NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|269995949|ref|NP_001161790|]
View 

scavenger receptor class A member 5 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 304-382 6.05e-17

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: 81.88  E-value: 6.05e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269995949 304 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERGERAE 382
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGP 208
PRK09039 super family cl32341
peptidoglycan -binding protein;
67-234 4.48e-04

peptidoglycan -binding protein;


The actual alignment was detected with superfamily member PRK09039:

Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.88  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995949  67 LLVFLILVGIFILA---VSRPRSSPDD-LKALTRNVNRLNESLRDMQLRLLQaplqadlteqvwkVQDALQNQTDSLLAL 142
Cdd:PRK09039  27 LLVIMFLLTVFVVAqffLSREISGKDSaLDRLNSQIAELADLLSLERQGNQD-------------LQDSVANLRASLSAA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995949 143 AGLVQRLEGTLWGLHAQAAQTEQAMALL---RDRTGQQSDSA--QLELYQLQVESNRSQllLQRHAGLLDGLARRVGVLG 217
Cdd:PRK09039  94 EAERSRLQALLAELAGAGAAAEGRAGELaqeLDSEKQVSARAlaQVELLNQQIAALRRQ--LAALEAALDASEKRDRESQ 171

                        170
                 ....*....|....*..
gi 269995949 218 EELADVGgalRGLNHSL 234
Cdd:PRK09039 172 AKIADLG---RRLNVAL 185
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 304-382 6.05e-17

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: 81.88  E-value: 6.05e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269995949 304 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERGERAE 382
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGP 208
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 318-373 5.02e-16

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: 71.76  E-value: 5.02e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 269995949  318 GKEGKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGE 373
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-382 1.60e-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: 74.56  E-value: 1.60e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 269995949 305 KGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMGMRGfKGDRGPKGEKGERGERAE 382
Cdd:NF038329 173 QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGP 249
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 304-382 6.41e-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: 72.63  E-value: 6.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995949 304 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPG-----ERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERG 378
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275


                 ....
gi 269995949 379 ERAE 382
Cdd:NF038329 276 KDGE 279
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 304-378 2.78e-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: 70.70  E-value: 2.78e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269995949 304 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERG 378
Cdd:NF038329 246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDG 320
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-382 1.37e-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: 65.70  E-value: 1.37e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 269995949 305 KGPPGPKGDQGNEGKEGKPGSPGLPGSRGlpgERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERGERAE 382
Cdd:NF038329 232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDG---PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQ 306
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-371 1.22e-08

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: 56.45  E-value: 1.22e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269995949 305 KGPPGPKGDQGNEGKEGKPGSPGLPGSRGLP------GERGDPGLPGPKGDDG---KLGATGPMGMRGFKGDRGPK 371
Cdd:NF038329 268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPgkdgkdGQNGKDGLPGKDGKDGqpgKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 336-382 8.18e-08

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: 53.76  E-value: 8.18e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 269995949 336 GERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERGERAE 382
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP 163
PRK09039 PRK09039
peptidoglycan -binding protein;
67-234 4.48e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.88  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995949  67 LLVFLILVGIFILA---VSRPRSSPDD-LKALTRNVNRLNESLRDMQLRLLQaplqadlteqvwkVQDALQNQTDSLLAL 142
Cdd:PRK09039  27 LLVIMFLLTVFVVAqffLSREISGKDSaLDRLNSQIAELADLLSLERQGNQD-------------LQDSVANLRASLSAA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995949 143 AGLVQRLEGTLWGLHAQAAQTEQAMALL---RDRTGQQSDSA--QLELYQLQVESNRSQllLQRHAGLLDGLARRVGVLG 217
Cdd:PRK09039  94 EAERSRLQALLAELAGAGAAAEGRAGELaqeLDSEKQVSARAlaQVELLNQQIAALRRQ--LAALEAALDASEKRDRESQ 171

                        170
                 ....*....|....*..
gi 269995949 218 EELADVGgalRGLNHSL 234
Cdd:PRK09039 172 AKIADLG---RRLNVAL 185
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
87-201 6.84e-04

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 41.37  E-value: 6.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995949  87 SPDDLKALTRN--------VNRLNESLRDMQLRLLQAPLQaDLTEQVWKVQDAL---QNQTdSLL-------ALAGLVQR 148
Cdd:COG3524  148 DPEDAQAIAEAllaeseelVNQLSERAREDAVRFAEEEVE-RAEERLRDAREALlafRNRN-GILdpeataeALLQLIAT 225

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 269995949 149 LEGTLwglhaqaAQTEQAMALLRDRTgqQSDSAQLELYQLQVESNRSQLLLQR 201
Cdd:COG3524  226 LEGQL-------AELEAELAALRSYL--SPNSPQVRQLRRRIAALEKQIAAER 269
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 304-382 6.05e-17

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: 81.88  E-value: 6.05e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269995949 304 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERGERAE 382
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGP 208
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 318-373 5.02e-16

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: 71.76  E-value: 5.02e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 269995949  318 GKEGKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGE 373
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 306-360 1.21e-15

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: 70.60  E-value: 1.21e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 269995949  306 GPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMG 360
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 321-377 5.98e-15

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: 68.67  E-value: 5.98e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 269995949  321 GKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGER 377
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-382 1.60e-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: 74.56  E-value: 1.60e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 269995949 305 KGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMGMRGfKGDRGPKGEKGERGERAE 382
Cdd:NF038329 173 QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGP 249
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 304-382 6.41e-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: 72.63  E-value: 6.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995949 304 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPG-----ERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERG 378
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275


                 ....
gi 269995949 379 ERAE 382
Cdd:NF038329 276 KDGE 279
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 304-355 1.34e-13

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: 64.82  E-value: 1.34e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 269995949  304 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGA 355
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 324-380 2.45e-13

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: 64.05  E-value: 2.45e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 269995949  324 GSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERGER 380
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 304-378 2.78e-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: 70.70  E-value: 2.78e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269995949 304 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERG 378
Cdd:NF038329 246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDG 320
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 306-358 4.37e-13

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: 63.28  E-value: 4.37e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 269995949  306 GPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGP 358
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 327-383 6.68e-13

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: 62.90  E-value: 6.68e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 269995949  327 GLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERGERAEC 383
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-382 1.37e-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: 65.70  E-value: 1.37e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 269995949 305 KGPPGPKGDQGNEGKEGKPGSPGLPGSRGlpgERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERGERAE 382
Cdd:NF038329 232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDG---PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQ 306
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 304-344 5.83e-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: 54.42  E-value: 5.83e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 269995949  304 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGLP 344
Cdd:pfam01391  17 PPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-371 1.22e-08

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: 56.45  E-value: 1.22e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269995949 305 KGPPGPKGDQGNEGKEGKPGSPGLPGSRGLP------GERGDPGLPGPKGDDG---KLGATGPMGMRGFKGDRGPK 371
Cdd:NF038329 268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPgkdgkdGQNGKDGLPGKDGKDGqpgKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 336-382 8.18e-08

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: 53.76  E-value: 8.18e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 269995949 336 GERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERGERAE 382
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP 163
PRK09039 PRK09039
peptidoglycan -binding protein;
67-234 4.48e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.88  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995949  67 LLVFLILVGIFILA---VSRPRSSPDD-LKALTRNVNRLNESLRDMQLRLLQaplqadlteqvwkVQDALQNQTDSLLAL 142
Cdd:PRK09039  27 LLVIMFLLTVFVVAqffLSREISGKDSaLDRLNSQIAELADLLSLERQGNQD-------------LQDSVANLRASLSAA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995949 143 AGLVQRLEGTLWGLHAQAAQTEQAMALL---RDRTGQQSDSA--QLELYQLQVESNRSQllLQRHAGLLDGLARRVGVLG 217
Cdd:PRK09039  94 EAERSRLQALLAELAGAGAAAEGRAGELaqeLDSEKQVSARAlaQVELLNQQIAALRRQ--LAALEAALDASEKRDRESQ 171

                        170
                 ....*....|....*..
gi 269995949 218 EELADVGgalRGLNHSL 234
Cdd:PRK09039 172 AKIADLG---RRLNVAL 185
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
87-201 6.84e-04

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 41.37  E-value: 6.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995949  87 SPDDLKALTRN--------VNRLNESLRDMQLRLLQAPLQaDLTEQVWKVQDAL---QNQTdSLL-------ALAGLVQR 148
Cdd:COG3524  148 DPEDAQAIAEAllaeseelVNQLSERAREDAVRFAEEEVE-RAEERLRDAREALlafRNRN-GILdpeataeALLQLIAT 225

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 269995949 149 LEGTLwglhaqaAQTEQAMALLRDRTgqQSDSAQLELYQLQVESNRSQLLLQR 201
Cdd:COG3524  226 LEGQL-------AELEAELAALRSYL--SPNSPQVRQLRRRIAALEKQIAAER 269
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 66-218 1.13e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995949  66 YLLVFLILVGIFILAVSRPRSSPDDLKALTRNVNRLNESLRDMQlrllqaplqadltEQVWKVQDALQNQTDSLLALAGL 145
Cdd:COG4942    4 LLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALK-------------KEEKALLKQLAALERRIAALARR 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269995949 146 VQRLEGTLWGLHAQAAQTEQAMALLRDRTGQQSDSAQLELYQLQVESNRSQLLLQRHAGLLDGLARRVGVLGE 218
Cdd:COG4942   71 IRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKY 143
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
89-228 7.18e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 7.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995949   89 DDLKALTRNVNRLNESLRDMQLRLLQAPLQ--ADLTEQVWKVQDALQNQTDSLLALAGLVQRLEGTLWGLHAQAAQTEQA 166
Cdd:COG4913   309 AELERLEARLDALREELDELEAQIRGNGGDrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269995949  167 MALLRDRTGQQSDSAQLELYQLQVESNRSQLLLQRHAGLLDGLARRVGVLGEELADVGGALR 228
Cdd:COG4913   389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH