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Conserved domains on  [gi|12229730|sp|O35167|]
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RecName: Full=Acetylcholinesterase collagenic tail peptide; AltName: Full=AChE Q subunit; AltName: Full=Acetylcholinesterase-associated collagen; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 146-291 8.68e-21

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: 94.20  E-value: 8.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12229730  146 GWPGPEGPRGEKGDVGMMGLPGSRGPMGSKGFPGSRGEKGSRGERGDLGPKGEKGFPGFPGMLGQKGEMGPKGESGIAGH 225
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12229730  226 RGPTGRPGKRGKQGQKGDSGIMGPPGKPGPSGQPGRQGPPGPPGPPSAGQL-VMGLKGERGFPGPPG 291
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAgKDGPRGDRGEAGPDG 272
DUF4215 pfam13948
Domain of unknown function (DUF4215); The function of this family is unknown.
 377-403 1.13e-05

Domain of unknown function (DUF4215); The function of this family is unknown.


:

Pssm-ID: 290659  Cd Length: 47  Bit Score: 42.39  E-value: 1.13e-05
                          10        20
                  ....*....|....*....|....*..
gi 12229730   377 LCGDGVLQPGEECDDGNPDVSDGCIDC 403
Cdd:pfam13948  20 ICGDGIIVNNEQCDDGNNLQFDGCYQC 46
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 146-291 8.68e-21

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: 94.20  E-value: 8.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12229730  146 GWPGPEGPRGEKGDVGMMGLPGSRGPMGSKGFPGSRGEKGSRGERGDLGPKGEKGFPGFPGMLGQKGEMGPKGESGIAGH 225
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12229730  226 RGPTGRPGKRGKQGQKGDSGIMGPPGKPGPSGQPGRQGPPGPPGPPSAGQL-VMGLKGERGFPGPPG 291
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAgKDGPRGDRGEAGPDG 272
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 104-245 1.16e-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: 88.04  E-value: 1.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12229730  104 GPQGPPGLPGKAGPKGEKGDLGRPGRKGRPGPPGVPGEPGPVGWPGPEGPRGEKGDVGMMGLPGSRGPMGSKGFPGSRGE 183
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12229730  184 KGSRGERGDLGPKGEKGFPGfpgmLGQKGEMGPKGESGIAGHRGPTGRPGKRGKQGQKGDSG 245
Cdd:NF038329 212 AGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 114-245 1.19e-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: 88.04  E-value: 1.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12229730  114 KAGPKGEKGDLGRPGRKGRPGPPGVPGEPGPVGWPGPEG--PRGEKGDVGMMGLPGSRGPMGSKGFPGSRGEKGSRGERG 191
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 12229730  192 DLGPKGEKGFPGFPGMLGQKGEMGPKGESGIAGHRGPTGRPGKRGKQGQKGDSG 245
Cdd:NF038329 273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 107-234 1.10e-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: 57.22  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12229730  107 GPPGLPGKAGPKGEkgdlgrpgrkgrpgppgvpgepgpvgwPGPEGPRGEKGDVGMMGLPGSRGPMGSKGFPGSRGEKGS 186
Cdd:NF038329 242 GPTGEDGPQGPDGP---------------------------AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGK 294

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 12229730  187 RGERGDLGPKGEKGFPGFPgmlGQKGEMGPKGESGIAGHRGPTGRPGK 234
Cdd:NF038329 295 DGLPGKDGKDGQNGKDGLP---GKDGKDGQPGKDGLPGKDGKDGQPGK 339
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 161-216 5.92e-08

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: 49.03  E-value: 5.92e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 12229730   161 GMMGLPGSRGPMGSKGFPGSRGEKGSRGERGDLGPKGEKGFPGFPGMLGQKGEMGP 216
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 197-245 1.08e-05

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: 47.59  E-value: 1.08e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 12229730  197 GEKGFPGFPGMLGQKGEMGPKGESGIAGHRGPTGRPGKRGKQGQKGDSG 245
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG 165
DUF4215 pfam13948
Domain of unknown function (DUF4215); The function of this family is unknown.
 377-403 1.13e-05

Domain of unknown function (DUF4215); The function of this family is unknown.


Pssm-ID: 290659  Cd Length: 47  Bit Score: 42.39  E-value: 1.13e-05
                          10        20
                  ....*....|....*....|....*..
gi 12229730   377 LCGDGVLQPGEECDDGNPDVSDGCIDC 403
Cdd:pfam13948  20 ICGDGIIVNNEQCDDGNNLQFDGCYQC 46
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 378-400 1.48e-05

Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.


