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Conserved domains on  [gi|568954605|ref|XP_006509374|]
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macrophage scavenger receptor types I and II isoform X1 [Mus musculus]

Protein Classification

scavenger receptor cysteine-rich domain-containing protein( domain architecture ID 10507596)

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

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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 ...
 386-443 1.66e-27

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: 105.50  E-value: 1.66e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568954605   386 VRLVGGSGAHEGRVEIFHQGQWGTICDDRWDIRAGQVVCRSLGYQEVLAVHKRAHFGQ 443
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGP 58
Macscav_rec pfam03523
Macrophage scavenger receptor;
154-202 9.07e-25

Macrophage scavenger receptor;


:

Pssm-ID: 460956  Cd Length: 49  Bit Score: 96.37  E-value: 9.07e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568954605  154 MEERIESISNSKADLIDTERFQNFSMATDQRLNDILLQLNSLISSVQEH 202
Cdd:pfam03523   1 MEKRIQYISDSEANLIDSEHFQNFSMTTDQRFNDVLLQLNTLVSSVQEH 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 306-367 8.70e-22

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: 88.32  E-value: 8.70e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568954605  306 GPPGPqgekgdRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPGP 367
Cdd:pfam01391   1 GPPGP------PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
GumC super family cl34566
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
149-288 2.13e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG3206:

Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605 149 EHMKDMEERIESISN------SKADLIDTERFQNFSMatdQRLNDILLQLNSLISSVQEHGNSLDAISKSLQSLNMTLLD 222
Cdd:COG3206  182 EQLPELRKELEEAEAaleefrQKNGLVDLSEEAKLLL---QQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568954605 223 VQLHTETLNVRVRESTAKQQedISKLEERVYKVSAEVQSVKEEQAHVEQEVKQEV-RVLNNITNDLR 288
Cdd:COG3206  259 LLQSPVIQQLRAQLAELEAE--LAELSARYTPNHPDVIALRAQIAALRAQLQQEAqRILASLEAELE 323
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 357-379 3.01e-03

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: 35.93  E-value: 3.01e-03
                          10        20
                  ....*....|....*....|...
gi 568954605  357 GKPGRSGSPGPKGQKGEKGSVGG 379
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGP 23
 
Name Accession Description Interval E-value
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 386-443 1.66e-27

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: 105.50  E-value: 1.66e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568954605   386 VRLVGGSGAHEGRVEIFHQGQWGTICDDRWDIRAGQVVCRSLGYQEVLAVHKRAHFGQ 443
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGP 58
Macscav_rec pfam03523
Macrophage scavenger receptor;
154-202 9.07e-25

Macrophage scavenger receptor;


Pssm-ID: 460956  Cd Length: 49  Bit Score: 96.37  E-value: 9.07e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568954605  154 MEERIESISNSKADLIDTERFQNFSMATDQRLNDILLQLNSLISSVQEH 202
Cdd:pfam03523   1 MEKRIQYISDSEANLIDSEHFQNFSMTTDQRFNDVLLQLNTLVSSVQEH 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 306-367 8.70e-22

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: 88.32  E-value: 8.70e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568954605  306 GPPGPqgekgdRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPGP 367
Cdd:pfam01391   1 GPPGP------PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 391-443 3.10e-20

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: 85.51  E-value: 3.10e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568954605  391 GSGAHEGRVEIFHQGQWGTICDDRWDIRAGQVVCRSLGYQE-VLAVHKRAHFGQ 443
Cdd:pfam00530   1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGaVSAPSGCSYFGP 54
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-408 4.87e-18

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 86.11  E-value: 4.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605 305 QGPPGPQGEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVGGSTPLK 384
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                         90       100
                 ....*....|....*....|....
gi 568954605 385 TVRLVGGSGAHEGRVEIFHQGQWG 408
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAG 231
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-408 2.56e-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: 81.10  E-value: 2.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605 305 QGPPGPQGEKGDRGLTGQTGPPGA---PGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPG--PKGQKGEKGSVGG 379
Cdd:NF038329 167 QGEAGPQGPAGKDGEAGAKGPAGEkgpQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGE 246

                         90       100
                 ....*....|....*....|....*....
gi 568954605 380 STPLKTVRLVGGSGAHEGRVEIFHQGQWG 408
Cdd:NF038329 247 DGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 306-378 3.91e-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: 71.09  E-value: 3.91e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568954605 306 GPPGPQGEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQigfPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVG 378
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ---NGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-378 1.12e-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: 69.55  E-value: 1.12e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568954605 305 QGPPGPQGEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGS---PGPKGQKGEKGSVG 378
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKdglPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 306-382 1.18e-11

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 66.47  E-value: 1.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605 306 GPPGPQ---GEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVGGSTP 382
Cdd:NF038329 266 GEAGPDgpdGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
306-394 1.79e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 56.58  E-value: 1.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605 306 GPPGPQGEKGDRGLTGQTGPPGAPGIRGiPGvkGDRGQIGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVGGSTPLKT 385
Cdd:COG5164   10 GPSDPGGVTTPAGSQGSTKPAQNQGSTR-PA--GNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86


                 ....*....
gi 568954605 386 vrlVGGSGA 394
Cdd:COG5164   87 ---QGGTRP 92
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
149-288 2.13e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605 149 EHMKDMEERIESISN------SKADLIDTERFQNFSMatdQRLNDILLQLNSLISSVQEHGNSLDAISKSLQSLNMTLLD 222
Cdd:COG3206  182 EQLPELRKELEEAEAaleefrQKNGLVDLSEEAKLLL---QQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568954605 223 VQLHTETLNVRVRESTAKQQedISKLEERVYKVSAEVQSVKEEQAHVEQEVKQEV-RVLNNITNDLR 288
Cdd:COG3206  259 LLQSPVIQQLRAQLAELEAE--LAELSARYTPNHPDVIALRAQIAALRAQLQQEAqRILASLEAELE 323
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 357-379 3.01e-03

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: 35.93  E-value: 3.01e-03
                          10        20
                  ....*....|....*....|...
gi 568954605  357 GKPGRSGSPGPKGQKGEKGSVGG 379
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGP 23
PTZ00146 PTZ00146
fibrillarin; Provisional
 312-401 4.82e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 38.95  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605 312 GEKGDRGltgqTGPPGAPGIRGipgvKGDRGQIGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSV-------------G 378
Cdd:PTZ00146   1 GMGGGFG----GGRGGGRGGGG----GGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPGKVIvvphrfpgvfiakG 72

                         90       100
                 ....*....|....*....|....
gi 568954605 379 GSTPLKTVRLVGGSGAH-EGRVEI 401
Cdd:PTZ00146  73 KSDALVTKNMVPGESVYgEKRISV 96
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 132-282 7.10e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 7.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605   132 MEKENTSKVEMRFTIIMEHMKDMEERIESISNSKADL--------IDTERFQNFSMATDQRLNDILLQLNSLISSVQEHG 203
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELeelieeleSELEALLNERASLEEALALLRSELEELSEELRELE 907

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568954605   204 NSLDAISKSLQSLNMTLLDVQLHTETLNVRVREstakQQEDISKLEERVYKVSAEVQSVKEEQahvEQEVKQEVRVLNN 282
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLEGLEVRIDN----LQERLSEEYSLTLEEAEALENKIEDD---EEEARRRLKRLEN 979
 
Name Accession Description Interval E-value
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 386-443 1.66e-27

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: 105.50  E-value: 1.66e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568954605   386 VRLVGGSGAHEGRVEIFHQGQWGTICDDRWDIRAGQVVCRSLGYQEVLAVHKRAHFGQ 443
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGP 58
Macscav_rec pfam03523
Macrophage scavenger receptor;
154-202 9.07e-25

