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Conserved domains on  [gi|564386766|ref|XP_006252266|]
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scavenger receptor class A member 5 isoform X1 [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 ...
 391-491 1.33e-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: 1.33e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386766   391 IRLVNGSGPHQGRVEVFHDRRWGTVCDDGWDKKDGDVVCRMLGFHSVEEVHRTARFGQGTGRIWMDDVNCKGTESSIFHC 470
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 564386766   471 QFSKWGVTNCGHAEDAGVTCT 491
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 319-374 7.34e-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: 7.34e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564386766  319 GKEGKPGSPGLPGSRGLPGERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGE 374
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK09039 super family cl32341
peptidoglycan -binding protein;
56-250 1.10e-04

peptidoglycan -binding protein;


The actual alignment was detected with superfamily member PRK09039:

Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 44.19  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386766  56 LSALKHAVLGLyLLVFLtlVGVFILavSRPRSSPDD-LKALTRNINRLNEsfrdmQLRLLQAPLQaDLteqvwkvQDALQ 134
Cdd:PRK09039  23 LSTLLLVIMFL-LTVFV--VAQFFL--SREISGKDSaLDRLNSQIAELAD-----LLSLERQGNQ-DL-------QDSVA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386766 135 NQTDSLLALAGLVQRLEGTLWGLHAQAAQTEQAVALL---RDRTGQQSDSA--QLELYQLQVESNRSQllLQRHAGLLDG 209
Cdd:PRK09039  85 NLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELaqeLDSEKQVSARAlaQVELLNQQIAALRRQ--LAALEAALDA 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 564386766 210 LAHRVGVLGEELADVGgalRGLNHSLSYDValhstwlQDLQ 250
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 ...
 391-491 1.33e-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: 1.33e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386766   391 IRLVNGSGPHQGRVEVFHDRRWGTVCDDGWDKKDGDVVCRMLGFHSVEEVHRTARFGQGTGRIWMDDVNCKGTESSIFHC 470
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 564386766   471 QFSKWGVTNCGHAEDAGVTCT 491
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 396-491 2.03e-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: 2.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386766  396 GSGPHQGRVEVFHDRRWGTVCDDGWDKKDGDVVCRMLGFHSVEEVHRT-ARFGQG-TGRIWMDDVNCKGTESSIFHCQFS 473
Cdd:pfam00530   1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSAPSGcSYFGPGsTGPIWLDDVRCSGNETSLWQCPHR 80

                          90
                  ....*....|....*...
gi 564386766  474 KWGVTNCGHAEDAGVTCT 491
Cdd:pfam00530  81 PWGNHNCSHSEDAGVICS 98
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 319-374 7.34e-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: 7.34e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564386766  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 ...
 305-381 1.05e-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: 85.34  E-value: 1.05e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564386766 305 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERGER 381
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQ 206
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-379 1.14e-13

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 73.02  E-value: 1.14e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564386766 305 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERG 379
Cdd:NF038329 246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDG 320
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 306-381 5.93e-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: 67.62  E-value: 5.93e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564386766 306 KGPPGPKGDQGNEGKEGKPGSPGLPGSRGlpgERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERGER 381
Cdd:NF038329 232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDG---PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKD 304
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 337-386 3.27e-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: 55.68  E-value: 3.27e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564386766 337 GERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERGER-AAGDM 386
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKgPAGPQ 167
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 307-361 2.28e-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: 2.28e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564386766 307 GPPGPKGDQGNEGKEGKPGSPGLPGSR---GLPGERGDPGMPGPKGDDGKLGATGPMG 361
Cdd:NF038329 281 GPVGPAGKDGQNGKDGLPGKDGKDGQNgkdGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
PRK09039 PRK09039
peptidoglycan -binding protein;
56-250 1.10e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 44.19  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386766  56 LSALKHAVLGLyLLVFLtlVGVFILavSRPRSSPDD-LKALTRNINRLNEsfrdmQLRLLQAPLQaDLteqvwkvQDALQ 134
Cdd:PRK09039  23 LSTLLLVIMFL-LTVFV--VAQFFL--SREISGKDSaLDRLNSQIAELAD-----LLSLERQGNQ-DL-------QDSVA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386766 135 NQTDSLLALAGLVQRLEGTLWGLHAQAAQTEQAVALL---RDRTGQQSDSA--QLELYQLQVESNRSQllLQRHAGLLDG 209
Cdd:PRK09039  85 NLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELaqeLDSEKQVSARAlaQVELLNQQIAALRRQ--LAALEAALDA 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 564386766 210 LAHRVGVLGEELADVGgalRGLNHSLSYDValhstwlQDLQ 250
Cdd:PRK09039 163 SEKRDRESQAKIADLG---RRLNVALAQRV-------QELN 193
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 67-313 4.58e-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: 4.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386766  67 YLLVFLTLVGVFILAVSRPRSSPDDLKALTRNINRLNEsfrdmqlrllqapLQADLTEQVWKVQDALQNQTDSLLALAGL 146
Cdd:COG4942    4 LLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEK-------------ELAALKKEEKALLKQLAALERRIAALARR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386766 147 VQRLEGTLWGLHAQAAQTEQAVALLRDRTGQQSDSAQLELYQLQVESNRSQLLL----------QRHAGLLDGLAHRVGV 216
Cdd:COG4942   71 IRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspedfldaVRRLQYLKYLAPARRE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386766 217 LGEELADVGGALRGLNHSLSYDVALHSTWLQDLQVLVSNASADTRRMRLVHMDMEMQLK---QELATLNVVTEDLR--LK 291
Cdd:COG4942  151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAelaAELAELQQEAEELEalIA 230

                        250       260
                 ....*....|....*....|...
gi 564386766 292 DWEHSIALR-NITLAKGPPGPKG 313
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 ...
 391-491 1.33e-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: 1.33e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386766   391 IRLVNGSGPHQGRVEVFHDRRWGTVCDDGWDKKDGDVVCRMLGFHSVEEVHRTARFGQGTGRIWMDDVNCKGTESSIFHC 470
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 564386766   471 QFSKWGVTNCGHAEDAGVTCT 491
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 396-491 2.03e-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: 2.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386766  396 GSGPHQGRVEVFHDRRWGTVCDDGWDKKDGDVVCRMLGFHSVEEVHRT-ARFGQG-TGRIWMDDVNCKGTESSIFHCQFS 473
Cdd:pfam00530   1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSAPSGcSYFGPGsTGPIWLDDVRCSGNETSLWQCPHR 80

                          90
                  ....*....|....*...
gi 564386766  474 KWGVTNCGHAEDAGVTCT 491
Cdd:pfam00530  81 PWGNHNCSHSEDAGVICS 98
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 319-374 7.34e-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: 7.34e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564386766  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 ...
 305-381 1.05e-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: 85.34  E-value: 1.05e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564386766 305 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERGER 381
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQ 206
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 322-378 1.55e-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: 1.55e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564386766  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 ...
 305-379 1.14e-13

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 73.02  E-value: 1.14e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564386766 305 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERG 379
Cdd:NF038329 246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDG 320
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 325-381 1.41e-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: 1.41e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564386766  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 1.92e-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: 1.92e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564386766  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 ...
 306-381 5.93e-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: 67.62  E-value: 5.93e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564386766 306 KGPPGPKGDQGNEGKEGKPGSPGLPGSRGlpgERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERGER 381
Cdd:NF038329 232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDG---PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKD 304
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 564386766  305 AKGPPGPKGDQGNEGKEGKPGSPGLPGSRGLPGERGDPGMPGPKG 349
Cdd:pfam01391  11 PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 328-383 3.01e-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: 58.66  E-value: 3.01e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564386766  328 GLPGSRGLPGErgdPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERGERAA 383
Cdd:pfam01391   1 GPPGPPGPPGP---PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 305-347 3.16e-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: 3.16e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 564386766  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 1.76e-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: 1.76e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 564386766  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 ...
 337-386 3.27e-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: 55.68  E-value: 3.27e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564386766 337 GERGDPGMPGPKGDDGKLGATGPMGMRGFKGERGPKGEKGERGER-AAGDM 386
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKgPAGPQ 167
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 307-361 2.28e-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: 2.28e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564386766 307 GPPGPKGDQGNEGKEGKPGSPGLPGSR---GLPGERGDPGMPGPKGDDGKLGATGPMG 361
Cdd:NF038329 281 GPVGPAGKDGQNGKDGLPGKDGKDGQNgkdGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
PRK09039 PRK09039
peptidoglycan -binding protein;
56-250 1.10e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 44.19  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386766  56 LSALKHAVLGLyLLVFLtlVGVFILavSRPRSSPDD-LKALTRNINRLNEsfrdmQLRLLQAPLQaDLteqvwkvQDALQ 134
Cdd:PRK09039  23 LSTLLLVIMFL-LTVFV--VAQFFL--SREISGKDSaLDRLNSQIAELAD-----LLSLERQGNQ-DL-------QDSVA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386766 135 NQTDSLLALAGLVQRLEGTLWGLHAQAAQTEQAVALL---RDRTGQQSDSA--QLELYQLQVESNRSQllLQRHAGLLDG 209
Cdd:PRK09039  85 NLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELaqeLDSEKQVSARAlaQVELLNQQIAALRRQ--LAALEAALDA 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 564386766 210 LAHRVGVLGEELADVGgalRGLNHSLSYDValhstwlQDLQ 250
Cdd:PRK09039 163 SEKRDRESQAKIADLG---RRLNVALAQRV-------QELN 193
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 67-313 4.58e-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: 4.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386766  67 YLLVFLTLVGVFILAVSRPRSSPDDLKALTRNINRLNEsfrdmqlrllqapLQADLTEQVWKVQDALQNQTDSLLALAGL 146
Cdd:COG4942    4 LLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEK-------------ELAALKKEEKALLKQLAALERRIAALARR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386766 147 VQRLEGTLWGLHAQAAQTEQAVALLRDRTGQQSDSAQLELYQLQVESNRSQLLL----------QRHAGLLDGLAHRVGV 216
Cdd:COG4942   71 IRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspedfldaVRRLQYLKYLAPARRE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386766 217 LGEELADVGGALRGLNHSLSYDVALHSTWLQDLQVLVSNASADTRRMRLVHMDMEMQLK---QELATLNVVTEDLR--LK 291
Cdd:COG4942  151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAelaAELAELQQEAEELEalIA 230

                        250       260
                 ....*....|....*....|...
gi 564386766 292 DWEHSIALR-NITLAKGPPGPKG 313
Cdd:COG4942  231 RLEAEAAAAaERTPAAGFAALKG 253
 
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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