Pssm-ID: 200169 [Multi-domain]  Cd Length: 38  Bit Score: 41.97  E-value: 1.48e-05
                          10        20
                  ....*....|....*....|...
gi 12229730   378 CGDGVLQPGEECDDGNPDVSDGC 400
Cdd:TIGR02232   4 CGDGIIEPGEECDDGNTTSGDGC 26
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 146-291 8.68e-21

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: 94.20  E-value: 8.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12229730  146 GWPGPEGPRGEKGDVGMMGLPGSRGPMGSKGFPGSRGEKGSRGERGDLGPKGEKGFPGFPGMLGQKGEMGPKGESGIAGH 225
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12229730  226 RGPTGRPGKRGKQGQKGDSGIMGPPGKPGPSGQPGRQGPPGPPGPPSAGQL-VMGLKGERGFPGPPG 291
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAgKDGPRGDRGEAGPDG 272
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 104-245 1.16e-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: 88.04  E-value: 1.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12229730  104 GPQGPPGLPGKAGPKGEKGDLGRPGRKGRPGPPGVPGEPGPVGWPGPEGPRGEKGDVGMMGLPGSRGPMGSKGFPGSRGE 183
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12229730  184 KGSRGERGDLGPKGEKGFPGfpgmLGQKGEMGPKGESGIAGHRGPTGRPGKRGKQGQKGDSG 245
Cdd:NF038329 212 AGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 114-245 1.19e-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: 88.04  E-value: 1.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12229730  114 KAGPKGEKGDLGRPGRKGRPGPPGVPGEPGPVGWPGPEG--PRGEKGDVGMMGLPGSRGPMGSKGFPGSRGEKGSRGERG 191
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 12229730  192 DLGPKGEKGFPGFPGMLGQKGEMGPKGESGIAGHRGPTGRPGKRGKQGQKGDSG 245
Cdd:NF038329 273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 107-234 1.10e-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: 57.22  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12229730  107 GPPGLPGKAGPKGEkgdlgrpgrkgrpgppgvpgepgpvgwPGPEGPRGEKGDVGMMGLPGSRGPMGSKGFPGSRGEKGS 186
Cdd:NF038329 242 GPTGEDGPQGPDGP---------------------------AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGK 294

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 12229730  187 RGERGDLGPKGEKGFPGFPgmlGQKGEMGPKGESGIAGHRGPTGRPGK 234
Cdd:NF038329 295 DGLPGKDGKDGQNGKDGLP---GKDGKDGQPGKDGLPGKDGKDGQPGK 339
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 161-216 5.92e-08

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: 49.03  E-value: 5.92e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 12229730   161 GMMGLPGSRGPMGSKGFPGSRGEKGSRGERGDLGPKGEKGFPGFPGMLGQKGEMGP 216
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 173-228 7.72e-08

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: 48.64  E-value: 7.72e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 12229730   173 GSKGFPGSRGEKGSRGERGDLGPKGEKGFPGFPGMLGQKGEMGPKGESGIAGHRGP 228
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 149-203 1.71e-06

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: 44.79  E-value: 1.71e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 12229730   149 GPEGPRGEKGDVGMMGLPGSRGPMGSKGFPGSRGEKGSRGERGDLGPKGEKGFPG 203
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 149-198 4.26e-06

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: 44.02  E-value: 4.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 12229730   149 GPEGPRGEKGDVGMMGLPGSRGPMGSKGFPGSRGEKGSRGERGDLGPKGE 198
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 197-245 1.08e-05

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: 47.59  E-value: 1.08e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 12229730  197 GEKGFPGFPGMLGQKGEMGPKGESGIAGHRGPTGRPGKRGKQGQKGDSG 245
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG 165
DUF4215 pfam13948
Domain of unknown function (DUF4215); The function of this family is unknown.
 377-403 1.13e-05

Domain of unknown function (DUF4215); The function of this family is unknown.


Pssm-ID: 290659  Cd Length: 47  Bit Score: 42.39  E-value: 1.13e-05
                          10        20
                  ....*....|....*....|....*..
gi 12229730   377 LCGDGVLQPGEECDDGNPDVSDGCIDC 403
Cdd:pfam13948  20 ICGDGIIVNNEQCDDGNNLQFDGCYQC 46
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 378-400 1.48e-05

Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.


Pssm-ID: 200169 [Multi-domain]  Cd Length: 38  Bit Score: 41.97  E-value: 1.48e-05
                          10        20
                  ....*....|....*....|...
gi 12229730   378 CGDGVLQPGEECDDGNPDVSDGC 400
Cdd:TIGR02232   4 CGDGIIEPGEECDDGNTTSGDGC 26
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 197-240 8.11e-04

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: 37.47  E-value: 8.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 12229730   197 GEKGFPGFPGMLGQKGEMGPKGESGIAGHRGPTGRPGKRGKQGQ 240
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGP 44
 
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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