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Conserved domains on  [gi|269995946|ref|NP_083179|]
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scavenger receptor class A member 5 isoform 1 [Mus musculus]

Protein Classification

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 ...
 389-489 5.71e-41

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: 142.10  E-value: 5.71e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946   389 IRLVNGSGPHQGRVEVFHDRRWGTVCDDGWDKKDGDVVCRMLGFHGVEEVYRTARFGQGTGRIWMDDVNCKGTESSIFHC 468
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 269995946   469 QFSKWGVTNCGHAEDAGVTCT 489
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 304-383 2.32e-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: 84.19  E-value: 2.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946 304 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERGERAGD 383
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA 209
PRK09039 super family cl32341
peptidoglycan -binding protein;
55-249 9.35e-05

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: 9.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946  55 LSALKHAVLGLyLLVFLilVGIFILavSRPRSSPDD-LKALTRNVNRLNESLRdmqlrlLQAPLQADLteqvwkvQDALQ 133
Cdd:PRK09039  23 LSTLLLVIMFL-LTVFV--VAQFFL--SREISGKDSaLDRLNSQIAELADLLS------LERQGNQDL-------QDSVA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946 134 NQTDSLLALAGLVQRLEGTLWGLHAQAAQTEQAMALL---RDRTGQQSDSA--QLELYQLQVESNRSQllLQRHAGLLDG 208
Cdd:PRK09039  85 NLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELaqeLDSEKQVSARAlaQVELLNQQIAALRRQ--LAALEAALDA 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 269995946 209 LARRVGVLGEELADVGgalRGLNHSLSYDValhstwlQDLQ 249
Cdd:PRK09039 163 SEKRDRESQAKIADLG---RRLNVALAQRV-------QELN 193
 
Name Accession Description Interval E-value
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 389-489 5.71e-41

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: 142.10  E-value: 5.71e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946   389 IRLVNGSGPHQGRVEVFHDRRWGTVCDDGWDKKDGDVVCRMLGFHGVEEVYRTARFGQGTGRIWMDDVNCKGTESSIFHC 468
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 269995946   469 QFSKWGVTNCGHAEDAGVTCT 489
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 394-489 2.36e-35

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: 127.11  E-value: 2.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946  394 GSGPHQGRVEVFHDRRWGTVCDDGWDKKDGDVVCRMLGFHGVEEVYRT-ARFGQG-TGRIWMDDVNCKGTESSIFHCQFS 471
Cdd:pfam00530   1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSAPSGcSYFGPGsTGPIWLDDVRCSGNETSLWQCPHR 80

                          90
                  ....*....|....*...
gi 269995946  472 KWGVTNCGHAEDAGVTCT 489
Cdd:pfam00530  81 PWGNHNCSHSEDAGVICS 98
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 304-383 2.32e-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: 84.19  E-value: 2.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946 304 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERGERAGD 383
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA 209
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 318-373 1.34e-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: 1.34e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 269995946  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 ...
 304-380 4.98e-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: 73.79  E-value: 4.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946 304 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPG-----ERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERG 378
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275


                 ..
gi 269995946 379 ER 380
Cdd:NF038329 276 KD 277
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 304-383 7.00e-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: 7.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946 304 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERGERAGD 383
Cdd:NF038329 246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD 325
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-383 8.03e-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: 67.24  E-value: 8.03e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269995946 305 KGPPGPKGDQGNEGKEGKPGSPGLPGSRGlpgERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERGERAGD 383
Cdd:NF038329 232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDG---PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN 307
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-371 4.49e-09

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: 58.38  E-value: 4.49e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269995946 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 ...
 336-379 5.13e-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: 55.30  E-value: 5.13e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 269995946 336 GERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERGE 379
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE 160
PRK09039 PRK09039
peptidoglycan -binding protein;
55-249 9.35e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 44.57  E-value: 9.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946  55 LSALKHAVLGLyLLVFLilVGIFILavSRPRSSPDD-LKALTRNVNRLNESLRdmqlrlLQAPLQADLteqvwkvQDALQ 133
Cdd:PRK09039  23 LSTLLLVIMFL-LTVFV--VAQFFL--SREISGKDSaLDRLNSQIAELADLLS------LERQGNQDL-------QDSVA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946 134 NQTDSLLALAGLVQRLEGTLWGLHAQAAQTEQAMALL---RDRTGQQSDSA--QLELYQLQVESNRSQllLQRHAGLLDG 208
Cdd:PRK09039  85 NLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELaqeLDSEKQVSARAlaQVELLNQQIAALRRQ--LAALEAALDA 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 269995946 209 LARRVGVLGEELADVGgalRGLNHSLSYDValhstwlQDLQ 249
Cdd:PRK09039 163 SEKRDRESQAKIADLG---RRLNVALAQRV-------QELN 193
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 66-312 1.41e-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: 43.98  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946  66 YLLVFLILVGIFILAVSRPRSSPDDLKALTRNVNRLNESLRDMQlrllqaplqadltEQVWKVQDALQNQTDSLLALAGL 145
Cdd:COG4942    4 LLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALK-------------KEEKALLKQLAALERRIAALARR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946 146 VQRLEGTLWGLHAQAAQTEQAMALLRDRTGQQSDSAQLELYQLQVESNRSQLLL----------QRHAGLLDGLARRVGV 215
Cdd:COG4942   71 IRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspedfldaVRRLQYLKYLAPARRE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946 216 LGEELADVGGALRGLNHSLSYDVALHSTWLQDLQVLVSNASADTRRMRLVHMDMEMQLK---QELATLNVVTEDLR--LK 290
Cdd:COG4942  151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAelaAELAELQQEAEELEalIA 230

                        250       260
                 ....*....|....*....|...
gi 269995946 291 DWEHSIALR-NITLAKGPPGPKG 312
Cdd:COG4942  231 RLEAEAAAAaERTPAAGFAALKG 253
 
Name Accession Description Interval E-value
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 389-489 5.71e-41

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: 142.10  E-value: 5.71e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946   389 IRLVNGSGPHQGRVEVFHDRRWGTVCDDGWDKKDGDVVCRMLGFHGVEEVYRTARFGQGTGRIWMDDVNCKGTESSIFHC 468
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 269995946   469 QFSKWGVTNCGHAEDAGVTCT 489
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 394-489 2.36e-35

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: 127.11  E-value: 2.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946  394 GSGPHQGRVEVFHDRRWGTVCDDGWDKKDGDVVCRMLGFHGVEEVYRT-ARFGQG-TGRIWMDDVNCKGTESSIFHCQFS 471
Cdd:pfam00530   1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSAPSGcSYFGPGsTGPIWLDDVRCSGNETSLWQCPHR 80

                          90
                  ....*....|....*...
gi 269995946  472 KWGVTNCGHAEDAGVTCT 489
Cdd:pfam00530  81 PWGNHNCSHSEDAGVICS 98
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 304-383 2.32e-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: 84.19  E-value: 2.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946 304 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERGERAGD 383
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA 209
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 318-373 1.34e-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: 1.34e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 269995946  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 3.35e-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: 72.53  E-value: 3.35e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 269995946  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 1.68e-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: 1.68e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 269995946  321 GKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGER 377
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 304-355 3.97e-14

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: 66.75  E-value: 3.97e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 269995946  304 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGA 355
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 304-380 4.98e-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: 73.79  E-value: 4.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946 304 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPG-----ERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERG 378
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275


                 ..
gi 269995946 379 ER 380
Cdd:NF038329 276 KD 277
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 304-383 7.00e-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: 7.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946 304 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERGERAGD 383
Cdd:NF038329 246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD 325
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 324-380 7.14e-14

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: 65.98  E-value: 7.14e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 269995946  324 GSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERGER 380
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 306-358 1.33e-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: 1.33e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 269995946  306 GPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGLPGPKGDDGKLGATGP 358
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-383 8.03e-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: 67.24  E-value: 8.03e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269995946 305 KGPPGPKGDQGNEGKEGKPGSPGLPGSRGlpgERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERGERAGD 383
Cdd:NF038329 232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDG---PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN 307
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 304-344 2.16e-10

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 55.96  E-value: 2.16e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 269995946  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 4.49e-09

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: 58.38  E-value: 4.49e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269995946 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 ...
 336-379 5.13e-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: 55.30  E-value: 5.13e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 269995946 336 GERGDPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGERGE 379
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE 160
PRK09039 PRK09039
peptidoglycan -binding protein;
55-249 9.35e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 44.57  E-value: 9.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946  55 LSALKHAVLGLyLLVFLilVGIFILavSRPRSSPDD-LKALTRNVNRLNESLRdmqlrlLQAPLQADLteqvwkvQDALQ 133
Cdd:PRK09039  23 LSTLLLVIMFL-LTVFV--VAQFFL--SREISGKDSaLDRLNSQIAELADLLS------LERQGNQDL-------QDSVA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946 134 NQTDSLLALAGLVQRLEGTLWGLHAQAAQTEQAMALL---RDRTGQQSDSA--QLELYQLQVESNRSQllLQRHAGLLDG 208
Cdd:PRK09039  85 NLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELaqeLDSEKQVSARAlaQVELLNQQIAALRRQ--LAALEAALDA 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 269995946 209 LARRVGVLGEELADVGgalRGLNHSLSYDValhstwlQDLQ 249
Cdd:PRK09039 163 SEKRDRESQAKIADLG---RRLNVALAQRV-------QELN 193
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 66-312 1.41e-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: 43.98  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946  66 YLLVFLILVGIFILAVSRPRSSPDDLKALTRNVNRLNESLRDMQlrllqaplqadltEQVWKVQDALQNQTDSLLALAGL 145
Cdd:COG4942    4 LLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALK-------------KEEKALLKQLAALERRIAALARR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946 146 VQRLEGTLWGLHAQAAQTEQAMALLRDRTGQQSDSAQLELYQLQVESNRSQLLL----------QRHAGLLDGLARRVGV 215
Cdd:COG4942   71 IRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspedfldaVRRLQYLKYLAPARRE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946 216 LGEELADVGGALRGLNHSLSYDVALHSTWLQDLQVLVSNASADTRRMRLVHMDMEMQLK---QELATLNVVTEDLR--LK 290
Cdd:COG4942  151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAelaAELAELQQEAEELEalIA 230

                        250       260
                 ....*....|....*....|...
gi 269995946 291 DWEHSIALR-NITLAKGPPGPKG 312
Cdd:COG4942  231 RLEAEAAAAaERTPAAGFAALKG 253
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
87-201 1.86e-04

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


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 43.69  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946  87 SPDDLKALTRN--------VNRLNESLRDMQLRLLQAPLQaDLTEQVWKVQDAL---QNQTdSLL-------ALAGLVQR 148
Cdd:COG3524  148 DPEDAQAIAEAllaeseelVNQLSERAREDAVRFAEEEVE-RAEERLRDAREALlafRNRN-GILdpeataeALLQLIAT 225

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 269995946 149 LEGTLwglhaqaAQTEQAMALLRDRTgqQSDSAQLELYQLQVESNRSQLLLQR 201
Cdd:COG3524  226 LEGQL-------AELEAELAALRSYL--SPNSPQVRQLRRRIAALEKQIAAER 269
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
89-228 4.53e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 4.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269995946   89 DDLKALTRNVNRLNESLRDMQLRLLQAPLQ--ADLTEQVWKVQDALQNQTDSLLALAGLVQRLEGTLWGLHAQAAQTEQA 166
Cdd:COG4913   309 AELERLEARLDALREELDELEAQIRGNGGDrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269995946  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.
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