NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2322055854|ref|NP_001400130|]
View 

scavenger receptor class A member 5 isoform 2 [Homo sapiens]

Protein Classification

scavenger receptor cysteine-rich domain-containing protein( domain architecture ID 10640959)

scavenger receptor cysteine-rich (SRCR) domain-containing protein os a member of the group B scavenger receptor cysteine-rich family (SRCR-SF), composed of tandem-repeats of the SRCR domain

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 350-450 2.35e-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: 142.48  E-value: 2.35e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854  350 IRLVNGSGPHEGRVEVYHDRRWGTVCDDGWDKKDGDVVCRMLGFRGVEEVYRTARFGQGTGRIWMDDVACKGTEETIFRC 429
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 2322055854  430 SFSKWGVTNCGHAEDASVTCN 450
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 261-340 6.96e-16

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: 79.56  E-value: 6.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854 261 AKGPPGPKGDQGDEGKEGRPGIPGLPGLRGLPGERGTPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGEKGDRAGD 340
Cdd:NF038329  130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA 209
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
46-256 1.79e-03

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


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854   46 DDLKALTRNVNRLNESFRDLQ-LRLLQAPLQadlteqVWKVQDALQNQSDSLLALAGAVQRLEGALWGLQAQAVQTEQAV 124
Cdd:COG4913    252 ELLEPIRELAERYAAARERLAeLEYLRAALR------LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854  125 ALLRDRTgQQSDTAQLElyQLQVESNSSQLLLRRHAGLLDGLARRVGILGEELADVGGVLRGLnhslsydVALHRTRLQD 204
Cdd:COG4913    326 DELEAQI-RGNGGDRLE--QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL-------RAEAAALLEA 395

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2322055854  205 LRVLVSNASEDTRRLRLAHVgmelQLKQELAMLNAVTEDLRLKDW---EHSIALR 256
Cdd:COG4913    396 LEEELEALEEALAEAEAALR----DLRRELRELEAEIASLERRKSnipARLLALR 446
 
Name Accession Description Interval E-value
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 350-450 2.35e-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: 142.48  E-value: 2.35e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854  350 IRLVNGSGPHEGRVEVYHDRRWGTVCDDGWDKKDGDVVCRMLGFRGVEEVYRTARFGQGTGRIWMDDVACKGTEETIFRC 429
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 2322055854  430 SFSKWGVTNCGHAEDASVTCN 450
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 355-450 1.05e-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: 124.80  E-value: 1.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854 355 GSGPHEGRVEVYHDRRWGTVCDDGWDKKDGDVVCRMLGFRGVEEVYRT-ARFGQG-TGRIWMDDVACKGTEETIFRCSFS 432
Cdd:pfam00530   1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSAPSGcSYFGPGsTGPIWLDDVRCSGNETSLWQCPHR 80

                          90
                  ....*....|....*...
gi 2322055854 433 KWGVTNCGHAEDASVTCN 450
Cdd:pfam00530  81 PWGNHNCSHSEDAGVICS 98
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 261-340 6.96e-16

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: 79.56  E-value: 6.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854 261 AKGPPGPKGDQGDEGKEGRPGIPGLPGLRGLPGERGTPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGEKGDRAGD 340
Cdd:NF038329  130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA 209
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 275-330 8.28e-16

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 71.37  E-value: 8.28e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2322055854 275 GKEGRPGIPGLPGLRGLPGERGTPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGE 330
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 261-335 5.97e-13

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 70.32  E-value: 5.97e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2322055854 261 AKGPPGPKGDQGDEGKEGRPGIPGLPGLRGLPGERGTPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGEKG 335
Cdd:NF038329  246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDG 320
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 261-337 5.31e-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: 5.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854 261 AKGPPGPKGDQGDEGKEGRPGIPGLPGLRGLPG-----ERGTPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGEKG 335
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275


                  ..
gi 2322055854 336 DR 337
Cdd:NF038329  276 KD 277
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 262-338 2.21e-08

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 56.07  E-value: 2.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854 262 KGPPGPKGDQGDEGKEGRPGIPGLPGLRGLP------GERGTPGLPGPKGDDG---KLGATGPMGMRGFKGDRGPKG-EK 331
Cdd:NF038329  268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPgkdgkdGQNGKDGLPGKDGKDGqpgKDGLPGKDGKDGQPGKPAPKTpEV 347


                  ....*..
gi 2322055854 332 GEKGDRA 338
Cdd:NF038329  348 PQKPDTA 354
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 293-336 1.14e-06

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: 50.67  E-value: 1.14e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2322055854 293 GERGTPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGEKGD 336
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE 160
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
46-256 1.79e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854   46 DDLKALTRNVNRLNESFRDLQ-LRLLQAPLQadlteqVWKVQDALQNQSDSLLALAGAVQRLEGALWGLQAQAVQTEQAV 124
Cdd:COG4913    252 ELLEPIRELAERYAAARERLAeLEYLRAALR------LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854  125 ALLRDRTgQQSDTAQLElyQLQVESNSSQLLLRRHAGLLDGLARRVGILGEELADVGGVLRGLnhslsydVALHRTRLQD 204
Cdd:COG4913    326 DELEAQI-RGNGGDRLE--QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL-------RAEAAALLEA 395

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2322055854  205 LRVLVSNASEDTRRLRLAHVgmelQLKQELAMLNAVTEDLRLKDW---EHSIALR 256
Cdd:COG4913    396 LEEELEALEEALAEAEAALR----DLRRELRELEAEIASLERRKSnipARLLALR 446
 
Name Accession Description Interval E-value
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 350-450 2.35e-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: 142.48  E-value: 2.35e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854  350 IRLVNGSGPHEGRVEVYHDRRWGTVCDDGWDKKDGDVVCRMLGFRGVEEVYRTARFGQGTGRIWMDDVACKGTEETIFRC 429
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 2322055854  430 SFSKWGVTNCGHAEDASVTCN 450
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 355-450 1.05e-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: 124.80  E-value: 1.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854 355 GSGPHEGRVEVYHDRRWGTVCDDGWDKKDGDVVCRMLGFRGVEEVYRT-ARFGQG-TGRIWMDDVACKGTEETIFRCSFS 432
Cdd:pfam00530   1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSAPSGcSYFGPGsTGPIWLDDVRCSGNETSLWQCPHR 80

                          90
                  ....*....|....*...
gi 2322055854 433 KWGVTNCGHAEDASVTCN 450
Cdd:pfam00530  81 PWGNHNCSHSEDAGVICS 98
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 261-340 6.96e-16

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: 79.56  E-value: 6.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854 261 AKGPPGPKGDQGDEGKEGRPGIPGLPGLRGLPGERGTPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGEKGDRAGD 340
Cdd:NF038329  130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA 209
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 275-330 8.28e-16

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 71.37  E-value: 8.28e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2322055854 275 GKEGRPGIPGLPGLRGLPGERGTPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGE 330
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 263-317 3.27e-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: 69.83  E-value: 3.27e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2322055854 263 GPPGPKGDQGDEGKEGRPGIPGLPGLRGLPGERGTPGLPGPKGDDGKLGATGPMG 317
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 278-333 8.75e-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: 65.59  E-value: 8.75e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2322055854 278 GRPGIPGLPGLRGLPGERGTPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGE 333
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 281-337 2.78e-13

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 64.05  E-value: 2.78e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2322055854 281 GIPGLPGLRGLPGERGTPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGEKGDR 337
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 261-312 5.78e-13

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 63.28  E-value: 5.78e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2322055854 261 AKGPPGPKGDQGDEGKEGRPGIPGLPGLRGLPGERGTPGLPGPKGDDGKLGA 312
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 261-335 5.97e-13

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 70.32  E-value: 5.97e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2322055854 261 AKGPPGPKGDQGDEGKEGRPGIPGLPGLRGLPGERGTPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGEKG 335
Cdd:NF038329  246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDG 320
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 263-315 6.76e-13

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 62.90  E-value: 6.76e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2322055854 263 GPPGPKGDQGDEGKEGRPGIPGLPGLRGLPGERGTPGLPGPKGDDGKLGATGP 315
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 261-337 5.31e-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: 5.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854 261 AKGPPGPKGDQGDEGKEGRPGIPGLPGLRGLPG-----ERGTPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGEKG 335
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275


                  ..
gi 2322055854 336 DR 337
Cdd:NF038329  276 KD 277
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 261-301 7.07e-10

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 54.42  E-value: 7.07e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2322055854 261 AKGPPGPKGDQGDEGKEGRPGIPGLPGLRGLPGERGTPGLP 301
Cdd:pfam01391  17 PPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 262-338 2.21e-08

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 56.07  E-value: 2.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854 262 KGPPGPKGDQGDEGKEGRPGIPGLPGLRGLP------GERGTPGLPGPKGDDG---KLGATGPMGMRGFKGDRGPKG-EK 331
Cdd:NF038329  268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPgkdgkdGQNGKDGLPGKDGKDGqpgKDGLPGKDGKDGQPGKPAPKTpEV 347


                  ....*..
gi 2322055854 332 GEKGDRA 338
Cdd:NF038329  348 PQKPDTA 354
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 293-336 1.14e-06

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: 50.67  E-value: 1.14e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2322055854 293 GERGTPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGEKGD 336
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE 160
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
46-256 1.79e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854   46 DDLKALTRNVNRLNESFRDLQ-LRLLQAPLQadlteqVWKVQDALQNQSDSLLALAGAVQRLEGALWGLQAQAVQTEQAV 124
Cdd:COG4913    252 ELLEPIRELAERYAAARERLAeLEYLRAALR------LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854  125 ALLRDRTgQQSDTAQLElyQLQVESNSSQLLLRRHAGLLDGLARRVGILGEELADVGGVLRGLnhslsydVALHRTRLQD 204
Cdd:COG4913    326 DELEAQI-RGNGGDRLE--QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL-------RAEAAALLEA 395

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2322055854  205 LRVLVSNASEDTRRLRLAHVgmelQLKQELAMLNAVTEDLRLKDW---EHSIALR 256
Cdd:COG4913    396 LEEELEALEEALAEAEAALR----DLRRELRELEAEIASLERRKSnipARLLALR 446
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
46-223 9.82e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 9.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854   46 DDLKALTRNVNRLNESFRDLQ--LRLLQAPLQA--DLTEQVWKVQD---------ALQNQSDSLLALAGAVQRLEGALWG 112
Cdd:COG4913    617 AELAELEEELAEAEERLEALEaeLDALQERREAlqRLAEYSWDEIDvasaereiaELEAELERLDASSDDLAALEEQLEE 696

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2322055854  113 LQAQAVQTEQAVALLRDRTGQ-QSDTAQLELYQLQVESNSSQLLLRRHAGLLDGLARRVGILGEElADVGGVLRGLnhsl 191
Cdd:COG4913    697 LEAELEELEEELDELKGEIGRlEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD-AVERELRENL---- 771

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2322055854  192 sydvalhRTRLQDLRVLVSNASEDTRRLRLAH 223
Cdd:COG4913    772 -------EERIDALRARLNRAEEELERAMRAF 796
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH