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Conserved domains on  [gi|145701009|ref|NP_536800|]
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acetylcholinesterase collagenic tail peptide isoform III precursor [Homo sapiens]

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 ...
 68-256 6.63e-24

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: 103.06  E-value: 6.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145701009  68 RGGRSP-GPPGLPGKTGPKGEKGELGRPGRKGRPGPPGVpgmpgpigwPGPEGPRGEKGDLGMMGLPGSRGPMGSKGYPG 146
Cdd:NF038329 119 KGEPGPaGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE---------RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145701009 147 SRGEKGSRGEKGDLGPKGEKGFPGFPGMLGQKGEMGPKGEPGiAGHRGPTGRPGKRGKQGQKGDSGvmgppgkpgpSGQP 226
Cdd:NF038329 190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDG----------PAGK 258

                        170       180       190
                 ....*....|....*....|....*....|
gi 145701009 227 GRPGPPGPPPAGQLIMGPKGERGFPGPPGR 256
Cdd:NF038329 259 DGPRGDRGEAGPDGPDGKDGERGPVGPAGK 288
myxo_disulf_rpt super family cl11785
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 339-363 7.70e-06

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.


The actual alignment was detected with superfamily member TIGR02232:

Pssm-ID: 200169 [Multi-domain]  Cd Length: 38  Bit Score: 42.36  E-value: 7.70e-06
                          10        20
                  ....*....|....*....|....*
gi 145701009  339 GTCGDGLLQPGEECDDGNSDVGDDC 363
Cdd:TIGR02232   2 PTCGDGIIEPGEECDDGNTTSGDGC 26
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 68-256 6.63e-24

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: 103.06  E-value: 6.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145701009  68 RGGRSP-GPPGLPGKTGPKGEKGELGRPGRKGRPGPPGVpgmpgpigwPGPEGPRGEKGDLGMMGLPGSRGPMGSKGYPG 146
Cdd:NF038329 119 KGEPGPaGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE---------RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145701009 147 SRGEKGSRGEKGDLGPKGEKGFPGFPGMLGQKGEMGPKGEPGiAGHRGPTGRPGKRGKQGQKGDSGvmgppgkpgpSGQP 226
Cdd:NF038329 190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDG----------PAGK 258

                        170       180       190
                 ....*....|....*....|....*....|
gi 145701009 227 GRPGPPGPPPAGQLIMGPKGERGFPGPPGR 256
Cdd:NF038329 259 DGPRGDRGEAGPDGPDGKDGERGPVGPAGK 288
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 73-256 5.19e-20

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: 91.51  E-value: 5.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145701009  73 PGPPGLPGKTGPKGEKGELGRPGRKGRPGPPGVPGMPGPIGWPGPEGPRGEKGDLGMMGLPGS--RGPMGSKGYPGSRGE 150
Cdd:NF038329 170 AGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGP 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145701009 151 KGSRGEKGDLGPKGEKGFPGFPGMLGQKGEMGPKGEPGIAGHRGPTGRPGKRGKQGQKGDSGVmgpPGKPGPSgqpgrpg 230
Cdd:NF038329 250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL---PGKDGKD------- 319

                        170       180
                 ....*....|....*....|....*.
gi 145701009 231 ppgpppagqlimGPKGERGFPGPPGR 256
Cdd:NF038329 320 ------------GQPGKDGLPGKDGK 333
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 74-226 2.79e-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: 86.50  E-value: 2.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145701009  74 GPPGLPGKTGPKGEKGELGRPGRKGRPGPPGVPGMPGPIGWPGPEGpRGEKGDLGMMGLPGSRGPMGSKGYPGSRGEKGS 153
Cdd:NF038329 186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145701009 154 RGEKGDLGPKGEKGFPGFPGMLGQKGEMGPKGEPGIAGHRGPTGRPGKRGKQGQKGDSGVMGPPGKPGPSGQP 226
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 140-195 4.83e-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: 49.41  E-value: 4.83e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145701009  140 GSKGYPGSRGEKGSRGEKGDLGPKGEKGFPGFPGMLGQKGEMGPKGEPGIAGHRGP 195
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 164-255 6.42e-07

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 51.44  E-value: 6.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145701009 164 GEKGFPGFPGMLGQKGEMGPKGEPGIAGHRGPTGRPGKRGKQGQKGDSGVMGPPGKPGPSGQPGRPGPPGPPPAgqliMG 243
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE----KG 192

                         90
                 ....*....|..
gi 145701009 244 PKGERGFPGPPG 255
Cdd:NF038329 193 PQGPRGETGPAG 204
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 339-363 7.70e-06

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: 42.36  E-value: 7.70e-06
                          10        20
                  ....*....|....*....|....*
gi 145701009  339 GTCGDGLLQPGEECDDGNSDVGDDC 363
Cdd:TIGR02232   2 PTCGDGIIEPGEECDDGNTTSGDGC 26
DUF4215 pfam13948
Domain of unknown function (DUF4215); The function of this family is unknown.
 341-366 2.44e-05

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


Pssm-ID: 290659  Cd Length: 47  Bit Score: 41.24  E-value: 2.44e-05
                          10        20
                  ....*....|....*....|....*.
gi 145701009  341 CGDGLLQPGEECDDGNSDVGDDCIRC 366
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 ...
 68-256 6.63e-24

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: 103.06  E-value: 6.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145701009  68 RGGRSP-GPPGLPGKTGPKGEKGELGRPGRKGRPGPPGVpgmpgpigwPGPEGPRGEKGDLGMMGLPGSRGPMGSKGYPG 146
Cdd:NF038329 119 KGEPGPaGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE---------RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145701009 147 SRGEKGSRGEKGDLGPKGEKGFPGFPGMLGQKGEMGPKGEPGiAGHRGPTGRPGKRGKQGQKGDSGvmgppgkpgpSGQP 226
Cdd:NF038329 190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDG----------PAGK 258

                        170       180       190
                 ....*....|....*....|....*....|
gi 145701009 227 GRPGPPGPPPAGQLIMGPKGERGFPGPPGR 256
Cdd:NF038329 259 DGPRGDRGEAGPDGPDGKDGERGPVGPAGK 288
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 73-256 5.19e-20

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: 91.51  E-value: 5.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145701009  73 PGPPGLPGKTGPKGEKGELGRPGRKGRPGPPGVPGMPGPIGWPGPEGPRGEKGDLGMMGLPGS--RGPMGSKGYPGSRGE 150
Cdd:NF038329 170 AGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGP 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145701009 151 KGSRGEKGDLGPKGEKGFPGFPGMLGQKGEMGPKGEPGIAGHRGPTGRPGKRGKQGQKGDSGVmgpPGKPGPSgqpgrpg 230
Cdd:NF038329 250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL---PGKDGKD------- 319

                        170       180
                 ....*....|....*....|....*.
gi 145701009 231 ppgpppagqlimGPKGERGFPGPPGR 256
Cdd:NF038329 320 ------------GQPGKDGLPGKDGK 333
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 74-226 2.79e-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: 86.50  E-value: 2.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145701009  74 GPPGLPGKTGPKGEKGELGRPGRKGRPGPPGVPGMPGPIGWPGPEGpRGEKGDLGMMGLPGSRGPMGSKGYPGSRGEKGS 153
Cdd:NF038329 186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145701009 154 RGEKGDLGPKGEKGFPGFPGMLGQKGEMGPKGEPGIAGHRGPTGRPGKRGKQGQKGDSGVMGPPGKPGPSGQP 226
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 140-195 4.83e-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: 49.41  E-value: 4.83e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145701009  140 GSKGYPGSRGEKGSRGEKGDLGPKGEKGFPGFPGMLGQKGEMGPKGEPGIAGHRGP 195
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 164-255 6.42e-07

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 51.44  E-value: 6.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145701009 164 GEKGFPGFPGMLGQKGEMGPKGEPGIAGHRGPTGRPGKRGKQGQKGDSGVMGPPGKPGPSGQPGRPGPPGPPPAgqliMG 243
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE----KG 192

                         90
                 ....*....|..
gi 145701009 244 PKGERGFPGPPG 255
Cdd:NF038329 193 PQGPRGETGPAG 204
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 119-173 1.51e-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: 1.51e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145701009  119 GPRGEKGDLGMMGLPGSRGPMGSKGYPGSRGEKGSRGEKGDLGPKGEKGFPGFPG 173
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 128-180 5.90e-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: 43.25  E-value: 5.90e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 145701009  128 GMMGLPGSRGPMGSKGYPGSRGEKGSRGEKGDLGPKGEKGFPGFPGMLGQKGE 180
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 339-363 7.70e-06

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: 42.36  E-value: 7.70e-06
                          10        20
                  ....*....|....*....|....*
gi 145701009  339 GTCGDGLLQPGEECDDGNSDVGDDC 363
Cdd:TIGR02232   2 PTCGDGIIEPGEECDDGNTTSGDGC 26
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 116-165 2.20e-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: 41.71  E-value: 2.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 145701009  116 GPEGPRGEKGDLGMMGLPGSRGPMGSKGYPGSRGEKGSRGEKGDLGPKGE 165
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
DUF4215 pfam13948
Domain of unknown function (DUF4215); The function of this family is unknown.
 341-366 2.44e-05

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


Pssm-ID: 290659  Cd Length: 47  Bit Score: 41.24  E-value: 2.44e-05
                          10        20
                  ....*....|....*....|....*.
gi 145701009  341 CGDGLLQPGEECDDGNSDVGDDCIRC 366
Cdd:pfam13948  21 CGDGIIVNNEQCDDGNNLQFDGCYQC 46
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 72-148 3.16e-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: 38.63  E-value: 3.16e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145701009   72 SPGPPGLPGKTGPKGEKGELGRpgrkgrpgppgvpgmpgpigwPGPEGPRGEKGDLGMMGLPGSRGPMGSKGYPGSR 148
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGP---------------------PGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
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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