgpp 546
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPA---------GPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD------ 179

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 157817432 547 gpegppgsqgpsGPQGKPGISGKAGSPGQRGATGPKGE 584
Cdd:NF038329 180 ------------GEAGAKGPAGEKGPQGPRGETGPAGE 205
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 469-583 9.33e-10

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: 61.07  E-value: 9.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817432 469 GDTGMKGPVGNKGPKGDpgslgppgpqgpqgqpgepgpVGERGPAGPRGFPGLKGSKGSFGTGGPRGQPGPkgdvgpPGP 548
Cdd:NF038329 236 GPDGDPGPTGEDGPQGP---------------------DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP------AGK 288

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 157817432 549 EGPPGSQGPSGPQGKPGISGKAGSPGQRGATGPKG 583
Cdd:NF038329 289 DGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 78-357 3.24e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 3.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817432    78 RKVDSLSEDISLAQSI--YNKKLVSMQENLQGLDPKALIncsfcREAEQLGQEIRKLQEELEGLQKMLLAQEVQLDQTSQ 155
Cdd:TIGR02168  200 RQLKSLERQAEKAERYkeLKAELRELELALLVLRLEELR-----EELEELQEELKEAEEELEELTAELQELEEKLEELRL 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817432   156 AHELLSTTSSQISQEMGTCSFSIHQVNQSLGLFLAQVRGWQATTAGMDISLKDLTQECYDVKAAVHQINFTVGQTAEWIH 235
Cdd:TIGR02168  275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817432   236 GIQRKTDEETLTLQKIVTDWQNYTRLFGGLRSTSAKTGEIVKTIQATLGASSQRISQNSESMHDLVLQVMGLQ-----LQ 310
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkleeAE 434

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 157817432   311 LDNISSFLDDHEENMHDLQYHtryaQNRTVERFESLEGRMASHEIEI 357
Cdd:TIGR02168  435 LKELQAELEELEEELEELQEE----LERLEEALEELREELEEAEQAL 477
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 468-584 6.06e-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: 71.09  E-value: 6.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817432 468 KGDTGMKGPVGNKGPKGDPGSLGPPGPQGPQGQPGEPGPVGERGPAGPRGFPGLKGSKGSFGTGGPRGQPGPKGDVGPPG 547
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 157817432 548 PEGPPGSQgpsGPQGKPGISGKAGSPGQRGATGPKGE 584
Cdd:NF038329 199 ETGPAGEQ---GPAGPAGPDGEAGPAGEDGPAGPAGD 232
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 508-584 1.69e-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: 62.51  E-value: 1.69e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157817432  508 GERGPAGPRGFPGLKGSKGSfgtGGPRGQPGPKgdvgppgpegppgsqgpsGPQGKPGISGKAGSPGQRGATGPKGE 584
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGP---PGPPGPPGPP------------------GEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 462-583 1.08e-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: 67.24  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817432 462 PGPRGFKGDTGMKGPVGNKGPKGDPGSLGPPGPQGPQGQPGEPGPVGERGPAGPRGFPGLKGSKGSFGTGGPRGQPGPKG 541
Cdd:NF038329 125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 157817432 542 DVGPPGPEGPPGSQGPSGPQGKPGIS-----GKAGSPGQRGATGPKG 583
Cdd:NF038329 205 EQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQG 251
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 467-584 2.00e-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: 2.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817432 467 FKGDTGMKGPVGNKGPKGDPGSLGPPGPQGPQgqpgepgpvGERGPAGPRGFPGLKGSKGSFGTGGPRGQPGPKgdvgpp 546
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPA---------GPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD------ 179

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 157817432 547 gpegppgsqgpsGPQGKPGISGKAGSPGQRGATGPKGE 584
Cdd:NF038329 180 ------------GEAGAKGPAGEKGPQGPRGETGPAGE 205
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 508-576 2.45e-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: 56.35  E-value: 2.45e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157817432  508 GERGPAGPRGFPGLKGSKGSFGTGGPRGQPGPKGDvgppgpegppgsqgpsgpQGKPGISGKAGSPGQR 576
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGP------------------PGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 469-583 9.33e-10

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: 61.07  E-value: 9.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817432 469 GDTGMKGPVGNKGPKGDpgslgppgpqgpqgqpgepgpVGERGPAGPRGFPGLKGSKGSFGTGGPRGQPGPkgdvgpPGP 548
Cdd:NF038329 236 GPDGDPGPTGEDGPQGP---------------------DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP------AGK 288

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 157817432 549 EGPPGSQGPSGPQGKPGISGKAGSPGQRGATGPKG 583
Cdd:NF038329 289 DGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 468-540 2.46e-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: 2.46e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157817432  468 KGDTGMKGPVGNKGPKgdpgslgppgpqgpqgqpgepgpvGERGPAGPRGFPGLKGSKGSFGTGGPRGQPGPK 540
Cdd:pfam01391   6 PGPPGPPGPPGPPGPP------------------------GPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 471-539 2.30e-07

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: 47.87  E-value: 2.30e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157817432  471 TGMKGPVGNKGPKgdpgslgppgpqgpqgqpgepgpvGERGPAGPRGFPGLKGSKGSFGTGGPRGQPGP 539
Cdd:pfam01391  12 PGPPGPPGPPGPP------------------------GPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 78-357 3.24e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 3.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817432    78 RKVDSLSEDISLAQSI--YNKKLVSMQENLQGLDPKALIncsfcREAEQLGQEIRKLQEELEGLQKMLLAQEVQLDQTSQ 155
Cdd:TIGR02168  200 RQLKSLERQAEKAERYkeLKAELRELELALLVLRLEELR-----EELEELQEELKEAEEELEELTAELQELEEKLEELRL 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817432   156 AHELLSTTSSQISQEMGTCSFSIHQVNQSLGLFLAQVRGWQATTAGMDISLKDLTQECYDVKAAVHQINFTVGQTAEWIH 235
Cdd:TIGR02168  275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817432   236 GIQRKTDEETLTLQKIVTDWQNYTRLFGGLRSTSAKTGEIVKTIQATLGASSQRISQNSESMHDLVLQVMGLQ-----LQ 310
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkleeAE 434

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 157817432   311 LDNISSFLDDHEENMHDLQYHtryaQNRTVERFESLEGRMASHEIEI 357
Cdd:TIGR02168  435 LKELQAELEELEEELEELQEE----LERLEEALEELREELEEAEQAL 477
 
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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