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Conserved domains on  [gi|209529666|ref|NP_001129327|]
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scavenger receptor class A member 5 [Rattus norvegicus]

Protein Classification

Collagen and SR domain-containing protein( domain architecture ID 13293794)

protein containing domains PRK09039, Collagen, and SR

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 390-490 1.36e-40

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


:

Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 141.33  E-value: 1.36e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666   390 IRLVNGSGPHQGRVEVFHDRRWGTVCDDGWDKKDGDVVCRMLGFHSVEEVHRTARFGQGTGRIWMDDVNCKGTESSIFHC 469
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 209529666   470 QFSKWGVTNCGHAEDAGVTCT 490
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 319-374 7.25e-18

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: 77.15  E-value: 7.25e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 209529666  319 GKEGKPGSPGLPGSRGLPGERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGE 374
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK09039 super family cl32341
peptidoglycan -binding protein;
56-235 1.02e-04

peptidoglycan -binding protein;


The actual alignment was detected with superfamily member PRK09039:

Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 44.57  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666  56 LSALKHAVLGLyLLVFLtlVGVFILavSRPRSSPDD-LKALTRNINRLNEsfrdmQLRLLQAPLQaDLteqvwkvQDALQ 134
Cdd:PRK09039  23 LSTLLLVIMFL-LTVFV--VAQFFL--SREISGKDSaLDRLNSQIAELAD-----LLSLERQGNQ-DL-------QDSVA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666 135 NQTDSLLALAGLVQRLEGTLWGLHAQAAQTEQAVALL---RDRTGQQSDSA--QLELYQLQVESNRSQllLQRHAGLLDG 209
Cdd:PRK09039  85 NLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELaqeLDSEKQVSARAlaQVELLNQQIAALRRQ--LAALEAALDA 162

                        170       180
                 ....*....|....*....|....*.
gi 209529666 210 LAHRVGVLGEELADVGgalRGLNHSL 235
Cdd:PRK09039 163 SEKRDRESQAKIADLG---RRLNVAL 185
 
Name Accession Description Interval E-value
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 390-490 1.36e-40

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 141.33  E-value: 1.36e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666   390 IRLVNGSGPHQGRVEVFHDRRWGTVCDDGWDKKDGDVVCRMLGFHSVEEVHRTARFGQGTGRIWMDDVNCKGTESSIFHC 469
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 209529666   470 QFSKWGVTNCGHAEDAGVTCT 490
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 395-490 2.02e-34

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 124.41  E-value: 2.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666  395 GSGPHQGRVEVFHDRRWGTVCDDGWDKKDGDVVCRMLGFHSVEEVHRT-ARFGQG-TGRIWMDDVNCKGTESSIFHCQFS 472
Cdd:pfam00530   1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSAPSGcSYFGPGsTGPIWLDDVRCSGNETSLWQCPHR 80

                          90
                  ....*....|....*...
gi 209529666  473 KWGVTNCGHAEDAGVTCT 490
Cdd:pfam00530  81 PWGNHNCSHSEDAGVICS 98
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 319-374 7.25e-18

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: 77.15  E-value: 7.25e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 209529666  319 GKEGKPGSPGLPGSRGLPGERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGE 374
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-384 9.01e-18

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: 85.34  E-value: 9.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666 305 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERGERAGD 384
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA 209
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-384 6.78e-14

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 73.40  E-value: 6.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666 305 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERGERAGD 384
Cdd:NF038329 246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD 325
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 306-384 4.07e-12

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: 68.01  E-value: 4.07e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209529666 306 KGPPGPKGDQGNEGKEGKPGSPGLPGSRGlpgERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERGERAGD 384
Cdd:NF038329 232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDG---PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN 307
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 337-380 6.19e-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: 54.91  E-value: 6.19e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 209529666 337 GERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERGE 380
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE 160
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 307-361 2.17e-07

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: 52.99  E-value: 2.17e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 209529666 307 GPPGPKGDQGNEGKEGKPGSPGLPGSR---GLPGERGDPGMPGPKGDDGKLGATGPMG 361
Cdd:NF038329 281 GPVGPAGKDGQNGKDGLPGKDGKDGQNgkdGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
PRK09039 PRK09039
peptidoglycan -binding protein;
56-235 1.02e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 44.57  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666  56 LSALKHAVLGLyLLVFLtlVGVFILavSRPRSSPDD-LKALTRNINRLNEsfrdmQLRLLQAPLQaDLteqvwkvQDALQ 134
Cdd:PRK09039  23 LSTLLLVIMFL-LTVFV--VAQFFL--SREISGKDSaLDRLNSQIAELAD-----LLSLERQGNQ-DL-------QDSVA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666 135 NQTDSLLALAGLVQRLEGTLWGLHAQAAQTEQAVALL---RDRTGQQSDSA--QLELYQLQVESNRSQllLQRHAGLLDG 209
Cdd:PRK09039  85 NLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELaqeLDSEKQVSARAlaQVELLNQQIAALRRQ--LAALEAALDA 162

                        170       180
                 ....*....|....*....|....*.
gi 209529666 210 LAHRVGVLGEELADVGgalRGLNHSL 235
Cdd:PRK09039 163 SEKRDRESQAKIADLG---RRLNVAL 185
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 67-313 4.22e-04

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: 42.44  E-value: 4.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666  67 YLLVFLTLVGVFILAVSRPRSSPDDLKALTRNINRLNEsfrdmqlrllqapLQADLTEQVWKVQDALQNQTDSLLALAGL 146
Cdd:COG4942    4 LLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEK-------------ELAALKKEEKALLKQLAALERRIAALARR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666 147 VQRLEGTLWGLHAQAAQTEQAVALLRDRTGQQSDSAQLELYQLQVESNRSQLLL----------QRHAGLLDGLAHRVGV 216
Cdd:COG4942   71 IRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspedfldaVRRLQYLKYLAPARRE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666 217 LGEELADVGGALRGLNHSLSYDVALHSTWLQDLQVLVSNASADTRRMRLVHMDMEMQLK---QELATLNVVTEDLR--LK 291
Cdd:COG4942  151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAelaAELAELQQEAEELEalIA 230

                        250       260
                 ....*....|....*....|...
gi 209529666 292 DWEHSIALR-NITLAKGPPGPKG 313
Cdd:COG4942  231 RLEAEAAAAaERTPAAGFAALKG 253
PHA03169 PHA03169
hypothetical protein; Provisional
 305-384 5.03e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.27  E-value: 5.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666 305 AKGPPGPKGDQGNEGKEGKPGSPGlPGSRGLPGERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERGERAGD 384
Cdd:PHA03169 122 NTSGSSPESPASHSPPPSPPSHPG-PHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTS 200
 
Name Accession Description Interval E-value
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 390-490 1.36e-40

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 141.33  E-value: 1.36e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666   390 IRLVNGSGPHQGRVEVFHDRRWGTVCDDGWDKKDGDVVCRMLGFHSVEEVHRTARFGQGTGRIWMDDVNCKGTESSIFHC 469
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 209529666   470 QFSKWGVTNCGHAEDAGVTCT 490
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 395-490 2.02e-34

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 124.41  E-value: 2.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666  395 GSGPHQGRVEVFHDRRWGTVCDDGWDKKDGDVVCRMLGFHSVEEVHRT-ARFGQG-TGRIWMDDVNCKGTESSIFHCQFS 472
Cdd:pfam00530   1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSAPSGcSYFGPGsTGPIWLDDVRCSGNETSLWQCPHR 80

                          90
                  ....*....|....*...
gi 209529666  473 KWGVTNCGHAEDAGVTCT 490
Cdd:pfam00530  81 PWGNHNCSHSEDAGVICS 98
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 319-374 7.25e-18

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: 77.15  E-value: 7.25e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 209529666  319 GKEGKPGSPGLPGSRGLPGERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGE 374
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-384 9.01e-18

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: 85.34  E-value: 9.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666 305 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERGERAGD 384
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA 209
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 322-378 1.56e-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: 73.68  E-value: 1.56e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 209529666  322 GKPGSPGLPGSRGLPGERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGER 378
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-384 6.78e-14

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 73.40  E-value: 6.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666 305 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERGERAGD 384
Cdd:NF038329 246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD 325
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 325-381 1.42e-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: 65.21  E-value: 1.42e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 209529666  325 GSPGLPGSRGLPGERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERGER 381
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 307-359 1.96e-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: 1.96e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 209529666  307 GPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGMPGPKGDDGKLGATGP 359
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 306-384 4.07e-12

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: 68.01  E-value: 4.07e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209529666 306 KGPPGPKGDQGNEGKEGKPGSPGLPGSRGlpgERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERGERAGD 384
Cdd:NF038329 232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDG---PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN 307
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 305-349 2.07e-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: 2.07e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 209529666  305 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGMPGPKG 349
Cdd:pfam01391  11 PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 305-347 3.15e-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: 58.27  E-value: 3.15e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 209529666  305 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGMPGP 347
Cdd:pfam01391  14 PPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 305-345 1.73e-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: 1.73e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 209529666  305 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGMP 345
Cdd:pfam01391  17 PPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 337-380 6.19e-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: 54.91  E-value: 6.19e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 209529666 337 GERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERGE 380
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE 160
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 307-361 2.17e-07

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: 52.99  E-value: 2.17e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 209529666 307 GPPGPKGDQGNEGKEGKPGSPGLPGSR---GLPGERGDPGMPGPKGDDGKLGATGPMG 361
Cdd:NF038329 281 GPVGPAGKDGQNGKDGLPGKDGKDGQNgkdGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
PRK09039 PRK09039
peptidoglycan -binding protein;
56-235 1.02e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 44.57  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666  56 LSALKHAVLGLyLLVFLtlVGVFILavSRPRSSPDD-LKALTRNINRLNEsfrdmQLRLLQAPLQaDLteqvwkvQDALQ 134
Cdd:PRK09039  23 LSTLLLVIMFL-LTVFV--VAQFFL--SREISGKDSaLDRLNSQIAELAD-----LLSLERQGNQ-DL-------QDSVA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666 135 NQTDSLLALAGLVQRLEGTLWGLHAQAAQTEQAVALL---RDRTGQQSDSA--QLELYQLQVESNRSQllLQRHAGLLDG 209
Cdd:PRK09039  85 NLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELaqeLDSEKQVSARAlaQVELLNQQIAALRRQ--LAALEAALDA 162

                        170       180
                 ....*....|....*....|....*.
gi 209529666 210 LAHRVGVLGEELADVGgalRGLNHSL 235
Cdd:PRK09039 163 SEKRDRESQAKIADLG---RRLNVAL 185
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 67-313 4.22e-04

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: 42.44  E-value: 4.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666  67 YLLVFLTLVGVFILAVSRPRSSPDDLKALTRNINRLNEsfrdmqlrllqapLQADLTEQVWKVQDALQNQTDSLLALAGL 146
Cdd:COG4942    4 LLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEK-------------ELAALKKEEKALLKQLAALERRIAALARR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666 147 VQRLEGTLWGLHAQAAQTEQAVALLRDRTGQQSDSAQLELYQLQVESNRSQLLL----------QRHAGLLDGLAHRVGV 216
Cdd:COG4942   71 IRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspedfldaVRRLQYLKYLAPARRE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666 217 LGEELADVGGALRGLNHSLSYDVALHSTWLQDLQVLVSNASADTRRMRLVHMDMEMQLK---QELATLNVVTEDLR--LK 291
Cdd:COG4942  151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAelaAELAELQQEAEELEalIA 230

                        250       260
                 ....*....|....*....|...
gi 209529666 292 DWEHSIALR-NITLAKGPPGPKG 313
Cdd:COG4942  231 RLEAEAAAAaERTPAAGFAALKG 253
PHA03169 PHA03169
hypothetical protein; Provisional
 305-384 5.03e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.27  E-value: 5.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209529666 305 AKGPPGPKGDQGNEGKEGKPGSPGlPGSRGLPGERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERGERAGD 384
Cdd:PHA03169 122 NTSGSSPESPASHSPPPSPPSHPG-PHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTS 200
 
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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