Macrophage scavenger receptor;


Pssm-ID: 460956  Cd Length: 49  Bit Score: 96.37  E-value: 9.07e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568954605  154 MEERIESISNSKADLIDTERFQNFSMATDQRLNDILLQLNSLISSVQEH 202
Cdd:pfam03523   1 MEKRIQYISDSEANLIDSEHFQNFSMTTDQRFNDVLLQLNTLVSSVQEH 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 306-367 8.70e-22

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: 88.32  E-value: 8.70e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568954605  306 GPPGPqgekgdRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPGP 367
Cdd:pfam01391   1 GPPGP------PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 391-443 3.10e-20

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: 85.51  E-value: 3.10e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568954605  391 GSGAHEGRVEIFHQGQWGTICDDRWDIRAGQVVCRSLGYQE-VLAVHKRAHFGQ 443
Cdd:pfam00530   1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGaVSAPSGCSYFGP 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 324-378 2.23e-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: 78.69  E-value: 2.23e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568954605  324 GPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVG 378
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-408 4.87e-18

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 86.11  E-value: 4.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605 305 QGPPGPQGEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVGGSTPLK 384
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                         90       100
                 ....*....|....*....|....
gi 568954605 385 TVRLVGGSGAHEGRVEIFHQGQWG 408
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAG 231
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-408 2.56e-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: 81.10  E-value: 2.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605 305 QGPPGPQGEKGDRGLTGQTGPPGA---PGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPG--PKGQKGEKGSVGG 379
Cdd:NF038329 167 QGEAGPQGPAGKDGEAGAKGPAGEkgpQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGE 246

                         90       100
                 ....*....|....*....|....*....
gi 568954605 380 STPLKTVRLVGGSGAHEGRVEIFHQGQWG 408
Cdd:NF038329 247 DGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 306-378 3.91e-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: 71.09  E-value: 3.91e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568954605 306 GPPGPQGEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQigfPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVG 378
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ---NGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-378 1.12e-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: 69.55  E-value: 1.12e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568954605 305 QGPPGPQGEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGS---PGPKGQKGEKGSVG 378
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKdglPGKDGKDGQNGKDG 311
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 305-359 5.62e-12

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: 60.59  E-value: 5.62e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568954605  305 QGPPGPQGEKGDRGLTGQTGPPGAPgirgipgvkgdrgqiGFPGGRGNPGAPGKP 359
Cdd:pfam01391  18 PGPPGPPGPPGPPGEPGPPGPPGPP---------------GPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 306-382 1.18e-11

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 66.47  E-value: 1.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605 306 GPPGPQ---GEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVGGSTP 382
Cdd:NF038329 266 GEAGPDgpdGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
306-394 1.79e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 56.58  E-value: 1.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605 306 GPPGPQGEKGDRGLTGQTGPPGAPGIRGiPGvkGDRGQIGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVGGSTPLKT 385
Cdd:COG5164   10 GPSDPGGVTTPAGSQGSTKPAQNQGSTR-PA--GNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86


                 ....*....
gi 568954605 386 vrlVGGSGA 394
Cdd:COG5164   87 ---QGGTRP 92
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
306-382 1.39e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 53.88  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605 306 GPPGPQGEKGDRGLTGQTGPPgAPGIRGIPGVKGDRGQIG----FPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVGGST 381
Cdd:COG5164  166 TPPGPGGSTTPPDDGGSTTPP-NKGETGTDIPTGGTPRQGpdgpVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERRG 244


                 .
gi 568954605 382 P 382
Cdd:COG5164  245 P 245
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
305-381 3.07e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 52.72  E-value: 3.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605 305 QGPPGPQGEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGR---GNPGAPGKPGRSGSPGPKGQKGEKGSV--GG 379
Cdd:COG5164   36 TRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTtpaQNQGGTRPAGNTGGTTPAGDGGATGPPddGG 115


                 ..
gi 568954605 380 ST 381
Cdd:COG5164  116 AT 117
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
305-381 7.23e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 51.57  E-value: 7.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605 305 QGPPGPQGEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNP---GAPGKPGRSGSPGPKGQKGEKGSV-GGS 380
Cdd:COG5164   54 TTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAgdgGATGPPDDGGATGPPDDGGSTTPPsGGS 133


                 .
gi 568954605 381 T 381
Cdd:COG5164  134 T 134
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
149-288 2.13e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605 149 EHMKDMEERIESISN------SKADLIDTERFQNFSMatdQRLNDILLQLNSLISSVQEHGNSLDAISKSLQSLNMTLLD 222
Cdd:COG3206  182 EQLPELRKELEEAEAaleefrQKNGLVDLSEEAKLLL---QQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568954605 223 VQLHTETLNVRVRESTAKQQedISKLEERVYKVSAEVQSVKEEQAHVEQEVKQEV-RVLNNITNDLR 288
Cdd:COG3206  259 LLQSPVIQQLRAQLAELEAE--LAELSARYTPNHPDVIALRAQIAALRAQLQQEAqRILASLEAELE 323
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 149-287 2.25e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 40.33  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605 149 EHMKDMEERIES-----------ISNSKADLIDTERfQNFSMAtDQRLNDILLQLNSLISSVQEHGNSLDAISKSLQ--- 214
Cdd:COG5185  377 EELDSFKDTIEStkesldeipqnQRGYAQEILATLE-DTLKAA-DRQIEELQRQIEQATSSNEEVSKLLNELISELNkvm 454

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568954605 215 --SLNMTLLDVQLHTETLNVRVRESTAKQQEDISKLEERVYKVSAEVQsvkEEQAHVEQEVKQEVRVLNNITNDL 287
Cdd:COG5185  455 reADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLE---KLRAKLERQLEGVRSKLDQVAESL 526
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 357-379 3.01e-03

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: 35.93  E-value: 3.01e-03
                          10        20
                  ....*....|....*....|...
gi 568954605  357 GKPGRSGSPGPKGQKGEKGSVGG 379
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGP 23
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
180-305 4.55e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 4.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605 180 ATDQRLNDILLQLNSLISSVQEHGNSLDAISKSLQSLNMTLLDVQLHTETLNVRVRESTAKQ---QEDISKLEERVYKVS 256
Cdd:COG4372   35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELaqaQEELESLQEEAEELQ 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568954605 257 AEVQSVKEEQAHVEQEVKQEVRVLNNITNDLRLKDWEHSQTLKNITFIQ 305
Cdd:COG4372  115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
PTZ00146 PTZ00146
fibrillarin; Provisional
 312-401 4.82e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 38.95  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605 312 GEKGDRGltgqTGPPGAPGIRGipgvKGDRGQIGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSV-------------G 378
Cdd:PTZ00146   1 GMGGGFG----GGRGGGRGGGG----GGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPGKVIvvphrfpgvfiakG 72

                         90       100
                 ....*....|....*....|....
gi 568954605 379 GSTPLKTVRLVGGSGAH-EGRVEI 401
Cdd:PTZ00146  73 KSDALVTKNMVPGESVYgEKRISV 96
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 132-282 7.10e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 7.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954605   132 MEKENTSKVEMRFTIIMEHMKDMEERIESISNSKADL--------IDTERFQNFSMATDQRLNDILLQLNSLISSVQEHG 203
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELeelieeleSELEALLNERASLEEALALLRSELEELSEELRELE 907

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568954605   204 NSLDAISKSLQSLNMTLLDVQLHTETLNVRVREstakQQEDISKLEERVYKVSAEVQSVKEEQahvEQEVKQEVRVLNN 282
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLEGLEVRIDN----LQERLSEEYSLTLEEAEALENKIEDD---EEEARRRLKRLEN 979
 
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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