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Conserved domains on  [gi|755548506|ref|XP_011243408|]
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acetylcholinesterase collagenic tail peptide isoform X2 [Mus musculus]

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 ...
 94-237 6.49e-19

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: 88.04  E-value: 6.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548506  94 PGPEGPR------GEKGDLGMMGLPGSRGPMGSKGFPGSRGEKGSRGERGDLGPKGEKGFPGFPGMLGQKGEMGPKGESG 167
Cdd:NF038329 122 PGPAGPAgpageqGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755548506 168 LAGHRGPTGRPGKRGKQGQKGDSGIMGPPGKPGPSGQPGRQGPPGPPGPPSAGQL-VMGLKGERGFPGPPG 237
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAgKDGPRGDRGEAGPDG 272
DUF4215 pfam13948
Domain of unknown function (DUF4215); The function of this family is unknown.
 323-348 1.10e-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: 1.10e-05
                          10        20
                  ....*....|....*....|....*.
gi 755548506  323 CGDGVLQPGEECDDGNPDVSDGCIDC 348
Cdd:pfam13948  21 CGDGIIVNNEQCDDGNNLQFDGCYQC 46
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 94-237 6.49e-19

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: 6.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548506  94 PGPEGPR------GEKGDLGMMGLPGSRGPMGSKGFPGSRGEKGSRGERGDLGPKGEKGFPGFPGMLGQKGEMGPKGESG 167
Cdd:NF038329 122 PGPAGPAgpageqGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755548506 168 LAGHRGPTGRPGKRGKQGQKGDSGIMGPPGKPGPSGQPGRQGPPGPPGPPSAGQL-VMGLKGERGFPGPPG 237
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAgKDGPRGDRGEAGPDG 272
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 50-191 9.91e-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: 84.57  E-value: 9.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548506  50 GPQGPPGLPGKTGPKGEKGDLGRPGRKGRPGPPGVPGMPGPVGWPGPEGPRGEKGDLGMMGLPGSRGPMGSKGFPGSRGE 129
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755548506 130 KGSRGERGDLGPKGEKGFPGfpgmLGQKGEMGPKGESGLAGHRGPTGRPGKRGKQGQKGDSG 191
Cdd:NF038329 212 AGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 60-191 2.99e-17

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 83.03  E-value: 2.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548506  60 KTGPKGEKGDLGRPGRKGRPGPPGVPGMPGPVGWPGPEG--PRGEKGDLGMMGLPGSRGPMGSKGFPGSRGEKGSRGERG 137
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755548506 138 DLGPKGEKGFPGFPGMLGQKGEMGPKGESGLAGHRGPTGRPGKRGKQGQKGDSG 191
Cdd:NF038329 273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 14-180 6.28e-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: 54.53  E-value: 6.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548506  14 RGSRSPLLSPDMKNLLELEASPSPCIQGSLGSPGPPGPQgppglpGKTGPKGEKGDLGRpgrkgrpgppgvpgmpgpvgw 93
Cdd:NF038329 203 AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDP------GPTGEDGPQGPDGP--------------------- 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548506  94 PGPEGPRGEKGDLGMMGLPGSRGPMGSKGFPGSRGEKGSRGERGDLGPKGEKGFPGFPgmlGQKGEMGPKGESGLAGHRG 173
Cdd:NF038329 256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLP---GKDGKDGQPGKDGLPGKDG 332


                 ....*..
gi 755548506 174 PTGRPGK 180
Cdd:NF038329 333 KDGQPGK 339
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 107-162 7.40e-07

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: 45.95  E-value: 7.40e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755548506  107 GMMGLPGSRGPMGSKGFPGSRGEKGSRGERGDLGPKGEKGFPGFPGMLGQKGEMGP 162
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
DUF4215 pfam13948
Domain of unknown function (DUF4215); The function of this family is unknown.
 323-348 1.10e-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: 1.10e-05
                          10        20
                  ....*....|....*....|....*.
gi 755548506  323 CGDGVLQPGEECDDGNPDVSDGCIDC 348
Cdd:pfam13948  21 CGDGIIVNNEQCDDGNNLQFDGCYQC 46
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 321-345 1.37e-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: 41.59  E-value: 1.37e-05
                          10        20
                  ....*....|....*....|....*
gi 755548506  321 GTCGDGVLQPGEECDDGNPDVSDGC 345
Cdd:TIGR02232   2 PTCGDGIIEPGEECDDGNTTSGDGC 26
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 143-237 2.39e-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: 46.05  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548506 143 GEKGFPGFPGMLGQKGEMGPKGESGLAGHRGPTGRPGKRGKQGQKGDSGIMGPPGKPGPSGQPGRQGPPGPPGPpsagql 222
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE------ 190

                         90
                 ....*....|....*
gi 755548506 223 vMGLKGERGFPGPPG 237
Cdd:NF038329 191 -KGPQGPRGETGPAG 204
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 94-237 6.49e-19

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: 6.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548506  94 PGPEGPR------GEKGDLGMMGLPGSRGPMGSKGFPGSRGEKGSRGERGDLGPKGEKGFPGFPGMLGQKGEMGPKGESG 167
Cdd:NF038329 122 PGPAGPAgpageqGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755548506 168 LAGHRGPTGRPGKRGKQGQKGDSGIMGPPGKPGPSGQPGRQGPPGPPGPPSAGQL-VMGLKGERGFPGPPG 237
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAgKDGPRGDRGEAGPDG 272
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 50-191 9.91e-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: 84.57  E-value: 9.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548506  50 GPQGPPGLPGKTGPKGEKGDLGRPGRKGRPGPPGVPGMPGPVGWPGPEGPRGEKGDLGMMGLPGSRGPMGSKGFPGSRGE 129
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755548506 130 KGSRGERGDLGPKGEKGFPGfpgmLGQKGEMGPKGESGLAGHRGPTGRPGKRGKQGQKGDSG 191
Cdd:NF038329 212 AGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 60-191 2.99e-17

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 83.03  E-value: 2.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548506  60 KTGPKGEKGDLGRPGRKGRPGPPGVPGMPGPVGWPGPEG--PRGEKGDLGMMGLPGSRGPMGSKGFPGSRGEKGSRGERG 137
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755548506 138 DLGPKGEKGFPGFPGMLGQKGEMGPKGESGLAGHRGPTGRPGKRGKQGQKGDSG 191
Cdd:NF038329 273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 14-180 6.28e-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: 54.53  E-value: 6.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548506  14 RGSRSPLLSPDMKNLLELEASPSPCIQGSLGSPGPPGPQgppglpGKTGPKGEKGDLGRpgrkgrpgppgvpgmpgpvgw 93
Cdd:NF038329 203 AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDP------GPTGEDGPQGPDGP--------------------- 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548506  94 PGPEGPRGEKGDLGMMGLPGSRGPMGSKGFPGSRGEKGSRGERGDLGPKGEKGFPGFPgmlGQKGEMGPKGESGLAGHRG 173
Cdd:NF038329 256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLP---GKDGKDGQPGKDGLPGKDG 332


                 ....*..
gi 755548506 174 PTGRPGK 180
Cdd:NF038329 333 KDGQPGK 339
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 107-162 7.40e-07

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: 45.95  E-value: 7.40e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755548506  107 GMMGLPGSRGPMGSKGFPGSRGEKGSRGERGDLGPKGEKGFPGFPGMLGQKGEMGP 162
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 113-167 1.10e-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: 45.18  E-value: 1.10e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755548506  113 GSRGPMGSKGFPGSRGEKGSRGERGDLGPKGEKGFPGFPGMLGQKGEMGPKGESG 167
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 116-170 1.84e-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: 1.84e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755548506  116 GPMGSKGFPGSRGEKGSRGERGDLGPKGEKGFPGFPGMLGQKGEMGPKGESGLAG 170
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
DUF4215 pfam13948
Domain of unknown function (DUF4215); The function of this family is unknown.
 323-348 1.10e-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: 1.10e-05
                          10        20
                  ....*....|....*....|....*.
gi 755548506  323 CGDGVLQPGEECDDGNPDVSDGCIDC 348
Cdd:pfam13948  21 CGDGIIVNNEQCDDGNNLQFDGCYQC 46
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 321-345 1.37e-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: 41.59  E-value: 1.37e-05
                          10        20
                  ....*....|....*....|....*
gi 755548506  321 GTCGDGVLQPGEECDDGNPDVSDGC 345
Cdd:TIGR02232   2 PTCGDGIIEPGEECDDGNTTSGDGC 26
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 143-237 2.39e-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: 46.05  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548506 143 GEKGFPGFPGMLGQKGEMGPKGESGLAGHRGPTGRPGKRGKQGQKGDSGIMGPPGKPGPSGQPGRQGPPGPPGPpsagql 222
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE------ 190

                         90
                 ....*....|....*
gi 755548506 223 vMGLKGERGFPGPPG 237
Cdd:NF038329 191 -KGPQGPRGETGPAG 204
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 95-144 2.82e-05

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: 41.33  E-value: 2.82e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 755548506   95 GPEGPRGEKGDLGMMGLPGSRGPMGSKGFPGSRGEKGSRGERGDLGPKGE 144
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 95-159 5.72e-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: 37.86  E-value: 5.72e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755548506   95 GPEGPRGEKGdlgmmgLPGSRGPMGSKGFPGSRGEkgsRGERGDLGPKGEKGFPGFPGMLGQKGE 159
Cdd:pfam01391   1 GPPGPPGPPG------PPGPPGPPGPPGPPGPPGP---PGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 143-186 5.41e-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: 34.78  E-value: 5.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 755548506  143 GEKGFPGFPGMLGQKGEMGPKGESGLAGHRGPTGRPGKRGKQGQ 186
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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